unique_id,web-scraper-start-url,sub_chapters_x,sub_chapters-href,paragraph,is_paragraph,sub_section_headings,fig_num,sub_chapters_y,images-src,image_caption
e5c0e21a-1489-47d9-a185-213cb2f3cb81,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Extracellular matrix,False,Extracellular matrix,,,,
05c7cea1-781e-412e-81e7-011b091e4872,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Glycocalyx,False,Glycocalyx,,,,
367289cc-3b54-4b75-8e3e-08c9f43562f2,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"In addition to the many proteins in the matrix, there are some essential carbohydrate components that make up the glycocalyx. This is a carbohydrate “coat” that forms a barrier around the plasma membrane, can bind regulatory factors, and can mediate cell–cell interactions.",True,Glycocalyx,,,,
5935552c-9b5f-4686-a4f0-9bda1f3dca11,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Proteins of the matrix,False,Proteins of the matrix,,,,
76eedcf2-67de-415a-807a-1f757a34cfbc,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"The major components of the extracellular matrix form a fibrous, secreted network.",True,Proteins of the matrix,,,,
fb721721-0f09-4164-b091-c933e9777b97,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Fibronectin,False,Fibronectin,,,,
dbfce310-1fa1-4a1d-8d41-cb324477279b,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Fibronectin is a dimer held together by disulfide bonds. These dimers assemble in structural modules that serve as binding sites for other proteins such as heparin, collagen, and fibrin. These proteins are the “matrix” that allows other proteins to dock, and it has RGD loops that serve as integrin binding sites.",True,Fibronectin,,,,
93f87f2a-8a97-44e8-bf55-e9856c190e46,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,integrin,False,integrin,,,,
b38f4947-aaad-4fe4-b097-cfb087fdbcd8,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Collagen,False,Collagen,,,,
a65b0332-4cea-4ce6-94c6-d5ebf2131845,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Collagen is synthesized by fibroblasts and is the most abundant protein in the body. There are twenty-seven types of collagen, and it is often a triple helix, stabilized by hydrogen bonding. There are additional nonfibrillar forms that can form web-like structures. Synthesis of collagen requires vitamin C for formation of hydroxyproline.",True,Collagen,,,,
021a1970-17c5-4945-bbc5-1265619b7533,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"As collagen is a major component to connective tissue, it plays key roles in tendons, cornea, blood vessels, hair, and cartilage. Disorders of collagen synthesis are implicated in osteogenesis imperfecta, dwarfism, and skeletal deformities.",True,Collagen,,,,
ad957705-f4e1-4bf0-8b92-86fed079c634,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Proteoglycans,False,Proteoglycans,,,,
b0871a89-2d06-48db-a376-ca140335415e,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Structurally proteoglycans contain both proteins plus glycosaminoglycans (carbohydrates) and take on a bottle-brush structure (figure 19.1). They assemble into larger complexes, bound to a central hyaluronic acid. The overall structure is negatively charged, which attracts water, allowing it to function as a cushion.",True,Proteoglycans,Figure 19.1,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
b0871a89-2d06-48db-a376-ca140335415e,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Structurally proteoglycans contain both proteins plus glycosaminoglycans (carbohydrates) and take on a bottle-brush structure (figure 19.1). They assemble into larger complexes, bound to a central hyaluronic acid. The overall structure is negatively charged, which attracts water, allowing it to function as a cushion.",True,Proteoglycans,Figure 19.1,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
c81993b5-773e-485c-a9e9-99d0b3c4d124,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Laminin,False,Laminin,,,,
ad6bb2ae-7974-4b61-84f4-cdff10635f4b,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Laminin consists of three glycoproteins linked through disulfide bonds. They bind cell-surface receptors and are important during development and cell migration.,True,Laminin,,,,
310b5e1e-38bc-4173-9b25-1521d5297c70,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Integrins,False,Integrins,,,,
c4c4ddaa-1c23-4573-885f-6b8df42e6944,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Integrins span the plasma membrane and connect the matrix to the cellular environment (inside-out or outside-in signaling). They are associated with fibronectin (RGD sequences) on the extracellular side and have both active and inactive states (figure 19.2).,True,Integrins,Figure 19.2,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
c4c4ddaa-1c23-4573-885f-6b8df42e6944,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Integrins span the plasma membrane and connect the matrix to the cellular environment (inside-out or outside-in signaling). They are associated with fibronectin (RGD sequences) on the extracellular side and have both active and inactive states (figure 19.2).,True,Integrins,Figure 19.2,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
c4f146f3-4daf-428d-9b7d-b66d7f42a5d5,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Matrix metalloproteinases,False,Matrix metalloproteinases,,,,
e53ede4c-f1b1-434a-a290-f74a6cab7466,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,The matrix is a dynamic component and is remodeled as a part of normal growth and development. It can also be reorganized as a result of disease or pathology such as arthritis or atherosclerosis.,True,Matrix metalloproteinases,,,,
82d1c6b4-9bae-4e4f-9e51-d83a79589fa3,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"A family of enzymes, termed matrix metalloproteinases, is responsible for this remodeling, and they require metal for catalysis. Zinc is the typical cofactor, although some enzymes in the family require cobalt.",True,Matrix metalloproteinases,,,,
d910cd22-6ed3-4ec0-be3d-0c8468220314,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,metalloproteinases,False,metalloproteinases,,,,
20f431f7-b994-4da2-9775-95b6df9f039c,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Cell adhesion to the substratum,False,Cell adhesion to the substratum,,,,
5e20a8af-bd88-4a9f-ba54-0e5f8f392ee1,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Focal adhesions and hemidesmosomes (figure 19.3) serve to anchor cells to the substratum.,True,Cell adhesion to the substratum,Figure 19.3,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
5e20a8af-bd88-4a9f-ba54-0e5f8f392ee1,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Focal adhesions and hemidesmosomes (figure 19.3) serve to anchor cells to the substratum.,True,Cell adhesion to the substratum,Figure 19.3,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
0b87d11d-8d5b-40c4-92e5-646d1230a5b2,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Focal adhesions are a cluster of rapidly assembling and disassembling proteins that involves a cluster of integrins connected to actin in the cytoskeleton.,True,Cell adhesion to the substratum,,,,
c7fd4e83-ce7b-43a8-ab5c-553da706ecae,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Hemidesmosomes are the tightest of all in vivo attachments. They consist of intermediate filaments (keratin) and form an attachment between the basal surface of epithelial cells to the basement membrane.,True,Cell adhesion to the substratum,,,,
102edb0a-890a-4432-8857-45037b1f258d,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Cell–cell adhesion,False,Cell–cell adhesion,,,,
fd60497d-ca0a-41c7-b1ec-4a8f4894f44a,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Cells attach to one another through interactions of cell adhesion molecules (CAMs). These interactions can be transient involving one protein on one cell and one on another cell. There are several major classes of CAMs with biological relevance. Their roles are summarized in the table below.,True,Cell–cell adhesion,,,,
5add5577-5603-4acf-aac1-72b96b98a8cf,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,CAMs,False,CAMs,,,,
ad4e0566-6ce4-4035-a313-c15ab3572995,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Table 19.1: Major classes of CAMs with biological relevance.,True,CAMs,,,,
edc183d4-870d-4cf5-831f-d458701f91f5,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,Cell–cell adhesive junctions,False,Cell–cell adhesive junctions,,,,
75b92a47-f91f-4014-b6cb-563833e7720f,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,There are four kinds of connections between cells:,False,There are four kinds of connections between cells:,,,,
05b7b429-f7c4-4d24-8605-e9ecba289a5c,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,19.1 References and resources,True,There are four kinds of connections between cells:,,,,
fb2083ca-79a2-4a58-9475-ef9550c8af16,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,There are four kinds of connections between cells:,,,,
9714d027-8bc9-41fe-a60e-5beaef4509f2,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 7: Interactions between Cells and Their Environment.",True,There are four kinds of connections between cells:,,,,
89475d98-4f42-4bb9-8069-aa6d7941f250,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 50–51.",True,There are four kinds of connections between cells:,,,,
17bda325-e1f5-40a8-a6d3-0bc58aa9100c,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Grey, Kindred, Figure 19.1 Overview of the extracellular matrix. 2021. https://archive.org/details/19.1_20210926. CC BY 4.0. Adapted from Figure 16. CC BY 4.0. From Open Oregon.",True,There are four kinds of connections between cells:,Figure 19.1,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
17bda325-e1f5-40a8-a6d3-0bc58aa9100c,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Grey, Kindred, Figure 19.1 Overview of the extracellular matrix. 2021. https://archive.org/details/19.1_20210926. CC BY 4.0. Adapted from Figure 16. CC BY 4.0. From Open Oregon.",True,There are four kinds of connections between cells:,Figure 19.1,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
97d89e54-ac5d-4caa-97de-f957bfb33b43,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Grey, Kindred, Figure 19.2 Schematic of integrin structure… 2021. CC BY SA 3.0. Adapted from Integrin by Odysseus1479. CC BY SA 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.2,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
97d89e54-ac5d-4caa-97de-f957bfb33b43,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Grey, Kindred, Figure 19.2 Schematic of integrin structure… 2021. CC BY SA 3.0. Adapted from Integrin by Odysseus1479. CC BY SA 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.2,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
b0b1d052-bc56-43dd-84cd-bfa43921a6b4,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Grey, Kindred, Figure 19.3 Summary of cell adhesion mechanisms. 2021. https://archive.org/details/19.3_20210926. CC BY 3.0. Adapted from 402 Types of Cell Junctions new by OpenStax College. CC BY 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.3,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
b0b1d052-bc56-43dd-84cd-bfa43921a6b4,https://pressbooks.lib.vt.edu/cellbio/,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/#chapter-107-section-1,"Grey, Kindred, Figure 19.3 Summary of cell adhesion mechanisms. 2021. https://archive.org/details/19.3_20210926. CC BY 3.0. Adapted from 402 Types of Cell Junctions new by OpenStax College. CC BY 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.3,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
c4bd9b12-d7f8-483e-9635-7686729f3943,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Extracellular matrix,False,Extracellular matrix,,,,
d22a49f8-2ebd-4ac6-8ef6-898c3c33a8b7,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Glycocalyx,False,Glycocalyx,,,,
bbdf38f2-105b-43fb-8ad5-1bd218c07429,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"In addition to the many proteins in the matrix, there are some essential carbohydrate components that make up the glycocalyx. This is a carbohydrate “coat” that forms a barrier around the plasma membrane, can bind regulatory factors, and can mediate cell–cell interactions.",True,Glycocalyx,,,,
5a5e32b9-147c-4abf-827d-951ae1e60d2b,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Proteins of the matrix,False,Proteins of the matrix,,,,
f1683048-a009-46ea-adda-9982b7355ada,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"The major components of the extracellular matrix form a fibrous, secreted network.",True,Proteins of the matrix,,,,
47e48df1-13b7-4c79-96f5-be1b2272aaa7,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Fibronectin,False,Fibronectin,,,,
470f771d-e8bb-45f4-8775-ea400d6621cd,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Fibronectin is a dimer held together by disulfide bonds. These dimers assemble in structural modules that serve as binding sites for other proteins such as heparin, collagen, and fibrin. These proteins are the “matrix” that allows other proteins to dock, and it has RGD loops that serve as integrin binding sites.",True,Fibronectin,,,,
834cd5ce-35a4-4504-9344-54680eb053eb,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,integrin,False,integrin,,,,
b431d6ab-0475-4b19-af9c-1bef66c8df40,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Collagen,False,Collagen,,,,
755bc1d9-f8e9-46e3-9147-3646b117d70f,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Collagen is synthesized by fibroblasts and is the most abundant protein in the body. There are twenty-seven types of collagen, and it is often a triple helix, stabilized by hydrogen bonding. There are additional nonfibrillar forms that can form web-like structures. Synthesis of collagen requires vitamin C for formation of hydroxyproline.",True,Collagen,,,,
b0f5a2d0-d8ae-421e-a352-7b644adf885d,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"As collagen is a major component to connective tissue, it plays key roles in tendons, cornea, blood vessels, hair, and cartilage. Disorders of collagen synthesis are implicated in osteogenesis imperfecta, dwarfism, and skeletal deformities.",True,Collagen,,,,
a186e3d3-cd56-4265-8d2c-7917a4a9c309,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Proteoglycans,False,Proteoglycans,,,,
33659c22-369b-45b3-b35b-5497946a382f,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Structurally proteoglycans contain both proteins plus glycosaminoglycans (carbohydrates) and take on a bottle-brush structure (figure 19.1). They assemble into larger complexes, bound to a central hyaluronic acid. The overall structure is negatively charged, which attracts water, allowing it to function as a cushion.",True,Proteoglycans,Figure 19.1,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
33659c22-369b-45b3-b35b-5497946a382f,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Structurally proteoglycans contain both proteins plus glycosaminoglycans (carbohydrates) and take on a bottle-brush structure (figure 19.1). They assemble into larger complexes, bound to a central hyaluronic acid. The overall structure is negatively charged, which attracts water, allowing it to function as a cushion.",True,Proteoglycans,Figure 19.1,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
5b65d6f1-d3a6-4938-a5d1-204e08265bee,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Laminin,False,Laminin,,,,
2317e2bb-ccbf-4cf6-8aaf-703083134c47,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Laminin consists of three glycoproteins linked through disulfide bonds. They bind cell-surface receptors and are important during development and cell migration.,True,Laminin,,,,
e968e8ad-78e3-402a-b5e1-640d92dcba98,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Integrins,False,Integrins,,,,
6c85bb66-6e06-4d46-b475-f0550da11cf9,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Integrins span the plasma membrane and connect the matrix to the cellular environment (inside-out or outside-in signaling). They are associated with fibronectin (RGD sequences) on the extracellular side and have both active and inactive states (figure 19.2).,True,Integrins,Figure 19.2,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
6c85bb66-6e06-4d46-b475-f0550da11cf9,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Integrins span the plasma membrane and connect the matrix to the cellular environment (inside-out or outside-in signaling). They are associated with fibronectin (RGD sequences) on the extracellular side and have both active and inactive states (figure 19.2).,True,Integrins,Figure 19.2,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
63a6d16f-0401-4e98-8852-9d952dbcb325,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Matrix metalloproteinases,False,Matrix metalloproteinases,,,,
5a519d98-6ae2-4ce1-bf1b-8b9dead8a3fc,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,The matrix is a dynamic component and is remodeled as a part of normal growth and development. It can also be reorganized as a result of disease or pathology such as arthritis or atherosclerosis.,True,Matrix metalloproteinases,,,,
22b3ff45-55bd-4e2e-9ee8-f2afadd2cb4a,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"A family of enzymes, termed matrix metalloproteinases, is responsible for this remodeling, and they require metal for catalysis. Zinc is the typical cofactor, although some enzymes in the family require cobalt.",True,Matrix metalloproteinases,,,,
edc6adbe-28fb-4de2-9e0b-20628aeec504,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,metalloproteinases,False,metalloproteinases,,,,
2ab561ad-10b5-44f0-93a1-715947e0e987,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Cell adhesion to the substratum,False,Cell adhesion to the substratum,,,,
4bd54dbf-dcd8-4294-9f81-09871b981ab8,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Focal adhesions and hemidesmosomes (figure 19.3) serve to anchor cells to the substratum.,True,Cell adhesion to the substratum,Figure 19.3,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
4bd54dbf-dcd8-4294-9f81-09871b981ab8,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Focal adhesions and hemidesmosomes (figure 19.3) serve to anchor cells to the substratum.,True,Cell adhesion to the substratum,Figure 19.3,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
38caa02c-90ab-4666-a309-4425f00d770d,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Focal adhesions are a cluster of rapidly assembling and disassembling proteins that involves a cluster of integrins connected to actin in the cytoskeleton.,True,Cell adhesion to the substratum,,,,
d587a6a7-3b4e-477e-a9ea-1e42c485784f,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Hemidesmosomes are the tightest of all in vivo attachments. They consist of intermediate filaments (keratin) and form an attachment between the basal surface of epithelial cells to the basement membrane.,True,Cell adhesion to the substratum,,,,
cb7a1b65-9753-4211-b995-7e13740df6c0,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Cell–cell adhesion,False,Cell–cell adhesion,,,,
eb62fd16-1261-4075-94c6-e59894165281,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Cells attach to one another through interactions of cell adhesion molecules (CAMs). These interactions can be transient involving one protein on one cell and one on another cell. There are several major classes of CAMs with biological relevance. Their roles are summarized in the table below.,True,Cell–cell adhesion,,,,
f303ea37-70f4-41e6-9c96-6ee8424776ef,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,CAMs,False,CAMs,,,,
c8ca5bcd-02c2-4c15-95cb-8f8144cffc15,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Table 19.1: Major classes of CAMs with biological relevance.,True,CAMs,,,,
0ce23148-6c26-4679-85d3-1522f7f454d2,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,Cell–cell adhesive junctions,False,Cell–cell adhesive junctions,,,,
d623c054-2a76-47fb-b093-18c2d1fe60bf,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,There are four kinds of connections between cells:,False,There are four kinds of connections between cells:,,,,
ee37b034-7940-4798-89b5-93b512b231a1,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,19.1 References and resources,True,There are four kinds of connections between cells:,,,,
b29f24ea-5711-4609-8ea0-212af7c14ed7,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,There are four kinds of connections between cells:,,,,
2196f611-411d-4421-b251-00d5ac073fa1,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 7: Interactions between Cells and Their Environment.",True,There are four kinds of connections between cells:,,,,
2e0496d6-d2aa-46c6-8ba6-703047de5e2b,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 50–51.",True,There are four kinds of connections between cells:,,,,
0d66a1fd-8e80-4200-a27f-33d3036cdde0,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Grey, Kindred, Figure 19.1 Overview of the extracellular matrix. 2021. https://archive.org/details/19.1_20210926. CC BY 4.0. Adapted from Figure 16. CC BY 4.0. From Open Oregon.",True,There are four kinds of connections between cells:,Figure 19.1,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
0d66a1fd-8e80-4200-a27f-33d3036cdde0,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Grey, Kindred, Figure 19.1 Overview of the extracellular matrix. 2021. https://archive.org/details/19.1_20210926. CC BY 4.0. Adapted from Figure 16. CC BY 4.0. From Open Oregon.",True,There are four kinds of connections between cells:,Figure 19.1,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
70f58304-947f-4525-8c3c-8feabb689b6c,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Grey, Kindred, Figure 19.2 Schematic of integrin structure… 2021. CC BY SA 3.0. Adapted from Integrin by Odysseus1479. CC BY SA 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.2,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
70f58304-947f-4525-8c3c-8feabb689b6c,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Grey, Kindred, Figure 19.2 Schematic of integrin structure… 2021. CC BY SA 3.0. Adapted from Integrin by Odysseus1479. CC BY SA 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.2,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
fa9efb64-0d74-47a4-9e41-b3c5aff3c729,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Grey, Kindred, Figure 19.3 Summary of cell adhesion mechanisms. 2021. https://archive.org/details/19.3_20210926. CC BY 3.0. Adapted from 402 Types of Cell Junctions new by OpenStax College. CC BY 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.3,19.1 Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
fa9efb64-0d74-47a4-9e41-b3c5aff3c729,https://pressbooks.lib.vt.edu/cellbio/,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/cellbio/chapter/extracellular-matrix/,"Grey, Kindred, Figure 19.3 Summary of cell adhesion mechanisms. 2021. https://archive.org/details/19.3_20210926. CC BY 3.0. Adapted from 402 Types of Cell Junctions new by OpenStax College. CC BY 3.0. From Wikimedia Commons.",True,There are four kinds of connections between cells:,Figure 19.3,19. Extracellular Matrix,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
1097bc3e-f06c-4a29-864a-de482fbea113,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,There are four kinds of connections between cells:,Figure 18.2,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
1097bc3e-f06c-4a29-864a-de482fbea113,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,There are four kinds of connections between cells:,Figure 18.2,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
1097bc3e-f06c-4a29-864a-de482fbea113,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,There are four kinds of connections between cells:,Figure 18.2,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
09a44727-5944-4178-965c-4d0737fb8dae,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Microfilaments thicken the cortex around the cellʼs inner edge. Like rubber bands, they resist tension. There are microtubules in the cellʼs interior where they maintain their shape by resisting compressive forces. There are intermediate filaments throughout the cell that hold organelles in place.",True,There are four kinds of connections between cells:,,,,
1c31ef23-d1fa-4002-9127-abf8baa76e11,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,cellʼs,False,cellʼs,,,,
fbf73b8b-6b6e-4378-b0b6-90ffd0b43e88,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Microfilaments,False,Microfilaments,,,,
3112c05a-0535-4cc7-bf13-49e7a6be1d3f,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
3112c05a-0535-4cc7-bf13-49e7a6be1d3f,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
3112c05a-0535-4cc7-bf13-49e7a6be1d3f,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
0907528b-eba0-4303-b1fc-1e30684edea4,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"ATP powers actin to assemble its filamentous form, which serves as a track for the movement of a motor protein we call myosin. This enables actin to engage in cellular events requiring motion, such as cell division in eukaryotic cells. Actin and myosin are plentiful in muscle cells.",True,Microfilaments,,,,
ae9368ca-d113-44a6-9610-2c36c38cf551,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Microfilaments also provide some rigidity and shape to the cell. They can depolymerize (disassemble) and reform quickly, thus enabling a cell to change its shape and move.",True,Microfilaments,,,,
0237f5f3-d7ad-451b-8760-affab16ab891,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Intermediate filaments,False,Intermediate filaments,,,,
2aa8d161-6203-4386-b283-24f5bd42a670,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
2aa8d161-6203-4386-b283-24f5bd42a670,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
2aa8d161-6203-4386-b283-24f5bd42a670,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
d1dccd26-9a40-494f-abcb-7c49affe18cd,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
d1dccd26-9a40-494f-abcb-7c49affe18cd,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
d1dccd26-9a40-494f-abcb-7c49affe18cd,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
76215f44-8d54-4ed7-844a-fcf22411f661,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,The intermediate filaments are the most diverse group of cytoskeletal elements. They are unbranched and rope-like with long fibrous subunits. There is no polarity associated with their assembly. Intermediate filaments are classified by their location and function. The table below summarizes various types of intermediate filaments.,True,Intermediate filaments,,,,
d6fef642-3bce-41a9-9c2c-11545bab765e,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Table 18.1: Proteins and their functions.,True,Intermediate filaments,,,,
d44eab6a-d0e6-43db-9554-eff7e76ea6b0,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Microtubules,False,Microtubules,,,,
26b7f8b5-499b-4534-bb31-63250e654fc5,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
26b7f8b5-499b-4534-bb31-63250e654fc5,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
26b7f8b5-499b-4534-bb31-63250e654fc5,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
a5907b4a-36a8-4a9c-b7be-6c5b8fd1e739,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Like microfilaments, microtubules can disassemble and reform quickly using GTP. The tube is formed from polymerized dimers of α-tubulin and β-tubulin, two globular proteins. These proteins form long chains that comprise the microtubuleʼs walls. The assembly is slow and occurs from the plus end, which is designated by a row of β-tubulin. Disassembly can occur rapidly at the plus end. (Note the minus end has a row of α-tubulin.)",True,Microtubules,,,,
f26c84b4-a62f-4216-840c-00246af64a25,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Microtubules are also the structural elements of flagella, cilia, and centrioles (the latter are the centrosomeʼs two perpendicular bodies). In animal cells, the centrosome is the microtubule-organizing center.",True,Microtubules,,,,
ce05d5ec-771b-4f5d-8c90-f8f19007b77a,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Flagella and cilia,False,Flagella and cilia,,,,
ffe12d1e-4b92-4b66-9e6e-23a8347017e7,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"The flagella (singular = flagellum) are long, hair-like structures that extend from the plasma membrane and enable an entire cell to move. When present, the cell has just one flagellum or a few flagella.",True,Flagella and cilia,,,,
87b0431a-fae2-4668-bf7e-d96bb4b3cdd9,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"However, when cilia (singular = cilium) are present, many of them extend along the plasma membraneʼs entire surface. They are short, hair-like structures that move entire cells (such as paramecia) or substances along the cellʼs outer surface (for example, the cilia of cells lining the Fallopian tubes that move the ovum toward the uterus, or cilia lining the cells of the respiratory tract that trap particulate matter and move it toward your nostrils).",True,Flagella and cilia,,,,
282b3b9b-78d6-46ee-87f1-eed28c5106e8,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
282b3b9b-78d6-46ee-87f1-eed28c5106e8,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
282b3b9b-78d6-46ee-87f1-eed28c5106e8,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
726f254e-67ce-4609-8923-825fe56deb98,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,18.1 References and resources,True,Flagella and cilia,,,,
8de04fb4-faa7-4d1a-9014-9ecd3be6078f,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Flagella and cilia,,,,
e8f59ea5-e5a2-48f7-9b0e-4623c1ff2211,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 9: The Cytoskeleton and Cell Mobility.",True,Flagella and cilia,,,,
9609c241-c248-44a9-93de-77484094e4c2,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 48–49.",True,Flagella and cilia,,,,
83d045d4-a113-419a-a82e-b49114ab94d1,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
83d045d4-a113-419a-a82e-b49114ab94d1,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
83d045d4-a113-419a-a82e-b49114ab94d1,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
b126b4fe-6763-4f7a-9e00-a8fe0ba6458e,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
b126b4fe-6763-4f7a-9e00-a8fe0ba6458e,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
b126b4fe-6763-4f7a-9e00-a8fe0ba6458e,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
2ef36588-367a-40af-b4dc-92a53d732992,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
2ef36588-367a-40af-b4dc-92a53d732992,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
2ef36588-367a-40af-b4dc-92a53d732992,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
6b71cbf7-abc4-412b-8e8e-017f154c34bf,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
6b71cbf7-abc4-412b-8e8e-017f154c34bf,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
6b71cbf7-abc4-412b-8e8e-017f154c34bf,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
397f0ccf-8a34-4bcc-b8c8-b229dc70a80d,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
397f0ccf-8a34-4bcc-b8c8-b229dc70a80d,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
397f0ccf-8a34-4bcc-b8c8-b229dc70a80d,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
edb741cd-16b6-4f76-9220-2e304a0031f5,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
edb741cd-16b6-4f76-9220-2e304a0031f5,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
edb741cd-16b6-4f76-9220-2e304a0031f5,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
0a91747f-a15f-400e-a97e-bf1356d4568c,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,18.2 Cell Movement,True,Flagella and cilia,,,,
488828ca-11e2-4912-8264-91505ead7037,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
488828ca-11e2-4912-8264-91505ead7037,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
488828ca-11e2-4912-8264-91505ead7037,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
2743b4f6-9212-41aa-9d46-f3971a8c2206,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,dyneins,False,dyneins,,,,
b4ba28c1-40d1-4d0e-851f-63e8692cca35,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,kinesins,False,kinesins,,,,
9b2a54cf-6318-4954-b251-54ace8491944,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,mechanochemical,False,mechanochemical,,,,
cec20ede-c0ae-4f1b-9bcf-cd46d8770691,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Myosin,False,Myosin,,,,
bee63800-123d-4c26-ab96-62c1f6a2793a,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Myosin can be characterized as conventional or unconventional, with characteristic head groups (that bind ATP) and unique tails. Myosin is essential for muscle contraction, and this occurs in striated muscle (skeletal and cardiac) after specific binding sites on the actin have been exposed in response to the interaction between calcium ions (Ca2+) and proteins (troponin and tropomyosin) that “shield” the actin-binding sites. Ca2+ is also required for the contraction of smooth muscle, although its role is different: here Ca2+ activates enzymes, which in turn activate myosin heads. All muscles require adenosine triphosphate (ATP) to continue the process of contracting, and they all relax when the Ca2+ is removed and the actin-binding sites are re-shielded.",True,Myosin,,,,
ede75fc9-afe1-4e19-887e-6088d2c53ff5,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Ca2,False,Ca2,,,,
c1c93de6-a9a6-4cd4-8d2c-605be8b27f70,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Dynein,False,Dynein,,,,
7d9c3e77-d9fa-4b4d-ab9b-60628d7c3a85,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Dynein is a large motor protein that typically transports organelles (lysosomes or endosomes). It moves toward the minus end (α-tubulin) of microtubules, which is in the direction of the cell body.",True,Dynein,,,,
aa182a00-d744-4225-ac63-cf25946f31eb,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,Kinesin,False,Kinesin,,,,
6f43e8d0-d4c4-4374-a988-8df817adf5cc,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
6f43e8d0-d4c4-4374-a988-8df817adf5cc,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
6f43e8d0-d4c4-4374-a988-8df817adf5cc,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
69f82ecb-d59a-4194-a202-44ced62a8233,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,18.2 References and resources,True,Kinesin,,,,
5069a7b3-ca78-4c32-ba1d-1476d75c5f9f,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
5069a7b3-ca78-4c32-ba1d-1476d75c5f9f,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
5069a7b3-ca78-4c32-ba1d-1476d75c5f9f,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
9119cb92-2bdc-4571-9c1c-ec1ea605b627,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
9119cb92-2bdc-4571-9c1c-ec1ea605b627,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
9119cb92-2bdc-4571-9c1c-ec1ea605b627,https://pressbooks.lib.vt.edu/cellbio/,18.2 Cell Movement,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-2,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
b3fa690a-e9a2-4552-84e0-89a3f06b857e,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,Kinesin,Figure 18.2,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
b3fa690a-e9a2-4552-84e0-89a3f06b857e,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,Kinesin,Figure 18.2,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
b3fa690a-e9a2-4552-84e0-89a3f06b857e,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,Kinesin,Figure 18.2,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
c98cf670-d13b-40c0-8a08-417cb2225997,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Microfilaments thicken the cortex around the cellʼs inner edge. Like rubber bands, they resist tension. There are microtubules in the cellʼs interior where they maintain their shape by resisting compressive forces. There are intermediate filaments throughout the cell that hold organelles in place.",True,Kinesin,,,,
21240361-52f2-4db7-b4c6-8e92f979774a,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,cellʼs,False,cellʼs,,,,
5d4c5d6b-0a8c-4230-87d6-d85f7acdf85a,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Microfilaments,False,Microfilaments,,,,
f1610ff8-c064-4b2b-becd-42e81e0c7393,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
f1610ff8-c064-4b2b-becd-42e81e0c7393,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
f1610ff8-c064-4b2b-becd-42e81e0c7393,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
011004a4-5a4b-40f7-ab7b-10990b9944b5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"ATP powers actin to assemble its filamentous form, which serves as a track for the movement of a motor protein we call myosin. This enables actin to engage in cellular events requiring motion, such as cell division in eukaryotic cells. Actin and myosin are plentiful in muscle cells.",True,Microfilaments,,,,
a4a35ed7-ef51-4b8e-a36f-5aa4e4dba62c,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Microfilaments also provide some rigidity and shape to the cell. They can depolymerize (disassemble) and reform quickly, thus enabling a cell to change its shape and move.",True,Microfilaments,,,,
90897c0e-2b3a-4c0c-b531-3d9bfb62aa1a,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Intermediate filaments,False,Intermediate filaments,,,,
6ab0fde9-2c51-430c-afdb-d6544aa42709,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
6ab0fde9-2c51-430c-afdb-d6544aa42709,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
6ab0fde9-2c51-430c-afdb-d6544aa42709,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
5606e50c-6dd1-4dd0-b13f-c8bd6e5cd6c8,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
5606e50c-6dd1-4dd0-b13f-c8bd6e5cd6c8,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
5606e50c-6dd1-4dd0-b13f-c8bd6e5cd6c8,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
0633b4f0-adbb-49e0-896e-f70844b3a33e,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,The intermediate filaments are the most diverse group of cytoskeletal elements. They are unbranched and rope-like with long fibrous subunits. There is no polarity associated with their assembly. Intermediate filaments are classified by their location and function. The table below summarizes various types of intermediate filaments.,True,Intermediate filaments,,,,
44e1c945-77f7-4842-8808-3cf20524435b,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Table 18.1: Proteins and their functions.,True,Intermediate filaments,,,,
34dc8788-58fd-42c6-b5e8-b809b67b7e2b,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Microtubules,False,Microtubules,,,,
a1cbdbf1-6ee8-42bd-9ecf-f7753a9870e2,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
a1cbdbf1-6ee8-42bd-9ecf-f7753a9870e2,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
a1cbdbf1-6ee8-42bd-9ecf-f7753a9870e2,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
4463b669-c14a-4486-9106-29550361c2f7,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Like microfilaments, microtubules can disassemble and reform quickly using GTP. The tube is formed from polymerized dimers of α-tubulin and β-tubulin, two globular proteins. These proteins form long chains that comprise the microtubuleʼs walls. The assembly is slow and occurs from the plus end, which is designated by a row of β-tubulin. Disassembly can occur rapidly at the plus end. (Note the minus end has a row of α-tubulin.)",True,Microtubules,,,,
a9ac98c2-d61f-4827-8971-6e8be1898218,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Microtubules are also the structural elements of flagella, cilia, and centrioles (the latter are the centrosomeʼs two perpendicular bodies). In animal cells, the centrosome is the microtubule-organizing center.",True,Microtubules,,,,
3230832c-7363-47bd-9443-6743666d7805,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Flagella and cilia,False,Flagella and cilia,,,,
514840b2-c7ab-4481-98de-c741ecc0480c,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"The flagella (singular = flagellum) are long, hair-like structures that extend from the plasma membrane and enable an entire cell to move. When present, the cell has just one flagellum or a few flagella.",True,Flagella and cilia,,,,
a5dba055-64ea-40c2-9943-f7c5c1ebf03b,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"However, when cilia (singular = cilium) are present, many of them extend along the plasma membraneʼs entire surface. They are short, hair-like structures that move entire cells (such as paramecia) or substances along the cellʼs outer surface (for example, the cilia of cells lining the Fallopian tubes that move the ovum toward the uterus, or cilia lining the cells of the respiratory tract that trap particulate matter and move it toward your nostrils).",True,Flagella and cilia,,,,
54e691c4-2e83-4c85-a48c-b273cfad30e1,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
54e691c4-2e83-4c85-a48c-b273cfad30e1,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
54e691c4-2e83-4c85-a48c-b273cfad30e1,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
5816007f-7241-4780-b297-53bc58cd25dd,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,18.1 References and resources,True,Flagella and cilia,,,,
ba4a6e0c-bee2-406c-aebf-1452df385b86,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Flagella and cilia,,,,
848b9e70-a61c-46fb-a6e6-2337ce8fd2e2,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 9: The Cytoskeleton and Cell Mobility.",True,Flagella and cilia,,,,
72af6047-4bba-47a9-b2cf-d1b80231b148,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 48–49.",True,Flagella and cilia,,,,
c0c0e796-302b-4e5d-bf2b-1b17b1ea1ab0,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
c0c0e796-302b-4e5d-bf2b-1b17b1ea1ab0,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
c0c0e796-302b-4e5d-bf2b-1b17b1ea1ab0,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
f134029b-8698-415b-ad86-441699178709,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
f134029b-8698-415b-ad86-441699178709,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
f134029b-8698-415b-ad86-441699178709,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
55eab4ab-4299-44b1-9b30-6a30907de360,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
55eab4ab-4299-44b1-9b30-6a30907de360,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
55eab4ab-4299-44b1-9b30-6a30907de360,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
1a153b12-018f-4dd8-afc4-7677983d45b5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
1a153b12-018f-4dd8-afc4-7677983d45b5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
1a153b12-018f-4dd8-afc4-7677983d45b5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
7a9dbdd0-32d7-47d8-b2c1-055e3bd1bfdf,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
7a9dbdd0-32d7-47d8-b2c1-055e3bd1bfdf,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
7a9dbdd0-32d7-47d8-b2c1-055e3bd1bfdf,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
b54b8dad-4826-486a-b265-43dd5974deb5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
b54b8dad-4826-486a-b265-43dd5974deb5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
b54b8dad-4826-486a-b265-43dd5974deb5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
cea2958d-ecf8-44f1-8dc7-66cfbb14bb96,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,18.2 Cell Movement,True,Flagella and cilia,,,,
672896a3-885f-457b-a152-8e22aba74a75,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
672896a3-885f-457b-a152-8e22aba74a75,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
672896a3-885f-457b-a152-8e22aba74a75,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
156c4cb7-8975-41ad-a944-bb4f1d6b4e73,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,dyneins,False,dyneins,,,,
9ac77243-9f03-47b4-b427-9076737a83be,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,kinesins,False,kinesins,,,,
01d01600-7462-4472-8144-5b779f184f30,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,mechanochemical,False,mechanochemical,,,,
ee8369df-f13c-47a7-846c-23e5dafc4455,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Myosin,False,Myosin,,,,
f33331f7-c513-4751-b426-a8c23a89aa2e,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Myosin can be characterized as conventional or unconventional, with characteristic head groups (that bind ATP) and unique tails. Myosin is essential for muscle contraction, and this occurs in striated muscle (skeletal and cardiac) after specific binding sites on the actin have been exposed in response to the interaction between calcium ions (Ca2+) and proteins (troponin and tropomyosin) that “shield” the actin-binding sites. Ca2+ is also required for the contraction of smooth muscle, although its role is different: here Ca2+ activates enzymes, which in turn activate myosin heads. All muscles require adenosine triphosphate (ATP) to continue the process of contracting, and they all relax when the Ca2+ is removed and the actin-binding sites are re-shielded.",True,Myosin,,,,
136221bb-a9b2-4828-b160-93235ea6e5da,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Ca2,False,Ca2,,,,
b7f70a6d-20f1-48e1-88a2-258b0fdfcb70,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Dynein,False,Dynein,,,,
a750eb9d-c0a0-4b4c-a834-dd15c8e5b1e9,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Dynein is a large motor protein that typically transports organelles (lysosomes or endosomes). It moves toward the minus end (α-tubulin) of microtubules, which is in the direction of the cell body.",True,Dynein,,,,
040358b4-0c83-47d0-b79e-83b4232ca0f8,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,Kinesin,False,Kinesin,,,,
6e0e7956-c3eb-477d-8f30-e86b5b2f240a,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
6e0e7956-c3eb-477d-8f30-e86b5b2f240a,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
6e0e7956-c3eb-477d-8f30-e86b5b2f240a,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
ec159646-18ac-4a97-9fb2-6fbf24c832a5,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,18.2 References and resources,True,Kinesin,,,,
8627818f-ad1b-4326-87e6-c176cf1cf634,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
8627818f-ad1b-4326-87e6-c176cf1cf634,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
8627818f-ad1b-4326-87e6-c176cf1cf634,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
6c667c3c-cb6e-4c83-a02d-6cf278288160,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
6c667c3c-cb6e-4c83-a02d-6cf278288160,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
6c667c3c-cb6e-4c83-a02d-6cf278288160,https://pressbooks.lib.vt.edu/cellbio/,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/#chapter-105-section-1,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
b9096105-542d-4a38-8ef7-2398342f6815,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,Kinesin,Figure 18.2,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
b9096105-542d-4a38-8ef7-2398342f6815,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,Kinesin,Figure 18.2,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
b9096105-542d-4a38-8ef7-2398342f6815,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"The collection of these fibers plays key roles in structure and support, intracellular transport, contractility and motility, as well as spacial organization (figure 18.2).",True,Kinesin,Figure 18.2,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
fbd5255a-ebc3-4562-9b86-b9966bbbacdc,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Microfilaments thicken the cortex around the cellʼs inner edge. Like rubber bands, they resist tension. There are microtubules in the cellʼs interior where they maintain their shape by resisting compressive forces. There are intermediate filaments throughout the cell that hold organelles in place.",True,Kinesin,,,,
7f795ad7-6502-44c5-8f10-59cd62543b50,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,cellʼs,False,cellʼs,,,,
2952544b-7e3c-489f-9130-80783f52c4f7,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Microfilaments,False,Microfilaments,,,,
96808f5a-275c-4a16-98ac-aecadaed4947,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
96808f5a-275c-4a16-98ac-aecadaed4947,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
96808f5a-275c-4a16-98ac-aecadaed4947,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Of the three types of protein fibers in the cytoskeleton, microfilaments are the narrowest. They function in cellular movement, have a diameter of about 7 to 8 nm, and are comprised of two globular protein intertwined strands, which we call actin (figure 18.3). For this reason, we also call microfilaments actin filaments.",True,Microfilaments,Figure 18.3,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
5e1cf9f2-1a93-41b4-b556-8abef9db32e6,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"ATP powers actin to assemble its filamentous form, which serves as a track for the movement of a motor protein we call myosin. This enables actin to engage in cellular events requiring motion, such as cell division in eukaryotic cells. Actin and myosin are plentiful in muscle cells.",True,Microfilaments,,,,
de2cc18e-d731-41f9-af84-97107eb14531,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Microfilaments also provide some rigidity and shape to the cell. They can depolymerize (disassemble) and reform quickly, thus enabling a cell to change its shape and move.",True,Microfilaments,,,,
c39f658a-7f93-4df7-944d-24661fefb5f2,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Intermediate filaments,False,Intermediate filaments,,,,
d2e5b306-c5af-45a7-9357-f4bb8d1826f9,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
d2e5b306-c5af-45a7-9357-f4bb8d1826f9,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
d2e5b306-c5af-45a7-9357-f4bb8d1826f9,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Several strands of fibrous proteins that are wound together comprise intermediate filaments (figure 18.4). These cytoskeleton elements get their name from the fact that their diameter, 10 to 12 nm, is between those of microfilaments and microtubules.",True,Intermediate filaments,Figure 18.4,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
94996251-5d63-4555-b808-da6b3302afca,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
94996251-5d63-4555-b808-da6b3302afca,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
94996251-5d63-4555-b808-da6b3302afca,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Intermediate filaments have no role in cell movement. Their function is purely structural. They bear tension, thus maintaining the cellʼs shape, and anchor the nucleus and other organelles in place (figure 18.1).",True,Intermediate filaments,Figure 18.1,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
94aa5a59-1b27-4370-a418-7ce1923a2f2c,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,The intermediate filaments are the most diverse group of cytoskeletal elements. They are unbranched and rope-like with long fibrous subunits. There is no polarity associated with their assembly. Intermediate filaments are classified by their location and function. The table below summarizes various types of intermediate filaments.,True,Intermediate filaments,,,,
175a71e0-1712-42e1-813c-77caa58fea3b,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Table 18.1: Proteins and their functions.,True,Intermediate filaments,,,,
f15f41f2-629a-46ff-a520-12b6accb7365,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Microtubules,False,Microtubules,,,,
86af9a0c-9120-49b2-aee3-9b7e681e5059,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
86af9a0c-9120-49b2-aee3-9b7e681e5059,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
86af9a0c-9120-49b2-aee3-9b7e681e5059,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"As their name implies, microtubules are small hollow tubes. With a diameter of about 25 nm, microtubules are cytoskeletonsʼ widest components. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell (figure 18.5).",True,Microtubules,Figure 18.5,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
3e3f447e-c941-40ca-a736-8880b5b652ab,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Like microfilaments, microtubules can disassemble and reform quickly using GTP. The tube is formed from polymerized dimers of α-tubulin and β-tubulin, two globular proteins. These proteins form long chains that comprise the microtubuleʼs walls. The assembly is slow and occurs from the plus end, which is designated by a row of β-tubulin. Disassembly can occur rapidly at the plus end. (Note the minus end has a row of α-tubulin.)",True,Microtubules,,,,
d3a07491-a4d8-4b32-a2e2-af361f470cfd,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Microtubules are also the structural elements of flagella, cilia, and centrioles (the latter are the centrosomeʼs two perpendicular bodies). In animal cells, the centrosome is the microtubule-organizing center.",True,Microtubules,,,,
a2ff2ebb-dedf-49ff-83fa-a22f7d7f8a6e,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Flagella and cilia,False,Flagella and cilia,,,,
cc5974e4-a2ac-41db-ac8f-e4be64cdc50b,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"The flagella (singular = flagellum) are long, hair-like structures that extend from the plasma membrane and enable an entire cell to move. When present, the cell has just one flagellum or a few flagella.",True,Flagella and cilia,,,,
7dd106ef-f0a7-494a-8bd9-218309a217fd,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"However, when cilia (singular = cilium) are present, many of them extend along the plasma membraneʼs entire surface. They are short, hair-like structures that move entire cells (such as paramecia) or substances along the cellʼs outer surface (for example, the cilia of cells lining the Fallopian tubes that move the ovum toward the uterus, or cilia lining the cells of the respiratory tract that trap particulate matter and move it toward your nostrils).",True,Flagella and cilia,,,,
44929793-a634-4dab-93da-7cc00720a184,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
44929793-a634-4dab-93da-7cc00720a184,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
44929793-a634-4dab-93da-7cc00720a184,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Despite their differences in length and number, flagella and cilia share a common structural arrangement of microtubules called a “9 + 2 array.” This is an appropriate name because a single flagellum or cilium is made of a ring of nine microtubule doublets, surrounding a single microtubule doublet (axoneme) in the center (figure 18.6).",True,Flagella and cilia,Figure 18.6,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
20eb96bd-f1de-4f80-bbd9-887644757793,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,18.1 References and resources,True,Flagella and cilia,,,,
55896417-7e9a-45c9-a472-46fc1da8fa88,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Flagella and cilia,,,,
0c118150-8a77-4cb4-8d8f-98e73ee41f03,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 9: The Cytoskeleton and Cell Mobility.",True,Flagella and cilia,,,,
7c788a44-609f-4c41-84c7-62f14fdaa59a,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 48–49.",True,Flagella and cilia,,,,
d78ff02f-7160-42b0-bafe-0fd482e1aa54,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
d78ff02f-7160-42b0-bafe-0fd482e1aa54,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
d78ff02f-7160-42b0-bafe-0fd482e1aa54,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Dartmouth Electron Microscope Facility, Dartmouth College. Figure 18.6 This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet. Scale bar data from Matt Russell. Public domain. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.6,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
a224bdc4-768d-41d1-b654-9ad017f6a4b2,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
a224bdc4-768d-41d1-b654-9ad017f6a4b2,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
a224bdc4-768d-41d1-b654-9ad017f6a4b2,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.1 Summary of the three major types of structural filaments. 2021. https://archive.org/details/18.1_20210926. CC BY 4.0. Adapted from Figure 3.18. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.1,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
074e5158-9212-42a3-ad3d-e9da67573e8e,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
074e5158-9212-42a3-ad3d-e9da67573e8e,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
074e5158-9212-42a3-ad3d-e9da67573e8e,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.2 Spatial organization of the three types of fibers… 2021. https://archive.org/details/18.2_20210926. CC BY 4.0. Adapted from Figure 4.22. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.2,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
ec7e1d27-1dd0-4d19-ac73-3112c565c711,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
ec7e1d27-1dd0-4d19-ac73-3112c565c711,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
ec7e1d27-1dd0-4d19-ac73-3112c565c711,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.3 Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments. 2021. https://archive.org/details/18.3_20210926. CC BY 4.0. Adapted from Figure 4.23. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.3,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
90878f1d-d05c-45ce-971c-bfd02a966921,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
90878f1d-d05c-45ce-971c-bfd02a966921,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
90878f1d-d05c-45ce-971c-bfd02a966921,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.4 Several strands of fibrous proteins that are wound together comprise intermediate filaments. 2021. https://archive.org/details/18.4_20210926. CC BY 4.0. Adapted from Figure 4.24. CC BY 4.0. From OpenStax.",True,Flagella and cilia,Figure 18.4,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
cef5179e-a6bd-4997-a9b5-03fb803e8454,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
cef5179e-a6bd-4997-a9b5-03fb803e8454,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
cef5179e-a6bd-4997-a9b5-03fb803e8454,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.5 Microtubules are hollow. Their walls consist of 13 polymerized dimers of \(\alpha\)-tubulin and \(\beta\)-tubulin. The left image shows the tube’s molecular structure. 2021. https://archive.org/details/18.5_20210926. CC BY-SA 4.0. Adapted from Microtubule structure esp by Posible2006. CC BY-SA 4.0. From Wikimedia Commons.",True,Flagella and cilia,Figure 18.5,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
92a627ee-8bd6-4269-bd8b-83ca75c80818,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,18.2 Cell Movement,True,Flagella and cilia,,,,
2a340c24-f197-47ee-8426-8db224cd1da2,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
2a340c24-f197-47ee-8426-8db224cd1da2,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
2a340c24-f197-47ee-8426-8db224cd1da2,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Motor proteins, such as myosins, dyneins, and kinesins (figure 18.7), move along cytoskeletal filaments via a force-dependent mechanism that is driven by the hydrolysis of ATP molecules. Motor proteins propel themselves along the cytoskeleton using a mechanochemical cycle of filament binding, conformational change, filament release, conformation reversal, and filament rebinding. In most cases, the conformational change(s) on the motor protein prevents subsequent nucleotide binding or hydrolysis until the prior round of hydrolysis and release is complete.",True,Flagella and cilia,Figure 18.7,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
1d29679f-132f-4a3c-8b0a-1537d4c4ac73,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,dyneins,False,dyneins,,,,
7517a2e3-b878-4328-b032-b75e94b0ae74,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,kinesins,False,kinesins,,,,
9d4f679c-6ef0-4b8d-941b-e19d1a5964b4,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,mechanochemical,False,mechanochemical,,,,
152b0fa4-e314-4a9e-b9dd-f7cf49081066,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Myosin,False,Myosin,,,,
c7b50e8b-81c7-4b8c-8196-e7fc158f6da1,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Myosin can be characterized as conventional or unconventional, with characteristic head groups (that bind ATP) and unique tails. Myosin is essential for muscle contraction, and this occurs in striated muscle (skeletal and cardiac) after specific binding sites on the actin have been exposed in response to the interaction between calcium ions (Ca2+) and proteins (troponin and tropomyosin) that “shield” the actin-binding sites. Ca2+ is also required for the contraction of smooth muscle, although its role is different: here Ca2+ activates enzymes, which in turn activate myosin heads. All muscles require adenosine triphosphate (ATP) to continue the process of contracting, and they all relax when the Ca2+ is removed and the actin-binding sites are re-shielded.",True,Myosin,,,,
39ab8ece-907e-4573-9ff2-8505dae9a47f,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Ca2,False,Ca2,,,,
4b1d11ca-2508-4029-b9d1-abcbec6be9d6,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Dynein,False,Dynein,,,,
aade0def-7738-45f7-ba05-2eed972159cd,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Dynein is a large motor protein that typically transports organelles (lysosomes or endosomes). It moves toward the minus end (α-tubulin) of microtubules, which is in the direction of the cell body.",True,Dynein,,,,
999fbb20-0126-43a4-b2ac-37b5d7931c5a,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,Kinesin,False,Kinesin,,,,
ac2c0310-c6d3-4437-81a2-5e1ce246ae72,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
ac2c0310-c6d3-4437-81a2-5e1ce246ae72,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
ac2c0310-c6d3-4437-81a2-5e1ce246ae72,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Kinesin is a relatively small motor protein that moves membrane-bound cargo (e.g., vesicles). In contrast to dynein, most move toward the plus end β-tubulin) of the microtubules, which is typically away from the cell body. Figure 18.8 nicely summarizes the location and general role of each of these motor proteins.",True,Kinesin,Figure 18.8,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
7f681032-a83b-4da5-ae48-c67293e595f9,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,18.2 References and resources,True,Kinesin,,,,
2fb20f42-44a3-4fbd-af86-2a30251d253c,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
2fb20f42-44a3-4fbd-af86-2a30251d253c,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
2fb20f42-44a3-4fbd-af86-2a30251d253c,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.7 Comparison of the three different motor proteins. 2021. CC BY SA 4.0. Adapted from Aufbau der Motorproteine by keine Autoren genannt. CC BY SA 4.0. From Wikimedia Commons.",True,Kinesin,Figure 18.7,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
8b8b3c8d-71f4-4e63-b5fb-f25f5c09ff24,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18.2 Cell Movement,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
8b8b3c8d-71f4-4e63-b5fb-f25f5c09ff24,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18.1 The Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
8b8b3c8d-71f4-4e63-b5fb-f25f5c09ff24,https://pressbooks.lib.vt.edu/cellbio/,18. Cytoskeleton,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoskeleton/,"Grey, Kindred, Figure 18.8 Summary of the roles and movement of the motor proteins along various cytoskeletal elements. 2021. CC BY 4.0. Adapted from A simplified model for myosin V (MyoE) function at the hyphal tip in Aspergillus nidulans – journal.pone.0031218.g009B by Taheri-Talesh N, Xiong Y, Oakley BR. CC BY 2.5. From Wikimedia Commons.",True,Kinesin,Figure 18.8,18. Cytoskeleton,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
7e25094b-421c-426c-988b-1d814d8fb940,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Organization of the nucleus,False,Organization of the nucleus,,,,
5fd5e4cd-b544-48af-8a83-cc519f8c4113,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Proteins called pore complexes lining the nuclear pores regulate the passage of materials into and out of the nucleus.,True,Organization of the nucleus,,,,
3b2d10f2-7d09-4392-aeea-565cefd9e45a,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
3b2d10f2-7d09-4392-aeea-565cefd9e45a,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
3b2d10f2-7d09-4392-aeea-565cefd9e45a,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
2125d5a5-c7ce-4180-bbf5-d3156d0ae3a8,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,cellʼs,False,cellʼs,,,,
9453294a-6f0c-415a-9437-38a02798f8fe,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Endomembrane system,False,Endomembrane system,,,,
43649321-a9b3-44c6-8292-c87d85fbfaa7,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
43649321-a9b3-44c6-8292-c87d85fbfaa7,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
43649321-a9b3-44c6-8292-c87d85fbfaa7,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
e0073d76-09c7-4f11-a795-5528a0bacc87,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Although not technically within the cell the plasma membrane is included in the endomembrane system because, it interacts with the other endomembranous organelles. The endomembrane system does not include the mitochondria. The system of intracellular membranes is designed to move proteins through both the secretory pathway (constitutive or regulated) and the endocytic pathways.",True,Endomembrane system,,,,
8e4704c0-fadf-4e2f-a185-a900226e9f9d,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,endomembranous,False,endomembranous,,,,
2e8f57ea-b949-4869-9ee0-26352acd5953,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,The endoplasmic reticulum (ER),False,The endoplasmic reticulum (ER),,,,
1cbd75ac-8c6e-4ef3-8625-1132b2949f66,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
1cbd75ac-8c6e-4ef3-8625-1132b2949f66,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
1cbd75ac-8c6e-4ef3-8625-1132b2949f66,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
b0fc56da-44eb-4cc8-b44e-375fdec273fc,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Smooth ER,False,Smooth ER,,,,
b7da4957-65f7-4efb-8079-491455d12c47,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The smooth endoplasmic reticulum (SER) is continuous with the rough ER (RER) but has few or no ribosomes on its cytoplasmic surface. SER functions include synthesis of carbohydrates, lipids, and steroid hormones; detoxification of medications and poisons; and storing calcium ions. In muscle cells, a specialized SER, the sarcoplasmic reticulum, is responsible for storing calcium ions that are needed to trigger the muscle cellsʼ coordinated contractions.",True,Smooth ER,,,,
1d447e8b-54e2-4d24-aeed-6dc291630a8d,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,RER,False,RER,,,,
5ebf3e71-d49a-4998-a077-a1594c6dd9ae,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Rough ER,False,Rough ER,,,,
94da6793-d969-4314-82a8-87095243de60,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Scientists have named the rough endoplasmic reticulum (RER) as such because the ribosomes attached to its cytoplasmic surface give it a studded appearance when viewing it through an electron microscope.,True,Rough ER,,,,
c1620deb-93b4-4cb8-9309-79bfc2928ab5,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Ribosomes transfer their newly synthesized proteins into the RERʼs lumen where they undergo structural modifications, such as folding or acquiring side chains. These modified proteins incorporate into cellular membranes, the ER, or other organellesʼ membranes. The proteins can also be secreted from the cell (such as protein hormones and enzymes). The RER also makes phospholipids for cellular membranes.",True,Rough ER,,,,
65a002d4-5fcc-4b8b-a65a-902ec499edc9,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"If the phospholipids or modified proteins are not destined to stay in the RER, they will reach their destinations via transport vesicles that bud from the RERʼs membrane.",True,Rough ER,,,,
42b7e56a-d60c-472c-954f-851d930e44b3,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Glycosylation,False,Glycosylation,,,,
541119b2-6654-4715-b29b-7257c554968a,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Nearly all RER-synthesized proteins are glycosylated with short-branched oligosaccharides. This occurs in an N-linked fashion on asparagine residues.,True,Glycosylation,,,,
6a297029-d540-4595-8698-aa21a9a22427,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Protein degradation,False,Protein degradation,,,,
49f28104-4d8b-49d1-bb52-73d5564f3e1f,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
49f28104-4d8b-49d1-bb52-73d5564f3e1f,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
49f28104-4d8b-49d1-bb52-73d5564f3e1f,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
7460cc39-4eee-4fe7-b5a0-2b07a41462f8,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"E3 ubiquitin ligase is often responsible for tagging aggregates with ubiquitin, which targets the protein to the proteasome. The proteasome consists of two subunits (19S and 20S) to make a functional 26S proteasome. Inside the proteasome, the polypeptide chains are cleaved back to their native amino acids and can be reused in other translational events. However, if the aggregates accumulate, in some instances they can contribute to any number of neurodegenerative disorders.",True,Protein degradation,,,,
8ee2027f-01c9-40e5-92e8-946360e2be42,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Golgi,False,Golgi,,,,
0987c00b-26db-4e7f-b7c2-6d1a2dd1ac31,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"When proteins exit the RER they are trafficked to the Golgi where they will incur further post-translational modifications and will translocate to their final destination. These modifications will include “pruning” of large oligosaccharides that were attached in the RER, glycosylation, sulfation, and phosphorylation. Additionally, some proteins require Golgi-associated cleavage to produce a mature protein ready for trafficking.",True,Golgi,,,,
49a585c0-76bd-4c2c-ae83-f2d637be3637,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,The Golgi is divided into trans and cis networks.,False,The Golgi is divided into trans and cis networks.,,,,
3156e662-7aec-40e5-8e09-161154311dd7,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"In the Golgi, O-linked glycosylation happens, and most mannose residues are removed. This is done by a large family of enzymes known as glycosyltranferases.",True,The Golgi is divided into trans and cis networks.,,,,
5fd4b46c-77c9-473b-84fc-56994174e594,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Protein localization,False,Protein localization,,,,
d635c27c-d365-4951-811f-d3ba9a6fdfeb,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Protein translation can take place on both free ribosomes and the RER. Free ribosomes translate proteins bound for the mitochondria, nucleus, and peroxisomes.",True,Protein localization,,,,
25fbf56c-9edd-4f30-b1ce-bd88136779d5,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The RER translates proteins for secretion, membrane-bound proteins, or soluble proteins.",True,Protein localization,,,,
7dd2b280-1dd8-4f20-b738-76de01bcf106,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Proteins translated on the RER are folded and processed into mature proteins in the lumen of the ER. Transcripts for protein products to be translated on the RER are characteristic of a signal sequence that is recognized by a signal recognition peptide. The signal sequence on the nascent polypeptide will be used to later target the protein to its correct location. The signal recognition peptide facilitates the docking of the ribosome complex on the ER, and the peptide is translated into the lumen of the ER. Inside the ER, the peptide is often associated with chaperones to assist in correct protein folding.",True,Protein localization,,,,
bd3454ea-1654-4d0b-9df6-4941be580ee5,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Localization using coat proteins (COP),False,Localization using coat proteins (COP),,,,
62a8f8fc-a78d-438f-b5c0-85ba3cd807da,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Once translated in the RER, proteins are trafficked in the cell using vesicle transport systems. The direction of the transport, ER to Golgi or Golgi to ER, is determined by the coat proteins on the vesicles.",True,Localization using coat proteins (COP),,,,
da968476-a060-4d62-a02b-137ab2c1b0bd,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The vesicles are targeted to the intended membrane by transport over microtubules in the cytosol. The fusion itself requires surface proteins, Snares, which facilitate the formation of a docking complex stabilizing the interaction between the vesicle and the intended membrane. GTP is required for fusion of the two membranes.",True,Localization using coat proteins (COP),,,,
bab2e6d6-cfd5-4e38-baac-6e0ba0596c35,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Lysosomes and peroxisomes,False,Lysosomes and peroxisomes,,,,
cd2a48c5-bbf1-4e75-bef4-83bb25040bc2,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Lysosomes are organelles formed by the fusion of a late endosome and a lysosomal-enzyme-filled vesicle secreted from the Golgi. Proteins are targeted to lysosomes by the presence of mannose 6-phosphate (acquired in the RER), and the presence of these tags are essential for trafficking to the lysosome.",True,Lysosomes and peroxisomes,,,,
722394f9-21c2-47f4-983e-30675bbd6068,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"The major function for these organelles is to break down macromolecules through enzymatic degradation. Both processes of autophagy and exocytosis can be facilitated. Lysosomal storage diseases are inherited metabolic diseases characterized by an abnormal buildup of various metabolic intermediates. Collectively, there are approximately fifty of these disorders, and they may affect different parts of the body. Clinical correlates include: Gaucher disease, Fabry disease, glycogen storage disease, mucopolisacaridosis, and sphingolipidoses.",True,Lysosomes and peroxisomes,,,,
462eb4c5-ee3b-4e93-a06a-8907a5112b10,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"This is in contrast to peroxisomes, which are formed by budding from the ER. They primarily perform hydrogen peroxide-mediated degradation of lipids (i.e., very long-chain fatty acids) and some amino acids. Zellweger syndrome is one of the heritable disorders of peroxisome biogenesis and results in infant death before six months.",True,Lysosomes and peroxisomes,,,,
4df50db6-2c03-4953-9886-3476f69bb217,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,17.1 References and resources,True,Lysosomes and peroxisomes,,,,
593d8a17-392a-439d-87f9-4b5e30f9cbad,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Lysosomes and peroxisomes,,,,
4cc4c798-c137-4039-8a5c-b9720561a1d2,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 8: Cytoplasmic Membrane Systems: Structure, Function, and Membrane Trafficking.",True,Lysosomes and peroxisomes,,,,
8519085e-908b-4ed1-a45f-7e8e69294a2d,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 46–47.",True,Lysosomes and peroxisomes,,,,
6aae58b1-7f94-440e-b2ce-37bcfa4d60c4,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
6aae58b1-7f94-440e-b2ce-37bcfa4d60c4,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
6aae58b1-7f94-440e-b2ce-37bcfa4d60c4,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
e661995a-7219-4ee0-8788-f13efc6efb57,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
e661995a-7219-4ee0-8788-f13efc6efb57,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
e661995a-7219-4ee0-8788-f13efc6efb57,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
1bb17ac1-1a76-4c8e-9a2e-e83cb9450430,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
1bb17ac1-1a76-4c8e-9a2e-e83cb9450430,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
1bb17ac1-1a76-4c8e-9a2e-e83cb9450430,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
086fbac3-c00e-4f2d-8274-9b693ab20e63,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Additional resources,False,Additional resources,,,,
87b0abcd-4cd2-4dc1-bf29-07cd4bfc994c,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,17.2 Endocytosis,True,Additional resources,,,,
dca0073c-a6b7-4036-af6e-f1e35b718cc1,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Endocytosis,False,Endocytosis,,,,
d52200f7-ac7f-4caa-83ae-0beb9eb2c58f,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Phagocytosis,False,Phagocytosis,,,,
7185bf0c-2836-421b-966d-d3309ff13fb8,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
7185bf0c-2836-421b-966d-d3309ff13fb8,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
7185bf0c-2836-421b-966d-d3309ff13fb8,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
bb1645a6-55ef-4042-baff-74ace4610d0f,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"In preparation for phagocytosis, a portion of the plasma membraneʼs inward-facing surface becomes coated with the protein clathrin, which stabilizes this membraneʼs section. The membraneʼs coated portion then extends from the cellʼs body and surrounds the particle, eventually enclosing it. Once the vesicle containing the particle is enclosed within the cell, the clathrin disengages from the membrane ,and the vesicle merges with a lysosome for breaking down the material in the newly formed compartment (endosome). When accessible nutrients from the vesicular contentsʼ degradation have been extracted, the newly formed endosome merges with the plasma membrane and releases its contents into the extracellular fluid. The endosomal membrane again becomes part of the plasma membrane.",True,Phagocytosis,,,,
79f8b841-4030-4699-8160-d5c4bd7e3076,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Receptor-mediated endocytosis,False,Receptor-mediated endocytosis,,,,
0f6add49-23d9-4f4a-ad74-d2d3b7d75e85,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
0f6add49-23d9-4f4a-ad74-d2d3b7d75e85,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
0f6add49-23d9-4f4a-ad74-d2d3b7d75e85,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
7fc6efd2-6812-4c10-85fb-254e01d94173,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"In receptor-mediated endocytosis, the cellʼs uptake of substances targets a single type of substance that binds to the receptor on the cell membraneʼs external surface.",True,Receptor-mediated endocytosis,,,,
c4fbf4db-6b52-43ac-8f82-59b9d3d706e6,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Clathrin attaches to the plasma membraneʼs cytoplasmic side. If a compoundʼs uptake is dependent on receptor-mediated endocytosis and the process is ineffective, the material will not be removed from the tissue fluids or blood. Instead, it will stay in those fluids and increase in concentration. The failure of receptor-mediated endocytosis causes some human diseases.",True,Receptor-mediated endocytosis,,,,
206db806-138f-46ac-9292-6ece23934ac7,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"For example, receptor-mediated endocytosis removes low-density lipoprotein or LDL from the blood. In the human genetic disease familial hypercholesterolemia, the LDL receptors are defective or missing entirely. People with this condition have life-threatening levels of cholesterol in their blood because their cells cannot clear LDL particles. See chapter 6.",True,Receptor-mediated endocytosis,,,,
9ae7adfa-5c0f-4bd1-989e-a4aedbff4a5a,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,Exocytosis,False,Exocytosis,,,,
5a2bb561-1157-46d0-8de7-449c7e6fcbac,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
5a2bb561-1157-46d0-8de7-449c7e6fcbac,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
5a2bb561-1157-46d0-8de7-449c7e6fcbac,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
dafc7e66-578a-4b3f-b0ed-72310debe357,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,17.2 References and resources,True,Exocytosis,,,,
8d2b739c-f54b-4c50-a1df-8915539a6ede,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Exocytosis,,,,
852c5438-5d39-4c8a-b176-1e67625ba63c,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 8: Cytoplasmic Membrane Systems: Structure, Function, and Membrane Trafficking.",True,Exocytosis,,,,
281f0c74-291c-4ff9-821c-fb7da8f3c2b4,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 46–47.",True,Exocytosis,,,,
c9f95463-d7b4-4a70-8691-e9b32dda0cb9,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
c9f95463-d7b4-4a70-8691-e9b32dda0cb9,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
c9f95463-d7b4-4a70-8691-e9b32dda0cb9,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
740bae32-2822-46e4-ae64-f54d07e8cd7b,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
740bae32-2822-46e4-ae64-f54d07e8cd7b,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
740bae32-2822-46e4-ae64-f54d07e8cd7b,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
017d18f8-e904-4371-905c-c35b23a07117,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
017d18f8-e904-4371-905c-c35b23a07117,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
017d18f8-e904-4371-905c-c35b23a07117,https://pressbooks.lib.vt.edu/cellbio/,17.2 Endocytosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-2,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
80b0067a-ea58-47bc-9313-c79338a928ef,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Organization of the nucleus,False,Organization of the nucleus,,,,
2932b52c-5728-4256-afd2-c001af86cc51,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Proteins called pore complexes lining the nuclear pores regulate the passage of materials into and out of the nucleus.,True,Organization of the nucleus,,,,
1e4fd146-ca36-4377-8c4e-4f1b6e52f764,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
1e4fd146-ca36-4377-8c4e-4f1b6e52f764,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
1e4fd146-ca36-4377-8c4e-4f1b6e52f764,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
1d08aacc-a32f-4550-80be-52c04eeb0fcc,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,cellʼs,False,cellʼs,,,,
61f7dc03-be81-4d2f-81a0-81a87bdab851,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Endomembrane system,False,Endomembrane system,,,,
0a136d20-7b29-4f4e-a9d2-bb7ea0f8ac7a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
0a136d20-7b29-4f4e-a9d2-bb7ea0f8ac7a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
0a136d20-7b29-4f4e-a9d2-bb7ea0f8ac7a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
13c61435-90c9-47e5-a2f9-00e28a4c7774,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Although not technically within the cell the plasma membrane is included in the endomembrane system because, it interacts with the other endomembranous organelles. The endomembrane system does not include the mitochondria. The system of intracellular membranes is designed to move proteins through both the secretory pathway (constitutive or regulated) and the endocytic pathways.",True,Endomembrane system,,,,
8a769274-3e28-4161-b3e5-f0c793b073a7,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,endomembranous,False,endomembranous,,,,
5fe6af6d-982a-4dc6-a020-9dfd13671646,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,The endoplasmic reticulum (ER),False,The endoplasmic reticulum (ER),,,,
ccbf5fa2-02c6-4dfe-8b59-dae165ba6ff9,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
ccbf5fa2-02c6-4dfe-8b59-dae165ba6ff9,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
ccbf5fa2-02c6-4dfe-8b59-dae165ba6ff9,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
9fa686b9-0631-4906-bdd8-a74a1302b640,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Smooth ER,False,Smooth ER,,,,
1741ffd2-3d01-415a-a879-21ec5e7f430e,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The smooth endoplasmic reticulum (SER) is continuous with the rough ER (RER) but has few or no ribosomes on its cytoplasmic surface. SER functions include synthesis of carbohydrates, lipids, and steroid hormones; detoxification of medications and poisons; and storing calcium ions. In muscle cells, a specialized SER, the sarcoplasmic reticulum, is responsible for storing calcium ions that are needed to trigger the muscle cellsʼ coordinated contractions.",True,Smooth ER,,,,
3915e2e3-9afc-4fab-a5c8-1085de0d32b9,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,RER,False,RER,,,,
46e782f8-4594-4d69-90b2-17c6c126147a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Rough ER,False,Rough ER,,,,
86b62243-92b6-483a-9bc4-2293fcbfbcf3,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Scientists have named the rough endoplasmic reticulum (RER) as such because the ribosomes attached to its cytoplasmic surface give it a studded appearance when viewing it through an electron microscope.,True,Rough ER,,,,
b1ab45c9-1ca8-4824-8b0c-475e19bfbcd6,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Ribosomes transfer their newly synthesized proteins into the RERʼs lumen where they undergo structural modifications, such as folding or acquiring side chains. These modified proteins incorporate into cellular membranes, the ER, or other organellesʼ membranes. The proteins can also be secreted from the cell (such as protein hormones and enzymes). The RER also makes phospholipids for cellular membranes.",True,Rough ER,,,,
2bac8e8b-c6ee-4012-aee8-025a32621257,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"If the phospholipids or modified proteins are not destined to stay in the RER, they will reach their destinations via transport vesicles that bud from the RERʼs membrane.",True,Rough ER,,,,
ed43f09c-78e2-4194-bf96-205d1b3a4b48,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Glycosylation,False,Glycosylation,,,,
e4eb6d0c-4d38-400c-88a6-6cff151bb459,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Nearly all RER-synthesized proteins are glycosylated with short-branched oligosaccharides. This occurs in an N-linked fashion on asparagine residues.,True,Glycosylation,,,,
925296f7-a5ab-4391-bc7a-c3a279884bd1,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Protein degradation,False,Protein degradation,,,,
d99f3f0e-dc5c-485e-a362-466dcc7b1c1c,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
d99f3f0e-dc5c-485e-a362-466dcc7b1c1c,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
d99f3f0e-dc5c-485e-a362-466dcc7b1c1c,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
a86becb9-445a-453c-9ef4-a6f90eaf20c8,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"E3 ubiquitin ligase is often responsible for tagging aggregates with ubiquitin, which targets the protein to the proteasome. The proteasome consists of two subunits (19S and 20S) to make a functional 26S proteasome. Inside the proteasome, the polypeptide chains are cleaved back to their native amino acids and can be reused in other translational events. However, if the aggregates accumulate, in some instances they can contribute to any number of neurodegenerative disorders.",True,Protein degradation,,,,
50047f6a-c70b-4506-a2b5-23cbbd23331c,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Golgi,False,Golgi,,,,
d666320b-3aaf-4b6e-9117-61521f118c7b,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"When proteins exit the RER they are trafficked to the Golgi where they will incur further post-translational modifications and will translocate to their final destination. These modifications will include “pruning” of large oligosaccharides that were attached in the RER, glycosylation, sulfation, and phosphorylation. Additionally, some proteins require Golgi-associated cleavage to produce a mature protein ready for trafficking.",True,Golgi,,,,
de304839-bd66-4436-84db-4c942c778f00,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,The Golgi is divided into trans and cis networks.,False,The Golgi is divided into trans and cis networks.,,,,
30b68f15-04d3-468d-9424-2c4a271f4eb8,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"In the Golgi, O-linked glycosylation happens, and most mannose residues are removed. This is done by a large family of enzymes known as glycosyltranferases.",True,The Golgi is divided into trans and cis networks.,,,,
139dbccb-aece-4934-a8d9-7ccb4655129a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Protein localization,False,Protein localization,,,,
9240d348-b209-479e-b237-b45614003788,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Protein translation can take place on both free ribosomes and the RER. Free ribosomes translate proteins bound for the mitochondria, nucleus, and peroxisomes.",True,Protein localization,,,,
f6cf420b-9bab-4373-be66-2aeee81dd812,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The RER translates proteins for secretion, membrane-bound proteins, or soluble proteins.",True,Protein localization,,,,
1e7f36eb-d611-4143-96d9-9af04ffa991f,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Proteins translated on the RER are folded and processed into mature proteins in the lumen of the ER. Transcripts for protein products to be translated on the RER are characteristic of a signal sequence that is recognized by a signal recognition peptide. The signal sequence on the nascent polypeptide will be used to later target the protein to its correct location. The signal recognition peptide facilitates the docking of the ribosome complex on the ER, and the peptide is translated into the lumen of the ER. Inside the ER, the peptide is often associated with chaperones to assist in correct protein folding.",True,Protein localization,,,,
7742f303-5fa0-4e38-8b9c-0447ec0c89e2,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Localization using coat proteins (COP),False,Localization using coat proteins (COP),,,,
a5028694-6381-475e-830c-26edbb59c948,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Once translated in the RER, proteins are trafficked in the cell using vesicle transport systems. The direction of the transport, ER to Golgi or Golgi to ER, is determined by the coat proteins on the vesicles.",True,Localization using coat proteins (COP),,,,
5ab72d2d-2948-455e-b211-1657a69f1e23,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The vesicles are targeted to the intended membrane by transport over microtubules in the cytosol. The fusion itself requires surface proteins, Snares, which facilitate the formation of a docking complex stabilizing the interaction between the vesicle and the intended membrane. GTP is required for fusion of the two membranes.",True,Localization using coat proteins (COP),,,,
dda015f5-ffed-4234-a231-0c04e0a3cf50,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Lysosomes and peroxisomes,False,Lysosomes and peroxisomes,,,,
1498f46a-71ad-40ac-821f-92a669940b0f,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Lysosomes are organelles formed by the fusion of a late endosome and a lysosomal-enzyme-filled vesicle secreted from the Golgi. Proteins are targeted to lysosomes by the presence of mannose 6-phosphate (acquired in the RER), and the presence of these tags are essential for trafficking to the lysosome.",True,Lysosomes and peroxisomes,,,,
d598689b-0523-4cd3-88c4-ecdc89a51295,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"The major function for these organelles is to break down macromolecules through enzymatic degradation. Both processes of autophagy and exocytosis can be facilitated. Lysosomal storage diseases are inherited metabolic diseases characterized by an abnormal buildup of various metabolic intermediates. Collectively, there are approximately fifty of these disorders, and they may affect different parts of the body. Clinical correlates include: Gaucher disease, Fabry disease, glycogen storage disease, mucopolisacaridosis, and sphingolipidoses.",True,Lysosomes and peroxisomes,,,,
88570358-cb62-48d1-94b2-0cb288a05090,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"This is in contrast to peroxisomes, which are formed by budding from the ER. They primarily perform hydrogen peroxide-mediated degradation of lipids (i.e., very long-chain fatty acids) and some amino acids. Zellweger syndrome is one of the heritable disorders of peroxisome biogenesis and results in infant death before six months.",True,Lysosomes and peroxisomes,,,,
f307f5d2-b6b2-4cfe-8b0a-7aed5a19f58b,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,17.1 References and resources,True,Lysosomes and peroxisomes,,,,
6ce8847d-10c9-46b4-abc5-58ace506df2a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Lysosomes and peroxisomes,,,,
bc9b9c86-c1d7-495a-b1ba-3d12a9f93509,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 8: Cytoplasmic Membrane Systems: Structure, Function, and Membrane Trafficking.",True,Lysosomes and peroxisomes,,,,
c0dc6442-6199-4803-90c9-51daaf9d47ae,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 46–47.",True,Lysosomes and peroxisomes,,,,
f0b18e9b-5716-480f-b314-042d78ae934c,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
f0b18e9b-5716-480f-b314-042d78ae934c,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
f0b18e9b-5716-480f-b314-042d78ae934c,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
9fd7d0f1-77fb-4c9b-a73e-4b31257113b8,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
9fd7d0f1-77fb-4c9b-a73e-4b31257113b8,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
9fd7d0f1-77fb-4c9b-a73e-4b31257113b8,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
76140e0e-75f3-48b0-9c28-3abcab39d42b,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
76140e0e-75f3-48b0-9c28-3abcab39d42b,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
76140e0e-75f3-48b0-9c28-3abcab39d42b,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
39292e78-d6c0-46bd-99e0-34eca16e8764,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Additional resources,False,Additional resources,,,,
45371f46-5c59-4ef2-8a2d-c1da6bfde5fe,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,17.2 Endocytosis,True,Additional resources,,,,
16f9eb7c-5b64-462d-b8c7-7cc58302b01d,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Endocytosis,False,Endocytosis,,,,
c6c4be28-0cd8-4bb2-9338-5a8ecdf3b2ed,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Phagocytosis,False,Phagocytosis,,,,
7c8028ae-f89a-44de-b41c-eb9ecb06402e,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
7c8028ae-f89a-44de-b41c-eb9ecb06402e,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
7c8028ae-f89a-44de-b41c-eb9ecb06402e,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
2c6c94ce-f466-4a04-8051-36f273981706,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"In preparation for phagocytosis, a portion of the plasma membraneʼs inward-facing surface becomes coated with the protein clathrin, which stabilizes this membraneʼs section. The membraneʼs coated portion then extends from the cellʼs body and surrounds the particle, eventually enclosing it. Once the vesicle containing the particle is enclosed within the cell, the clathrin disengages from the membrane ,and the vesicle merges with a lysosome for breaking down the material in the newly formed compartment (endosome). When accessible nutrients from the vesicular contentsʼ degradation have been extracted, the newly formed endosome merges with the plasma membrane and releases its contents into the extracellular fluid. The endosomal membrane again becomes part of the plasma membrane.",True,Phagocytosis,,,,
5558b5e2-110f-404c-b44f-bad2f335a96f,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Receptor-mediated endocytosis,False,Receptor-mediated endocytosis,,,,
1e0d753a-0838-47ee-898c-b1d286d66d64,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
1e0d753a-0838-47ee-898c-b1d286d66d64,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
1e0d753a-0838-47ee-898c-b1d286d66d64,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
4de6b8e7-122a-4dd5-bde5-da75e4b43fd2,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"In receptor-mediated endocytosis, the cellʼs uptake of substances targets a single type of substance that binds to the receptor on the cell membraneʼs external surface.",True,Receptor-mediated endocytosis,,,,
493a5106-c9f6-4d92-ba0a-f8abf4239a11,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Clathrin attaches to the plasma membraneʼs cytoplasmic side. If a compoundʼs uptake is dependent on receptor-mediated endocytosis and the process is ineffective, the material will not be removed from the tissue fluids or blood. Instead, it will stay in those fluids and increase in concentration. The failure of receptor-mediated endocytosis causes some human diseases.",True,Receptor-mediated endocytosis,,,,
9ff9f87e-6e9c-4471-8b76-076de8e0d160,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"For example, receptor-mediated endocytosis removes low-density lipoprotein or LDL from the blood. In the human genetic disease familial hypercholesterolemia, the LDL receptors are defective or missing entirely. People with this condition have life-threatening levels of cholesterol in their blood because their cells cannot clear LDL particles. See chapter 6.",True,Receptor-mediated endocytosis,,,,
fcf09d23-410e-4dfc-affd-e5654ec5ce9a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,Exocytosis,False,Exocytosis,,,,
11d94567-e3c1-40e0-899d-7efcba58aadd,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
11d94567-e3c1-40e0-899d-7efcba58aadd,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
11d94567-e3c1-40e0-899d-7efcba58aadd,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
94663549-dbd0-4dea-bbdc-59e72d2a4445,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,17.2 References and resources,True,Exocytosis,,,,
378fa5bf-07d1-4266-9870-85631b87612a,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Exocytosis,,,,
5ec2fae1-841e-455b-bfbf-97bf39ca59b4,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 8: Cytoplasmic Membrane Systems: Structure, Function, and Membrane Trafficking.",True,Exocytosis,,,,
e38d3cb7-459a-4ddb-a5eb-50bd252f7bf2,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 46–47.",True,Exocytosis,,,,
4e4116b7-c550-4024-854d-c5190af96c59,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
4e4116b7-c550-4024-854d-c5190af96c59,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
4e4116b7-c550-4024-854d-c5190af96c59,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
a994ee73-c31b-4a39-bcfd-891e56293088,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
a994ee73-c31b-4a39-bcfd-891e56293088,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
a994ee73-c31b-4a39-bcfd-891e56293088,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
07fc4949-ac9d-46f6-a60a-2d1a439bdb77,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
07fc4949-ac9d-46f6-a60a-2d1a439bdb77,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
07fc4949-ac9d-46f6-a60a-2d1a439bdb77,https://pressbooks.lib.vt.edu/cellbio/,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/#chapter-102-section-1,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
d0a1c7d8-71ca-422d-9b28-74fb49d06250,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Organization of the nucleus,False,Organization of the nucleus,,,,
12469f84-9200-45ed-8ecb-12e5f963b029,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Proteins called pore complexes lining the nuclear pores regulate the passage of materials into and out of the nucleus.,True,Organization of the nucleus,,,,
49cfd871-9760-4a08-9c7d-51d31ee30e4e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
49cfd871-9760-4a08-9c7d-51d31ee30e4e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
49cfd871-9760-4a08-9c7d-51d31ee30e4e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple light microscope, called a nucleolus (plural = nucleoli). The nucleolus is a region of the nucleus that is responsible for manufacturing the RNA necessary for construction of ribosomes. Once synthesized, newly made ribosomal subunits exit the cellʼs nucleus through the nuclear pores (figure 17.1). Proteins entering the nucleus require nuclear localization signals, while proteins exiting require nuclear export signals.",True,Organization of the nucleus,Figure 17.1,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
5c766d93-cce0-4298-a7e5-a1d07aea948c,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,cellʼs,False,cellʼs,,,,
55f4ddb6-4843-490a-9b6d-d8891b22a520,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Endomembrane system,False,Endomembrane system,,,,
22d7c6d3-dd62-4b2a-89e2-2ccbfd00adfc,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
22d7c6d3-dd62-4b2a-89e2-2ccbfd00adfc,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
22d7c6d3-dd62-4b2a-89e2-2ccbfd00adfc,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The endomembrane system (endo = “within”) is a group of membranes and organelles (figure 17.2) in eukaryotic cells that work together to modify, package, and transport lipids and proteins. It includes the nuclear envelope as well as:",True,Endomembrane system,Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
49840684-66c2-400f-912e-9bca05b51328,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Although not technically within the cell the plasma membrane is included in the endomembrane system because, it interacts with the other endomembranous organelles. The endomembrane system does not include the mitochondria. The system of intracellular membranes is designed to move proteins through both the secretory pathway (constitutive or regulated) and the endocytic pathways.",True,Endomembrane system,,,,
5dfe5d8d-9813-4aac-a020-c5cf88591527,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,endomembranous,False,endomembranous,,,,
7cfa1cb3-1de8-4386-a8e7-317c97f14cb1,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,The endoplasmic reticulum (ER),False,The endoplasmic reticulum (ER),,,,
f14d2439-1bb5-4833-b614-597ce1d76084,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
f14d2439-1bb5-4833-b614-597ce1d76084,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
f14d2439-1bb5-4833-b614-597ce1d76084,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The endoplasmic reticulum (ER) (figure 17.2) is a series of interconnected membranous sacs and tubules that collectively modify proteins and synthesize lipids. However, these two functions take place in separate areas of the ER: the rough ER and the smooth ER, respectively.",True,The endoplasmic reticulum (ER),Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
31eb51e6-cfa2-4dc8-83ce-fccdda2a7c1b,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Smooth ER,False,Smooth ER,,,,
695ec4f5-4c24-4d50-a982-8e28802b74e8,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The smooth endoplasmic reticulum (SER) is continuous with the rough ER (RER) but has few or no ribosomes on its cytoplasmic surface. SER functions include synthesis of carbohydrates, lipids, and steroid hormones; detoxification of medications and poisons; and storing calcium ions. In muscle cells, a specialized SER, the sarcoplasmic reticulum, is responsible for storing calcium ions that are needed to trigger the muscle cellsʼ coordinated contractions.",True,Smooth ER,,,,
ac26e8ae-fe12-4365-a143-e8f2db6e108e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,RER,False,RER,,,,
35e562fe-36a0-43c3-bfa0-aca20059e939,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Rough ER,False,Rough ER,,,,
36143831-88d9-46cd-8cfc-63a8a660e551,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Scientists have named the rough endoplasmic reticulum (RER) as such because the ribosomes attached to its cytoplasmic surface give it a studded appearance when viewing it through an electron microscope.,True,Rough ER,,,,
e91c0149-63e0-4ce5-9d75-597341a8546c,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Ribosomes transfer their newly synthesized proteins into the RERʼs lumen where they undergo structural modifications, such as folding or acquiring side chains. These modified proteins incorporate into cellular membranes, the ER, or other organellesʼ membranes. The proteins can also be secreted from the cell (such as protein hormones and enzymes). The RER also makes phospholipids for cellular membranes.",True,Rough ER,,,,
2e4bcf98-73d4-43aa-9b22-3e593b8cbefa,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"If the phospholipids or modified proteins are not destined to stay in the RER, they will reach their destinations via transport vesicles that bud from the RERʼs membrane.",True,Rough ER,,,,
ae4a593f-13fd-42c5-b66e-36ed331729a9,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Glycosylation,False,Glycosylation,,,,
52ef2d80-fbae-4bb2-99bd-e3c2330a46a8,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Nearly all RER-synthesized proteins are glycosylated with short-branched oligosaccharides. This occurs in an N-linked fashion on asparagine residues.,True,Glycosylation,,,,
adbca3cb-de0e-4116-b5a3-d4fb07faefab,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Protein degradation,False,Protein degradation,,,,
911c0a4f-8c51-4899-b27f-bdeb23efa13f,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
911c0a4f-8c51-4899-b27f-bdeb23efa13f,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
911c0a4f-8c51-4899-b27f-bdeb23efa13f,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"If proteins arenʼt folded properly, this can contribute to a host of disease processes related to misfolding events. Typically, folding is facilitated in the ER using chaperones (BiP), but if the protein is altered (due to mutation), this can lead to aggregation. Accumulation of BiP can initiate the unfolded protein response (UPR) (figure 17.3).",True,Protein degradation,Figure 17.3,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
e0b6e96e-0398-4838-b448-f89484e00e40,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"E3 ubiquitin ligase is often responsible for tagging aggregates with ubiquitin, which targets the protein to the proteasome. The proteasome consists of two subunits (19S and 20S) to make a functional 26S proteasome. Inside the proteasome, the polypeptide chains are cleaved back to their native amino acids and can be reused in other translational events. However, if the aggregates accumulate, in some instances they can contribute to any number of neurodegenerative disorders.",True,Protein degradation,,,,
5b441ba6-c28a-45e6-b4d4-aa088e01fa97,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Golgi,False,Golgi,,,,
22551d1a-f263-4b0f-9f51-fc16e508dec9,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"When proteins exit the RER they are trafficked to the Golgi where they will incur further post-translational modifications and will translocate to their final destination. These modifications will include “pruning” of large oligosaccharides that were attached in the RER, glycosylation, sulfation, and phosphorylation. Additionally, some proteins require Golgi-associated cleavage to produce a mature protein ready for trafficking.",True,Golgi,,,,
c94ac9d3-1871-44ee-bb04-904b8e56ed47,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,The Golgi is divided into trans and cis networks.,False,The Golgi is divided into trans and cis networks.,,,,
6aa3e867-d2d1-47e2-9ca5-5d47ab37d33e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"In the Golgi, O-linked glycosylation happens, and most mannose residues are removed. This is done by a large family of enzymes known as glycosyltranferases.",True,The Golgi is divided into trans and cis networks.,,,,
715db048-61da-4091-b6dc-e8243a2981dd,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Protein localization,False,Protein localization,,,,
58308459-b807-449a-b918-b9406d7babf2,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Protein translation can take place on both free ribosomes and the RER. Free ribosomes translate proteins bound for the mitochondria, nucleus, and peroxisomes.",True,Protein localization,,,,
fb22ec30-2fae-4dbe-abb6-e49604da3c3f,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The RER translates proteins for secretion, membrane-bound proteins, or soluble proteins.",True,Protein localization,,,,
db956df7-3e78-4b3d-b479-31cd9127acf0,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Proteins translated on the RER are folded and processed into mature proteins in the lumen of the ER. Transcripts for protein products to be translated on the RER are characteristic of a signal sequence that is recognized by a signal recognition peptide. The signal sequence on the nascent polypeptide will be used to later target the protein to its correct location. The signal recognition peptide facilitates the docking of the ribosome complex on the ER, and the peptide is translated into the lumen of the ER. Inside the ER, the peptide is often associated with chaperones to assist in correct protein folding.",True,Protein localization,,,,
943dff78-fba0-4d53-8a2a-840e7f99d603,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Localization using coat proteins (COP),False,Localization using coat proteins (COP),,,,
b8f5a361-ebef-4147-a002-2ce665d202d8,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Once translated in the RER, proteins are trafficked in the cell using vesicle transport systems. The direction of the transport, ER to Golgi or Golgi to ER, is determined by the coat proteins on the vesicles.",True,Localization using coat proteins (COP),,,,
9e395088-f3f8-4781-8baa-749011192f6d,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The vesicles are targeted to the intended membrane by transport over microtubules in the cytosol. The fusion itself requires surface proteins, Snares, which facilitate the formation of a docking complex stabilizing the interaction between the vesicle and the intended membrane. GTP is required for fusion of the two membranes.",True,Localization using coat proteins (COP),,,,
65073f6d-c192-4a3c-a487-8929b228f2d3,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Lysosomes and peroxisomes,False,Lysosomes and peroxisomes,,,,
5744d972-ffa9-49eb-9163-e55f3a22bce1,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Lysosomes are organelles formed by the fusion of a late endosome and a lysosomal-enzyme-filled vesicle secreted from the Golgi. Proteins are targeted to lysosomes by the presence of mannose 6-phosphate (acquired in the RER), and the presence of these tags are essential for trafficking to the lysosome.",True,Lysosomes and peroxisomes,,,,
ded462f0-182b-4ce2-befe-dca2b4a584b2,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"The major function for these organelles is to break down macromolecules through enzymatic degradation. Both processes of autophagy and exocytosis can be facilitated. Lysosomal storage diseases are inherited metabolic diseases characterized by an abnormal buildup of various metabolic intermediates. Collectively, there are approximately fifty of these disorders, and they may affect different parts of the body. Clinical correlates include: Gaucher disease, Fabry disease, glycogen storage disease, mucopolisacaridosis, and sphingolipidoses.",True,Lysosomes and peroxisomes,,,,
2815b303-95c8-4088-8516-35e754d20278,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"This is in contrast to peroxisomes, which are formed by budding from the ER. They primarily perform hydrogen peroxide-mediated degradation of lipids (i.e., very long-chain fatty acids) and some amino acids. Zellweger syndrome is one of the heritable disorders of peroxisome biogenesis and results in infant death before six months.",True,Lysosomes and peroxisomes,,,,
59d0c0cc-1338-42fb-b434-8672b026bb5a,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,17.1 References and resources,True,Lysosomes and peroxisomes,,,,
3ceffa4f-9766-4f65-984d-1f587a2bdc52,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Lysosomes and peroxisomes,,,,
fc4b9657-4de5-40e5-a148-4ca03fb260c5,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 8: Cytoplasmic Membrane Systems: Structure, Function, and Membrane Trafficking.",True,Lysosomes and peroxisomes,,,,
c5a710d3-c16d-46c9-85f0-2de8315e666e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 46–47.",True,Lysosomes and peroxisomes,,,,
d25b4e2c-a0f7-4459-aea9-71e7c5d0f080,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
d25b4e2c-a0f7-4459-aea9-71e7c5d0f080,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
d25b4e2c-a0f7-4459-aea9-71e7c5d0f080,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Grey, Kindred, Figure 17.2 Interaction of the endomembrane systems. 2021. https://archive.org/details/17.2_20210926. CC BY 4.0. Adapted from Figure 4.18. CC BY 4.0. From OpenStax.",True,Lysosomes and peroxisomes,Figure 17.2,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
9d1cc520-02a4-4e1f-94c3-7b26d5bcd3ba,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
9d1cc520-02a4-4e1f-94c3-7b26d5bcd3ba,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
9d1cc520-02a4-4e1f-94c3-7b26d5bcd3ba,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Grey, Kindred, Figure 17.3: Unfolded protein response in the RER. 2021. CC BY 4.0. Adapted from ProteinQS en by Vojtěch Dostál. Public domain. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.3,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
c65fbf59-acfc-469a-8f2e-9af75730f34e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
c65fbf59-acfc-469a-8f2e-9af75730f34e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
c65fbf59-acfc-469a-8f2e-9af75730f34e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Orlov I, Schertel A, Zuber G, et al. Figure 17.1 EM of the nucleus and nucleolus. CC BY-SA 4.0. From Wikimedia Commons.",True,Lysosomes and peroxisomes,Figure 17.1,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
15ae2f09-eeba-4971-988f-2734be84182f,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Additional resources,False,Additional resources,,,,
a04692b5-90c3-4aaf-99bb-eeb50756cec5,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,17.2 Endocytosis,True,Additional resources,,,,
a7eba650-9b39-49c0-b6e3-2c17ebc782ff,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Endocytosis,False,Endocytosis,,,,
612c79b3-212d-4693-b585-4218b210edd0,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Phagocytosis,False,Phagocytosis,,,,
344f0672-8347-4cb8-bc46-e0d81a607190,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
344f0672-8347-4cb8-bc46-e0d81a607190,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
344f0672-8347-4cb8-bc46-e0d81a607190,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Phagocytosis (the condition of “cell eating”) is the process by which a cell takes in large particles, such as other cells or relatively large particles. For example, when microorganisms invade the human body, a type of white blood cell, a neutrophil, will remove the invaders through this process, surrounding and engulfing the microorganism, which the neutrophil then destroys (figure 17.4).",True,Phagocytosis,Figure 17.4,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
fe9843dc-b7b1-4b10-9068-fc4c98fed947,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"In preparation for phagocytosis, a portion of the plasma membraneʼs inward-facing surface becomes coated with the protein clathrin, which stabilizes this membraneʼs section. The membraneʼs coated portion then extends from the cellʼs body and surrounds the particle, eventually enclosing it. Once the vesicle containing the particle is enclosed within the cell, the clathrin disengages from the membrane ,and the vesicle merges with a lysosome for breaking down the material in the newly formed compartment (endosome). When accessible nutrients from the vesicular contentsʼ degradation have been extracted, the newly formed endosome merges with the plasma membrane and releases its contents into the extracellular fluid. The endosomal membrane again becomes part of the plasma membrane.",True,Phagocytosis,,,,
5834d95e-41a0-47fe-81a1-52af7c8db1c7,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Receptor-mediated endocytosis,False,Receptor-mediated endocytosis,,,,
643d576e-97c2-44a5-9b65-c6cd07bc6066,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
643d576e-97c2-44a5-9b65-c6cd07bc6066,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
643d576e-97c2-44a5-9b65-c6cd07bc6066,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,A targeted variation of endocytosis employs receptor proteins in the plasma membrane that have a specific binding affinity for certain substances (figure 17.5).,True,Receptor-mediated endocytosis,Figure 17.5,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
9b5e757a-2269-4611-8810-1d3a0ad8c0ae,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"In receptor-mediated endocytosis, the cellʼs uptake of substances targets a single type of substance that binds to the receptor on the cell membraneʼs external surface.",True,Receptor-mediated endocytosis,,,,
c9b7730b-7b7d-4a59-921e-6682a6d101d0,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Clathrin attaches to the plasma membraneʼs cytoplasmic side. If a compoundʼs uptake is dependent on receptor-mediated endocytosis and the process is ineffective, the material will not be removed from the tissue fluids or blood. Instead, it will stay in those fluids and increase in concentration. The failure of receptor-mediated endocytosis causes some human diseases.",True,Receptor-mediated endocytosis,,,,
828d7f4d-aa7a-4b17-985c-738883322a8b,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"For example, receptor-mediated endocytosis removes low-density lipoprotein or LDL from the blood. In the human genetic disease familial hypercholesterolemia, the LDL receptors are defective or missing entirely. People with this condition have life-threatening levels of cholesterol in their blood because their cells cannot clear LDL particles. See chapter 6.",True,Receptor-mediated endocytosis,,,,
dd30c29d-dad2-42c1-989b-2cfb11640e87,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,Exocytosis,False,Exocytosis,,,,
b69377d4-996e-4ffc-a9ce-cc1c0baec829,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
b69377d4-996e-4ffc-a9ce-cc1c0baec829,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
b69377d4-996e-4ffc-a9ce-cc1c0baec829,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Exocytosis is the opposite of the processes we discussed above in that its purpose is to expel material from the cell into the extracellular fluid. Waste material is enveloped in a membrane and fuses with the plasma membraneʼs interior. This fusion opens the membranous envelope on the cellʼs exterior, and the waste material expels into the extracellular space. Other examples of cells releasing molecules via exocytosis include extracellular matrix protein secretion and neurotransmitter secretion into the synaptic cleft by synaptic vesicles (figure 17.6).",True,Exocytosis,Figure 17.6,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
a0091009-29af-4c7c-92ca-810136259584,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,17.2 References and resources,True,Exocytosis,,,,
b4dee895-908e-418b-8a47-238876850667,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Exocytosis,,,,
be716811-4857-4f6f-bee3-9491688cd8a7,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 8: Cytoplasmic Membrane Systems: Structure, Function, and Membrane Trafficking.",True,Exocytosis,,,,
cd7755ec-dc99-4b89-876e-8cfb0575d951,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 46–47.",True,Exocytosis,,,,
ea312bd1-c87f-44d3-b523-ac986b63f24e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
ea312bd1-c87f-44d3-b523-ac986b63f24e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
ea312bd1-c87f-44d3-b523-ac986b63f24e,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.4 General process of phagocytosis… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 308. Figure 8.46 A summary of phagocytic pathway. 2014.",True,Exocytosis,Figure 17.4,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
053d9a07-5ce6-4ac5-8675-6e99f2795b2b,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
053d9a07-5ce6-4ac5-8675-6e99f2795b2b,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
053d9a07-5ce6-4ac5-8675-6e99f2795b2b,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.5 Receptor mediated endocytosis, LDL-receptor is a classic example of this process. Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 306. Figure 8.42 The endocytic pathway. 2014.",True,Exocytosis,Figure 17.5,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
358d7a1b-f7ad-47fa-9d45-9478c6476d8a,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17.2 Endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
358d7a1b-f7ad-47fa-9d45-9478c6476d8a,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17.1 Cellular Organelles and the Endomembrane System,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
358d7a1b-f7ad-47fa-9d45-9478c6476d8a,https://pressbooks.lib.vt.edu/cellbio/,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/cellbio/chapter/cytoplasmic-membranes/,"Alberts B, Johnson A, Lewis J, et al. Figure 17.6 Exocytosis: vesicles containing substances fuse with the plasma membrane… Adapted under Fair Use from Cell and Molecular Biology. 6th Ed. pp 299. Figure 35 A summary of the autophagic pathway. 2014.",True,Exocytosis,Figure 17.6,17. Cytoplasmic Membranes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
b7c285ad-fb5d-4e59-8278-268a0ad5a28e,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,cellʼs,False,cellʼs,,,,
16cd8d49-7209-4522-981a-f2c0218d8f32,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Fluid mosaic model,False,Fluid mosaic model,,,,
3f0380cf-e47f-4898-8d8d-8eb24fcacc3f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
3f0380cf-e47f-4898-8d8d-8eb24fcacc3f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
3f0380cf-e47f-4898-8d8d-8eb24fcacc3f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
3f0380cf-e47f-4898-8d8d-8eb24fcacc3f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
0e259dec-203c-4685-ad89-8bf00956355a,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Lipids,False,Lipids,,,,
1aaaa479-7562-457c-862c-ee45c3078db6,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
1aaaa479-7562-457c-862c-ee45c3078db6,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
1aaaa479-7562-457c-862c-ee45c3078db6,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
1aaaa479-7562-457c-862c-ee45c3078db6,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
86afc5f2-d822-4a3a-90d0-83a18b76c5d2,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,membraneʼs,False,membraneʼs,,,,
7274ab3e-d8d9-43c4-b536-f40c41657f29,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,phosphatecontaining,False,phosphatecontaining,,,,
f6bcd43e-c81e-4adf-a95e-067d460fed2d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
f6bcd43e-c81e-4adf-a95e-067d460fed2d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
f6bcd43e-c81e-4adf-a95e-067d460fed2d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
f6bcd43e-c81e-4adf-a95e-067d460fed2d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
6ac81ef3-05dc-47f3-bcd4-821977696124,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
6ac81ef3-05dc-47f3-bcd4-821977696124,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
6ac81ef3-05dc-47f3-bcd4-821977696124,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
6ac81ef3-05dc-47f3-bcd4-821977696124,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
8cb485a0-6961-4782-aa36-64a6e2728db0,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Proteins,False,Proteins,,,,
ab3854f9-af84-402b-821f-13be82d02ba2,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Proteins comprise the plasma membrane’s second major component. Integral proteins, or integrins, as their name suggests, integrate completely into the membrane structure, and their hydrophobic membranespanning regions interact with the phospholipid bilayerʼs hydrophobic region.",True,Proteins,,,,
21662ef8-6e1e-4793-8938-0c3eab44d3f2,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Peripheral proteins are on the membrane’s exterior and interior surfaces, attached either to integral proteins or to phospholipids. Peripheral proteins, along with integral proteins, may serve as enzymes, as structural attachments for the cytoskeletonʼs fibers, or as part of the cellʼs recognition sites. Scientists sometimes refer to these as “cell-specific” proteins. The body recognizes its own proteins and attacks foreign proteins associated with invasive pathogens. Additional proteins can be lipid anchored on the exterior of the membrane.",True,Proteins,,,,
78430f96-285b-4339-8360-89abc5d9ed11,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Carbohydrates,False,Carbohydrates,,,,
bf3ded8b-b18f-4281-887e-5c844e353489,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Carbohydrates are the third major plasma membrane component. They are always on the cell’s exterior surface and are bound either to proteins (forming glycoproteins) or to lipids (forming glycolipids). These carbohydrate chains may consist of two to sixty monosaccharide units and can be either straight or branched. Along with peripheral proteins, carbohydrates form specialized sites on the cell surface that allow cells to recognize each other. We collectively refer to these carbohydrates on the cellʼs exterior surface — the carbohydrate components of both glycoproteins and glycolipids — as the glycocalyx (meaning “sugar coating”). The glycocalyx is highly hydrophilic and attracts large amounts of water to the cellʼs surface. This aids in the cellʼs interaction with its watery environment and in the cellʼs ability to obtain substances dissolved in the water.",True,Carbohydrates,,,,
73ea4578-d700-4933-813d-fec8e17478e1,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Membrane fluidity,False,Membrane fluidity,,,,
e95c58bc-9740-4db8-96fd-a1ba38612c49,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,The integral proteins and lipids exist in the membrane as separate but loosely attached molecules. The membraneʼs mosaic characteristics explain some but not all of its fluidity. There are two other factors that help maintain this fluid characteristic.,True,Membrane fluidity,,,,
66ac4fb8-4015-45c2-a56d-7cf08e5ca809,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"One factor is the nature of the phospholipids themselves. In their saturated form, the fatty acids in phospholipid tails are saturated with bound hydrogen atoms. There are no double bonds between adjacent carbon atoms. This results in tails that are relatively straight. In contrast, unsaturated fatty acids do not contain a maximal number of hydrogen atoms, but they do contain some double bonds between adjacent carbon atoms.",True,Membrane fluidity,,,,
306cf956-2726-4a2a-a6ec-51ebf8f9fe44,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Temperature can also influence membrane rigidity. Decreasing temperatures compress saturated fatty acids with their straight tails, and they press in on each other, making a dense and fairly rigid membrane. If unsaturated fatty acids are compressed, the “kinks” in their tails elbow adjacent phospholipid molecules away, maintaining some space between the phospholipid molecules. This “elbow room” helps maintain fluidity in the membrane at temperatures at which membranes with saturated fatty acid tails in their phospholipids would “freeze” or solidify.",True,Membrane fluidity,,,,
bad7fc51-1890-40dc-97ca-570cc46c1a67,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,16.1 References and resources,True,Membrane fluidity,,,,
16a73f7b-8f0f-4424-bb56-adc72ca0e16d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Membrane fluidity,,,,
20714ecd-650e-4675-ab00-fbea5ac8287c,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 4: The Structure and Function of the Plasma Membrane.",True,Membrane fluidity,,,,
6654f888-3e5c-441e-9b9c-9c1e9777bd93,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 49.",True,Membrane fluidity,,,,
59d11a3f-7f4b-44e7-ae02-2f9b891133c5,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
59d11a3f-7f4b-44e7-ae02-2f9b891133c5,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
59d11a3f-7f4b-44e7-ae02-2f9b891133c5,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
59d11a3f-7f4b-44e7-ae02-2f9b891133c5,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
3ff3ca4f-5a82-49a2-a5a7-6793947f4a11,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
3ff3ca4f-5a82-49a2-a5a7-6793947f4a11,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
3ff3ca4f-5a82-49a2-a5a7-6793947f4a11,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
3ff3ca4f-5a82-49a2-a5a7-6793947f4a11,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
ad7d5783-686d-472a-9aa3-7829d23624f7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
ad7d5783-686d-472a-9aa3-7829d23624f7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
ad7d5783-686d-472a-9aa3-7829d23624f7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
ad7d5783-686d-472a-9aa3-7829d23624f7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
b15d658a-4218-426b-afc4-fdfaa2f1ae76,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,16.2 Passive Transport,True,Membrane fluidity,,,,
965cce02-2bce-4a5d-a2db-e75a1eecce4e,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Plasma membranes must allow certain substances to enter and leave a cell, and prevent some harmful materials from entering and some essential materials from leaving. In other words, plasma membranes are selectively permeable; they allow some substances to pass through, but not others. If they were to lose this selectivity, the cell would no longer be able to sustain itself, and it would be destroyed. There are four major types of transport across the cell membrane:",True,Membrane fluidity,,,,
d0456482-8bd5-483f-876b-d25c4e749298,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Recall that plasma membranes are amphiphilic: they have hydrophilic and hydrophobic regions. This characteristic helps move some materials through the membrane and hinders the movement of others.,True,Membrane fluidity,,,,
d83b6775-e57b-45c0-8b7c-500d29e22081,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Nonpolar and lipid-soluble material with a low molecular weight can easily slip through the membraneʼs hydrophobic lipid core. Substances such as the fat-soluble vitamins A, D, E, and K readily pass through the plasma membranes in the digestive tract and other tissues. Fat-soluble drugs and hormones also gain easy entry into cells and readily transport themselves into the bodyʼs tissues and organs. Oxygen and carbon dioxide molecules have no charge and pass through membranes by simple diffusion.",True,Membrane fluidity,,,,
04fd86c5-fc8d-4d18-9b70-f820a27bf83b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,bodyʼs,False,bodyʼs,,,,
b63e7f3f-7264-45ee-be4f-224934a38653,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Polar substances present problems for the membrane. While some polar molecules connect easily with the cellʼs outside, they cannot readily pass through the plasma membraneʼs lipid core.",True,bodyʼs,,,,
954b4752-4277-4e56-96a2-09138ff15c1e,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Additionally, while small ions could easily slip through the spaces in the membraneʼs mosaic, their charge prevents them from doing so. Ions such as sodium, potassium, calcium, and chloride must have special means of penetrating plasma membranes. Simple sugars and amino acids also need the help of various transmembrane proteins (channels) to transport themselves across plasma membranes.",True,bodyʼs,,,,
05698224-5506-465e-b615-c1a8f1ce8f24,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Diffusion,False,Diffusion,,,,
550b5322-064f-4663-85ac-508ce5d2973f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
550b5322-064f-4663-85ac-508ce5d2973f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
550b5322-064f-4663-85ac-508ce5d2973f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
550b5322-064f-4663-85ac-508ce5d2973f,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
58993281-a2ff-4b30-a9e0-d097f7bc1f00,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Osmosis,False,Osmosis,,,,
ce084e63-75ad-44d1-a3c2-d458cdc0faf7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
ce084e63-75ad-44d1-a3c2-d458cdc0faf7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
ce084e63-75ad-44d1-a3c2-d458cdc0faf7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
ce084e63-75ad-44d1-a3c2-d458cdc0faf7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
33829b14-8e01-4c4f-a3c9-f1f829819bb4,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,waterʼs,False,waterʼs,,,,
39cf07af-2ff6-4df5-b7ef-fc79147a42b2,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Tonicity,False,Tonicity,,,,
03b182e5-c8eb-4e62-b07c-2be720582254,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Tonicity describes how an extracellular solution can change a cellʼs volume by affecting osmosis. A solutionʼs tonicity often directly correlates with the solutionʼs osmolarity. Osmolarity describes the solutionʼs total solute concentration.,True,Tonicity,,,,
5cf65267-78b7-4467-b0fb-3db1907ba32b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In a situation in which a membrane, permeable to water though not to the solute, separates two different osmolarities, water will move from the membraneʼs side with lower osmolarity (and more water) to the side with higher osmolarity (and less water).",True,Tonicity,,,,
80f92819-f535-4318-9d7f-13d8523c52ff,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Hypotonic solutions,False,Hypotonic solutions,,,,
a7c4b0a1-f661-4dfa-bd7e-2e418865e319,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In a hypotonic situation, the extracellular fluid has lower osmolarity than the fluid inside the cell, and water enters the cell. It also means that the extracellular fluid has a higher water concentration in the solution than does the cell. In this situation, water will follow its concentration gradient and enter the cell.",True,Hypotonic solutions,,,,
daf187e2-cec5-438b-a62a-f42587513078,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Hypertonic solutions,False,Hypertonic solutions,,,,
a805d183-b16b-4455-80c8-1f1ea6a79630,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"As for a hypertonic solution, the prefix “hyper” refers to the extracellular fluid having a higher osmolarity than the cellʼs cytoplasm; therefore, the fluid contains less water than the cell does. Because the cell has a relatively higher water concentration, water will leave the cell.",True,Hypertonic solutions,,,,
1e19eb60-8ff0-42cd-ab2b-b49f1fabfadc,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Isotonic solutions,False,Isotonic solutions,,,,
17b21802-7f8e-4717-ab97-8368080a8d50,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
17b21802-7f8e-4717-ab97-8368080a8d50,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
17b21802-7f8e-4717-ab97-8368080a8d50,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
17b21802-7f8e-4717-ab97-8368080a8d50,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
c2f7dfc8-6e1a-4d92-bf6c-57db3773cf6a,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Factors that affect diffusion,False,Factors that affect diffusion,,,,
5aa4a9c2-f447-4216-b125-65e52d5c396d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Molecules move constantly in a random manner, at a rate that depends on their mass, their environment, and the amount of thermal energy they possess, which in turn is a function of temperature. While diffusion will go forward in the presence of a substanceʼs concentration gradient, several factors affect the diffusion rate:",True,Factors that affect diffusion,,,,
ed9de680-7510-49e9-9f7e-e3fd7c2e72a4,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Facilitated transport (diffusion),False,Facilitated transport (diffusion),,,,
dde6c2dc-0381-4f54-9d80-094006be5006,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In facilitated transport, or facilitated diffusion, materials diffuse across the plasma membrane with the help of membrane proteins. A concentration gradient exists that would allow these materials to diffuse into the cell without expending cellular energy. However, these materials are polar molecules or ions that the cell membraneʼs hydrophobic parts repel. Facilitated transport proteins shield these materials from the membraneʼs repulsive force, allowing them to diffuse into the cell.",True,Facilitated transport (diffusion),,,,
5622f022-5992-4a5c-be51-876d65c5f257,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Ion channels,False,Ion channels,,,,
02363e2c-0819-4eb4-b6ee-da074c4f3551,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
02363e2c-0819-4eb4-b6ee-da074c4f3551,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
02363e2c-0819-4eb4-b6ee-da074c4f3551,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
02363e2c-0819-4eb4-b6ee-da074c4f3551,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
91a46208-db56-4a32-b18e-380a6f726afe,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Channel proteins are either open at all times or they are “gated,” which controls the channelʼs opening. The gating can be controlled by volatage, ligand (such as ATP), or mechanical stimulus. When a particular ion attaches to the channel protein, it may control the opening, or other mechanisms or substances may be involved.",True,Ion channels,,,,
8f80ee92-5e64-4024-8e2d-a38b2339e1fe,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"In some tissues, sodium and chloride ions pass freely through open channels, whereas in other tissues a gate must open to allow passage. Cells involved in transmitting electrical impulses, such as nerve and muscle cells, have gated channels for sodium, potassium, and calcium in their membranes. Opening and closing these channels changes the relative concentrations on opposing sides of the membrane of these ions, resulting in facilitating electrical transmission along membranes (in the case of nerve cells) or in muscle contraction (in the case of muscle cells).",True,Ion channels,,,,
29e2d27c-375e-4ea6-814d-399cb3c7efce,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Carrier proteins,False,Carrier proteins,,,,
d4dd56cb-80ff-40e9-bc71-702cd7070e76,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
d4dd56cb-80ff-40e9-bc71-702cd7070e76,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
d4dd56cb-80ff-40e9-bc71-702cd7070e76,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
d4dd56cb-80ff-40e9-bc71-702cd7070e76,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
4bc1a57f-2fd7-4991-8c3d-5067ece820b7,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Depending on the gradient, the material may move in the opposite direction. Carrier proteins are typically specific for a single substance. This selectivity adds to the plasma membraneʼs overall selectivity. One group of carrier proteins, glucose transport proteins, or GLUTs, are involved in transporting glucose and other hexose sugars through plasma membranes within the body.",True,Carrier proteins,,,,
b3861f4b-743e-45f6-82f3-01cec421df8d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Channel and carrier proteins transport material at different rates. Channel proteins transport much more quickly than carrier proteins. Channel proteins facilitate diffusion at a rate of tens of millions of molecules per second, whereas carrier proteins work at a rate of a thousand to a million molecules per second.",True,Carrier proteins,,,,
c1a691d9-5eca-4329-bd04-ce256f63fd1d,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,16.2 References and resources,True,Carrier proteins,,,,
ff73a605-6d7d-4f6e-b936-58be9db9c20e,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
ff73a605-6d7d-4f6e-b936-58be9db9c20e,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
ff73a605-6d7d-4f6e-b936-58be9db9c20e,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
ff73a605-6d7d-4f6e-b936-58be9db9c20e,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
07a00a86-c41d-4051-bb6e-9bea13a31b18,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
07a00a86-c41d-4051-bb6e-9bea13a31b18,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
07a00a86-c41d-4051-bb6e-9bea13a31b18,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
07a00a86-c41d-4051-bb6e-9bea13a31b18,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
6f5c79fb-3be1-4c05-a639-6b755809ce51,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
6f5c79fb-3be1-4c05-a639-6b755809ce51,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
6f5c79fb-3be1-4c05-a639-6b755809ce51,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
6f5c79fb-3be1-4c05-a639-6b755809ce51,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
4488bf3b-b43a-4b89-8a17-3cb1d8daf6bc,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
4488bf3b-b43a-4b89-8a17-3cb1d8daf6bc,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
4488bf3b-b43a-4b89-8a17-3cb1d8daf6bc,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
4488bf3b-b43a-4b89-8a17-3cb1d8daf6bc,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
9dd753d9-f995-4b3b-b975-5931a92a5c6b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
9dd753d9-f995-4b3b-b975-5931a92a5c6b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
9dd753d9-f995-4b3b-b975-5931a92a5c6b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
9dd753d9-f995-4b3b-b975-5931a92a5c6b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
e37885a6-dda6-4a4d-93b9-a16ec574d053,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,16.3 Active Transport,True,Carrier proteins,,,,
43b5c5a7-5f74-43f1-adbb-3e6ccd388a50,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Active transport mechanisms require the cellʼs energy, usually in the form of adenosine triphosphate (ATP). If a substance must move into the cell against its concentration gradient — that is, if the substanceʼs concentration inside the cell is greater than its concentration in the extracellular fluid (and vice versa) — the cell must use energy to move the substance.",True,Carrier proteins,,,,
a54e9980-0dd2-463c-86e3-6a52c6e553ad,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,substanceʼs,False,substanceʼs,,,,
c00ef62d-67f0-4d2c-b96c-ba8314e1aa69,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Electrochemical gradient,False,Electrochemical gradient,,,,
592203af-40f2-4feb-9c5d-549ae9bc410a,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"We have discussed simple concentration gradients — a substanceʼs differential concentrations across a space or a membrane — but in living systems, gradients are more complex. Because ions move into and out of cells and because cells contain proteins that do not move across the membrane and are mostly negatively charged, there is also an electrical gradient, a difference of charge, across the plasma membrane.",True,Electrochemical gradient,,,,
5aed8114-d399-45ab-9a93-39d29b148c07,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
5aed8114-d399-45ab-9a93-39d29b148c07,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
5aed8114-d399-45ab-9a93-39d29b148c07,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
5aed8114-d399-45ab-9a93-39d29b148c07,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
7389b1ba-8dd3-4a4e-81c2-cf1111612373,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Moving against a gradient,False,Moving against a gradient,,,,
258bd17c-8099-4a4c-8925-728e90aeeeba,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Two mechanisms exist for transporting small molecular weight material and small molecules:,True,Moving against a gradient,,,,
5be74941-c7ad-4969-b56e-57cb1407fed8,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Carrier proteins for active transport,False,Carrier proteins for active transport,,,,
7c1a33aa-913e-41d8-8aa2-39b34a888287,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
7c1a33aa-913e-41d8-8aa2-39b34a888287,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
7c1a33aa-913e-41d8-8aa2-39b34a888287,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
7c1a33aa-913e-41d8-8aa2-39b34a888287,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
ee00c13b-f472-422c-a746-01152e74316a,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"All of these transporters can also transport small, uncharged organic molecules like glucose. These three types of carrier proteins are also in facilitated diffusion, but they do not require ATP to work in that process.",True,Carrier proteins for active transport,,,,
28fcbcc1-7191-4cce-b560-4a8699ea8406,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Primary active transport,False,Primary active transport,,,,
b639ad1c-a650-448e-80d6-6cd69a936402,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
b639ad1c-a650-448e-80d6-6cd69a936402,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
b639ad1c-a650-448e-80d6-6cd69a936402,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
b639ad1c-a650-448e-80d6-6cd69a936402,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
1775a1f9-4e20-4993-8eda-677b4596c87b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"One of the most important pumps in animal cells is the sodium-potassium pump (Na+-K+ ATPase), which maintains the electrochemical gradient (and the correct concentrations of Na+ and K+) in living cells. The sodium-potassium pump moves K+ into the cell while moving Na+ out at the same time, at a ratio of three Na+ for every two K+ ions moved in. The Na+-K+ ATPase exists in two forms, depending on its orientation to the cellʼs interior or exterior and its affinity for either sodium or potassium ions. The process consists of the following six steps.",True,Primary active transport,,,,
cfbbb420-c769-433e-9b12-68e8a0e28b11,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Secondary active transport (cotransport),False,Secondary active transport (cotransport),,,,
ba20f276-ee73-48e1-8787-1094d2c45a24,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Secondary active transport brings sodium ions, and possibly other compounds, into the cell. As sodium ion concentrations build up outside of the plasma membrane because of the primary active transport process, this creates an electrochemical gradient. If a channel protein exists and is open, the sodium ions will pull through the membrane. This movement transports other substances that can attach themselves to the transport protein through the membrane. Many amino acids, as well as glucose, enter a cell this way.",True,Secondary active transport (cotransport),,,,
c69e4231-cac7-4fec-9ec8-8f9491b854ac,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,16.3 References and resources,True,Secondary active transport (cotransport),,,,
5cd74a77-5b4e-4680-92ff-5a79c94c9f38,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,Text,False,Text,,,,
7a17934e-76e6-4eee-9727-322edc699d49,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
7a17934e-76e6-4eee-9727-322edc699d49,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
7a17934e-76e6-4eee-9727-322edc699d49,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
7a17934e-76e6-4eee-9727-322edc699d49,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
23f1991f-b023-460a-a8b9-63c52c00bc00,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
23f1991f-b023-460a-a8b9-63c52c00bc00,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
23f1991f-b023-460a-a8b9-63c52c00bc00,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
23f1991f-b023-460a-a8b9-63c52c00bc00,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
b6936001-2396-40f5-a803-c4e0c22f779b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
b6936001-2396-40f5-a803-c4e0c22f779b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
b6936001-2396-40f5-a803-c4e0c22f779b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
b6936001-2396-40f5-a803-c4e0c22f779b,https://pressbooks.lib.vt.edu/cellbio/,16.3 Active Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-3,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
f1503403-bef3-4c83-bc5e-c7e741542b7f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,cellʼs,False,cellʼs,,,,
69aaccde-0ee2-4578-a311-e0bf78f8eed7,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Fluid mosaic model,False,Fluid mosaic model,,,,
0a878ba2-9bfe-4b87-b311-6a5dfb528a2b,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
0a878ba2-9bfe-4b87-b311-6a5dfb528a2b,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
0a878ba2-9bfe-4b87-b311-6a5dfb528a2b,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
0a878ba2-9bfe-4b87-b311-6a5dfb528a2b,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
15794fb4-80ae-4a0a-8d06-0c63bd723600,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Lipids,False,Lipids,,,,
7f997664-e124-456b-ba3d-daa9bf47e531,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
7f997664-e124-456b-ba3d-daa9bf47e531,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
7f997664-e124-456b-ba3d-daa9bf47e531,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
7f997664-e124-456b-ba3d-daa9bf47e531,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
66aefe54-0dad-4495-a8d5-24ab57c5f0b2,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,membraneʼs,False,membraneʼs,,,,
c83bf755-ec9a-4294-8c90-f4cd97c71e14,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,phosphatecontaining,False,phosphatecontaining,,,,
c51400e9-4169-49e1-a078-abe8e48b55fa,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
c51400e9-4169-49e1-a078-abe8e48b55fa,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
c51400e9-4169-49e1-a078-abe8e48b55fa,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
c51400e9-4169-49e1-a078-abe8e48b55fa,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
94e1bf17-5f58-48e3-8679-bb5a9efaec68,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
94e1bf17-5f58-48e3-8679-bb5a9efaec68,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
94e1bf17-5f58-48e3-8679-bb5a9efaec68,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
94e1bf17-5f58-48e3-8679-bb5a9efaec68,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
fa7a2076-fbbe-433f-b488-c19799b6d43d,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Proteins,False,Proteins,,,,
0bee910e-c9f5-49c9-a960-a740154b6df8,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Proteins comprise the plasma membrane’s second major component. Integral proteins, or integrins, as their name suggests, integrate completely into the membrane structure, and their hydrophobic membranespanning regions interact with the phospholipid bilayerʼs hydrophobic region.",True,Proteins,,,,
37caad0f-8b42-461a-aa74-1a6e2f108992,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Peripheral proteins are on the membrane’s exterior and interior surfaces, attached either to integral proteins or to phospholipids. Peripheral proteins, along with integral proteins, may serve as enzymes, as structural attachments for the cytoskeletonʼs fibers, or as part of the cellʼs recognition sites. Scientists sometimes refer to these as “cell-specific” proteins. The body recognizes its own proteins and attacks foreign proteins associated with invasive pathogens. Additional proteins can be lipid anchored on the exterior of the membrane.",True,Proteins,,,,
1a4c06a3-8471-4536-822d-974a830791ac,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Carbohydrates,False,Carbohydrates,,,,
34a70af6-1432-47d1-bdf7-85f96a98946d,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Carbohydrates are the third major plasma membrane component. They are always on the cell’s exterior surface and are bound either to proteins (forming glycoproteins) or to lipids (forming glycolipids). These carbohydrate chains may consist of two to sixty monosaccharide units and can be either straight or branched. Along with peripheral proteins, carbohydrates form specialized sites on the cell surface that allow cells to recognize each other. We collectively refer to these carbohydrates on the cellʼs exterior surface — the carbohydrate components of both glycoproteins and glycolipids — as the glycocalyx (meaning “sugar coating”). The glycocalyx is highly hydrophilic and attracts large amounts of water to the cellʼs surface. This aids in the cellʼs interaction with its watery environment and in the cellʼs ability to obtain substances dissolved in the water.",True,Carbohydrates,,,,
4121d9e8-098e-4e1f-b85f-c9fdb4cbdf86,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Membrane fluidity,False,Membrane fluidity,,,,
508b543f-7b96-4ed0-9a31-fb34e3aacb44,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,The integral proteins and lipids exist in the membrane as separate but loosely attached molecules. The membraneʼs mosaic characteristics explain some but not all of its fluidity. There are two other factors that help maintain this fluid characteristic.,True,Membrane fluidity,,,,
3f7ee1ee-fb77-4a07-a07a-c380845a2b25,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"One factor is the nature of the phospholipids themselves. In their saturated form, the fatty acids in phospholipid tails are saturated with bound hydrogen atoms. There are no double bonds between adjacent carbon atoms. This results in tails that are relatively straight. In contrast, unsaturated fatty acids do not contain a maximal number of hydrogen atoms, but they do contain some double bonds between adjacent carbon atoms.",True,Membrane fluidity,,,,
18988aaf-6c54-4413-85b8-23c948cbdf33,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Temperature can also influence membrane rigidity. Decreasing temperatures compress saturated fatty acids with their straight tails, and they press in on each other, making a dense and fairly rigid membrane. If unsaturated fatty acids are compressed, the “kinks” in their tails elbow adjacent phospholipid molecules away, maintaining some space between the phospholipid molecules. This “elbow room” helps maintain fluidity in the membrane at temperatures at which membranes with saturated fatty acid tails in their phospholipids would “freeze” or solidify.",True,Membrane fluidity,,,,
f5282a50-eb74-4f81-a59e-b0d62357906b,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,16.1 References and resources,True,Membrane fluidity,,,,
a27390ec-e771-4854-ac60-6608185b6b2e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Membrane fluidity,,,,
3728b807-2c22-4953-bf68-5497eb102dc4,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 4: The Structure and Function of the Plasma Membrane.",True,Membrane fluidity,,,,
fd6f9b29-b38b-4421-89bc-ed6c16fb8831,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 49.",True,Membrane fluidity,,,,
928f7eb6-2c62-4227-bfa7-8928248d778c,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
928f7eb6-2c62-4227-bfa7-8928248d778c,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
928f7eb6-2c62-4227-bfa7-8928248d778c,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
928f7eb6-2c62-4227-bfa7-8928248d778c,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
043a60d3-36a8-43e8-88c2-aa5ca2fa14da,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
043a60d3-36a8-43e8-88c2-aa5ca2fa14da,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
043a60d3-36a8-43e8-88c2-aa5ca2fa14da,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
043a60d3-36a8-43e8-88c2-aa5ca2fa14da,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
b04d5a1b-68b8-4a58-98d9-4d712dfd9151,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
b04d5a1b-68b8-4a58-98d9-4d712dfd9151,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
b04d5a1b-68b8-4a58-98d9-4d712dfd9151,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
b04d5a1b-68b8-4a58-98d9-4d712dfd9151,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
67f3ba66-b1c3-4a0a-bdc3-bca3055e2bb8,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,16.2 Passive Transport,True,Membrane fluidity,,,,
4fdfdc11-039f-453a-b7a4-8c5652857fe8,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Plasma membranes must allow certain substances to enter and leave a cell, and prevent some harmful materials from entering and some essential materials from leaving. In other words, plasma membranes are selectively permeable; they allow some substances to pass through, but not others. If they were to lose this selectivity, the cell would no longer be able to sustain itself, and it would be destroyed. There are four major types of transport across the cell membrane:",True,Membrane fluidity,,,,
49645371-dd87-460c-b775-2289e4db2190,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Recall that plasma membranes are amphiphilic: they have hydrophilic and hydrophobic regions. This characteristic helps move some materials through the membrane and hinders the movement of others.,True,Membrane fluidity,,,,
3137e09a-8e9b-47e9-bc58-5086de3da7bd,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Nonpolar and lipid-soluble material with a low molecular weight can easily slip through the membraneʼs hydrophobic lipid core. Substances such as the fat-soluble vitamins A, D, E, and K readily pass through the plasma membranes in the digestive tract and other tissues. Fat-soluble drugs and hormones also gain easy entry into cells and readily transport themselves into the bodyʼs tissues and organs. Oxygen and carbon dioxide molecules have no charge and pass through membranes by simple diffusion.",True,Membrane fluidity,,,,
ced87c46-cbe5-490d-8dcf-ad44e20a8e63,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,bodyʼs,False,bodyʼs,,,,
78a03cda-2678-4af0-960b-fb99af2a8753,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Polar substances present problems for the membrane. While some polar molecules connect easily with the cellʼs outside, they cannot readily pass through the plasma membraneʼs lipid core.",True,bodyʼs,,,,
da6db9f3-4825-4f22-8b7a-7e8337446aac,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Additionally, while small ions could easily slip through the spaces in the membraneʼs mosaic, their charge prevents them from doing so. Ions such as sodium, potassium, calcium, and chloride must have special means of penetrating plasma membranes. Simple sugars and amino acids also need the help of various transmembrane proteins (channels) to transport themselves across plasma membranes.",True,bodyʼs,,,,
344ed827-5b64-4d44-bbb5-114b2abab461,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Diffusion,False,Diffusion,,,,
83b1796e-b005-4be7-b2f7-aa2ce1b5b99f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
83b1796e-b005-4be7-b2f7-aa2ce1b5b99f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
83b1796e-b005-4be7-b2f7-aa2ce1b5b99f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
83b1796e-b005-4be7-b2f7-aa2ce1b5b99f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
6d486648-79cd-4e12-b5b5-5d4a3953351d,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Osmosis,False,Osmosis,,,,
748fd54c-c933-4161-9f41-ec08d9d548e6,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
748fd54c-c933-4161-9f41-ec08d9d548e6,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
748fd54c-c933-4161-9f41-ec08d9d548e6,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
748fd54c-c933-4161-9f41-ec08d9d548e6,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
04289b4c-9417-47a1-9815-a9cf0657ccfd,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,waterʼs,False,waterʼs,,,,
e8210fe4-852f-4671-b909-6bc34104be91,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Tonicity,False,Tonicity,,,,
046adfb0-dd6a-4cb2-bf54-40e2e9d9508c,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Tonicity describes how an extracellular solution can change a cellʼs volume by affecting osmosis. A solutionʼs tonicity often directly correlates with the solutionʼs osmolarity. Osmolarity describes the solutionʼs total solute concentration.,True,Tonicity,,,,
a1396afd-e496-44f3-bcbc-146297d8675f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In a situation in which a membrane, permeable to water though not to the solute, separates two different osmolarities, water will move from the membraneʼs side with lower osmolarity (and more water) to the side with higher osmolarity (and less water).",True,Tonicity,,,,
f56802d0-8356-49b9-8752-60b3effa95a8,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Hypotonic solutions,False,Hypotonic solutions,,,,
54cf2be4-85ff-4fd2-bcf3-3636d16cc199,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In a hypotonic situation, the extracellular fluid has lower osmolarity than the fluid inside the cell, and water enters the cell. It also means that the extracellular fluid has a higher water concentration in the solution than does the cell. In this situation, water will follow its concentration gradient and enter the cell.",True,Hypotonic solutions,,,,
7d9bb9b2-0d2a-4d70-8bfa-727debfc2d6f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Hypertonic solutions,False,Hypertonic solutions,,,,
b7ad2d7b-c85f-4677-9e2e-2f46526321bd,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"As for a hypertonic solution, the prefix “hyper” refers to the extracellular fluid having a higher osmolarity than the cellʼs cytoplasm; therefore, the fluid contains less water than the cell does. Because the cell has a relatively higher water concentration, water will leave the cell.",True,Hypertonic solutions,,,,
8a05c9e2-8afe-433e-9377-96c2abb78050,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Isotonic solutions,False,Isotonic solutions,,,,
1972d17b-6ae7-4f8a-a862-6726d39ef599,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
1972d17b-6ae7-4f8a-a862-6726d39ef599,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
1972d17b-6ae7-4f8a-a862-6726d39ef599,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
1972d17b-6ae7-4f8a-a862-6726d39ef599,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
c81be53e-1fe4-41d0-8cb5-fe1efbfc80e7,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Factors that affect diffusion,False,Factors that affect diffusion,,,,
c7154d6f-0413-4799-83f9-0f9def2f0195,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Molecules move constantly in a random manner, at a rate that depends on their mass, their environment, and the amount of thermal energy they possess, which in turn is a function of temperature. While diffusion will go forward in the presence of a substanceʼs concentration gradient, several factors affect the diffusion rate:",True,Factors that affect diffusion,,,,
5b1a8235-abbe-4291-bcc4-217e6d1e41da,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Facilitated transport (diffusion),False,Facilitated transport (diffusion),,,,
6f4f23a6-b989-4d24-b8e8-e3b7917587ef,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In facilitated transport, or facilitated diffusion, materials diffuse across the plasma membrane with the help of membrane proteins. A concentration gradient exists that would allow these materials to diffuse into the cell without expending cellular energy. However, these materials are polar molecules or ions that the cell membraneʼs hydrophobic parts repel. Facilitated transport proteins shield these materials from the membraneʼs repulsive force, allowing them to diffuse into the cell.",True,Facilitated transport (diffusion),,,,
54902153-883d-476f-b963-c61e5760ab05,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Ion channels,False,Ion channels,,,,
d59f8fde-8bca-4175-9276-57db6b7bf130,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
d59f8fde-8bca-4175-9276-57db6b7bf130,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
d59f8fde-8bca-4175-9276-57db6b7bf130,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
d59f8fde-8bca-4175-9276-57db6b7bf130,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
baff4c89-bf1a-4a17-93d3-b3580020ef8c,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Channel proteins are either open at all times or they are “gated,” which controls the channelʼs opening. The gating can be controlled by volatage, ligand (such as ATP), or mechanical stimulus. When a particular ion attaches to the channel protein, it may control the opening, or other mechanisms or substances may be involved.",True,Ion channels,,,,
e658a7fd-e903-44d7-a760-c7e8b76f1705,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"In some tissues, sodium and chloride ions pass freely through open channels, whereas in other tissues a gate must open to allow passage. Cells involved in transmitting electrical impulses, such as nerve and muscle cells, have gated channels for sodium, potassium, and calcium in their membranes. Opening and closing these channels changes the relative concentrations on opposing sides of the membrane of these ions, resulting in facilitating electrical transmission along membranes (in the case of nerve cells) or in muscle contraction (in the case of muscle cells).",True,Ion channels,,,,
29f43d1a-76ee-43d5-b067-a7388497c767,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Carrier proteins,False,Carrier proteins,,,,
421d22ce-cd2a-4e90-88c5-aecb1300c0e4,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
421d22ce-cd2a-4e90-88c5-aecb1300c0e4,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
421d22ce-cd2a-4e90-88c5-aecb1300c0e4,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
421d22ce-cd2a-4e90-88c5-aecb1300c0e4,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
644a1ee3-1399-49ef-8368-2954c5d51f8f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Depending on the gradient, the material may move in the opposite direction. Carrier proteins are typically specific for a single substance. This selectivity adds to the plasma membraneʼs overall selectivity. One group of carrier proteins, glucose transport proteins, or GLUTs, are involved in transporting glucose and other hexose sugars through plasma membranes within the body.",True,Carrier proteins,,,,
7e9cd47d-a25d-471b-b0d3-95ac12e639c5,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Channel and carrier proteins transport material at different rates. Channel proteins transport much more quickly than carrier proteins. Channel proteins facilitate diffusion at a rate of tens of millions of molecules per second, whereas carrier proteins work at a rate of a thousand to a million molecules per second.",True,Carrier proteins,,,,
def5cb91-cf91-457a-aae7-d7a48d38376c,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,16.2 References and resources,True,Carrier proteins,,,,
60cae1b9-71c7-47f3-9077-b719aa763e3e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
60cae1b9-71c7-47f3-9077-b719aa763e3e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
60cae1b9-71c7-47f3-9077-b719aa763e3e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
60cae1b9-71c7-47f3-9077-b719aa763e3e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
46fe86eb-e1ba-4785-bb00-a0375ffc4eb1,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
46fe86eb-e1ba-4785-bb00-a0375ffc4eb1,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
46fe86eb-e1ba-4785-bb00-a0375ffc4eb1,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
46fe86eb-e1ba-4785-bb00-a0375ffc4eb1,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
40ef3498-45cd-4e41-8256-8a60a737844d,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
40ef3498-45cd-4e41-8256-8a60a737844d,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
40ef3498-45cd-4e41-8256-8a60a737844d,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
40ef3498-45cd-4e41-8256-8a60a737844d,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
f40adbe6-f2af-4f61-bcc8-6de24da00f97,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
f40adbe6-f2af-4f61-bcc8-6de24da00f97,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
f40adbe6-f2af-4f61-bcc8-6de24da00f97,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
f40adbe6-f2af-4f61-bcc8-6de24da00f97,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
18e2be7e-6caa-4f5e-851e-fd78504d744f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
18e2be7e-6caa-4f5e-851e-fd78504d744f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
18e2be7e-6caa-4f5e-851e-fd78504d744f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
18e2be7e-6caa-4f5e-851e-fd78504d744f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
16d42b3b-4785-4885-8cd5-778c6ef23b4b,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,16.3 Active Transport,True,Carrier proteins,,,,
effbbe05-7748-4eaf-a847-57e032cc7ac1,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Active transport mechanisms require the cellʼs energy, usually in the form of adenosine triphosphate (ATP). If a substance must move into the cell against its concentration gradient — that is, if the substanceʼs concentration inside the cell is greater than its concentration in the extracellular fluid (and vice versa) — the cell must use energy to move the substance.",True,Carrier proteins,,,,
7acaaa24-2b39-4708-be7c-8edda2905cf3,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,substanceʼs,False,substanceʼs,,,,
d381b337-15d0-4d6a-88f6-1256db54c11e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Electrochemical gradient,False,Electrochemical gradient,,,,
bd9037ee-987f-4a6e-92be-455c81d1e19e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"We have discussed simple concentration gradients — a substanceʼs differential concentrations across a space or a membrane — but in living systems, gradients are more complex. Because ions move into and out of cells and because cells contain proteins that do not move across the membrane and are mostly negatively charged, there is also an electrical gradient, a difference of charge, across the plasma membrane.",True,Electrochemical gradient,,,,
04bc3369-effc-44a4-a57c-f29d513e0e5e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
04bc3369-effc-44a4-a57c-f29d513e0e5e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
04bc3369-effc-44a4-a57c-f29d513e0e5e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
04bc3369-effc-44a4-a57c-f29d513e0e5e,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
b8fcfda1-9ec1-4719-8dc8-c6ffb64f65eb,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Moving against a gradient,False,Moving against a gradient,,,,
27a8cf24-3885-4831-9a65-26c5d726f9d9,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Two mechanisms exist for transporting small molecular weight material and small molecules:,True,Moving against a gradient,,,,
3812685a-ebc0-44dd-ba64-2555c94c60c0,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Carrier proteins for active transport,False,Carrier proteins for active transport,,,,
352fa066-6bb3-4543-a246-90fdbf83e4d2,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
352fa066-6bb3-4543-a246-90fdbf83e4d2,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
352fa066-6bb3-4543-a246-90fdbf83e4d2,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
352fa066-6bb3-4543-a246-90fdbf83e4d2,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
6ff10ba1-c5a0-47f3-a819-a389188bbca9,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"All of these transporters can also transport small, uncharged organic molecules like glucose. These three types of carrier proteins are also in facilitated diffusion, but they do not require ATP to work in that process.",True,Carrier proteins for active transport,,,,
e49ca128-0cf5-484d-9777-27d86a16fdd0,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Primary active transport,False,Primary active transport,,,,
7e0e125b-1e76-409c-b3ca-a0b746ee9652,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
7e0e125b-1e76-409c-b3ca-a0b746ee9652,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
7e0e125b-1e76-409c-b3ca-a0b746ee9652,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
7e0e125b-1e76-409c-b3ca-a0b746ee9652,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
8d30dce8-f358-4c7c-b409-40af57065c6b,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"One of the most important pumps in animal cells is the sodium-potassium pump (Na+-K+ ATPase), which maintains the electrochemical gradient (and the correct concentrations of Na+ and K+) in living cells. The sodium-potassium pump moves K+ into the cell while moving Na+ out at the same time, at a ratio of three Na+ for every two K+ ions moved in. The Na+-K+ ATPase exists in two forms, depending on its orientation to the cellʼs interior or exterior and its affinity for either sodium or potassium ions. The process consists of the following six steps.",True,Primary active transport,,,,
3e4f0d1f-55bf-41a8-ba0c-0172da28a496,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Secondary active transport (cotransport),False,Secondary active transport (cotransport),,,,
cf6b9402-175c-4d30-9919-6c8b671708c2,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Secondary active transport brings sodium ions, and possibly other compounds, into the cell. As sodium ion concentrations build up outside of the plasma membrane because of the primary active transport process, this creates an electrochemical gradient. If a channel protein exists and is open, the sodium ions will pull through the membrane. This movement transports other substances that can attach themselves to the transport protein through the membrane. Many amino acids, as well as glucose, enter a cell this way.",True,Secondary active transport (cotransport),,,,
cee23552-9607-4d66-90ac-f2caf9ef11a2,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,16.3 References and resources,True,Secondary active transport (cotransport),,,,
142577eb-c6f1-4026-8864-b5f94bd314fb,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,Text,False,Text,,,,
35f1dfd0-a543-493c-803f-95346a86d11f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
35f1dfd0-a543-493c-803f-95346a86d11f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
35f1dfd0-a543-493c-803f-95346a86d11f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
35f1dfd0-a543-493c-803f-95346a86d11f,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
09047f72-f277-42e3-81d8-5de4a853aef9,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
09047f72-f277-42e3-81d8-5de4a853aef9,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
09047f72-f277-42e3-81d8-5de4a853aef9,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
09047f72-f277-42e3-81d8-5de4a853aef9,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
d03dfee2-b337-4303-b4ad-c85527aa79cd,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
d03dfee2-b337-4303-b4ad-c85527aa79cd,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
d03dfee2-b337-4303-b4ad-c85527aa79cd,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
d03dfee2-b337-4303-b4ad-c85527aa79cd,https://pressbooks.lib.vt.edu/cellbio/,16.2 Passive Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-2,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
f6b65217-2f8d-4cc3-a64f-dcdeb6195e82,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,cellʼs,False,cellʼs,,,,
c6844fb2-4d72-419f-ae65-d5f12adfbac0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Fluid mosaic model,False,Fluid mosaic model,,,,
c1c114a6-5ad4-49a4-a6b8-ae6a76f806f3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
c1c114a6-5ad4-49a4-a6b8-ae6a76f806f3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
c1c114a6-5ad4-49a4-a6b8-ae6a76f806f3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
c1c114a6-5ad4-49a4-a6b8-ae6a76f806f3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
162c0964-e199-4b9b-aa16-1a4080294ac4,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Lipids,False,Lipids,,,,
5e59892d-c675-4c29-860e-de8244688bd1,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
5e59892d-c675-4c29-860e-de8244688bd1,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
5e59892d-c675-4c29-860e-de8244688bd1,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
5e59892d-c675-4c29-860e-de8244688bd1,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
2968f6c1-382f-4dce-bedf-85ae802f484b,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,membraneʼs,False,membraneʼs,,,,
f44cc4d3-53fe-45e0-a84f-5bb6626824ae,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,phosphatecontaining,False,phosphatecontaining,,,,
48028cfd-5f08-4646-ac29-56449cd50358,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
48028cfd-5f08-4646-ac29-56449cd50358,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
48028cfd-5f08-4646-ac29-56449cd50358,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
48028cfd-5f08-4646-ac29-56449cd50358,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
9b789651-0a92-432e-aa52-16741056c407,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
9b789651-0a92-432e-aa52-16741056c407,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
9b789651-0a92-432e-aa52-16741056c407,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
9b789651-0a92-432e-aa52-16741056c407,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
3cc71a27-25cb-4abb-a364-5e36acd8b750,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Proteins,False,Proteins,,,,
3f84e031-1ebd-4f57-8e76-e5d2d0270db6,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Proteins comprise the plasma membrane’s second major component. Integral proteins, or integrins, as their name suggests, integrate completely into the membrane structure, and their hydrophobic membranespanning regions interact with the phospholipid bilayerʼs hydrophobic region.",True,Proteins,,,,
e3506dce-6891-40ed-8440-82b2c78042a7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Peripheral proteins are on the membrane’s exterior and interior surfaces, attached either to integral proteins or to phospholipids. Peripheral proteins, along with integral proteins, may serve as enzymes, as structural attachments for the cytoskeletonʼs fibers, or as part of the cellʼs recognition sites. Scientists sometimes refer to these as “cell-specific” proteins. The body recognizes its own proteins and attacks foreign proteins associated with invasive pathogens. Additional proteins can be lipid anchored on the exterior of the membrane.",True,Proteins,,,,
ea290436-6daf-4895-96ff-03d843e0f4ed,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Carbohydrates,False,Carbohydrates,,,,
e8396e27-7f6a-4c3e-9748-37e30e4265b7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Carbohydrates are the third major plasma membrane component. They are always on the cell’s exterior surface and are bound either to proteins (forming glycoproteins) or to lipids (forming glycolipids). These carbohydrate chains may consist of two to sixty monosaccharide units and can be either straight or branched. Along with peripheral proteins, carbohydrates form specialized sites on the cell surface that allow cells to recognize each other. We collectively refer to these carbohydrates on the cellʼs exterior surface — the carbohydrate components of both glycoproteins and glycolipids — as the glycocalyx (meaning “sugar coating”). The glycocalyx is highly hydrophilic and attracts large amounts of water to the cellʼs surface. This aids in the cellʼs interaction with its watery environment and in the cellʼs ability to obtain substances dissolved in the water.",True,Carbohydrates,,,,
170167d9-35ce-41a6-b893-a1b23a7592a7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Membrane fluidity,False,Membrane fluidity,,,,
459b4786-c256-4c3c-86ec-74749b438311,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,The integral proteins and lipids exist in the membrane as separate but loosely attached molecules. The membraneʼs mosaic characteristics explain some but not all of its fluidity. There are two other factors that help maintain this fluid characteristic.,True,Membrane fluidity,,,,
a9361081-3270-4ddd-8d8d-b6a9fce9f93f,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"One factor is the nature of the phospholipids themselves. In their saturated form, the fatty acids in phospholipid tails are saturated with bound hydrogen atoms. There are no double bonds between adjacent carbon atoms. This results in tails that are relatively straight. In contrast, unsaturated fatty acids do not contain a maximal number of hydrogen atoms, but they do contain some double bonds between adjacent carbon atoms.",True,Membrane fluidity,,,,
35e9de48-8598-44f5-8672-655f64935169,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Temperature can also influence membrane rigidity. Decreasing temperatures compress saturated fatty acids with their straight tails, and they press in on each other, making a dense and fairly rigid membrane. If unsaturated fatty acids are compressed, the “kinks” in their tails elbow adjacent phospholipid molecules away, maintaining some space between the phospholipid molecules. This “elbow room” helps maintain fluidity in the membrane at temperatures at which membranes with saturated fatty acid tails in their phospholipids would “freeze” or solidify.",True,Membrane fluidity,,,,
7e950323-4169-4baf-9749-07eed724ff5f,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,16.1 References and resources,True,Membrane fluidity,,,,
27ce9ec2-2960-4e99-9df7-3009c6b79373,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Membrane fluidity,,,,
e6b7c5dc-625b-4e54-a0f9-b893101a9eab,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 4: The Structure and Function of the Plasma Membrane.",True,Membrane fluidity,,,,
86930dbd-9a0d-4d8a-80df-618af07ee856,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 49.",True,Membrane fluidity,,,,
67069872-1b79-4b53-9aee-d588d79c7a07,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
67069872-1b79-4b53-9aee-d588d79c7a07,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
67069872-1b79-4b53-9aee-d588d79c7a07,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
67069872-1b79-4b53-9aee-d588d79c7a07,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
a53e387e-f22c-4818-b919-61ee1686199b,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
a53e387e-f22c-4818-b919-61ee1686199b,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
a53e387e-f22c-4818-b919-61ee1686199b,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
a53e387e-f22c-4818-b919-61ee1686199b,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
671336fc-106e-4680-971b-985338f839f2,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
671336fc-106e-4680-971b-985338f839f2,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
671336fc-106e-4680-971b-985338f839f2,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
671336fc-106e-4680-971b-985338f839f2,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
44638176-ba70-453e-8229-bd3d1c59f878,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,16.2 Passive Transport,True,Membrane fluidity,,,,
05860424-f843-4d80-b136-d2a7a2cc880a,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Plasma membranes must allow certain substances to enter and leave a cell, and prevent some harmful materials from entering and some essential materials from leaving. In other words, plasma membranes are selectively permeable; they allow some substances to pass through, but not others. If they were to lose this selectivity, the cell would no longer be able to sustain itself, and it would be destroyed. There are four major types of transport across the cell membrane:",True,Membrane fluidity,,,,
10ffdd24-4c1a-4c03-881b-e13e9986f3d3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Recall that plasma membranes are amphiphilic: they have hydrophilic and hydrophobic regions. This characteristic helps move some materials through the membrane and hinders the movement of others.,True,Membrane fluidity,,,,
eaf12b9c-9bc0-4222-92f7-212187759933,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Nonpolar and lipid-soluble material with a low molecular weight can easily slip through the membraneʼs hydrophobic lipid core. Substances such as the fat-soluble vitamins A, D, E, and K readily pass through the plasma membranes in the digestive tract and other tissues. Fat-soluble drugs and hormones also gain easy entry into cells and readily transport themselves into the bodyʼs tissues and organs. Oxygen and carbon dioxide molecules have no charge and pass through membranes by simple diffusion.",True,Membrane fluidity,,,,
8ab9614f-55f9-4707-b40b-7fa29232aefc,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,bodyʼs,False,bodyʼs,,,,
ff192858-012b-4e2e-8c02-c16350159768,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Polar substances present problems for the membrane. While some polar molecules connect easily with the cellʼs outside, they cannot readily pass through the plasma membraneʼs lipid core.",True,bodyʼs,,,,
d82f23e6-9d64-42b2-a552-5554b8d0daaf,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Additionally, while small ions could easily slip through the spaces in the membraneʼs mosaic, their charge prevents them from doing so. Ions such as sodium, potassium, calcium, and chloride must have special means of penetrating plasma membranes. Simple sugars and amino acids also need the help of various transmembrane proteins (channels) to transport themselves across plasma membranes.",True,bodyʼs,,,,
f7bd0515-895b-43ac-9eb0-e3dcca2b964c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Diffusion,False,Diffusion,,,,
0e638b81-aed9-41ad-9600-4a0fdc16d390,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
0e638b81-aed9-41ad-9600-4a0fdc16d390,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
0e638b81-aed9-41ad-9600-4a0fdc16d390,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
0e638b81-aed9-41ad-9600-4a0fdc16d390,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
de45518a-d142-4cf8-a93c-65b38c05f4a7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Osmosis,False,Osmosis,,,,
8ac822f4-20f3-4b5c-9c7a-27ce0afdd689,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
8ac822f4-20f3-4b5c-9c7a-27ce0afdd689,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
8ac822f4-20f3-4b5c-9c7a-27ce0afdd689,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
8ac822f4-20f3-4b5c-9c7a-27ce0afdd689,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
020776fc-ca6e-4fff-867b-895cc1aa2a69,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,waterʼs,False,waterʼs,,,,
cc4a0e11-47ce-4341-9c01-2de8cb4e1115,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Tonicity,False,Tonicity,,,,
9a7dc429-aa96-48c4-9396-12d15bb0aa3c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Tonicity describes how an extracellular solution can change a cellʼs volume by affecting osmosis. A solutionʼs tonicity often directly correlates with the solutionʼs osmolarity. Osmolarity describes the solutionʼs total solute concentration.,True,Tonicity,,,,
b46a54bd-1d7d-45e1-adec-4728f095c9be,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In a situation in which a membrane, permeable to water though not to the solute, separates two different osmolarities, water will move from the membraneʼs side with lower osmolarity (and more water) to the side with higher osmolarity (and less water).",True,Tonicity,,,,
6794ebde-ea60-4a0f-9653-5273c443486c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Hypotonic solutions,False,Hypotonic solutions,,,,
277b07ce-5259-425d-b8cb-143a3199de1e,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In a hypotonic situation, the extracellular fluid has lower osmolarity than the fluid inside the cell, and water enters the cell. It also means that the extracellular fluid has a higher water concentration in the solution than does the cell. In this situation, water will follow its concentration gradient and enter the cell.",True,Hypotonic solutions,,,,
b70b8233-97c0-4992-957a-0553e65adb13,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Hypertonic solutions,False,Hypertonic solutions,,,,
e5384b02-715f-4618-a976-40e8d357d54d,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"As for a hypertonic solution, the prefix “hyper” refers to the extracellular fluid having a higher osmolarity than the cellʼs cytoplasm; therefore, the fluid contains less water than the cell does. Because the cell has a relatively higher water concentration, water will leave the cell.",True,Hypertonic solutions,,,,
94f082b2-914e-4d7e-8db8-3d2b180de502,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Isotonic solutions,False,Isotonic solutions,,,,
5fae0dd5-6ffb-4234-9b75-19d1f4af87b8,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
5fae0dd5-6ffb-4234-9b75-19d1f4af87b8,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
5fae0dd5-6ffb-4234-9b75-19d1f4af87b8,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
5fae0dd5-6ffb-4234-9b75-19d1f4af87b8,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
2115b1ff-bd04-4cd7-a59a-f67880dc3b01,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Factors that affect diffusion,False,Factors that affect diffusion,,,,
4cd60d23-fcfe-414d-9ad5-979a5d1c55ed,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Molecules move constantly in a random manner, at a rate that depends on their mass, their environment, and the amount of thermal energy they possess, which in turn is a function of temperature. While diffusion will go forward in the presence of a substanceʼs concentration gradient, several factors affect the diffusion rate:",True,Factors that affect diffusion,,,,
846cdc87-1d3f-4847-915e-552a10d14620,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Facilitated transport (diffusion),False,Facilitated transport (diffusion),,,,
acad576c-e542-49b9-85a4-0107a0b78cc9,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In facilitated transport, or facilitated diffusion, materials diffuse across the plasma membrane with the help of membrane proteins. A concentration gradient exists that would allow these materials to diffuse into the cell without expending cellular energy. However, these materials are polar molecules or ions that the cell membraneʼs hydrophobic parts repel. Facilitated transport proteins shield these materials from the membraneʼs repulsive force, allowing them to diffuse into the cell.",True,Facilitated transport (diffusion),,,,
5c766f96-5e2c-447d-ae3b-732e0f6d4df2,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Ion channels,False,Ion channels,,,,
001bbac6-47fe-4196-a2b5-69289c794cf3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
001bbac6-47fe-4196-a2b5-69289c794cf3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
001bbac6-47fe-4196-a2b5-69289c794cf3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
001bbac6-47fe-4196-a2b5-69289c794cf3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
5e34e054-6350-4d13-a31f-ee9e0498c8fd,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Channel proteins are either open at all times or they are “gated,” which controls the channelʼs opening. The gating can be controlled by volatage, ligand (such as ATP), or mechanical stimulus. When a particular ion attaches to the channel protein, it may control the opening, or other mechanisms or substances may be involved.",True,Ion channels,,,,
a465692a-9ac4-4d8f-99de-d0e799a9df3c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"In some tissues, sodium and chloride ions pass freely through open channels, whereas in other tissues a gate must open to allow passage. Cells involved in transmitting electrical impulses, such as nerve and muscle cells, have gated channels for sodium, potassium, and calcium in their membranes. Opening and closing these channels changes the relative concentrations on opposing sides of the membrane of these ions, resulting in facilitating electrical transmission along membranes (in the case of nerve cells) or in muscle contraction (in the case of muscle cells).",True,Ion channels,,,,
038d3c63-285f-41ed-8134-a00a7d98a9df,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Carrier proteins,False,Carrier proteins,,,,
41e40a88-5a35-4a11-a0f4-ef9f2c084600,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
41e40a88-5a35-4a11-a0f4-ef9f2c084600,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
41e40a88-5a35-4a11-a0f4-ef9f2c084600,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
41e40a88-5a35-4a11-a0f4-ef9f2c084600,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
94fe56f0-8ecc-45f1-9ce3-8d03e652fd63,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Depending on the gradient, the material may move in the opposite direction. Carrier proteins are typically specific for a single substance. This selectivity adds to the plasma membraneʼs overall selectivity. One group of carrier proteins, glucose transport proteins, or GLUTs, are involved in transporting glucose and other hexose sugars through plasma membranes within the body.",True,Carrier proteins,,,,
5b2ae374-6267-4ee3-bccb-32c2b8d537b6,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Channel and carrier proteins transport material at different rates. Channel proteins transport much more quickly than carrier proteins. Channel proteins facilitate diffusion at a rate of tens of millions of molecules per second, whereas carrier proteins work at a rate of a thousand to a million molecules per second.",True,Carrier proteins,,,,
473ac450-743c-4fc6-b241-dc4dd2700490,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,16.2 References and resources,True,Carrier proteins,,,,
1a6771d7-c244-4a5b-94ad-96ded22a312f,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
1a6771d7-c244-4a5b-94ad-96ded22a312f,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
1a6771d7-c244-4a5b-94ad-96ded22a312f,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
1a6771d7-c244-4a5b-94ad-96ded22a312f,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
c685082b-2105-4015-842e-75c6a91d897c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
c685082b-2105-4015-842e-75c6a91d897c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
c685082b-2105-4015-842e-75c6a91d897c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
c685082b-2105-4015-842e-75c6a91d897c,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
0e56914b-e225-49de-a5b1-68407aeb0e4a,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
0e56914b-e225-49de-a5b1-68407aeb0e4a,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
0e56914b-e225-49de-a5b1-68407aeb0e4a,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
0e56914b-e225-49de-a5b1-68407aeb0e4a,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
133a2c37-dde4-4ae6-a51b-b90a6bfb36a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
133a2c37-dde4-4ae6-a51b-b90a6bfb36a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
133a2c37-dde4-4ae6-a51b-b90a6bfb36a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
133a2c37-dde4-4ae6-a51b-b90a6bfb36a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
aa172767-1635-4b68-9c03-73a1be8c24c6,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
aa172767-1635-4b68-9c03-73a1be8c24c6,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
aa172767-1635-4b68-9c03-73a1be8c24c6,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
aa172767-1635-4b68-9c03-73a1be8c24c6,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
baea0749-ccd3-44d7-af58-f213e9971365,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,16.3 Active Transport,True,Carrier proteins,,,,
51c4b123-b5f4-46d6-852e-a2d3b2b9a7cf,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Active transport mechanisms require the cellʼs energy, usually in the form of adenosine triphosphate (ATP). If a substance must move into the cell against its concentration gradient — that is, if the substanceʼs concentration inside the cell is greater than its concentration in the extracellular fluid (and vice versa) — the cell must use energy to move the substance.",True,Carrier proteins,,,,
150c3e5c-c5b3-460e-bbef-9637a8010001,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,substanceʼs,False,substanceʼs,,,,
6cdf9310-bf6f-475e-9101-f66874a493d7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Electrochemical gradient,False,Electrochemical gradient,,,,
d7df5c4d-c903-494c-b401-52303b36bdf4,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"We have discussed simple concentration gradients — a substanceʼs differential concentrations across a space or a membrane — but in living systems, gradients are more complex. Because ions move into and out of cells and because cells contain proteins that do not move across the membrane and are mostly negatively charged, there is also an electrical gradient, a difference of charge, across the plasma membrane.",True,Electrochemical gradient,,,,
681e9af3-8c3f-4cc0-b2ac-f6eb9f740eb0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
681e9af3-8c3f-4cc0-b2ac-f6eb9f740eb0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
681e9af3-8c3f-4cc0-b2ac-f6eb9f740eb0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
681e9af3-8c3f-4cc0-b2ac-f6eb9f740eb0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
13aa426a-6bc0-47ac-8719-3b5d5636cbe3,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Moving against a gradient,False,Moving against a gradient,,,,
f1cd169f-89ce-4a30-826f-8bf640f9f4ca,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Two mechanisms exist for transporting small molecular weight material and small molecules:,True,Moving against a gradient,,,,
603d7374-aa2b-471a-9d2b-22380807e25b,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Carrier proteins for active transport,False,Carrier proteins for active transport,,,,
6a69b076-ea64-4d7a-beff-3641a88e7bed,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
6a69b076-ea64-4d7a-beff-3641a88e7bed,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
6a69b076-ea64-4d7a-beff-3641a88e7bed,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
6a69b076-ea64-4d7a-beff-3641a88e7bed,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
5163ee07-3f89-43b0-80e1-ba70640c9852,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"All of these transporters can also transport small, uncharged organic molecules like glucose. These three types of carrier proteins are also in facilitated diffusion, but they do not require ATP to work in that process.",True,Carrier proteins for active transport,,,,
3fa102ce-d1bf-4cd2-9740-cd5e52dfacb0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Primary active transport,False,Primary active transport,,,,
a5df118d-47fc-43a4-b145-ad90ef285c96,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
a5df118d-47fc-43a4-b145-ad90ef285c96,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
a5df118d-47fc-43a4-b145-ad90ef285c96,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
a5df118d-47fc-43a4-b145-ad90ef285c96,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
be765bc8-28c8-446c-b068-d449fdf7a24e,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"One of the most important pumps in animal cells is the sodium-potassium pump (Na+-K+ ATPase), which maintains the electrochemical gradient (and the correct concentrations of Na+ and K+) in living cells. The sodium-potassium pump moves K+ into the cell while moving Na+ out at the same time, at a ratio of three Na+ for every two K+ ions moved in. The Na+-K+ ATPase exists in two forms, depending on its orientation to the cellʼs interior or exterior and its affinity for either sodium or potassium ions. The process consists of the following six steps.",True,Primary active transport,,,,
7db43b93-0bb2-4adc-8534-7389a4d878f4,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Secondary active transport (cotransport),False,Secondary active transport (cotransport),,,,
6bcdd115-3769-4c94-b743-9c53b96c1093,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Secondary active transport brings sodium ions, and possibly other compounds, into the cell. As sodium ion concentrations build up outside of the plasma membrane because of the primary active transport process, this creates an electrochemical gradient. If a channel protein exists and is open, the sodium ions will pull through the membrane. This movement transports other substances that can attach themselves to the transport protein through the membrane. Many amino acids, as well as glucose, enter a cell this way.",True,Secondary active transport (cotransport),,,,
37031aec-f46a-4a1d-a82d-64757aef3883,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,16.3 References and resources,True,Secondary active transport (cotransport),,,,
b170191f-b1f6-45fd-913e-236c7b73b670,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,Text,False,Text,,,,
cb2b3347-ece1-460a-b45e-f463a9f683c7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
cb2b3347-ece1-460a-b45e-f463a9f683c7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
cb2b3347-ece1-460a-b45e-f463a9f683c7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
cb2b3347-ece1-460a-b45e-f463a9f683c7,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
fdc2cd2c-c3fa-4bd4-83ab-f54f09b2c7a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
fdc2cd2c-c3fa-4bd4-83ab-f54f09b2c7a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
fdc2cd2c-c3fa-4bd4-83ab-f54f09b2c7a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
fdc2cd2c-c3fa-4bd4-83ab-f54f09b2c7a0,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
23d0ed0d-3dee-48c0-afee-731c01a450ef,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
23d0ed0d-3dee-48c0-afee-731c01a450ef,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
23d0ed0d-3dee-48c0-afee-731c01a450ef,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
23d0ed0d-3dee-48c0-afee-731c01a450ef,https://pressbooks.lib.vt.edu/cellbio/,16.1 Components and Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/#chapter-100-section-1,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
3aa1d99e-5dd4-4793-a0da-d2889c8ae233,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,cellʼs,False,cellʼs,,,,
97c59860-29dd-470a-9cad-6a252285ad16,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Fluid mosaic model,False,Fluid mosaic model,,,,
fbd0e19d-59a7-4043-aa46-81bbe786d26d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
fbd0e19d-59a7-4043-aa46-81bbe786d26d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
fbd0e19d-59a7-4043-aa46-81bbe786d26d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
fbd0e19d-59a7-4043-aa46-81bbe786d26d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The fluid mosaic model describes the plasma membrane structure as a mosaic of components — including phospholipids, cholesterol, proteins, and carbohydrates — that gives the membrane a fluid character. Plasma membranes range from 5 to 10 nm in thickness (figure 16.1). The protein, lipid, and carbohydrate proportions in the plasma membrane vary with cell type.",True,Fluid mosaic model,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
85bbe5f7-2466-47d6-9981-8f4e9f34d4da,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Lipids,False,Lipids,,,,
8fd9f8ea-8acc-45db-8092-b1bfcd60929d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
8fd9f8ea-8acc-45db-8092-b1bfcd60929d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
8fd9f8ea-8acc-45db-8092-b1bfcd60929d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
8fd9f8ea-8acc-45db-8092-b1bfcd60929d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The membraneʼs main fabric comprises amphiphilic, phospholipid molecules. The hydrophilic or “water-loving” areas of these molecules (figure 16.2) are in contact with the aqueous fluid both inside and outside the cell. Hydrophobic or “water-hating” molecules tend to be nonpolar. They interact with other nonpolar molecules in chemical reactions, but generally do not interact with polar molecules. A phospholipid molecule consists of a three-carbon glycerol backbone with two fatty acid molecules attached. This arrangement gives the overall molecule a head area (the phosphatecontaining group), which has a polar character or negative charge, and a tail area (the fatty acids), which has no charge. The head can form hydrogen bonds, but the tail cannot (figure 16.2).",True,Lipids,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
3db1d942-bf35-4698-9532-23bbdc4b5a49,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,membraneʼs,False,membraneʼs,,,,
ecdf356a-3c04-47df-b49b-91c2a2064d80,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,phosphatecontaining,False,phosphatecontaining,,,,
d5b09bd6-4f07-4c57-8c01-a9fd3c7623bd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
d5b09bd6-4f07-4c57-8c01-a9fd3c7623bd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
d5b09bd6-4f07-4c57-8c01-a9fd3c7623bd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
d5b09bd6-4f07-4c57-8c01-a9fd3c7623bd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Cholesterol, another lipid comprised of four fused carbon rings, is situated alongside the phospholipids in the membraneʼs core (figure 16.2).",True,phosphatecontaining,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
a6153e24-86a6-47ac-918f-08ecfcab4250,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
a6153e24-86a6-47ac-918f-08ecfcab4250,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
a6153e24-86a6-47ac-918f-08ecfcab4250,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
a6153e24-86a6-47ac-918f-08ecfcab4250,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Specific phospholipids play key roles in the membrane; phosphatidylcholine, serine, inositol, and ethanolamine (figure 16.3) play various roles in the membrane.",True,phosphatecontaining,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
4f48a816-efea-4659-bb05-c3b85fd509f5,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Proteins,False,Proteins,,,,
05d56409-09b7-402e-b21c-c0bc3866a109,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Proteins comprise the plasma membrane’s second major component. Integral proteins, or integrins, as their name suggests, integrate completely into the membrane structure, and their hydrophobic membranespanning regions interact with the phospholipid bilayerʼs hydrophobic region.",True,Proteins,,,,
27805fe0-4b65-4435-b652-16aacf63200f,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Peripheral proteins are on the membrane’s exterior and interior surfaces, attached either to integral proteins or to phospholipids. Peripheral proteins, along with integral proteins, may serve as enzymes, as structural attachments for the cytoskeletonʼs fibers, or as part of the cellʼs recognition sites. Scientists sometimes refer to these as “cell-specific” proteins. The body recognizes its own proteins and attacks foreign proteins associated with invasive pathogens. Additional proteins can be lipid anchored on the exterior of the membrane.",True,Proteins,,,,
b620877f-b4dc-4c65-a48c-42d0ad86147e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Carbohydrates,False,Carbohydrates,,,,
6498bdb5-af54-4ed6-90f3-c2898db0504e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Carbohydrates are the third major plasma membrane component. They are always on the cell’s exterior surface and are bound either to proteins (forming glycoproteins) or to lipids (forming glycolipids). These carbohydrate chains may consist of two to sixty monosaccharide units and can be either straight or branched. Along with peripheral proteins, carbohydrates form specialized sites on the cell surface that allow cells to recognize each other. We collectively refer to these carbohydrates on the cellʼs exterior surface — the carbohydrate components of both glycoproteins and glycolipids — as the glycocalyx (meaning “sugar coating”). The glycocalyx is highly hydrophilic and attracts large amounts of water to the cellʼs surface. This aids in the cellʼs interaction with its watery environment and in the cellʼs ability to obtain substances dissolved in the water.",True,Carbohydrates,,,,
38309814-0508-461e-9f93-c7967d8565e9,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Membrane fluidity,False,Membrane fluidity,,,,
98506886-1e0a-41d3-a949-e6d7a223321a,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,The integral proteins and lipids exist in the membrane as separate but loosely attached molecules. The membraneʼs mosaic characteristics explain some but not all of its fluidity. There are two other factors that help maintain this fluid characteristic.,True,Membrane fluidity,,,,
8f7d6f28-3a66-43f0-929f-d21b0c96f723,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"One factor is the nature of the phospholipids themselves. In their saturated form, the fatty acids in phospholipid tails are saturated with bound hydrogen atoms. There are no double bonds between adjacent carbon atoms. This results in tails that are relatively straight. In contrast, unsaturated fatty acids do not contain a maximal number of hydrogen atoms, but they do contain some double bonds between adjacent carbon atoms.",True,Membrane fluidity,,,,
990d86f4-663d-4081-a4c0-262996c6a5b0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Temperature can also influence membrane rigidity. Decreasing temperatures compress saturated fatty acids with their straight tails, and they press in on each other, making a dense and fairly rigid membrane. If unsaturated fatty acids are compressed, the “kinks” in their tails elbow adjacent phospholipid molecules away, maintaining some space between the phospholipid molecules. This “elbow room” helps maintain fluidity in the membrane at temperatures at which membranes with saturated fatty acid tails in their phospholipids would “freeze” or solidify.",True,Membrane fluidity,,,,
98872f5a-955c-482e-9add-a5b591347e9c,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,16.1 References and resources,True,Membrane fluidity,,,,
be345d43-6be8-4a05-87ba-b1a6b494b481,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 4: Cell Structure, Chapter 5: Structure and Function of the Plasma Membranes.",True,Membrane fluidity,,,,
bd267ed5-3560-4dce-aeb1-ee62d9ce0a96,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 4: The Structure and Function of the Plasma Membrane.",True,Membrane fluidity,,,,
59bec2c7-3611-4e51-93d6-abb6a2fd9416,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 49.",True,Membrane fluidity,,,,
94595bdb-f2c0-4220-8128-4d0e411260a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
94595bdb-f2c0-4220-8128-4d0e411260a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
94595bdb-f2c0-4220-8128-4d0e411260a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
94595bdb-f2c0-4220-8128-4d0e411260a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.1 Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness. 2021. https://archive.org/details/16.1_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.1,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
38a8caf4-aeae-4db9-92d4-a7c9a413b62c,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
38a8caf4-aeae-4db9-92d4-a7c9a413b62c,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
38a8caf4-aeae-4db9-92d4-a7c9a413b62c,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
38a8caf4-aeae-4db9-92d4-a7c9a413b62c,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.2 Structure of a phospholipid. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.2_20210926. CC BY-SA 4.0. Added Cell membrane detailed diagram 4 vi by P.T.Đ. CC BY-SA 4.0. From Wikimedia Commons.",True,Membrane fluidity,Figure 16.2,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
946826a3-4b06-4aeb-b9be-312da3c59ef4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
946826a3-4b06-4aeb-b9be-312da3c59ef4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
946826a3-4b06-4aeb-b9be-312da3c59ef4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
946826a3-4b06-4aeb-b9be-312da3c59ef4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.3 Important membrane lipids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/16.3_20210926. CC BY 4.0.",True,Membrane fluidity,Figure 16.3,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
a16f682e-8b8e-421c-a0cb-0c224b88dbb3,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,16.2 Passive Transport,True,Membrane fluidity,,,,
0e1c969c-a1b3-4296-afc9-7a55ac433a38,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Plasma membranes must allow certain substances to enter and leave a cell, and prevent some harmful materials from entering and some essential materials from leaving. In other words, plasma membranes are selectively permeable; they allow some substances to pass through, but not others. If they were to lose this selectivity, the cell would no longer be able to sustain itself, and it would be destroyed. There are four major types of transport across the cell membrane:",True,Membrane fluidity,,,,
9d7ef8d1-ea76-411b-a78d-a6b3794b2353,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Recall that plasma membranes are amphiphilic: they have hydrophilic and hydrophobic regions. This characteristic helps move some materials through the membrane and hinders the movement of others.,True,Membrane fluidity,,,,
6b1aa613-4e5f-4189-ad9c-7ff448eb820b,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Nonpolar and lipid-soluble material with a low molecular weight can easily slip through the membraneʼs hydrophobic lipid core. Substances such as the fat-soluble vitamins A, D, E, and K readily pass through the plasma membranes in the digestive tract and other tissues. Fat-soluble drugs and hormones also gain easy entry into cells and readily transport themselves into the bodyʼs tissues and organs. Oxygen and carbon dioxide molecules have no charge and pass through membranes by simple diffusion.",True,Membrane fluidity,,,,
674e2c14-f03e-40fb-8fa4-0c1b350f01dd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,bodyʼs,False,bodyʼs,,,,
7f001f9e-a8ed-4ad3-b174-f7da05949b99,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Polar substances present problems for the membrane. While some polar molecules connect easily with the cellʼs outside, they cannot readily pass through the plasma membraneʼs lipid core.",True,bodyʼs,,,,
5d46aa83-5241-4a30-9887-0f8a67bb518d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Additionally, while small ions could easily slip through the spaces in the membraneʼs mosaic, their charge prevents them from doing so. Ions such as sodium, potassium, calcium, and chloride must have special means of penetrating plasma membranes. Simple sugars and amino acids also need the help of various transmembrane proteins (channels) to transport themselves across plasma membranes.",True,bodyʼs,,,,
f9baf677-d6b1-40b0-ad85-687394715407,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Diffusion,False,Diffusion,,,,
e8457e53-1bad-4d37-b469-c2aa86347a41,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
e8457e53-1bad-4d37-b469-c2aa86347a41,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
e8457e53-1bad-4d37-b469-c2aa86347a41,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
e8457e53-1bad-4d37-b469-c2aa86347a41,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Diffusion is a passive process of transport. A single substance moves from a high concentration to a low concentration area until the concentration is equal across a space (figure 16.4). Materials move within the cellʼs cytosol by diffusion, and certain materials move through the plasma membrane by diffusion such as lipids and fat-soluble vitamins. Diffusion expends no energy. On the contrary, concentration gradients are a form of potential energy, which dissipates as the gradient is eliminated.",True,Diffusion,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
f5626990-2dec-4b14-880d-8baa08d7b04b,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Osmosis,False,Osmosis,,,,
ec427a35-c30a-4ebd-bb7e-823839d4a718,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
ec427a35-c30a-4ebd-bb7e-823839d4a718,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
ec427a35-c30a-4ebd-bb7e-823839d4a718,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
ec427a35-c30a-4ebd-bb7e-823839d4a718,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Osmosis is the movement of water through a semipermeable membrane according to the waterʼs concentration gradient across the membrane, which is inversely proportional to the solute’s concentration. While diffusion transports material across membranes and within cells, osmosis transports only water across a membrane, and the membrane limits the solute’s diffusion in the water (figure 16.5). Not surprisingly, the aquaporins that facilitate water movement play a large role in osmosis, most prominently in red blood cells and the membranes of kidney tubules. In osmosis, water always moves from an area of higher water concentration to one of lower concentration.",True,Osmosis,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
5cbe9c7e-b75b-4196-ba38-35709e292dfd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,waterʼs,False,waterʼs,,,,
f498a58d-0a65-4f1b-b738-c2719e1913bf,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Tonicity,False,Tonicity,,,,
8a0a71f2-71dd-422d-a2f9-e213115602b2,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Tonicity describes how an extracellular solution can change a cellʼs volume by affecting osmosis. A solutionʼs tonicity often directly correlates with the solutionʼs osmolarity. Osmolarity describes the solutionʼs total solute concentration.,True,Tonicity,,,,
11cc9b9f-55d2-4077-a027-8873f1f2b86e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In a situation in which a membrane, permeable to water though not to the solute, separates two different osmolarities, water will move from the membraneʼs side with lower osmolarity (and more water) to the side with higher osmolarity (and less water).",True,Tonicity,,,,
18efe9f8-df15-4345-930d-c7a691d768b7,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Hypotonic solutions,False,Hypotonic solutions,,,,
4ecb042f-33f0-48d9-9905-36ecebd67e44,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In a hypotonic situation, the extracellular fluid has lower osmolarity than the fluid inside the cell, and water enters the cell. It also means that the extracellular fluid has a higher water concentration in the solution than does the cell. In this situation, water will follow its concentration gradient and enter the cell.",True,Hypotonic solutions,,,,
44b31efb-6ce1-454b-bc86-436f3cd95556,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Hypertonic solutions,False,Hypertonic solutions,,,,
96cec816-5f81-4522-9e7e-17c467a392d8,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"As for a hypertonic solution, the prefix “hyper” refers to the extracellular fluid having a higher osmolarity than the cellʼs cytoplasm; therefore, the fluid contains less water than the cell does. Because the cell has a relatively higher water concentration, water will leave the cell.",True,Hypertonic solutions,,,,
bd7e8f50-fb58-48be-9e54-7b27894260fd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Isotonic solutions,False,Isotonic solutions,,,,
299f1779-c82e-4b4f-8dc6-141405aaf1a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
299f1779-c82e-4b4f-8dc6-141405aaf1a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
299f1779-c82e-4b4f-8dc6-141405aaf1a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
299f1779-c82e-4b4f-8dc6-141405aaf1a0,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In an isotonic solution, the extracellular fluid has the same osmolarity as the cell. If the cellʼs osmolarity matches that of the extracellular fluid, there will be no net movement of water into or out of the cell, although water will still move in and out. Osmotic pressure changes red blood cellsʼ shape in hypertonic, isotonic, and hypotonic solutions (figure 16.6).",True,Isotonic solutions,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
34c5ef57-e832-4365-bbe6-7911375ef9f9,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Factors that affect diffusion,False,Factors that affect diffusion,,,,
0c5969fb-771a-46bf-9b89-d7a3deeb2c97,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Molecules move constantly in a random manner, at a rate that depends on their mass, their environment, and the amount of thermal energy they possess, which in turn is a function of temperature. While diffusion will go forward in the presence of a substanceʼs concentration gradient, several factors affect the diffusion rate:",True,Factors that affect diffusion,,,,
2ee4325a-defc-40db-867c-9fc93db57716,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Facilitated transport (diffusion),False,Facilitated transport (diffusion),,,,
be187407-1f53-4f5b-91b7-b03a3b2b56ca,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In facilitated transport, or facilitated diffusion, materials diffuse across the plasma membrane with the help of membrane proteins. A concentration gradient exists that would allow these materials to diffuse into the cell without expending cellular energy. However, these materials are polar molecules or ions that the cell membraneʼs hydrophobic parts repel. Facilitated transport proteins shield these materials from the membraneʼs repulsive force, allowing them to diffuse into the cell.",True,Facilitated transport (diffusion),,,,
d09a27b9-cbe3-4eab-9031-044448ed12e8,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Ion channels,False,Ion channels,,,,
4f2df11f-ab72-4967-a30b-ad16b4cdf259,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
4f2df11f-ab72-4967-a30b-ad16b4cdf259,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
4f2df11f-ab72-4967-a30b-ad16b4cdf259,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
4f2df11f-ab72-4967-a30b-ad16b4cdf259,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Channels are specific for the transported substance. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids. In addition, they have a hydrophilic channel through their core that provides a hydrated opening through the membrane layers (figure 16.7).",True,Ion channels,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
f6cdf27d-e5d1-4742-9823-41874e326b72,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Channel proteins are either open at all times or they are “gated,” which controls the channelʼs opening. The gating can be controlled by volatage, ligand (such as ATP), or mechanical stimulus. When a particular ion attaches to the channel protein, it may control the opening, or other mechanisms or substances may be involved.",True,Ion channels,,,,
b346dba0-337a-403c-9167-430a20efc3e3,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"In some tissues, sodium and chloride ions pass freely through open channels, whereas in other tissues a gate must open to allow passage. Cells involved in transmitting electrical impulses, such as nerve and muscle cells, have gated channels for sodium, potassium, and calcium in their membranes. Opening and closing these channels changes the relative concentrations on opposing sides of the membrane of these ions, resulting in facilitating electrical transmission along membranes (in the case of nerve cells) or in muscle contraction (in the case of muscle cells).",True,Ion channels,,,,
a332bb7e-95e5-4d17-a063-79db0bdae453,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Carrier proteins,False,Carrier proteins,,,,
e8c5a089-4e2a-44c5-9bf4-0fc25595b3f4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
e8c5a089-4e2a-44c5-9bf4-0fc25595b3f4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
e8c5a089-4e2a-44c5-9bf4-0fc25595b3f4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
e8c5a089-4e2a-44c5-9bf4-0fc25595b3f4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Another type of protein embedded in the plasma membrane is a carrier protein. This aptly named protein binds a substance and, thus triggers a change of its own shape, moving the bound molecule from the cellʼs outside to its interior (figure 16.8).",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
dbb715c6-555f-4580-9db7-c7372ebd6ccd,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Depending on the gradient, the material may move in the opposite direction. Carrier proteins are typically specific for a single substance. This selectivity adds to the plasma membraneʼs overall selectivity. One group of carrier proteins, glucose transport proteins, or GLUTs, are involved in transporting glucose and other hexose sugars through plasma membranes within the body.",True,Carrier proteins,,,,
ce877d9d-a9c8-4de8-9a3e-7bd678622a5d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Channel and carrier proteins transport material at different rates. Channel proteins transport much more quickly than carrier proteins. Channel proteins facilitate diffusion at a rate of tens of millions of molecules per second, whereas carrier proteins work at a rate of a thousand to a million molecules per second.",True,Carrier proteins,,,,
37c7aecd-a1c6-42cf-be64-851160a72a9e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,16.2 References and resources,True,Carrier proteins,,,,
af30c154-4767-4969-8a70-4210e8dc0596,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
af30c154-4767-4969-8a70-4210e8dc0596,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
af30c154-4767-4969-8a70-4210e8dc0596,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
af30c154-4767-4969-8a70-4210e8dc0596,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.4 Diffusion across the plasma membrane. 2021. https://archive.org/details/16.4_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.4,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
40866ce8-b363-4e5b-a3f3-2df9db328812,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
40866ce8-b363-4e5b-a3f3-2df9db328812,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
40866ce8-b363-4e5b-a3f3-2df9db328812,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
40866ce8-b363-4e5b-a3f3-2df9db328812,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.5 Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can. 2021. https://archive.org/details/16.5_20210926. CC BY 4.0.",True,Carrier proteins,Figure 16.5,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
7ef93344-4f99-4bab-abfe-3ab63fb190ad,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
7ef93344-4f99-4bab-abfe-3ab63fb190ad,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
7ef93344-4f99-4bab-abfe-3ab63fb190ad,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
7ef93344-4f99-4bab-abfe-3ab63fb190ad,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.6 Comparison of red blood cell morphology in isotonic, hypertonic and hypotonic solutions. 2021. https://archive.org/details/16.6_20210926. CC BY 4.0. Added Osmotic pressure on blood cells diagram by LadyofHats. Public domain. From Wikimedia Commons.",True,Carrier proteins,Figure 16.6,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
766aeae0-d550-4c59-97e2-82c862fe9d79,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
766aeae0-d550-4c59-97e2-82c862fe9d79,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
766aeae0-d550-4c59-97e2-82c862fe9d79,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
766aeae0-d550-4c59-97e2-82c862fe9d79,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.7 Protein channel. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.7,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
c98eb2ed-edb9-4a92-a505-dd49db4b3e68,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
c98eb2ed-edb9-4a92-a505-dd49db4b3e68,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
c98eb2ed-edb9-4a92-a505-dd49db4b3e68,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
c98eb2ed-edb9-4a92-a505-dd49db4b3e68,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.8 Carrier proteins… Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.7 Common types of transport mechanisms for human cells. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Carrier proteins,Figure 16.8,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
b7f6b481-6397-477d-b335-dfd7cd9e60ee,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,16.3 Active Transport,True,Carrier proteins,,,,
1fa92927-3ba7-4d43-bd57-28732ea1c563,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Active transport mechanisms require the cellʼs energy, usually in the form of adenosine triphosphate (ATP). If a substance must move into the cell against its concentration gradient — that is, if the substanceʼs concentration inside the cell is greater than its concentration in the extracellular fluid (and vice versa) — the cell must use energy to move the substance.",True,Carrier proteins,,,,
21dc3245-f731-476e-966d-8db1f6edd96d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,substanceʼs,False,substanceʼs,,,,
ca01ced1-5d15-4fc9-bcb5-caa50201d670,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Electrochemical gradient,False,Electrochemical gradient,,,,
57e6a6d9-8ef6-4958-a3ba-a266184e9ea4,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"We have discussed simple concentration gradients — a substanceʼs differential concentrations across a space or a membrane — but in living systems, gradients are more complex. Because ions move into and out of cells and because cells contain proteins that do not move across the membrane and are mostly negatively charged, there is also an electrical gradient, a difference of charge, across the plasma membrane.",True,Electrochemical gradient,,,,
1d6cf415-38d6-4498-97ec-67148fae773d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
1d6cf415-38d6-4498-97ec-67148fae773d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
1d6cf415-38d6-4498-97ec-67148fae773d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
1d6cf415-38d6-4498-97ec-67148fae773d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"The interior of living cells is electrically negative with respect to the extracellular fluid in which they are bathed, and at the same time, cells have higher concentrations of potassium (K+) and lower concentrations of sodium (Na+) than the extracellular fluid. Thus in a living cell, the concentration gradient of Na+ tends to drive it into the cell, and its electrical gradient (a positive ion) also drives it inward to the negatively charged interior. However, the situation is more complex for other elements such as potassium. The electrical gradient of K+, a positive ion, also drives it into the cell, but the concentration gradient of K+ drives K+ out of the cell (figure 16.9). We call the combined concentration gradient and electrical charge that affects an ion its electrochemical gradient.",True,Electrochemical gradient,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
51d891b0-f1e9-476d-abf4-6aae20d7a3bf,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Moving against a gradient,False,Moving against a gradient,,,,
dbf32d11-d1d7-49f4-8eaa-c2dc0cd3ad4b,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Two mechanisms exist for transporting small molecular weight material and small molecules:,True,Moving against a gradient,,,,
fb0ae908-0a11-4e14-a4cb-0e798676d99b,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Carrier proteins for active transport,False,Carrier proteins for active transport,,,,
8b6edb18-3972-407a-ad73-8d82762c1a31,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
8b6edb18-3972-407a-ad73-8d82762c1a31,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
8b6edb18-3972-407a-ad73-8d82762c1a31,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
8b6edb18-3972-407a-ad73-8d82762c1a31,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,An important membrane adaptation for active transport is the presence of specific carrier proteins or pumps to facilitate movement. There are three protein types or transporters (figure 16.10).,True,Carrier proteins for active transport,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
32817420-f590-4cd7-8476-b1b79e7b2c7e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"All of these transporters can also transport small, uncharged organic molecules like glucose. These three types of carrier proteins are also in facilitated diffusion, but they do not require ATP to work in that process.",True,Carrier proteins for active transport,,,,
fe72eb4d-64d2-413d-b725-4ad9018b7aa3,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Primary active transport,False,Primary active transport,,,,
97aec11b-6149-42ee-9a3d-b5a5e62f8f59,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
97aec11b-6149-42ee-9a3d-b5a5e62f8f59,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
97aec11b-6149-42ee-9a3d-b5a5e62f8f59,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
97aec11b-6149-42ee-9a3d-b5a5e62f8f59,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,The primary active transport that functions with the active transport of sodium and potassium allows secondary active transport to occur. The second transport method is still active because it depends on using energy as does primary transport (figure 16.11).,True,Primary active transport,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
0cadb72c-f1b4-449f-885b-cc9cae99b7e8,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"One of the most important pumps in animal cells is the sodium-potassium pump (Na+-K+ ATPase), which maintains the electrochemical gradient (and the correct concentrations of Na+ and K+) in living cells. The sodium-potassium pump moves K+ into the cell while moving Na+ out at the same time, at a ratio of three Na+ for every two K+ ions moved in. The Na+-K+ ATPase exists in two forms, depending on its orientation to the cellʼs interior or exterior and its affinity for either sodium or potassium ions. The process consists of the following six steps.",True,Primary active transport,,,,
e6efd8e3-fb25-4202-92a7-a39bd986a817,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Secondary active transport (cotransport),False,Secondary active transport (cotransport),,,,
43287c27-4e27-4d2e-8e6a-68821a10d5fb,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Secondary active transport brings sodium ions, and possibly other compounds, into the cell. As sodium ion concentrations build up outside of the plasma membrane because of the primary active transport process, this creates an electrochemical gradient. If a channel protein exists and is open, the sodium ions will pull through the membrane. This movement transports other substances that can attach themselves to the transport protein through the membrane. Many amino acids, as well as glucose, enter a cell this way.",True,Secondary active transport (cotransport),,,,
04f8a324-e47d-4924-9fa0-611ce60c2403,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,16.3 References and resources,True,Secondary active transport (cotransport),,,,
3a725658-117d-4350-be98-a34e77b330ce,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,Text,False,Text,,,,
5db8ac40-8e23-4850-9224-3523bbc0525d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
5db8ac40-8e23-4850-9224-3523bbc0525d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
5db8ac40-8e23-4850-9224-3523bbc0525d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
5db8ac40-8e23-4850-9224-3523bbc0525d,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.9 Electrochemical gradients. 2021. https://archive.org/details/16.9_20210926. CC BY 4.0. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.9,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
b65bc84b-37c9-451f-b8bd-e7bc53d9776e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
b65bc84b-37c9-451f-b8bd-e7bc53d9776e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
b65bc84b-37c9-451f-b8bd-e7bc53d9776e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
b65bc84b-37c9-451f-b8bd-e7bc53d9776e,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Grey, Kindred, Figure 16.10 Different types of carrier proteins for active transport. 2021. https://archive.org/details/16.10. CC BY 4.0.",True,Text,Figure 16.10,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
414dc373-d30b-4651-aa9f-55ab1ab12584,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.3 Active Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
414dc373-d30b-4651-aa9f-55ab1ab12584,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.2 Passive Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
414dc373-d30b-4651-aa9f-55ab1ab12584,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16.1 Components and Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
414dc373-d30b-4651-aa9f-55ab1ab12584,https://pressbooks.lib.vt.edu/cellbio/,16. Plasma Membrane,https://pressbooks.lib.vt.edu/cellbio/chapter/plasma-membrane/,"Lieberman M, Peet A. Figure 16.11 Primary active transport. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 175 Figure 10.10 Active transport by Na+,K+-ATPase. 2017. Added Cell membrane detailed diagram blank by LadyofHats. Public domain. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 16.11,16. Plasma Membrane,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
18cc6256-46dc-4c76-8eba-9461c14b30da,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
18cc6256-46dc-4c76-8eba-9461c14b30da,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
18cc6256-46dc-4c76-8eba-9461c14b30da,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
18cc6256-46dc-4c76-8eba-9461c14b30da,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
b1dc2151-7c47-4be7-9461-8f2f5668070d,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,General characteristics:,False,General characteristics:,,,,
835fc60e-6eee-4668-af1e-5f2f7e5778ca,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Once at the intended location it will bind to its receptor, which can be intracellular or extracellular, to elicit a response.",True,General characteristics:,,,,
cadbf255-4284-4303-91d1-4ffd81ca5c12,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,This could be in the form of:,False,This could be in the form of:,,,,
f06a4a80-3829-44d0-84d1-35e8dc987901,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Finally, the signal can be terminated by:",False,"Finally, the signal can be terminated by:",,,,
1fc6e81e-45e3-47ba-b782-c12b2d669c1a,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The outcome of a signaling cascade is diverse. For example, elevated insulin may signal for increased uptake and storage of glucose (see section 15.3) or a signal may initiate apoptosis (see section 15.2).",True,"Finally, the signal can be terminated by:",,,,
16080df6-bcec-41cf-9739-b35b73febbc8,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Types of ligands,False,Types of ligands,,,,
23ce4cb4-a7ff-48ae-9b7e-2289cda29887,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,General G-protein-coupled receptor cascade,False,General G-protein-coupled receptor cascade,,,,
c69f7d88-963f-43a4-897f-56138a3a5d55,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"G-protein-coupled receptors (GPCR) can come in several different classes: Gαs, Gαi, and Gαq. Activation of a Gαs (activated by glucagon) will increase the second messenger cAMP, while both Gαi or Gαt cascades function to reduce cAMP, either through inhibition of adenylyl cyclase (also known as adenylate cyclase) or through activation of phosphodiesterase, respectively.",True,General G-protein-coupled receptor cascade,,,,
4f207cd9-a49f-4df1-9cbb-6924f30aceb5,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
4f207cd9-a49f-4df1-9cbb-6924f30aceb5,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
4f207cd9-a49f-4df1-9cbb-6924f30aceb5,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
4f207cd9-a49f-4df1-9cbb-6924f30aceb5,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
ee345500-bf40-46ce-8548-ec0633bac1b4,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Phosphatidylinositol-derived second messengers,False,Phosphatidylinositol-derived second messengers,,,,
0ef9d026-dd74-4257-8a9c-d956a9d8ad65,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
0ef9d026-dd74-4257-8a9c-d956a9d8ad65,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
0ef9d026-dd74-4257-8a9c-d956a9d8ad65,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
0ef9d026-dd74-4257-8a9c-d956a9d8ad65,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
8c84013d-f70e-4dfb-93db-8d1c7b3a8ca5,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The common membrane component, phosphatidylinositol (PI), can be phosphorylated (by any number of kinases) to form PI 4,5-bisphosphate. This molecule can undergo two different fates.",True,Phosphatidylinositol-derived second messengers,,,,
f6c6d4f5-af94-4dfd-b13f-14fdb087e9d6,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"This cascade will become important for calcium signaling, which is modulated through interactions of IP3 with the mitochondria.",True,Phosphatidylinositol-derived second messengers,,,,
321fbd6d-c0cb-42c9-9944-6330ed19145a,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Changes in intracellular calcium can alter membrane permeability through calcium-induced calcium release.,True,Phosphatidylinositol-derived second messengers,,,,
71d9f061-10b5-48f5-bbbc-74363bb037d2,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Receptor Tyrosine Kinase (RTK),False,Receptor Tyrosine Kinase (RTK),,,,
9a636f45-22df-47e7-95c9-e201fe8eb5a1,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,RTKs are in the cell membrane and typically function as a dimer.,True,Receptor Tyrosine Kinase (RTK),,,,
c0024496-a849-49c0-abce-e94a3b6e5ecb,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Two major cascades are activated downstream of insulin and other growth hormones:,True,Receptor Tyrosine Kinase (RTK),,,,
fb30a238-c26f-483e-860e-ee28bdcbe0e7,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Jak-STAT and serine threonine kinases,False,Jak-STAT and serine threonine kinases,,,,
b874d354-d9fc-44a6-969c-f2021202bef8,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Jak-STATs are also types of tyrosine kinases. The difference here is that these receptors lack autocatalytic abilities and require an intracellular kinase (Jak) to phosphorylate the transcription factor STAT. Jak-STAT signaling is most commonly associated with immune cell signaling.,True,Jak-STAT and serine threonine kinases,,,,
a5aad8ee-abfc-4f18-87db-cf309aff65a3,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Serine threonine kinase,False,Serine threonine kinase,,,,
4d30968e-7ddb-42b2-ac61-df75564afec1,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"This receptor family encompasses many of the growth factors for the body (EGF, VEGF, and TGF-β). These receptors usually form heterodimers, and the Type II receptor will autophosphorylate the Type I receptor upon ligand binding. These receptors have an autocatalytic domain that will phosphorylate and typically activate a transcription factor.",True,Serine threonine kinase,,,,
67cf019a-f4a4-487e-a3c6-927538f19842,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Intracellular receptors,False,Intracellular receptors,,,,
bc1aff8d-2b6c-47ae-ae88-615c84df7104,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Intracellular receptors bind hydrophobic chemical messengers such as steroid hormones. Binding of the intracellular receptor (which could be cytosolic or nuclear) usually elicits a transcriptional response. Cortisol is an example of a hormone that binds an intracellular receptor. It is released from the adrenal cortex and diffuses into the bloodstream attached to serum albumin and steroid hormone-binding globulin. After diffusing through the plasma membrane, it binds to the cortisol receptor (intracellular receptor) in the cytosol and forms a homodimer exposing a nuclear localization signal (NLS). Exposure of the NLS targets the complex to the nucleus.",True,Intracellular receptors,,,,
6d9a08f6-e781-4bdc-b609-58cc0d1563ae,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Intracellular receptors commonly have three domains:,False,Intracellular receptors commonly have three domains:,,,,
853647f9-4a5b-40eb-8cca-22b248334914,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Intracellular receptors will function as a transcriptional activator by binding specific DNA elements, altering transcription of downstream genes. The signal is terminated by the lowering of the concentration of the hormone.",True,Intracellular receptors commonly have three domains:,,,,
757655ad-19d0-4bd0-a662-30ea46d8656a,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,NO as a messenger,False,NO as a messenger,,,,
b0fff953-f683-4a4e-913d-f3121f7388e0,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Nitric oxide NO is a gas that also acts as a ligand. It is able to diffuse directly across the plasma membrane, and one of its roles is to interact with receptors in smooth muscle and induce relaxation of the tissue.",True,NO as a messenger,,,,
17707305-a984-4dcb-bce5-09f5714567b6,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"NO has a very short half-life and, therefore, only functions over short distances. It activates guanylyl cyclase to synthesize cGMP. This in turn results in smooth muscle relaxation.",True,NO as a messenger,,,,
c372d548-9d92-41a6-baf5-21da6998b388,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Nitroglycerin, a treatment for heart disease, acts by triggering the release of NO, which causes blood vessels to dilate (expand), thus restoring blood flow to the heart. NO has become better known recently because the pathway that it affects is targeted by prescription medications for erectile dysfunction, such as Viagra (erection involves dilated blood vessels).",True,NO as a messenger,,,,
24559bee-77d1-4eb8-8620-c28e5020d266,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,15.1 References and resources,True,NO as a messenger,,,,
e8322c26-db78-49a3-b8dd-b45b0c71ad1f,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 9: Cell Communication, Chapter 10: Cell Reproduction.",True,NO as a messenger,,,,
d4dfe93a-b6fb-4aff-ad3c-fcb46143b6ff,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 15: Cell Signaling and Signal Transduction.",True,NO as a messenger,,,,
758dc906-b92f-4b14-a2fc-aa133168286d,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 85, 208, 238.",True,NO as a messenger,,,,
8fa154cf-9bdc-4bea-ba2f-d6a9072b052c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
8fa154cf-9bdc-4bea-ba2f-d6a9072b052c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
8fa154cf-9bdc-4bea-ba2f-d6a9072b052c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
8fa154cf-9bdc-4bea-ba2f-d6a9072b052c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
3ffb2d6e-e84a-4137-95a2-6676b5d39c3a,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
3ffb2d6e-e84a-4137-95a2-6676b5d39c3a,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
3ffb2d6e-e84a-4137-95a2-6676b5d39c3a,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
3ffb2d6e-e84a-4137-95a2-6676b5d39c3a,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
bde69e23-b55d-4222-b4fc-e0461c672c16,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
bde69e23-b55d-4222-b4fc-e0461c672c16,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
bde69e23-b55d-4222-b4fc-e0461c672c16,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
bde69e23-b55d-4222-b4fc-e0461c672c16,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
3ec80053-f207-4b61-874e-ef509ab1e69c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
3ec80053-f207-4b61-874e-ef509ab1e69c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
3ec80053-f207-4b61-874e-ef509ab1e69c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
3ec80053-f207-4b61-874e-ef509ab1e69c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
94395013-298d-447a-9a66-58fbdd65edbd,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
94395013-298d-447a-9a66-58fbdd65edbd,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
94395013-298d-447a-9a66-58fbdd65edbd,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
94395013-298d-447a-9a66-58fbdd65edbd,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
6af147b6-1810-4da0-a36a-5796f8e0ea98,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,15.2 Apoptosis,True,NO as a messenger,,,,
6cad671f-c018-410c-9f66-a3fe485377fd,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Both cell proliferation and apoptosis (controlled/programed cell death) are decisive processes within a cell. Keep in mind, apoptosis is distinct from cell necrosis, in which cell death is usually attributable to physical or chemical damage and rapidly spontaneous; think explosion.",True,NO as a messenger,,,,
8706319e-1bbe-43b8-91c8-6f112a40d628,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Apoptosis is genetically programmed cell death, which leads to “tidy” breakdown and disposal of cells. Morphologically, apoptosis is characterized by shrinking of the cell, changes in the cell membrane (with the formation of small blebs known as “apoptotic bodies”), shrinking of the nucleus, chromatin condensation, and fragmentation of DNA. Macrophages and other phagocytic cells recognize this signal and remove apoptotic cells by phagocytosis without inflammatory phenomena developing. Apoptosis regulates the growth of normal tissues and removes unwanted cells in a controlled manner.",True,NO as a messenger,,,,
1e55f670-59fc-41c7-af6c-593280627676,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
1e55f670-59fc-41c7-af6c-593280627676,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
1e55f670-59fc-41c7-af6c-593280627676,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
1e55f670-59fc-41c7-af6c-593280627676,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
16cd9a25-1c90-4de4-8832-b5143a6003ec,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,procaspases,False,procaspases,,,,
4805349c-c1ff-4126-88bc-aa4b65d02a35,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,laminins,False,laminins,,,,
2d2ea78c-4bff-4582-8cdf-60acafdb2d5c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,snRP,False,snRP,,,,
372b7621-b2de-44d5-a452-8bcd90d758ca,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,DNAses,False,DNAses,,,,
451ff452-c375-4f9a-bd47-946edb050dd7,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The extrinsic pathway for apoptosis is triggered on the cell surface by ligands that bind to receptors of the tumor necrosis factor family (TNFR, “death receptors”). These include Fas receptors, which are present on the plasma membrane of most cells in the body. When Fas ligands bind to a cellʼs Fas receptors, trimerization of the receptors takes place via the adapter protein FADD (“Fas-associated death domain”), which activates the initiator caspases 8 and 10 inside the cell, setting in motion the apoptotic process.",True,DNAses,,,,
13ab2e8e-1195-4f1b-bbd0-6e806d9cc3c5,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,TNFR,False,TNFR,,,,
6df11538-e332-46aa-8ffa-d9b1ad129880,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,cellʼs,False,cellʼs,,,,
ce96461f-328f-419d-b156-d5d0a8bf835c,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,FADD,False,FADD,,,,
a9781994-89af-472d-bcff-7f0e2db51b1f,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,caspases,False,caspases,,,,
ece97080-3152-4b73-a754-86cb2cd01e04,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The intrinsic, mitochondrial pathway is triggered by genotoxic (DNA damage) or oxidative stress. Aided by Bcl proteins, chemical stress makes the outer mitochondrial membrane leaky. As a result, mitochondrial proteins reach the cytoplasm. Cytochrome c in particular then triggers the caspase cascade by binding to the adapter protein Apaf1 and promoting formation of an apoptosome, a wheel-shaped heptamer that recruits initiator procaspase 9 and activates it to caspase 9.",True,caspases,,,,
c19d8db4-e9b5-44c0-8d6b-ed28366b30da,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The Bcl protein family not only includes proapoptotic proteins (Bax, Bak, and Bim) but also proteins that inhibit apoptosis (including Bcl2). Extracellular growth factors ensure inactivation of Bad or replication of Bcl 2, thus preventing apoptosis.",True,caspases,,,,
a20a473d-9d5e-4284-95cc-4a9b3e94c271,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,15.2 References and resources,True,caspases,,,,
8c57fb9e-9591-45f7-9097-a335ab558014,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
8c57fb9e-9591-45f7-9097-a335ab558014,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
8c57fb9e-9591-45f7-9097-a335ab558014,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
8c57fb9e-9591-45f7-9097-a335ab558014,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
9aa89210-9ac5-4c00-a2b3-a64d8b6be901,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,15.3 Membrane Potential,True,caspases,,,,
c4397bc4-7135-4bfd-b860-b813ae1bf1f7,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
c4397bc4-7135-4bfd-b860-b813ae1bf1f7,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
c4397bc4-7135-4bfd-b860-b813ae1bf1f7,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
c4397bc4-7135-4bfd-b860-b813ae1bf1f7,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
9b44f4c4-8502-4c26-8e9e-1093f6595ba0,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,The action potential,False,The action potential,,,,
0a9d8ffe-5a4e-4010-ac4b-c407dd229849,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Resting membrane potential describes the steady state of the cell, which is a dynamic process that is balanced by ion leakage and ion pumping. Without any outside influence, it will not change. To get an electrical signal started, the membrane potential has to change (summary in figures 15.8 and 15.9).",True,The action potential,,,,
7dcf946c-f1ae-470d-9fa8-b7055e391d7d,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,15.3 References and resources,True,The action potential,,,,
7b467edb-d844-4d3e-861d-28b438fdc926,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,Text,False,Text,,,,
faca939c-e608-40f0-8044-8a608583e085,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
faca939c-e608-40f0-8044-8a608583e085,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
faca939c-e608-40f0-8044-8a608583e085,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
faca939c-e608-40f0-8044-8a608583e085,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
9f4888c0-f11f-42f3-ac6b-d0a9c7f89e5d,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
9f4888c0-f11f-42f3-ac6b-d0a9c7f89e5d,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
9f4888c0-f11f-42f3-ac6b-d0a9c7f89e5d,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
9f4888c0-f11f-42f3-ac6b-d0a9c7f89e5d,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
baf260bc-ef35-4eb2-9c96-302ff06b1148,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
baf260bc-ef35-4eb2-9c96-302ff06b1148,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
baf260bc-ef35-4eb2-9c96-302ff06b1148,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
baf260bc-ef35-4eb2-9c96-302ff06b1148,https://pressbooks.lib.vt.edu/cellbio/,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-3,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
547a7d66-d5ce-4585-a3a3-66b364ca6b44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
547a7d66-d5ce-4585-a3a3-66b364ca6b44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
547a7d66-d5ce-4585-a3a3-66b364ca6b44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
547a7d66-d5ce-4585-a3a3-66b364ca6b44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
ae9134a0-3abe-467b-88d4-1c858bb1e560,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,General characteristics:,False,General characteristics:,,,,
ebdd48fb-375a-4e6f-8dc3-9f7db96988bf,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Once at the intended location it will bind to its receptor, which can be intracellular or extracellular, to elicit a response.",True,General characteristics:,,,,
273a6a50-8c02-4c47-a0c7-8ed36a6d4ee4,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,This could be in the form of:,False,This could be in the form of:,,,,
4ba45ffd-1bf1-4836-9096-a63323ed829a,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Finally, the signal can be terminated by:",False,"Finally, the signal can be terminated by:",,,,
93c93074-3816-4163-b818-595f7871a2ad,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The outcome of a signaling cascade is diverse. For example, elevated insulin may signal for increased uptake and storage of glucose (see section 15.3) or a signal may initiate apoptosis (see section 15.2).",True,"Finally, the signal can be terminated by:",,,,
5cdf6897-49d6-4813-bef9-2b9816acdd4a,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Types of ligands,False,Types of ligands,,,,
4f07d543-ee6c-4e39-ae6b-f66f76670359,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,General G-protein-coupled receptor cascade,False,General G-protein-coupled receptor cascade,,,,
04336b41-af3e-4e14-8a44-c9f131fd0cb9,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"G-protein-coupled receptors (GPCR) can come in several different classes: Gαs, Gαi, and Gαq. Activation of a Gαs (activated by glucagon) will increase the second messenger cAMP, while both Gαi or Gαt cascades function to reduce cAMP, either through inhibition of adenylyl cyclase (also known as adenylate cyclase) or through activation of phosphodiesterase, respectively.",True,General G-protein-coupled receptor cascade,,,,
bcbcd976-b5cc-46e9-9e42-f1bc2f25a47f,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
bcbcd976-b5cc-46e9-9e42-f1bc2f25a47f,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
bcbcd976-b5cc-46e9-9e42-f1bc2f25a47f,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
bcbcd976-b5cc-46e9-9e42-f1bc2f25a47f,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
a80eb327-4e35-4d10-a14c-457269e4e2ec,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Phosphatidylinositol-derived second messengers,False,Phosphatidylinositol-derived second messengers,,,,
f7cc8965-759b-48f5-81a6-5d5756114bfa,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
f7cc8965-759b-48f5-81a6-5d5756114bfa,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
f7cc8965-759b-48f5-81a6-5d5756114bfa,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
f7cc8965-759b-48f5-81a6-5d5756114bfa,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
a50ce96e-3cb3-4112-b596-3c3fc6486b2e,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The common membrane component, phosphatidylinositol (PI), can be phosphorylated (by any number of kinases) to form PI 4,5-bisphosphate. This molecule can undergo two different fates.",True,Phosphatidylinositol-derived second messengers,,,,
4faa3edd-1c30-4f3c-b0c6-811ba49c3941,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"This cascade will become important for calcium signaling, which is modulated through interactions of IP3 with the mitochondria.",True,Phosphatidylinositol-derived second messengers,,,,
133b4836-1f6b-4257-9e25-e30b0fe8da24,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Changes in intracellular calcium can alter membrane permeability through calcium-induced calcium release.,True,Phosphatidylinositol-derived second messengers,,,,
13675493-e407-49f8-b046-260c11cc3d36,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Receptor Tyrosine Kinase (RTK),False,Receptor Tyrosine Kinase (RTK),,,,
3ee91153-cc7c-4647-9328-46649be0742c,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,RTKs are in the cell membrane and typically function as a dimer.,True,Receptor Tyrosine Kinase (RTK),,,,
69bc7ad7-412b-4dc1-aab0-e3f2f8b0ee2b,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Two major cascades are activated downstream of insulin and other growth hormones:,True,Receptor Tyrosine Kinase (RTK),,,,
32ac696c-5a75-4f34-b588-6cb348c069b8,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Jak-STAT and serine threonine kinases,False,Jak-STAT and serine threonine kinases,,,,
03a79811-08a1-4a2e-a069-8f123a2e5f70,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Jak-STATs are also types of tyrosine kinases. The difference here is that these receptors lack autocatalytic abilities and require an intracellular kinase (Jak) to phosphorylate the transcription factor STAT. Jak-STAT signaling is most commonly associated with immune cell signaling.,True,Jak-STAT and serine threonine kinases,,,,
e58a4860-7b5a-4501-a7cc-bc727abd66f3,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Serine threonine kinase,False,Serine threonine kinase,,,,
3d7995dc-8d3f-4238-b86e-3534993eacd4,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"This receptor family encompasses many of the growth factors for the body (EGF, VEGF, and TGF-β). These receptors usually form heterodimers, and the Type II receptor will autophosphorylate the Type I receptor upon ligand binding. These receptors have an autocatalytic domain that will phosphorylate and typically activate a transcription factor.",True,Serine threonine kinase,,,,
b91651b7-a71b-4c48-a97a-22582644acae,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Intracellular receptors,False,Intracellular receptors,,,,
715a2468-317d-43f2-8648-7f8fbe5345cb,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Intracellular receptors bind hydrophobic chemical messengers such as steroid hormones. Binding of the intracellular receptor (which could be cytosolic or nuclear) usually elicits a transcriptional response. Cortisol is an example of a hormone that binds an intracellular receptor. It is released from the adrenal cortex and diffuses into the bloodstream attached to serum albumin and steroid hormone-binding globulin. After diffusing through the plasma membrane, it binds to the cortisol receptor (intracellular receptor) in the cytosol and forms a homodimer exposing a nuclear localization signal (NLS). Exposure of the NLS targets the complex to the nucleus.",True,Intracellular receptors,,,,
99798044-da6a-457e-b474-e7f94d2f392b,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Intracellular receptors commonly have three domains:,False,Intracellular receptors commonly have three domains:,,,,
8387646f-a15d-4fe8-93f7-e7ae067366d5,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Intracellular receptors will function as a transcriptional activator by binding specific DNA elements, altering transcription of downstream genes. The signal is terminated by the lowering of the concentration of the hormone.",True,Intracellular receptors commonly have three domains:,,,,
e7576511-665e-46c2-a4f0-41376c07d831,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,NO as a messenger,False,NO as a messenger,,,,
326bd23f-c31b-43e8-aedc-d9727a18a908,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Nitric oxide NO is a gas that also acts as a ligand. It is able to diffuse directly across the plasma membrane, and one of its roles is to interact with receptors in smooth muscle and induce relaxation of the tissue.",True,NO as a messenger,,,,
6e2b7b85-0675-45d3-8256-a36478bc3981,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"NO has a very short half-life and, therefore, only functions over short distances. It activates guanylyl cyclase to synthesize cGMP. This in turn results in smooth muscle relaxation.",True,NO as a messenger,,,,
b86013e8-d337-40de-9a34-0c585709fcc6,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Nitroglycerin, a treatment for heart disease, acts by triggering the release of NO, which causes blood vessels to dilate (expand), thus restoring blood flow to the heart. NO has become better known recently because the pathway that it affects is targeted by prescription medications for erectile dysfunction, such as Viagra (erection involves dilated blood vessels).",True,NO as a messenger,,,,
4e565732-50cc-4450-8539-81bddee6fc5e,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,15.1 References and resources,True,NO as a messenger,,,,
9f208f94-af99-481d-ae5a-98e586c11157,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 9: Cell Communication, Chapter 10: Cell Reproduction.",True,NO as a messenger,,,,
c06d256b-b9ee-4c5e-9b84-f63a28a2e0e4,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 15: Cell Signaling and Signal Transduction.",True,NO as a messenger,,,,
6fc83ea7-d0db-4807-8682-2c1a7618b63c,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 85, 208, 238.",True,NO as a messenger,,,,
5c7d1161-7c04-4050-a34c-f1a8af67b460,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
5c7d1161-7c04-4050-a34c-f1a8af67b460,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
5c7d1161-7c04-4050-a34c-f1a8af67b460,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
5c7d1161-7c04-4050-a34c-f1a8af67b460,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
5d46c124-3616-48ec-90f7-b90eb315c6d1,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
5d46c124-3616-48ec-90f7-b90eb315c6d1,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
5d46c124-3616-48ec-90f7-b90eb315c6d1,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
5d46c124-3616-48ec-90f7-b90eb315c6d1,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
ca46ee14-350f-4e39-b321-837659bfa852,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
ca46ee14-350f-4e39-b321-837659bfa852,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
ca46ee14-350f-4e39-b321-837659bfa852,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
ca46ee14-350f-4e39-b321-837659bfa852,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
0a30c9a1-ff80-48c2-bd1c-4431ebc0cf44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
0a30c9a1-ff80-48c2-bd1c-4431ebc0cf44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
0a30c9a1-ff80-48c2-bd1c-4431ebc0cf44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
0a30c9a1-ff80-48c2-bd1c-4431ebc0cf44,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
f4a211df-6df8-49e0-b701-d35b25353552,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
f4a211df-6df8-49e0-b701-d35b25353552,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
f4a211df-6df8-49e0-b701-d35b25353552,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
f4a211df-6df8-49e0-b701-d35b25353552,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
d60ae172-2fb8-46bb-ba9d-f9fdf5d87f65,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,15.2 Apoptosis,True,NO as a messenger,,,,
5b912fe5-800e-432b-8388-3b253438ae0b,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Both cell proliferation and apoptosis (controlled/programed cell death) are decisive processes within a cell. Keep in mind, apoptosis is distinct from cell necrosis, in which cell death is usually attributable to physical or chemical damage and rapidly spontaneous; think explosion.",True,NO as a messenger,,,,
ee0c3065-bfb8-4530-b993-03dc41d50d10,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Apoptosis is genetically programmed cell death, which leads to “tidy” breakdown and disposal of cells. Morphologically, apoptosis is characterized by shrinking of the cell, changes in the cell membrane (with the formation of small blebs known as “apoptotic bodies”), shrinking of the nucleus, chromatin condensation, and fragmentation of DNA. Macrophages and other phagocytic cells recognize this signal and remove apoptotic cells by phagocytosis without inflammatory phenomena developing. Apoptosis regulates the growth of normal tissues and removes unwanted cells in a controlled manner.",True,NO as a messenger,,,,
caa067ec-cb55-4aa4-8121-b0ca78e410b8,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
caa067ec-cb55-4aa4-8121-b0ca78e410b8,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
caa067ec-cb55-4aa4-8121-b0ca78e410b8,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
caa067ec-cb55-4aa4-8121-b0ca78e410b8,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
fcc9047a-4918-4e22-9108-840ae0831d12,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,procaspases,False,procaspases,,,,
64dddd80-e5e2-42ed-a817-b25deaf1fc72,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,laminins,False,laminins,,,,
25394c24-2863-45e1-86fd-859753159fe1,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,snRP,False,snRP,,,,
7c89d555-0026-4cd8-8edf-685bc21bca42,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,DNAses,False,DNAses,,,,
d0002603-1a40-4cc5-ac95-50658a8cff1f,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The extrinsic pathway for apoptosis is triggered on the cell surface by ligands that bind to receptors of the tumor necrosis factor family (TNFR, “death receptors”). These include Fas receptors, which are present on the plasma membrane of most cells in the body. When Fas ligands bind to a cellʼs Fas receptors, trimerization of the receptors takes place via the adapter protein FADD (“Fas-associated death domain”), which activates the initiator caspases 8 and 10 inside the cell, setting in motion the apoptotic process.",True,DNAses,,,,
f83e8ede-9d66-4673-8dda-ad42ba807d8d,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,TNFR,False,TNFR,,,,
1e68ac84-8b11-4ac9-a51e-2a274d828b1f,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,cellʼs,False,cellʼs,,,,
3d471ca4-a36a-4652-8d1d-0533ba497902,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,FADD,False,FADD,,,,
878c74ad-a54c-4be8-9d08-1be5a2bab18c,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,caspases,False,caspases,,,,
bce98479-4517-4a2a-ac61-db487a3efec4,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The intrinsic, mitochondrial pathway is triggered by genotoxic (DNA damage) or oxidative stress. Aided by Bcl proteins, chemical stress makes the outer mitochondrial membrane leaky. As a result, mitochondrial proteins reach the cytoplasm. Cytochrome c in particular then triggers the caspase cascade by binding to the adapter protein Apaf1 and promoting formation of an apoptosome, a wheel-shaped heptamer that recruits initiator procaspase 9 and activates it to caspase 9.",True,caspases,,,,
ad123478-1aa3-40fb-9618-67372a39a05c,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The Bcl protein family not only includes proapoptotic proteins (Bax, Bak, and Bim) but also proteins that inhibit apoptosis (including Bcl2). Extracellular growth factors ensure inactivation of Bad or replication of Bcl 2, thus preventing apoptosis.",True,caspases,,,,
815f2d2c-54e2-48c9-85d8-32fcdd1786d7,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,15.2 References and resources,True,caspases,,,,
bdbf2eff-ae3d-4719-b167-e5dd157892ef,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
bdbf2eff-ae3d-4719-b167-e5dd157892ef,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
bdbf2eff-ae3d-4719-b167-e5dd157892ef,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
bdbf2eff-ae3d-4719-b167-e5dd157892ef,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
62bf5440-7127-4a7c-8161-7cc67cb8d41d,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,15.3 Membrane Potential,True,caspases,,,,
cf5c282c-c660-4436-95bc-9ee90af27fdc,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
cf5c282c-c660-4436-95bc-9ee90af27fdc,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
cf5c282c-c660-4436-95bc-9ee90af27fdc,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
cf5c282c-c660-4436-95bc-9ee90af27fdc,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
4e70b488-4f4b-4d5d-add6-222c6ae89089,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,The action potential,False,The action potential,,,,
657983e3-cf45-4f3c-989e-8e0ee48adf7d,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Resting membrane potential describes the steady state of the cell, which is a dynamic process that is balanced by ion leakage and ion pumping. Without any outside influence, it will not change. To get an electrical signal started, the membrane potential has to change (summary in figures 15.8 and 15.9).",True,The action potential,,,,
bd7e58bd-f22c-41f3-837b-09d7c677ea18,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,15.3 References and resources,True,The action potential,,,,
4382332a-a755-4ee6-9868-7e1635aa6026,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,Text,False,Text,,,,
e5123648-741b-40a4-8011-a7d1a29f02eb,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
e5123648-741b-40a4-8011-a7d1a29f02eb,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
e5123648-741b-40a4-8011-a7d1a29f02eb,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
e5123648-741b-40a4-8011-a7d1a29f02eb,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
30ea499f-7a0e-402f-b83f-c45da34b8c02,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
30ea499f-7a0e-402f-b83f-c45da34b8c02,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
30ea499f-7a0e-402f-b83f-c45da34b8c02,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
30ea499f-7a0e-402f-b83f-c45da34b8c02,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
3352dfc5-ec70-47f0-8869-042809473477,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
3352dfc5-ec70-47f0-8869-042809473477,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
3352dfc5-ec70-47f0-8869-042809473477,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
3352dfc5-ec70-47f0-8869-042809473477,https://pressbooks.lib.vt.edu/cellbio/,15.2 Apoptosis,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-2,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
2ce7f122-6025-44a8-b1c3-45eb612a5998,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
2ce7f122-6025-44a8-b1c3-45eb612a5998,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
2ce7f122-6025-44a8-b1c3-45eb612a5998,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
2ce7f122-6025-44a8-b1c3-45eb612a5998,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
120c285c-0fe2-4c13-8389-ebcc251e426a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,General characteristics:,False,General characteristics:,,,,
ad022063-67a3-474f-810b-c2b2b744b52c,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Once at the intended location it will bind to its receptor, which can be intracellular or extracellular, to elicit a response.",True,General characteristics:,,,,
d6416dc2-1577-4722-9fff-73d2b41c8653,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,This could be in the form of:,False,This could be in the form of:,,,,
390e83bc-da0b-4fd5-a786-fccb3fe85785,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Finally, the signal can be terminated by:",False,"Finally, the signal can be terminated by:",,,,
b650d6c2-d866-411c-8a3d-a284faa93fd1,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The outcome of a signaling cascade is diverse. For example, elevated insulin may signal for increased uptake and storage of glucose (see section 15.3) or a signal may initiate apoptosis (see section 15.2).",True,"Finally, the signal can be terminated by:",,,,
4fe20751-bb81-4f85-80f9-704bfcce1fbf,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Types of ligands,False,Types of ligands,,,,
d48c90a1-eb56-4650-97bc-9e370990c32a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,General G-protein-coupled receptor cascade,False,General G-protein-coupled receptor cascade,,,,
822d99da-5ade-4ee0-924b-2810e65a2ce2,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"G-protein-coupled receptors (GPCR) can come in several different classes: Gαs, Gαi, and Gαq. Activation of a Gαs (activated by glucagon) will increase the second messenger cAMP, while both Gαi or Gαt cascades function to reduce cAMP, either through inhibition of adenylyl cyclase (also known as adenylate cyclase) or through activation of phosphodiesterase, respectively.",True,General G-protein-coupled receptor cascade,,,,
07e3f620-ff96-4caa-b609-55b55a34e118,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
07e3f620-ff96-4caa-b609-55b55a34e118,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
07e3f620-ff96-4caa-b609-55b55a34e118,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
07e3f620-ff96-4caa-b609-55b55a34e118,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
dc4a3f3c-cf46-49d8-b4fb-d394ccdc8c70,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Phosphatidylinositol-derived second messengers,False,Phosphatidylinositol-derived second messengers,,,,
a804a4be-448b-44bb-96ea-f7e5fa848596,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
a804a4be-448b-44bb-96ea-f7e5fa848596,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
a804a4be-448b-44bb-96ea-f7e5fa848596,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
a804a4be-448b-44bb-96ea-f7e5fa848596,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
003d8798-22c8-4677-b02d-9be2cf3bfdf8,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The common membrane component, phosphatidylinositol (PI), can be phosphorylated (by any number of kinases) to form PI 4,5-bisphosphate. This molecule can undergo two different fates.",True,Phosphatidylinositol-derived second messengers,,,,
b9e4a604-c759-455d-aced-af9e7dda0ced,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"This cascade will become important for calcium signaling, which is modulated through interactions of IP3 with the mitochondria.",True,Phosphatidylinositol-derived second messengers,,,,
6555c8b2-93eb-460b-bcdf-0e84f719a954,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Changes in intracellular calcium can alter membrane permeability through calcium-induced calcium release.,True,Phosphatidylinositol-derived second messengers,,,,
c3f2103c-0116-44bf-a33a-636bf40ed1fd,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Receptor Tyrosine Kinase (RTK),False,Receptor Tyrosine Kinase (RTK),,,,
271e7fb5-e966-48a3-92a1-1c7c6adcbb94,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,RTKs are in the cell membrane and typically function as a dimer.,True,Receptor Tyrosine Kinase (RTK),,,,
0aa26184-9617-4cc8-915f-be18bb451a7c,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Two major cascades are activated downstream of insulin and other growth hormones:,True,Receptor Tyrosine Kinase (RTK),,,,
31b74b92-13a3-4bf4-a575-3bb1db36249b,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Jak-STAT and serine threonine kinases,False,Jak-STAT and serine threonine kinases,,,,
0fed9e69-e753-4833-9af7-5e4b4d5dac9a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Jak-STATs are also types of tyrosine kinases. The difference here is that these receptors lack autocatalytic abilities and require an intracellular kinase (Jak) to phosphorylate the transcription factor STAT. Jak-STAT signaling is most commonly associated with immune cell signaling.,True,Jak-STAT and serine threonine kinases,,,,
cb0812ac-609a-4234-8e10-ea602493fdab,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Serine threonine kinase,False,Serine threonine kinase,,,,
1609dd1c-ae8b-42db-984d-8fb6c4775f34,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"This receptor family encompasses many of the growth factors for the body (EGF, VEGF, and TGF-β). These receptors usually form heterodimers, and the Type II receptor will autophosphorylate the Type I receptor upon ligand binding. These receptors have an autocatalytic domain that will phosphorylate and typically activate a transcription factor.",True,Serine threonine kinase,,,,
1e34847e-6086-44bd-a79b-adb7832fc7c4,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Intracellular receptors,False,Intracellular receptors,,,,
8f6a7cd0-faa7-47bf-9709-689c7ed8ecc8,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Intracellular receptors bind hydrophobic chemical messengers such as steroid hormones. Binding of the intracellular receptor (which could be cytosolic or nuclear) usually elicits a transcriptional response. Cortisol is an example of a hormone that binds an intracellular receptor. It is released from the adrenal cortex and diffuses into the bloodstream attached to serum albumin and steroid hormone-binding globulin. After diffusing through the plasma membrane, it binds to the cortisol receptor (intracellular receptor) in the cytosol and forms a homodimer exposing a nuclear localization signal (NLS). Exposure of the NLS targets the complex to the nucleus.",True,Intracellular receptors,,,,
f4010749-76ac-4fd4-98f8-7736533cb194,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Intracellular receptors commonly have three domains:,False,Intracellular receptors commonly have three domains:,,,,
15b6b9aa-4071-41e8-ad78-37ce994d37c1,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Intracellular receptors will function as a transcriptional activator by binding specific DNA elements, altering transcription of downstream genes. The signal is terminated by the lowering of the concentration of the hormone.",True,Intracellular receptors commonly have three domains:,,,,
f0390f72-0f8a-4a59-b861-5f0810408ec8,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,NO as a messenger,False,NO as a messenger,,,,
d9ba8464-5744-4b3d-84a6-c228c7763343,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Nitric oxide NO is a gas that also acts as a ligand. It is able to diffuse directly across the plasma membrane, and one of its roles is to interact with receptors in smooth muscle and induce relaxation of the tissue.",True,NO as a messenger,,,,
7232c947-8441-4742-a61b-c9b5c7111554,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"NO has a very short half-life and, therefore, only functions over short distances. It activates guanylyl cyclase to synthesize cGMP. This in turn results in smooth muscle relaxation.",True,NO as a messenger,,,,
06662992-676f-4edf-9226-27d738355be2,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Nitroglycerin, a treatment for heart disease, acts by triggering the release of NO, which causes blood vessels to dilate (expand), thus restoring blood flow to the heart. NO has become better known recently because the pathway that it affects is targeted by prescription medications for erectile dysfunction, such as Viagra (erection involves dilated blood vessels).",True,NO as a messenger,,,,
ba818057-f948-4717-b1a8-e40ed4742252,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,15.1 References and resources,True,NO as a messenger,,,,
2ec54f70-dc66-4b93-a110-ae4c4ee9a4a7,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 9: Cell Communication, Chapter 10: Cell Reproduction.",True,NO as a messenger,,,,
8af3add5-df4e-47dd-b95e-fa17d63e4809,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 15: Cell Signaling and Signal Transduction.",True,NO as a messenger,,,,
78aac4ec-9ea1-42e9-bc4f-8da944caac82,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 85, 208, 238.",True,NO as a messenger,,,,
f92cc2c3-bdf3-4af0-86d1-bddf96d2e3ae,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
f92cc2c3-bdf3-4af0-86d1-bddf96d2e3ae,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
f92cc2c3-bdf3-4af0-86d1-bddf96d2e3ae,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
f92cc2c3-bdf3-4af0-86d1-bddf96d2e3ae,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
b3f6a526-34b1-41de-9dfa-dc2d0ac17a68,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
b3f6a526-34b1-41de-9dfa-dc2d0ac17a68,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
b3f6a526-34b1-41de-9dfa-dc2d0ac17a68,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
b3f6a526-34b1-41de-9dfa-dc2d0ac17a68,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
ffe41c71-1cd0-4119-af90-046abd405bb7,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
ffe41c71-1cd0-4119-af90-046abd405bb7,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
ffe41c71-1cd0-4119-af90-046abd405bb7,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
ffe41c71-1cd0-4119-af90-046abd405bb7,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
6c819427-7b6c-41e5-ac59-e0941e6ac128,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
6c819427-7b6c-41e5-ac59-e0941e6ac128,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
6c819427-7b6c-41e5-ac59-e0941e6ac128,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
6c819427-7b6c-41e5-ac59-e0941e6ac128,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
ae8f51f4-7acd-44df-a598-be0ecf56db2a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
ae8f51f4-7acd-44df-a598-be0ecf56db2a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
ae8f51f4-7acd-44df-a598-be0ecf56db2a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
ae8f51f4-7acd-44df-a598-be0ecf56db2a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
728f0ae0-9d0c-4a40-914b-2a2c0c4bbc73,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,15.2 Apoptosis,True,NO as a messenger,,,,
e94d64b9-118d-440f-b125-f8224fad11f4,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Both cell proliferation and apoptosis (controlled/programed cell death) are decisive processes within a cell. Keep in mind, apoptosis is distinct from cell necrosis, in which cell death is usually attributable to physical or chemical damage and rapidly spontaneous; think explosion.",True,NO as a messenger,,,,
77d5a08c-8b08-4e24-9dbe-07569f27e68c,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Apoptosis is genetically programmed cell death, which leads to “tidy” breakdown and disposal of cells. Morphologically, apoptosis is characterized by shrinking of the cell, changes in the cell membrane (with the formation of small blebs known as “apoptotic bodies”), shrinking of the nucleus, chromatin condensation, and fragmentation of DNA. Macrophages and other phagocytic cells recognize this signal and remove apoptotic cells by phagocytosis without inflammatory phenomena developing. Apoptosis regulates the growth of normal tissues and removes unwanted cells in a controlled manner.",True,NO as a messenger,,,,
537be130-9fbb-42d7-aae2-0c80ec121bcb,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
537be130-9fbb-42d7-aae2-0c80ec121bcb,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
537be130-9fbb-42d7-aae2-0c80ec121bcb,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
537be130-9fbb-42d7-aae2-0c80ec121bcb,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
88c5c6ed-4690-4aa4-ba55-a5caea2c9eaa,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,procaspases,False,procaspases,,,,
a1fcdb76-6ede-4f77-87e7-bd46d351bc94,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,laminins,False,laminins,,,,
dabbbe53-be19-4b18-9008-b2d25a2f1592,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,snRP,False,snRP,,,,
2f2a0f7b-2d4b-4a75-82eb-69d50a7f7dc8,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,DNAses,False,DNAses,,,,
3345344f-d053-4036-a9f2-6cc9350e4286,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The extrinsic pathway for apoptosis is triggered on the cell surface by ligands that bind to receptors of the tumor necrosis factor family (TNFR, “death receptors”). These include Fas receptors, which are present on the plasma membrane of most cells in the body. When Fas ligands bind to a cellʼs Fas receptors, trimerization of the receptors takes place via the adapter protein FADD (“Fas-associated death domain”), which activates the initiator caspases 8 and 10 inside the cell, setting in motion the apoptotic process.",True,DNAses,,,,
e67f54b9-ef08-41a9-867c-0154b5152682,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,TNFR,False,TNFR,,,,
b9602b2c-c6dc-4be5-8a58-3dc7ebeed7e0,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,cellʼs,False,cellʼs,,,,
0d55e331-1d94-4f9b-9470-0fe5d47d22eb,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,FADD,False,FADD,,,,
7d5710c6-d20e-43ed-9a74-00d889d4e8a7,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,caspases,False,caspases,,,,
9ee28302-a521-4f39-b658-33ac237b9c45,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The intrinsic, mitochondrial pathway is triggered by genotoxic (DNA damage) or oxidative stress. Aided by Bcl proteins, chemical stress makes the outer mitochondrial membrane leaky. As a result, mitochondrial proteins reach the cytoplasm. Cytochrome c in particular then triggers the caspase cascade by binding to the adapter protein Apaf1 and promoting formation of an apoptosome, a wheel-shaped heptamer that recruits initiator procaspase 9 and activates it to caspase 9.",True,caspases,,,,
2db995d0-e43e-47ec-8c48-fad0196b557a,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The Bcl protein family not only includes proapoptotic proteins (Bax, Bak, and Bim) but also proteins that inhibit apoptosis (including Bcl2). Extracellular growth factors ensure inactivation of Bad or replication of Bcl 2, thus preventing apoptosis.",True,caspases,,,,
b0500e4f-6023-4e4a-8e44-96eab37acb0d,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,15.2 References and resources,True,caspases,,,,
8003a9d9-0d2e-4b0a-9f5c-94d2c149aa5c,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
8003a9d9-0d2e-4b0a-9f5c-94d2c149aa5c,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
8003a9d9-0d2e-4b0a-9f5c-94d2c149aa5c,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
8003a9d9-0d2e-4b0a-9f5c-94d2c149aa5c,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
849b875e-e3d4-4766-b53b-2251a140d474,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,15.3 Membrane Potential,True,caspases,,,,
97436b9a-925d-463e-b341-dd9aebe19ce1,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
97436b9a-925d-463e-b341-dd9aebe19ce1,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
97436b9a-925d-463e-b341-dd9aebe19ce1,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
97436b9a-925d-463e-b341-dd9aebe19ce1,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
ae99919d-fa39-4bef-a9d7-1a340434ed73,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,The action potential,False,The action potential,,,,
11333785-f659-426a-8e20-e7b8a1215630,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Resting membrane potential describes the steady state of the cell, which is a dynamic process that is balanced by ion leakage and ion pumping. Without any outside influence, it will not change. To get an electrical signal started, the membrane potential has to change (summary in figures 15.8 and 15.9).",True,The action potential,,,,
255f6a11-2b41-49b8-9b0f-a2f7ea0c1e65,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,15.3 References and resources,True,The action potential,,,,
dcf66f2d-5826-444a-bdc0-1a4b08488841,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,Text,False,Text,,,,
39cc49c3-b997-433e-96b2-826826bcbdfa,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
39cc49c3-b997-433e-96b2-826826bcbdfa,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
39cc49c3-b997-433e-96b2-826826bcbdfa,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
39cc49c3-b997-433e-96b2-826826bcbdfa,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
4e295c56-70a7-42c3-8336-d9a7c9f287ba,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
4e295c56-70a7-42c3-8336-d9a7c9f287ba,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
4e295c56-70a7-42c3-8336-d9a7c9f287ba,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
4e295c56-70a7-42c3-8336-d9a7c9f287ba,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
c87d5616-5997-4fd3-9b28-9cc1bdb97654,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
c87d5616-5997-4fd3-9b28-9cc1bdb97654,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
c87d5616-5997-4fd3-9b28-9cc1bdb97654,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
c87d5616-5997-4fd3-9b28-9cc1bdb97654,https://pressbooks.lib.vt.edu/cellbio/,15.1 Cell Communication,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/#chapter-98-section-1,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
23226bd3-2b41-4814-b5ae-982e5f344af4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
23226bd3-2b41-4814-b5ae-982e5f344af4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
23226bd3-2b41-4814-b5ae-982e5f344af4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
23226bd3-2b41-4814-b5ae-982e5f344af4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Generally speaking, it uses various communication modalities to sense and respond to neighboring cells and environmental cues, which can be categorized into the following types of communication (figure 15.1):",True,Text,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
bb612050-e24f-47bc-91e4-d32cfddaf9de,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,General characteristics:,False,General characteristics:,,,,
a7cb94a6-c4c4-44d3-867f-f609cf4b7178,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Once at the intended location it will bind to its receptor, which can be intracellular or extracellular, to elicit a response.",True,General characteristics:,,,,
57e6fd00-abda-421e-ba7a-3a2842534290,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,This could be in the form of:,False,This could be in the form of:,,,,
4a119069-ed4a-4674-9091-476de9186463,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Finally, the signal can be terminated by:",False,"Finally, the signal can be terminated by:",,,,
23a20fdf-80f3-4bad-b486-7676a9599fb8,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The outcome of a signaling cascade is diverse. For example, elevated insulin may signal for increased uptake and storage of glucose (see section 15.3) or a signal may initiate apoptosis (see section 15.2).",True,"Finally, the signal can be terminated by:",,,,
53517dfe-6138-46b1-a97c-8b1f154d192c,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Types of ligands,False,Types of ligands,,,,
e96ea358-3456-40a8-a9d8-2960fe57fa1f,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,General G-protein-coupled receptor cascade,False,General G-protein-coupled receptor cascade,,,,
a3d885c7-5451-4e6c-9b4d-796068cff1bb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"G-protein-coupled receptors (GPCR) can come in several different classes: Gαs, Gαi, and Gαq. Activation of a Gαs (activated by glucagon) will increase the second messenger cAMP, while both Gαi or Gαt cascades function to reduce cAMP, either through inhibition of adenylyl cyclase (also known as adenylate cyclase) or through activation of phosphodiesterase, respectively.",True,General G-protein-coupled receptor cascade,,,,
269cc298-4f03-42f8-aa1d-fb85082d5090,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
269cc298-4f03-42f8-aa1d-fb85082d5090,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
269cc298-4f03-42f8-aa1d-fb85082d5090,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
269cc298-4f03-42f8-aa1d-fb85082d5090,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The classic cascade starts with hormone binding, to an extracellular domain of a seven-helix receptor (GPCR), which causes a conformational change in the receptor that is transmitted to a G protein on the cytosolic side of the membrane (figure 15.3).",True,General G-protein-coupled receptor cascade,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
e65c4acb-a995-4fe7-ab0c-a3c4b02c3b17,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Phosphatidylinositol-derived second messengers,False,Phosphatidylinositol-derived second messengers,,,,
1f4c2542-dd91-43ef-9a87-e5caa8e35251,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
1f4c2542-dd91-43ef-9a87-e5caa8e35251,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
1f4c2542-dd91-43ef-9a87-e5caa8e35251,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
1f4c2542-dd91-43ef-9a87-e5caa8e35251,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Phosphatidylinositols are membrane-bound compounds that can be phosphorylated or cleaved to function as second messengers in a signaling cascade (figure 15.4).,True,Phosphatidylinositol-derived second messengers,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
594ee6de-20cc-4f53-8d99-fe81a61e76a8,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The common membrane component, phosphatidylinositol (PI), can be phosphorylated (by any number of kinases) to form PI 4,5-bisphosphate. This molecule can undergo two different fates.",True,Phosphatidylinositol-derived second messengers,,,,
473a385b-24b9-459f-b9c5-1a720615d0c4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"This cascade will become important for calcium signaling, which is modulated through interactions of IP3 with the mitochondria.",True,Phosphatidylinositol-derived second messengers,,,,
9081a8b7-8a3b-43cf-9d4d-8af768292d80,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Changes in intracellular calcium can alter membrane permeability through calcium-induced calcium release.,True,Phosphatidylinositol-derived second messengers,,,,
0c08dbe1-fe30-4603-8136-42b2567ced54,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Receptor Tyrosine Kinase (RTK),False,Receptor Tyrosine Kinase (RTK),,,,
854a1d29-63f2-47f5-89c8-27355ab2735e,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,RTKs are in the cell membrane and typically function as a dimer.,True,Receptor Tyrosine Kinase (RTK),,,,
b7fb1212-0563-4634-ae60-681ad62c8eba,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Two major cascades are activated downstream of insulin and other growth hormones:,True,Receptor Tyrosine Kinase (RTK),,,,
a15a7966-0962-472f-89e9-f2e187e78483,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Jak-STAT and serine threonine kinases,False,Jak-STAT and serine threonine kinases,,,,
52a0ddc7-34bf-41d0-a584-caf61dc4e29b,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Jak-STATs are also types of tyrosine kinases. The difference here is that these receptors lack autocatalytic abilities and require an intracellular kinase (Jak) to phosphorylate the transcription factor STAT. Jak-STAT signaling is most commonly associated with immune cell signaling.,True,Jak-STAT and serine threonine kinases,,,,
268fc8e0-9725-4913-a937-cb95472c531c,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Serine threonine kinase,False,Serine threonine kinase,,,,
b6343813-70d9-4a2b-8c41-fef52b39d596,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"This receptor family encompasses many of the growth factors for the body (EGF, VEGF, and TGF-β). These receptors usually form heterodimers, and the Type II receptor will autophosphorylate the Type I receptor upon ligand binding. These receptors have an autocatalytic domain that will phosphorylate and typically activate a transcription factor.",True,Serine threonine kinase,,,,
399d520c-203a-421f-ab03-53af11133d93,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Intracellular receptors,False,Intracellular receptors,,,,
4cd5c967-4019-4338-9e2f-eea3d34ec781,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Intracellular receptors bind hydrophobic chemical messengers such as steroid hormones. Binding of the intracellular receptor (which could be cytosolic or nuclear) usually elicits a transcriptional response. Cortisol is an example of a hormone that binds an intracellular receptor. It is released from the adrenal cortex and diffuses into the bloodstream attached to serum albumin and steroid hormone-binding globulin. After diffusing through the plasma membrane, it binds to the cortisol receptor (intracellular receptor) in the cytosol and forms a homodimer exposing a nuclear localization signal (NLS). Exposure of the NLS targets the complex to the nucleus.",True,Intracellular receptors,,,,
b14fecb6-ef81-4662-ad94-af2a708e0205,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Intracellular receptors commonly have three domains:,False,Intracellular receptors commonly have three domains:,,,,
ab7a3168-510c-42f5-a456-59cd3f0d3702,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Intracellular receptors will function as a transcriptional activator by binding specific DNA elements, altering transcription of downstream genes. The signal is terminated by the lowering of the concentration of the hormone.",True,Intracellular receptors commonly have three domains:,,,,
2abd9a43-151e-4f8a-ad6b-10b63256782c,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,NO as a messenger,False,NO as a messenger,,,,
f2d11c4f-2408-4726-b49d-5ce5e5494f05,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Nitric oxide NO is a gas that also acts as a ligand. It is able to diffuse directly across the plasma membrane, and one of its roles is to interact with receptors in smooth muscle and induce relaxation of the tissue.",True,NO as a messenger,,,,
b99425d4-9fc7-4f3d-808c-bc7390fb3630,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"NO has a very short half-life and, therefore, only functions over short distances. It activates guanylyl cyclase to synthesize cGMP. This in turn results in smooth muscle relaxation.",True,NO as a messenger,,,,
d96b78d4-ef1c-4fd4-83dc-4e18e0756e67,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Nitroglycerin, a treatment for heart disease, acts by triggering the release of NO, which causes blood vessels to dilate (expand), thus restoring blood flow to the heart. NO has become better known recently because the pathway that it affects is targeted by prescription medications for erectile dysfunction, such as Viagra (erection involves dilated blood vessels).",True,NO as a messenger,,,,
01fcab2c-f130-4347-9cb2-b752ca600bd2,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,15.1 References and resources,True,NO as a messenger,,,,
bd9112dc-8573-4f09-85c3-51094e09e9e1,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 9: Cell Communication, Chapter 10: Cell Reproduction.",True,NO as a messenger,,,,
376f40e1-34ab-4b4f-a1e3-bad7d1dea4aa,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 15: Cell Signaling and Signal Transduction.",True,NO as a messenger,,,,
278bed9b-abe0-4c46-90ab-ae8ff863e65b,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 85, 208, 238.",True,NO as a messenger,,,,
ae037594-edca-4e34-8a6e-ee7896176fe4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
ae037594-edca-4e34-8a6e-ee7896176fe4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
ae037594-edca-4e34-8a6e-ee7896176fe4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
ae037594-edca-4e34-8a6e-ee7896176fe4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.1 Summary of types of cell signaling. 2021. https://archive.org/details/15.1_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.1,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
39adda96-9f70-4fe4-8d0d-fc57089aaa4d,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
39adda96-9f70-4fe4-8d0d-fc57089aaa4d,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
39adda96-9f70-4fe4-8d0d-fc57089aaa4d,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
39adda96-9f70-4fe4-8d0d-fc57089aaa4d,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.2 Examples of steroid hormones. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/15.2_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.2,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
b989e347-f73a-4a36-8c6e-3b3c9875d948,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
b989e347-f73a-4a36-8c6e-3b3c9875d948,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
b989e347-f73a-4a36-8c6e-3b3c9875d948,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
b989e347-f73a-4a36-8c6e-3b3c9875d948,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.3 Common G-protein coupled receptor signaling cascade. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.3,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
a9a45103-7070-497c-9196-c5b3460cdcbc,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
a9a45103-7070-497c-9196-c5b3460cdcbc,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
a9a45103-7070-497c-9196-c5b3460cdcbc,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
a9a45103-7070-497c-9196-c5b3460cdcbc,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.4 Signaling cascade initiated by DAG and IP3. 2021. https://archive.org/details/15.4_20210926. CC BY 4.0.",True,NO as a messenger,Figure 15.4,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
15f222a3-5c2f-40ef-930b-cfba3f9c66fb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
15f222a3-5c2f-40ef-930b-cfba3f9c66fb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
15f222a3-5c2f-40ef-930b-cfba3f9c66fb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
15f222a3-5c2f-40ef-930b-cfba3f9c66fb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.5 Receptor Tyrosine kinase signaling. 2021. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,NO as a messenger,Figure 15.5,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
2b4ae4a3-eec9-4dd5-8392-a18319fc41c3,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,15.2 Apoptosis,True,NO as a messenger,,,,
c587955d-523f-476c-8d6b-1fa329fb200c,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Both cell proliferation and apoptosis (controlled/programed cell death) are decisive processes within a cell. Keep in mind, apoptosis is distinct from cell necrosis, in which cell death is usually attributable to physical or chemical damage and rapidly spontaneous; think explosion.",True,NO as a messenger,,,,
25b01762-cdeb-4e9d-9ff9-a8de35e5edc9,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Apoptosis is genetically programmed cell death, which leads to “tidy” breakdown and disposal of cells. Morphologically, apoptosis is characterized by shrinking of the cell, changes in the cell membrane (with the formation of small blebs known as “apoptotic bodies”), shrinking of the nucleus, chromatin condensation, and fragmentation of DNA. Macrophages and other phagocytic cells recognize this signal and remove apoptotic cells by phagocytosis without inflammatory phenomena developing. Apoptosis regulates the growth of normal tissues and removes unwanted cells in a controlled manner.",True,NO as a messenger,,,,
0bfbdffe-25ac-4668-9ab6-8b1eb7bf17b5,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
0bfbdffe-25ac-4668-9ab6-8b1eb7bf17b5,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
0bfbdffe-25ac-4668-9ab6-8b1eb7bf17b5,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
0bfbdffe-25ac-4668-9ab6-8b1eb7bf17b5,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Caspases are a family of enzymes that control this process. These are cysteine proteases that cleave proteins next to aspartate residues when they become activated. When a cell receives an apoptotic signal, the procaspases become active and begin the process of protein degradation starting with the cleavage of laminins in the nuclear envelope, protein kinases, transcription factors, snRP proteins, and inhibitors of special DNAses, which are able to fragment the nuclear DNA (figure 15.6).",True,NO as a messenger,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
ce740451-0a63-4450-ae3a-cc247283e50f,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,procaspases,False,procaspases,,,,
bd9a0394-d386-49f1-9302-62809e57973b,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,laminins,False,laminins,,,,
8450703d-126f-465e-9da7-ca295feb44e2,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,snRP,False,snRP,,,,
9581eb88-fb77-4c2f-bb15-c20975fc3a25,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,DNAses,False,DNAses,,,,
a496ff28-a3e2-4036-a0da-32ab6bd71069,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The extrinsic pathway for apoptosis is triggered on the cell surface by ligands that bind to receptors of the tumor necrosis factor family (TNFR, “death receptors”). These include Fas receptors, which are present on the plasma membrane of most cells in the body. When Fas ligands bind to a cellʼs Fas receptors, trimerization of the receptors takes place via the adapter protein FADD (“Fas-associated death domain”), which activates the initiator caspases 8 and 10 inside the cell, setting in motion the apoptotic process.",True,DNAses,,,,
a79933ad-fe0b-4bbf-b96c-52e421f9308b,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,TNFR,False,TNFR,,,,
9440905b-9259-4ec7-8846-7d00950f7cb7,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,cellʼs,False,cellʼs,,,,
a18e8854-1a52-49e3-a828-98c8d08adc57,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,FADD,False,FADD,,,,
f93c0904-2998-4f10-b206-4748f6528a6c,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,caspases,False,caspases,,,,
43821c4f-13ef-4056-8bac-1c37a0e1559f,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The intrinsic, mitochondrial pathway is triggered by genotoxic (DNA damage) or oxidative stress. Aided by Bcl proteins, chemical stress makes the outer mitochondrial membrane leaky. As a result, mitochondrial proteins reach the cytoplasm. Cytochrome c in particular then triggers the caspase cascade by binding to the adapter protein Apaf1 and promoting formation of an apoptosome, a wheel-shaped heptamer that recruits initiator procaspase 9 and activates it to caspase 9.",True,caspases,,,,
2a06a96e-9f69-4cd6-86fb-bc00fc237fea,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The Bcl protein family not only includes proapoptotic proteins (Bax, Bak, and Bim) but also proteins that inhibit apoptosis (including Bcl2). Extracellular growth factors ensure inactivation of Bad or replication of Bcl 2, thus preventing apoptosis.",True,caspases,,,,
766cf24e-37e5-42d4-a21d-4e195501e2f5,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,15.2 References and resources,True,caspases,,,,
b4894be6-827e-4e95-aa25-24e0afec74bb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
b4894be6-827e-4e95-aa25-24e0afec74bb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
b4894be6-827e-4e95-aa25-24e0afec74bb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
b4894be6-827e-4e95-aa25-24e0afec74bb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.6 Comparison of intrinsic and extrinsic apoptosis pathways. 2021. https://archive.org/details/15.6_20210926. CC BY-SA 3.0. Added Model № 2 of apoptosome formation and activation of caspase-9 and caspase-3 (hy) by Brat Ural. CC BY-SA 3.0. From Wikimedia Commons. Added ion channel by Léa Lortal from the Noun Project.",True,caspases,Figure 15.6,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
21fcf389-6774-4cb3-b7b8-dcd722cdb940,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,15.3 Membrane Potential,True,caspases,,,,
3da7cb84-4acc-4e09-9dfd-369b6c3ac8ce,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
3da7cb84-4acc-4e09-9dfd-369b6c3ac8ce,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
3da7cb84-4acc-4e09-9dfd-369b6c3ac8ce,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
3da7cb84-4acc-4e09-9dfd-369b6c3ac8ce,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"The electrical state of the cell membrane can have several variations. These are all variations in the membrane potential. A potential is a distribution of charge across the cell membrane, measured in millivolts (mV). The standard is to compare the inside of the cell relative to the outside, so the membrane potential is a value representing the charge on the intracellular side of the membrane based on the outside being zero, relatively speaking. Neurons harvest this membrane potential to generate or propagate a nerve impulse (figure 15.7).",True,caspases,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
c8dc186f-3117-4b8e-8d02-7614117fc3b9,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,The action potential,False,The action potential,,,,
6009ae92-4823-4944-90db-7ec8b033d7a4,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Resting membrane potential describes the steady state of the cell, which is a dynamic process that is balanced by ion leakage and ion pumping. Without any outside influence, it will not change. To get an electrical signal started, the membrane potential has to change (summary in figures 15.8 and 15.9).",True,The action potential,,,,
453f4611-02c6-498e-9824-fe088512d8cf,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,15.3 References and resources,True,The action potential,,,,
a7efadfb-c9df-40b4-af90-0d4b852abf24,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,Text,False,Text,,,,
6541ceed-23b6-48df-88bf-5b2095405f57,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
6541ceed-23b6-48df-88bf-5b2095405f57,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
6541ceed-23b6-48df-88bf-5b2095405f57,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
6541ceed-23b6-48df-88bf-5b2095405f57,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.7 Neurotransmission by acetylcholine. 2021. https://archive.org/details/15.7_20210926. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Text,Figure 15.7,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
94b8c761-5963-4963-b601-3bbf012b479e,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
94b8c761-5963-4963-b601-3bbf012b479e,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
94b8c761-5963-4963-b601-3bbf012b479e,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
94b8c761-5963-4963-b601-3bbf012b479e,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Grey, Kindred, Figure 15.9 Summary of the action potential as it relates to change in ion concentration across the membrane. 2021. https://archive.org/details/15.9_20210926. CC BY 4.0.",True,Text,Figure 15.9,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
2da96765-bca5-484a-b0ef-fdda7d763fdb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.3 Membrane Potential,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
2da96765-bca5-484a-b0ef-fdda7d763fdb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.2 Apoptosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
2da96765-bca5-484a-b0ef-fdda7d763fdb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15.1 Cell Communication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
2da96765-bca5-484a-b0ef-fdda7d763fdb,https://pressbooks.lib.vt.edu/cellbio/,15. Cellular Signaling,https://pressbooks.lib.vt.edu/cellbio/chapter/cellular-signaling/,"Lieberman M, Peet A. Figure 15.8 Summary of the action potential to membrane potential. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 199. Figure 11.11 Signal transduction by tyrosine receptors. 2017.",True,Text,Figure 15.8,15. Cellular Signaling,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
8db4cfd9-e82e-4c83-b3df-ca7c6dddbea5,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Population genetics,False,Population genetics,,,,
01a12528-3789-4f92-a0ff-6c660292a9cc,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"It is important to remember that these inheritance patterns are not characteristic of all genetic traits, and there are many factors that influence an individual’s phenotype.",True,Population genetics,,,,
8b350d3a-022f-452c-b4cb-e3c02de08327,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Traits can be either dominant or recessive in nature such that in the case of dominant traits conditions manifest in heterozygotes (individuals with just one copy of the mutant allele).,True,Population genetics,,,,
71a4625d-7aa3-4392-b312-c3f5aaa731de,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Recessive traits,False,Recessive traits,,,,
c4367282-08db-46cd-a25a-f3d9b63c0adf,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"When speaking of the children of carrier parents, two-thirds of the healthy siblings of an affected child are heterozygous carriers.",True,Recessive traits,,,,
238f37a3-8b83-45aa-b123-a50fcf036a1d,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"If an individual with an autosomal recessive disorder has children, a disease-causing mutation will be transmitted to all of them (either of the two mutant alleles). The consequences for the child depends on this individual’s partner. If the partner is homozygous for the normal allele of the respective gene (as in the majority of cases), all offspring will be nonaffected heterozygous carriers. If the partner, however, is a carrier (the likelihood is approximately 0.5 to 1 percent for the more frequent recessive disorders), statistically, half of the offspring will be affected (homozygous or compound heterozygous), and the other half will be carriers. If both partners should have the same recessive disorder (caused by mutations in the same gene), all offspring will be homozygous/compound heterozygous and affected.",True,Recessive traits,,,,
7324330f-6e38-4bb5-954e-62c0a08903c6,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,nonaffected,False,nonaffected,,,,
96527e0b-fd29-4fd7-9f25-61d34cdeafdb,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Dominant traits,False,Dominant traits,,,,
c6b09c2d-9b96-4e46-8feb-e13c46701735,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Semidominance or incomplete dominance,False,Semidominance or incomplete dominance,,,,
5d14c88c-b3de-4afb-829e-4b0c0fdb8e98,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"For most disorders inherited as dominant traits, homozygosity for a disease-causing mutation results in a much more severe clinical phenotype than heterozygosity. An example is familial hypercholesterolemia, a genetic disorder resulting from mutations of the low-density lipoprotein (LDL) receptor gene. Individuals with a heterozygous loss-of-function mutation show elevated LDL cholesterol levels (greater than 7 to 10 mmol/ L) and typically suffer their first myocardial infarction in midlife. Homozygous individuals have a much higher LDL cholesterol level (10 to 30 mmol/ L), with the onset of symptoms in early childhood and coronary heart disease as early as school age.",True,Semidominance or incomplete dominance,,,,
6eb03c18-d700-41d6-8ee4-be8723a5c46a,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"In these examples, the phenotype of heterozygotes (Aa) is somewhere in between the phenotypes of wild-type and mutant homozygotes (AA and aa). The inheritance pattern is called semidominant or incompletely dominant, in contrast to complete dominance that is found in very few conditions, such as Huntington’s disease, in which the phenotype of the heterozygous and homozygous mutation carriers is more or less identical. It is worth thinking about reasons why a condition may show complete penetrance. For practical purposes, both types of conditions may be called dominant because the definition rests on the clinical phenotype in the heterozygote, irrespective of what is observed in the homozygote.",True,Semidominance or incomplete dominance,,,,
c5c8322c-dcf6-4c9d-a4bd-6673811e4020,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Codominance,False,Codominance,,,,
d1da2ebf-dc0b-4eca-99bf-2523c8a877ee,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"There are a few cases in which two alleles of the same gene code for proteins with different specific functions, both of which may be found simultaneously in (compound) heterozygous individuals. Such alleles are said to be codominant to each other. The classic example is the ABO blood group system, in which individuals with genotype AB show phenotypic characteristics of allele A as well as allele B, and there is also a null allele that causes complete loss of protein function.",True,Codominance,,,,
c5b4eef4-fbce-41bb-92bf-1e48206b829c,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Sex-linked traits,False,Sex-linked traits,,,,
df16c02a-e157-40f4-916d-783ac7a1e855,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"X-linked recessive traits do not typically manifest when there is a normal copy of the gene (e.g., in females). In contrast nearly all X-linked recessive traits are fully evident in males because they only have one copy of the X chromosome, and thus do not have a normal copy of the gene to compensate for the mutant copy. For that same reason, women are rarely affected by X-linked recessive diseases, however, they are affected when they have two copies of the mutant allele.",True,Sex-linked traits,,,,
21e0910b-5dc1-4747-b883-23636396ec05,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,If a man is affected with an X-linked recessive condition:,False,If a man is affected with an X-linked recessive condition:,,,,
eced94eb-fd9b-4499-87c7-9a6f2f9c82a7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"X-linked dominant disorders clinically manifest when only one copy of the mutant allele is present. There is no transmission from father to son, but there can be transmission from father to daughter (all daughters of an affected male will be affected since the father has only one X chromosome to transmit). Children of an affected woman have a 50 percent chance of inheriting the X chromosome with the mutant allele. Phenotypic presentation of X-linked traits can be influenced by lyonization or X-inactivation. As one X chromosome is randomly expressed in all female cells, the differential patterns of X-inactivation can alter phenotype in female carriers of X-linked recessive disorders and X-linked dominant disorders.",True,If a man is affected with an X-linked recessive condition:,,,,
f1828482-2024-4592-aa35-2de31825ec76,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Calculation of risk,False,Calculation of risk,,,,
0ef23a0e-a93e-4862-9480-1d9e01d40b98,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"One of the most important considerations of genetic counseling is calculating risk. Mathematics is only the first step; equally important is communicating the probability that the event will occur. There are a number of ways to say that an event will not occur with absolute certainty. Studies have shown that these terms are understood and evaluated differently by different individuals. Another factor that varies between patients is that events are evaluated according to whether the result will be considered positive or negative and by which consequences they will have. For example, the probability that, beginning at age forty-five, mothers have a 5 percent risk of giving birth to a child with a chromosomal disorder is generally considered a high risk. In cancer, on the other hand, a survival chance of 5 percent is considered low.",True,Calculation of risk,,,,
17a42006-a945-46eb-aee2-99d1656ec55c,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Hardy-Weinberg equations,False,Hardy-Weinberg equations,,,,
df384e1e-1d9a-402d-a161-c04cb1eb778d,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"The Hardy-Weinberg law rests on the assumption that there are two different alleles at a certain locus; these alleles are named “p” and “q” (i.e., a normal allele [traditionally p] and a variant allele [traditionally q]). Since there are only these two alleles, p + q = 1.",True,Hardy-Weinberg equations,,,,
50f8a678-7242-4a59-bc33-85204400e0df,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"In humans, if the respective gene occurs in two copies on only one autosome, the frequency of the three possible genotypes is calculated from the binominal distribution, which is often represented as:",True,Hardy-Weinberg equations,,,,
35b000da-22ab-47bd-98a7-713146d68cfe,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,p2 + 2pq + q2 = 1,False,p2 + 2pq + q2 = 1,,,,
263968ea-7af9-440d-9849-207f5db850a2,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,p is the frequency of the ʻAʼ allele,False,p is the frequency of the ʻAʼ allele,,,,
4a913fa0-80e3-4cf6-9312-2cbf1f427a74,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,q is the frequency of the ʻaʼ allele,False,q is the frequency of the ʻaʼ allele,,,,
1da5af24-0db9-46e2-bd2d-891dad4b44fb,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,p2 = the frequency of the AA genotype,False,p2 = the frequency of the AA genotype,,,,
9fdb05b8-240b-4066-b70f-e812fe9013ef,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,q2 = the frequency of the aa genotype,False,q2 = the frequency of the aa genotype,,,,
f1030fcf-39e6-4e27-81bb-caa93ee4f7e3,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,2pq = the frequency of the Aa genotype,False,2pq = the frequency of the Aa genotype,,,,
54700b37-bad6-4e68-854f-c204cc2b4eeb,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,The Hardy-Weinberg law only applies to an “ideal population” that meets the following criteria:,True,2pq = the frequency of the Aa genotype,,,,
2ef94731-0973-47c2-bb39-e441753a2e3e,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"The one factor that has practical implications among this group of criteria is random mating, since the Hardy-Weinberg law cannot be applied if there is frequent intermarriage. In such cases, rare recessive disorders occur with much greater frequency than would be expected from the frequency of heterozygosity. The other criteria are more relevant to whether or not the allele or genotype frequencies remain constant or whether the incidence of a disorder changes.",True,2pq = the frequency of the Aa genotype,,,,
58bdfd2b-e9e2-41f8-94a7-f849a78b0ad2,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Cystic fibrosis is a recessive condition that affects 1/2,500 births in the Caucasian population:",True,2pq = the frequency of the Aa genotype,,,,
45e18136-4ba6-49ee-9dea-3e32eca77c67,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Frequency of the recessive allele:,False,Frequency of the recessive allele:,,,,
9b0e6fe2-1934-4e15-8c15-b302eef403a1,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"q2 = 1/2,500 = 0.0004",True,Frequency of the recessive allele:,,,,
d9f2ebbb-d477-42b6-8fac-e456310beaf6,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,q = 0.02,True,Frequency of the recessive allele:,,,,
e279801e-445c-4014-bc95-a49b2dc731bc,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Frequency of the dominant allele:,False,Frequency of the dominant allele:,,,,
21948c4d-0178-422d-8593-be4a974e84c4,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,1 – 0.02 = 0.98 = p,True,Frequency of the dominant allele:,,,,
700187bb-ff1c-488b-b340-25c0141fd1dc,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,14.1 References and resources,True,Frequency of the dominant allele:,,,,
bdff4636-1d7b-47c9-aed3-773ba16621cd,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Frequency of the dominant allele:,,,,
f6a67306-8963-4d95-a9f2-8330504080e8,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Frequency of the dominant allele:,,,,
50b6d50a-3c9e-4be5-90af-0611fbed528b,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Frequency of the dominant allele:,,,,
a70df9ba-52d9-411e-8c29-d0504377da99,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
a70df9ba-52d9-411e-8c29-d0504377da99,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
a70df9ba-52d9-411e-8c29-d0504377da99,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
a70df9ba-52d9-411e-8c29-d0504377da99,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
c7773cc9-9af7-4731-8248-ef904bb2dc17,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
c7773cc9-9af7-4731-8248-ef904bb2dc17,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
c7773cc9-9af7-4731-8248-ef904bb2dc17,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
c7773cc9-9af7-4731-8248-ef904bb2dc17,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
8b71f44b-38df-4dc0-98d4-82b7a74588bb,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Additional resources,False,Additional resources,,,,
b44f6426-7f61-492a-bb25-cca17ef783dd,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,14.2 Non-Mendelian Inheritance,True,Additional resources,,,,
d1296041-94c4-4749-95bb-7c5387f35ff5,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"The majority of genetic disorders are not inherited in a Mendelian fashion. Even in cases where Mendelian genetics can predict genotype, the disease phenotype may not be displayed or may be variable due to external influences. This section describes some additional factors that influence presentation and inheritance patterns.",True,Additional resources,,,,
72b8404a-4a28-4f4c-bc41-c30c39a353fa,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
72b8404a-4a28-4f4c-bc41-c30c39a353fa,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
72b8404a-4a28-4f4c-bc41-c30c39a353fa,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
72b8404a-4a28-4f4c-bc41-c30c39a353fa,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
51306d88-d853-4baa-9cbf-2cdf55e39cb7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
51306d88-d853-4baa-9cbf-2cdf55e39cb7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
51306d88-d853-4baa-9cbf-2cdf55e39cb7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
51306d88-d853-4baa-9cbf-2cdf55e39cb7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
3d258d36-7301-41c3-8a7e-50ab2b9d9133,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Extranuclear inheritance,False,Extranuclear inheritance,,,,
546505ca-2408-4d24-9d61-57a21542b1f5,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Mitochondria are unique in that they have multiple copies of a circular chromosome. This DNA is independent of nuclear DNA and inherited from the mother.,True,Extranuclear inheritance,,,,
f9a83560-60fd-4e80-a82d-7ac388c514fe,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
f9a83560-60fd-4e80-a82d-7ac388c514fe,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
f9a83560-60fd-4e80-a82d-7ac388c514fe,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
f9a83560-60fd-4e80-a82d-7ac388c514fe,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
1e3f5a07-6c9c-4ed6-b7f4-ceaf8d97ab9f,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Heteroplasmy is a term referring to the diversity of the mitochondrial genome within each cell. During cell division, mitochondria are divided randomly between the two daughter cells, and therefore the percentage of affected mitochondrial DNA (mtDNA) will also be variable within the offspring. The mitochondria generate energy for the rest of the cell, therefore disease transmitted through mitochondrial inheritance affects high-energy organs (this is a good example of pleiotropy).",True,Extranuclear inheritance,,,,
3337493e-c1e9-4a0f-8ab2-48c982b90258,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Genomic imprinting,False,Genomic imprinting,,,,
c498a007-be4c-4ebf-a506-2edb466a7abc,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Genetic information is not just stored in the actual code (e.g., ATCG), but also for many genes hereditary information is transmitted with a parental-specific imprint based on whether the gene was transmitted from the father or from the mother. This imprint can be thought of as the font of the genome (e.g., ATCG vs. ATCG vs. ATCG). For these imprinted genes, even though the nucleotide sequence in the maternal and paternal copies is identical, the expression differs depending on the parental imprint. Genomic imprinting is the most well-characterized epigenetic transmission of gene regulation. Often in cases, the imprinting of one allele is essential for a normal phenotype, and loss of imprinting or uniparental disomy (inheritance of both loci from a single parental source) can cause inappropriate expression patterns.",True,Genomic imprinting,,,,
fd594808-a520-4760-8dff-ee0a8416f8fd,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,ATCG,False,ATCG,,,,
73b0c853-d50a-47ad-9d96-aeedc31ad31e,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Differential methylation of genomic DNA is a central mechanism in the regulation of the expression of genes. Of special importance is the methylation of cytosine in CpG (cytosine-phosphorus-guanine) dinucleotides. Many genes have numerous “CpG islands” with a large number of CpG dinucleotides located upstream of the transcriptional start. Hypermethylation in this region results in transcriptional silencing, meaning the gene can no longer be read. The methylation pattern of DNA and, consequently, the activity pattern of the genes are generally transmitted as a stable trait in mitosis; however, for imprinted or epigenetically sensitive genes, this “trait” is reset in meiosis.",True,ATCG,,,,
75e4931c-c10f-4d82-8b9f-43db7bc18d34,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Trinucleotide repeat disorders,False,Trinucleotide repeat disorders,,,,
57d4037c-af1a-4ef7-9399-4fba65103c73,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
57d4037c-af1a-4ef7-9399-4fba65103c73,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
57d4037c-af1a-4ef7-9399-4fba65103c73,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
57d4037c-af1a-4ef7-9399-4fba65103c73,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
604dac48-3af5-40d1-bbaa-035508fca9b1,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Triplicate repeat disorders are also characteristic of anticipation where the affected phenotype of individuals becomes progressively worse with each generation. Classic repeat disorders include Fragile X and Huntingtonʼs disease. In the case of Fragile X, the repeated region becomes hypermethylated and the methylation pattern expands into the promoter region for the gene. This will lead to silencing of the transcript. The gene itself, FMR1, is involved in mRNA splicing, and the loss of this gene product has a pleiotropic effect.",True,Trinucleotide repeat disorders,,,,
c31fb12a-2d98-4037-87f3-ac7c2f2d7503,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,14.2 References and resources,True,Trinucleotide repeat disorders,,,,
7ebe83bd-3fbd-493e-9280-03b5324fa7f6,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Text,False,Text,,,,
b0ae63f0-7219-40e9-aafd-a33afb6d43d9,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
b0ae63f0-7219-40e9-aafd-a33afb6d43d9,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
b0ae63f0-7219-40e9-aafd-a33afb6d43d9,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
b0ae63f0-7219-40e9-aafd-a33afb6d43d9,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
b42eb69a-10a3-4862-8a16-b774100d759c,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
b42eb69a-10a3-4862-8a16-b774100d759c,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
b42eb69a-10a3-4862-8a16-b774100d759c,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
b42eb69a-10a3-4862-8a16-b774100d759c,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
3e89a806-2482-4bc6-87bc-615f124ba307,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
3e89a806-2482-4bc6-87bc-615f124ba307,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
3e89a806-2482-4bc6-87bc-615f124ba307,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
3e89a806-2482-4bc6-87bc-615f124ba307,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
4c40c5fe-8426-4b90-98ef-202551e09788,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),True,Text,,,,
e5f8b84d-9def-42fb-b50a-88f6d1ffc5f7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"There is tremendous interest in finding specific genes that predispose individuals to common disease traits, most of which follow complex inheritance patterns rather than Mendelian (single gene) patterns. Physicians will find frequent references in the medical literature related to the search for genes with high predictive value in common disorders.",True,Text,,,,
f99fffb5-cb0a-4426-a355-db96f3677516,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"While we know the DNA sequence of the vast majority of the coding regions of the genome, we still do not understand the full function of the majority of genes or how they are involved in human health conditions. There are two major approaches to identifying genetic loci, which contribute to disease presentation: linkage analysis and genome-wide association studies.",True,Text,,,,
e0501f85-5e7e-465f-9758-f6bdc3306be0,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Linkage analysis,False,Linkage analysis,,,,
95ae640d-bbf7-4ba7-9701-4bf418bc8c12,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Linkage analysis relies on the fact that disease-causing mutations are inherited jointly (linked) with genetic markers located in their immediate vicinity. In order for a gene and a genetic marker to be linked, they must be syntenic, meaning they must be located on the same chromosome. Most genes or markers within the human genome are inherited independently of one another, and therefore are transmitted together 50 percent of the time.",True,Linkage analysis,,,,
94516c11-2ea6-48de-b315-925357a29ac1,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Linkage between two genes means that they tend to be inherited together more often than expected by chance.,True,Linkage analysis,,,,
81c9f4f6-38e4-4d6a-987a-fb186154a6f7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"For linkage to occur, two conditions must be met:",False,"For linkage to occur, two conditions must be met:",,,,
89c2199d-7df6-47ef-a661-a2adb655b9a1,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Syntenic genes may become detached from one another through crossing over (or recombination). For large chromosomes, crossing over is so common that genes at opposite ends of the chromosome are inherited together no more often than if they resided on entirely different chromosomes.",True,"For linkage to occur, two conditions must be met:",,,,
5ecb5062-be21-47b6-857f-d4b88861b38e,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"When markers are close enough together on the same chromosome, crossing over fails to separate them frequently enough for them to be inherited independently of one another. This is evidenced by coinheritance of greater than 50 percent.",True,"For linkage to occur, two conditions must be met:",,,,
441daa8d-be56-4ad8-960a-cec991558edd,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"The unit of measure in linkage studies is “centimorgans.” This concept can be confusing because we refer to the “distance” between two traits, but what is measured experimentally is the frequency of coinheritance, not physical distance.",True,"For linkage to occur, two conditions must be met:",,,,
33a2d8ce-42e5-401e-bca6-076592f8a368,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
33a2d8ce-42e5-401e-bca6-076592f8a368,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
33a2d8ce-42e5-401e-bca6-076592f8a368,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
33a2d8ce-42e5-401e-bca6-076592f8a368,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
5da29400-62c9-43ee-99de-bf2751172856,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"The further apart two genes or markers are on the same chromosome increases the probability of a crossover occurring in between the two markers. Studies to determine linkage require the careful study of large numbers of parents and their offspring. Careful study of the family relationships across three generations allows linkage phases to be determined. In this case, the grandparents’ information is required to determine how the genes are initially linked in the parents, and the grandchildren are studied to determine recombination events (crossing over) that separate the genes or markers during meiosis in the parents.",True,"For linkage to occur, two conditions must be met:",,,,
b8187711-490a-45ba-a3cf-7731c045b8b9,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Distance can be expressed in cM as described previously, or in terms of theta (θ), which are proportions. Remember, both are measures of probability, not physical distance. Linkage determinations are based on the fundamental rules of probability and binomial mathematics. Like any probability issue, a ratio greater than one reflects odds in favor (of linkage), and less than one reflects odds against.",True,"For linkage to occur, two conditions must be met:",,,,
eed374b7-d783-4045-bbc6-0ffdad5c9b2e,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"For linkage studies, each family represents an independent estimate of the odds in favor of (or against) linkage. The property within standard probability laws is the concept of joint probability. To determine joint probability, meaning the chance that BOTH of two events will happen, we use what is often called the “AND rule.” The AND rule applies whenever the probabilities under study are independent of one another.",True,"For linkage to occur, two conditions must be met:",,,,
eaa4b884-d485-4c10-afae-822e67f1001f,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Multiplying the results of many families is challenging, and was particularly so before computer resources became readily available. It is simpler mathematically to add numbers. We can move from multiplication to addition if we simply use the log of the probability instead of the probability number itself. Remember that the log of a number that is less than one is a negative number, and for a number greater than one, it is a positive number. Using a log conversion makes it simple to see if the ratio of the odds is favorable (positive) or unfavorable. The term “LOD score” refers to the log (base 10) of the odds of linkage, looking across a series of independent families.",True,"For linkage to occur, two conditions must be met:",,,,
f5c3e44c-0c83-4bd9-9869-0e01002b6dae,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,There really are just two things to remember about LOD scores:,True,"For linkage to occur, two conditions must be met:",,,,
1f06be4a-c989-419b-afcf-5eea6eea19ef,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Genome-wide association studies (GWAS),False,Genome-wide association studies (GWAS),,,,
9c1873bc-3395-4547-b81a-5b39d92e3ba3,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Population association is easily confused with the concepts surrounding linkage. These studies look for a statistical association between a marker (often a single nucleotide polymorphism or SNP) and a specific trait. The concept of population association can be exploited to simultaneously study a very large number of detectable genetic markers (SNPs) in patient populations with common disorders.,True,Genome-wide association studies (GWAS),,,,
df1d7f5b-d4d7-4aaf-8505-da6577a48c60,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
df1d7f5b-d4d7-4aaf-8505-da6577a48c60,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
df1d7f5b-d4d7-4aaf-8505-da6577a48c60,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
df1d7f5b-d4d7-4aaf-8505-da6577a48c60,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
83e189a5-b5d6-4da4-bb74-07a26297c2a7,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"For more information on these types of studies, please see: https://www.genome.gov/20019523/geno…ies-factsheet/.",True,Genome-wide association studies (GWAS),,,,
63a5e78c-76a1-4e96-b119-9cdc3c5b8fda,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,14.3 References and resources,True,Genome-wide association studies (GWAS),,,,
b06b4521-aa76-4a66-b570-f70cbc33f515,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Genome-wide association studies (GWAS),,,,
741677e2-4c96-4098-b38e-8272afbca11e,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Genome-wide association studies (GWAS),,,,
cebc5bd4-7375-4f54-8976-63606b77d14d,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Genome-wide association studies (GWAS),,,,
cdbfb549-131f-41ee-b593-9fb2f7ec086b,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
cdbfb549-131f-41ee-b593-9fb2f7ec086b,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
cdbfb549-131f-41ee-b593-9fb2f7ec086b,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
cdbfb549-131f-41ee-b593-9fb2f7ec086b,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
3ca5339d-88f8-466d-8643-4ecbc9d029e6,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
3ca5339d-88f8-466d-8643-4ecbc9d029e6,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
3ca5339d-88f8-466d-8643-4ecbc9d029e6,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
3ca5339d-88f8-466d-8643-4ecbc9d029e6,https://pressbooks.lib.vt.edu/cellbio/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-3,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
121f1e17-9906-4c87-adf3-01bab5705c9c,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Population genetics,False,Population genetics,,,,
5d8d46c6-d3e6-4b94-a833-8e0d91aec0ed,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"It is important to remember that these inheritance patterns are not characteristic of all genetic traits, and there are many factors that influence an individual’s phenotype.",True,Population genetics,,,,
bec75703-23c9-4658-8370-321558dbb948,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Traits can be either dominant or recessive in nature such that in the case of dominant traits conditions manifest in heterozygotes (individuals with just one copy of the mutant allele).,True,Population genetics,,,,
521c135a-271c-435c-9b5d-5ac5a605fe86,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Recessive traits,False,Recessive traits,,,,
dcd3a9af-f793-44ab-bdc4-924e91766660,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"When speaking of the children of carrier parents, two-thirds of the healthy siblings of an affected child are heterozygous carriers.",True,Recessive traits,,,,
83a7c2c1-c0c5-4d2d-b37c-d26aaeae1aae,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"If an individual with an autosomal recessive disorder has children, a disease-causing mutation will be transmitted to all of them (either of the two mutant alleles). The consequences for the child depends on this individual’s partner. If the partner is homozygous for the normal allele of the respective gene (as in the majority of cases), all offspring will be nonaffected heterozygous carriers. If the partner, however, is a carrier (the likelihood is approximately 0.5 to 1 percent for the more frequent recessive disorders), statistically, half of the offspring will be affected (homozygous or compound heterozygous), and the other half will be carriers. If both partners should have the same recessive disorder (caused by mutations in the same gene), all offspring will be homozygous/compound heterozygous and affected.",True,Recessive traits,,,,
ab264257-afed-4bcd-8cd9-b6c3070d80d1,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,nonaffected,False,nonaffected,,,,
6e5c1456-2563-4a70-90a8-fd50cd53966f,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Dominant traits,False,Dominant traits,,,,
1b7d5480-5979-423e-8629-02dfcd3afa09,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Semidominance or incomplete dominance,False,Semidominance or incomplete dominance,,,,
972bfe7f-5551-4b3f-b4ac-84747c5bb6a4,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"For most disorders inherited as dominant traits, homozygosity for a disease-causing mutation results in a much more severe clinical phenotype than heterozygosity. An example is familial hypercholesterolemia, a genetic disorder resulting from mutations of the low-density lipoprotein (LDL) receptor gene. Individuals with a heterozygous loss-of-function mutation show elevated LDL cholesterol levels (greater than 7 to 10 mmol/ L) and typically suffer their first myocardial infarction in midlife. Homozygous individuals have a much higher LDL cholesterol level (10 to 30 mmol/ L), with the onset of symptoms in early childhood and coronary heart disease as early as school age.",True,Semidominance or incomplete dominance,,,,
5aba02b0-e5e2-4d3e-837c-698c0ee49393,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"In these examples, the phenotype of heterozygotes (Aa) is somewhere in between the phenotypes of wild-type and mutant homozygotes (AA and aa). The inheritance pattern is called semidominant or incompletely dominant, in contrast to complete dominance that is found in very few conditions, such as Huntington’s disease, in which the phenotype of the heterozygous and homozygous mutation carriers is more or less identical. It is worth thinking about reasons why a condition may show complete penetrance. For practical purposes, both types of conditions may be called dominant because the definition rests on the clinical phenotype in the heterozygote, irrespective of what is observed in the homozygote.",True,Semidominance or incomplete dominance,,,,
ea32342a-5cd0-461e-ad6c-0d77940c52a4,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Codominance,False,Codominance,,,,
de205b27-89c9-4f9f-9b5a-7b76892f1bde,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"There are a few cases in which two alleles of the same gene code for proteins with different specific functions, both of which may be found simultaneously in (compound) heterozygous individuals. Such alleles are said to be codominant to each other. The classic example is the ABO blood group system, in which individuals with genotype AB show phenotypic characteristics of allele A as well as allele B, and there is also a null allele that causes complete loss of protein function.",True,Codominance,,,,
a939c6e8-7ff6-4d29-91ac-d9cc21b75b23,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Sex-linked traits,False,Sex-linked traits,,,,
2d2273a8-6775-4df3-b8df-07d1ad89db67,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"X-linked recessive traits do not typically manifest when there is a normal copy of the gene (e.g., in females). In contrast nearly all X-linked recessive traits are fully evident in males because they only have one copy of the X chromosome, and thus do not have a normal copy of the gene to compensate for the mutant copy. For that same reason, women are rarely affected by X-linked recessive diseases, however, they are affected when they have two copies of the mutant allele.",True,Sex-linked traits,,,,
236bb78e-b722-4688-81f6-9479744f7bc1,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,If a man is affected with an X-linked recessive condition:,False,If a man is affected with an X-linked recessive condition:,,,,
a9ecc392-64d1-4cc1-b2a1-d663af95d793,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"X-linked dominant disorders clinically manifest when only one copy of the mutant allele is present. There is no transmission from father to son, but there can be transmission from father to daughter (all daughters of an affected male will be affected since the father has only one X chromosome to transmit). Children of an affected woman have a 50 percent chance of inheriting the X chromosome with the mutant allele. Phenotypic presentation of X-linked traits can be influenced by lyonization or X-inactivation. As one X chromosome is randomly expressed in all female cells, the differential patterns of X-inactivation can alter phenotype in female carriers of X-linked recessive disorders and X-linked dominant disorders.",True,If a man is affected with an X-linked recessive condition:,,,,
99b0e8bd-3802-4781-b1fb-06b21bdf96e1,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Calculation of risk,False,Calculation of risk,,,,
35011c8a-32ab-4eda-b909-d6e71846851f,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"One of the most important considerations of genetic counseling is calculating risk. Mathematics is only the first step; equally important is communicating the probability that the event will occur. There are a number of ways to say that an event will not occur with absolute certainty. Studies have shown that these terms are understood and evaluated differently by different individuals. Another factor that varies between patients is that events are evaluated according to whether the result will be considered positive or negative and by which consequences they will have. For example, the probability that, beginning at age forty-five, mothers have a 5 percent risk of giving birth to a child with a chromosomal disorder is generally considered a high risk. In cancer, on the other hand, a survival chance of 5 percent is considered low.",True,Calculation of risk,,,,
b5b11934-94dd-4d07-bc6c-48eb1cc7d29f,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Hardy-Weinberg equations,False,Hardy-Weinberg equations,,,,
8321b63e-fc1c-4a20-b86f-cd9aca8bd806,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"The Hardy-Weinberg law rests on the assumption that there are two different alleles at a certain locus; these alleles are named “p” and “q” (i.e., a normal allele [traditionally p] and a variant allele [traditionally q]). Since there are only these two alleles, p + q = 1.",True,Hardy-Weinberg equations,,,,
4454b16f-a5c2-474f-868f-0035bcb95413,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"In humans, if the respective gene occurs in two copies on only one autosome, the frequency of the three possible genotypes is calculated from the binominal distribution, which is often represented as:",True,Hardy-Weinberg equations,,,,
bebf08f7-8421-4046-b23f-6557ae240c45,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,p2 + 2pq + q2 = 1,False,p2 + 2pq + q2 = 1,,,,
b5d4b762-7202-4aac-8e2f-1061104c3e29,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,p is the frequency of the ʻAʼ allele,False,p is the frequency of the ʻAʼ allele,,,,
db384ca8-1ba3-4f92-911c-9fbcefb8ddbd,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,q is the frequency of the ʻaʼ allele,False,q is the frequency of the ʻaʼ allele,,,,
e728fd02-deef-4564-8079-e418c8fd3511,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,p2 = the frequency of the AA genotype,False,p2 = the frequency of the AA genotype,,,,
b5510e49-f3e3-490d-ac0d-62b756de4684,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,q2 = the frequency of the aa genotype,False,q2 = the frequency of the aa genotype,,,,
7957ac5f-1bf1-429e-8de0-65b35375b3b7,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,2pq = the frequency of the Aa genotype,False,2pq = the frequency of the Aa genotype,,,,
1c210792-acdb-4159-b534-433ea8b32f71,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,The Hardy-Weinberg law only applies to an “ideal population” that meets the following criteria:,True,2pq = the frequency of the Aa genotype,,,,
36758451-f840-4961-8ecb-449546abe21d,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"The one factor that has practical implications among this group of criteria is random mating, since the Hardy-Weinberg law cannot be applied if there is frequent intermarriage. In such cases, rare recessive disorders occur with much greater frequency than would be expected from the frequency of heterozygosity. The other criteria are more relevant to whether or not the allele or genotype frequencies remain constant or whether the incidence of a disorder changes.",True,2pq = the frequency of the Aa genotype,,,,
a4956e72-47bf-4f2a-adf5-f517d2fcf987,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Cystic fibrosis is a recessive condition that affects 1/2,500 births in the Caucasian population:",True,2pq = the frequency of the Aa genotype,,,,
40749a8d-15ea-4ca9-8534-e17aa5ed39a8,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Frequency of the recessive allele:,False,Frequency of the recessive allele:,,,,
f7a81b66-f5d8-4037-9f1f-8956ca835d49,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"q2 = 1/2,500 = 0.0004",True,Frequency of the recessive allele:,,,,
f5976114-3c9e-422d-a292-d534e61ba50d,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,q = 0.02,True,Frequency of the recessive allele:,,,,
41a23e8a-002d-40d4-b1fb-d6fda06784da,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Frequency of the dominant allele:,False,Frequency of the dominant allele:,,,,
8c8570c0-09df-4210-a06a-9add9d243402,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,1 – 0.02 = 0.98 = p,True,Frequency of the dominant allele:,,,,
3e131d55-07f9-46be-b4eb-c1aed12b899a,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,14.1 References and resources,True,Frequency of the dominant allele:,,,,
1a954dfc-4e02-4bab-b2d3-c1fea371e3de,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Frequency of the dominant allele:,,,,
f546d8d1-a4c7-471c-82c5-88f0ff818e38,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Frequency of the dominant allele:,,,,
6244cebf-8896-455d-8775-21d06b674d77,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Frequency of the dominant allele:,,,,
2a4390a4-07d4-479e-8a10-26ae24a2fe8a,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
2a4390a4-07d4-479e-8a10-26ae24a2fe8a,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
2a4390a4-07d4-479e-8a10-26ae24a2fe8a,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
2a4390a4-07d4-479e-8a10-26ae24a2fe8a,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
86914017-3179-465e-a093-f54620d1e824,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
86914017-3179-465e-a093-f54620d1e824,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
86914017-3179-465e-a093-f54620d1e824,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
86914017-3179-465e-a093-f54620d1e824,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
a1e491b2-ab21-48ed-a0b6-afbe0a669855,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Additional resources,False,Additional resources,,,,
7279aa4c-8c6f-4703-af62-201a936411b1,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,14.2 Non-Mendelian Inheritance,True,Additional resources,,,,
4d3afd01-3347-4676-a268-97106286a273,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"The majority of genetic disorders are not inherited in a Mendelian fashion. Even in cases where Mendelian genetics can predict genotype, the disease phenotype may not be displayed or may be variable due to external influences. This section describes some additional factors that influence presentation and inheritance patterns.",True,Additional resources,,,,
843c5a2c-27ff-4d69-8c81-4351c6f2273e,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
843c5a2c-27ff-4d69-8c81-4351c6f2273e,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
843c5a2c-27ff-4d69-8c81-4351c6f2273e,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
843c5a2c-27ff-4d69-8c81-4351c6f2273e,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
a9a0e7f3-42c6-427b-acef-2d42f8b76bc0,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
a9a0e7f3-42c6-427b-acef-2d42f8b76bc0,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
a9a0e7f3-42c6-427b-acef-2d42f8b76bc0,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
a9a0e7f3-42c6-427b-acef-2d42f8b76bc0,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
298032be-b2cc-4f4a-b1de-8ae0b24130ba,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Extranuclear inheritance,False,Extranuclear inheritance,,,,
c6f8f3ad-a9a8-4503-8357-e4847a5cf993,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Mitochondria are unique in that they have multiple copies of a circular chromosome. This DNA is independent of nuclear DNA and inherited from the mother.,True,Extranuclear inheritance,,,,
499fa4cd-0355-4354-91e6-f52c7d966f12,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
499fa4cd-0355-4354-91e6-f52c7d966f12,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
499fa4cd-0355-4354-91e6-f52c7d966f12,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
499fa4cd-0355-4354-91e6-f52c7d966f12,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
f10145c9-78aa-4891-8d3b-af87aca494ce,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Heteroplasmy is a term referring to the diversity of the mitochondrial genome within each cell. During cell division, mitochondria are divided randomly between the two daughter cells, and therefore the percentage of affected mitochondrial DNA (mtDNA) will also be variable within the offspring. The mitochondria generate energy for the rest of the cell, therefore disease transmitted through mitochondrial inheritance affects high-energy organs (this is a good example of pleiotropy).",True,Extranuclear inheritance,,,,
8396daea-ed48-439c-bb65-5d7d0f775ce1,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Genomic imprinting,False,Genomic imprinting,,,,
016d46a1-4178-4dcc-83bf-7dda8d61fdae,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Genetic information is not just stored in the actual code (e.g., ATCG), but also for many genes hereditary information is transmitted with a parental-specific imprint based on whether the gene was transmitted from the father or from the mother. This imprint can be thought of as the font of the genome (e.g., ATCG vs. ATCG vs. ATCG). For these imprinted genes, even though the nucleotide sequence in the maternal and paternal copies is identical, the expression differs depending on the parental imprint. Genomic imprinting is the most well-characterized epigenetic transmission of gene regulation. Often in cases, the imprinting of one allele is essential for a normal phenotype, and loss of imprinting or uniparental disomy (inheritance of both loci from a single parental source) can cause inappropriate expression patterns.",True,Genomic imprinting,,,,
846b5cc8-25c7-4e9f-bc19-f60da416ea82,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,ATCG,False,ATCG,,,,
28a1bf5f-3ba1-42d1-80f8-c4f1a361b5bb,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Differential methylation of genomic DNA is a central mechanism in the regulation of the expression of genes. Of special importance is the methylation of cytosine in CpG (cytosine-phosphorus-guanine) dinucleotides. Many genes have numerous “CpG islands” with a large number of CpG dinucleotides located upstream of the transcriptional start. Hypermethylation in this region results in transcriptional silencing, meaning the gene can no longer be read. The methylation pattern of DNA and, consequently, the activity pattern of the genes are generally transmitted as a stable trait in mitosis; however, for imprinted or epigenetically sensitive genes, this “trait” is reset in meiosis.",True,ATCG,,,,
191063e6-bb05-427a-ae55-bcfc5febd2aa,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Trinucleotide repeat disorders,False,Trinucleotide repeat disorders,,,,
3cdf4fdb-867d-4686-a26d-6c3cedb8d794,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
3cdf4fdb-867d-4686-a26d-6c3cedb8d794,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
3cdf4fdb-867d-4686-a26d-6c3cedb8d794,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
3cdf4fdb-867d-4686-a26d-6c3cedb8d794,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
57ff291d-505f-4934-ad3e-53e41164551f,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Triplicate repeat disorders are also characteristic of anticipation where the affected phenotype of individuals becomes progressively worse with each generation. Classic repeat disorders include Fragile X and Huntingtonʼs disease. In the case of Fragile X, the repeated region becomes hypermethylated and the methylation pattern expands into the promoter region for the gene. This will lead to silencing of the transcript. The gene itself, FMR1, is involved in mRNA splicing, and the loss of this gene product has a pleiotropic effect.",True,Trinucleotide repeat disorders,,,,
6863288e-7819-43eb-8ca5-8d63a9125bfc,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,14.2 References and resources,True,Trinucleotide repeat disorders,,,,
e190b531-87cc-4a10-907c-7545ddb7b78e,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Text,False,Text,,,,
b8e5b795-4ed2-4a3b-9e98-996bd601a057,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
b8e5b795-4ed2-4a3b-9e98-996bd601a057,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
b8e5b795-4ed2-4a3b-9e98-996bd601a057,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
b8e5b795-4ed2-4a3b-9e98-996bd601a057,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
db87c4bc-e674-4699-a749-fd1530faeebe,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
db87c4bc-e674-4699-a749-fd1530faeebe,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
db87c4bc-e674-4699-a749-fd1530faeebe,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
db87c4bc-e674-4699-a749-fd1530faeebe,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
bdc30b1d-8919-4379-96b5-e98829eb6687,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
bdc30b1d-8919-4379-96b5-e98829eb6687,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
bdc30b1d-8919-4379-96b5-e98829eb6687,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
bdc30b1d-8919-4379-96b5-e98829eb6687,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
563ed18e-facc-445d-95f5-cd8c8f596cce,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),True,Text,,,,
5684cd77-b2c6-41db-90e5-002d476700be,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"There is tremendous interest in finding specific genes that predispose individuals to common disease traits, most of which follow complex inheritance patterns rather than Mendelian (single gene) patterns. Physicians will find frequent references in the medical literature related to the search for genes with high predictive value in common disorders.",True,Text,,,,
e9d1281c-b4b5-4404-9e69-fa924fbfb3e6,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"While we know the DNA sequence of the vast majority of the coding regions of the genome, we still do not understand the full function of the majority of genes or how they are involved in human health conditions. There are two major approaches to identifying genetic loci, which contribute to disease presentation: linkage analysis and genome-wide association studies.",True,Text,,,,
fa291dca-319b-4320-aedd-6a5dc060948d,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Linkage analysis,False,Linkage analysis,,,,
2ee321d6-2d0a-47fb-ba22-c3b30c54f43a,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Linkage analysis relies on the fact that disease-causing mutations are inherited jointly (linked) with genetic markers located in their immediate vicinity. In order for a gene and a genetic marker to be linked, they must be syntenic, meaning they must be located on the same chromosome. Most genes or markers within the human genome are inherited independently of one another, and therefore are transmitted together 50 percent of the time.",True,Linkage analysis,,,,
20e14fb8-d86d-4555-b7c4-89203a3a8ba9,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Linkage between two genes means that they tend to be inherited together more often than expected by chance.,True,Linkage analysis,,,,
3c078d1b-beea-443f-bc87-2f4cb910c401,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"For linkage to occur, two conditions must be met:",False,"For linkage to occur, two conditions must be met:",,,,
2d98cce9-cfea-4a0b-9a1a-06d690050d96,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Syntenic genes may become detached from one another through crossing over (or recombination). For large chromosomes, crossing over is so common that genes at opposite ends of the chromosome are inherited together no more often than if they resided on entirely different chromosomes.",True,"For linkage to occur, two conditions must be met:",,,,
f9b2e917-782b-4181-a0fb-079b68665646,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"When markers are close enough together on the same chromosome, crossing over fails to separate them frequently enough for them to be inherited independently of one another. This is evidenced by coinheritance of greater than 50 percent.",True,"For linkage to occur, two conditions must be met:",,,,
eb294ce2-2586-4d0b-b2b7-5c0f34263c60,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"The unit of measure in linkage studies is “centimorgans.” This concept can be confusing because we refer to the “distance” between two traits, but what is measured experimentally is the frequency of coinheritance, not physical distance.",True,"For linkage to occur, two conditions must be met:",,,,
ae5d3ac8-33e1-4a27-b3e6-db394b8a2f20,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
ae5d3ac8-33e1-4a27-b3e6-db394b8a2f20,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
ae5d3ac8-33e1-4a27-b3e6-db394b8a2f20,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
ae5d3ac8-33e1-4a27-b3e6-db394b8a2f20,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
497dd710-08fb-4955-a4c2-81ae5e13c2a8,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"The further apart two genes or markers are on the same chromosome increases the probability of a crossover occurring in between the two markers. Studies to determine linkage require the careful study of large numbers of parents and their offspring. Careful study of the family relationships across three generations allows linkage phases to be determined. In this case, the grandparents’ information is required to determine how the genes are initially linked in the parents, and the grandchildren are studied to determine recombination events (crossing over) that separate the genes or markers during meiosis in the parents.",True,"For linkage to occur, two conditions must be met:",,,,
65b6c98a-2ea5-4668-ac86-efa508e6c093,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Distance can be expressed in cM as described previously, or in terms of theta (θ), which are proportions. Remember, both are measures of probability, not physical distance. Linkage determinations are based on the fundamental rules of probability and binomial mathematics. Like any probability issue, a ratio greater than one reflects odds in favor (of linkage), and less than one reflects odds against.",True,"For linkage to occur, two conditions must be met:",,,,
171af539-5100-48a0-8ab6-8d4f46283d5f,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"For linkage studies, each family represents an independent estimate of the odds in favor of (or against) linkage. The property within standard probability laws is the concept of joint probability. To determine joint probability, meaning the chance that BOTH of two events will happen, we use what is often called the “AND rule.” The AND rule applies whenever the probabilities under study are independent of one another.",True,"For linkage to occur, two conditions must be met:",,,,
1f90e09a-b5aa-45f6-a63b-546ef5202869,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Multiplying the results of many families is challenging, and was particularly so before computer resources became readily available. It is simpler mathematically to add numbers. We can move from multiplication to addition if we simply use the log of the probability instead of the probability number itself. Remember that the log of a number that is less than one is a negative number, and for a number greater than one, it is a positive number. Using a log conversion makes it simple to see if the ratio of the odds is favorable (positive) or unfavorable. The term “LOD score” refers to the log (base 10) of the odds of linkage, looking across a series of independent families.",True,"For linkage to occur, two conditions must be met:",,,,
4601a7b2-771e-4da6-88fa-f5a93e3b674d,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,There really are just two things to remember about LOD scores:,True,"For linkage to occur, two conditions must be met:",,,,
cd34e71c-2579-4f67-88ee-2d838784881d,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Genome-wide association studies (GWAS),False,Genome-wide association studies (GWAS),,,,
4485750f-cc86-47a0-b9ef-7e98437dbc36,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Population association is easily confused with the concepts surrounding linkage. These studies look for a statistical association between a marker (often a single nucleotide polymorphism or SNP) and a specific trait. The concept of population association can be exploited to simultaneously study a very large number of detectable genetic markers (SNPs) in patient populations with common disorders.,True,Genome-wide association studies (GWAS),,,,
08412255-fba7-4fdb-9894-89a6cb44eb5c,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
08412255-fba7-4fdb-9894-89a6cb44eb5c,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
08412255-fba7-4fdb-9894-89a6cb44eb5c,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
08412255-fba7-4fdb-9894-89a6cb44eb5c,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
1e497a94-fe98-48c1-9cbb-98aa9c03cbd7,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"For more information on these types of studies, please see: https://www.genome.gov/20019523/geno…ies-factsheet/.",True,Genome-wide association studies (GWAS),,,,
097f4e70-f754-4610-8ac4-89ae16170e75,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,14.3 References and resources,True,Genome-wide association studies (GWAS),,,,
5513ddd9-aaf7-40db-bab3-6478fe735e82,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Genome-wide association studies (GWAS),,,,
e40df908-ff0d-4ab4-9786-00150631bb48,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Genome-wide association studies (GWAS),,,,
b85a4335-7578-4157-9755-dccf7d06a658,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Genome-wide association studies (GWAS),,,,
5bf319ac-4c83-4e57-be74-aa298482cdec,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
5bf319ac-4c83-4e57-be74-aa298482cdec,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
5bf319ac-4c83-4e57-be74-aa298482cdec,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
5bf319ac-4c83-4e57-be74-aa298482cdec,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
57dcba38-1434-4014-a4f2-04288a679653,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
57dcba38-1434-4014-a4f2-04288a679653,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
57dcba38-1434-4014-a4f2-04288a679653,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
57dcba38-1434-4014-a4f2-04288a679653,https://pressbooks.lib.vt.edu/cellbio/,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-2,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
fd2d953d-9b26-4124-8158-7a7767f7aa73,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Population genetics,False,Population genetics,,,,
1fb03769-b84d-44a8-9a12-d41f9204b6e0,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"It is important to remember that these inheritance patterns are not characteristic of all genetic traits, and there are many factors that influence an individual’s phenotype.",True,Population genetics,,,,
4cf077f8-2df3-438c-bc48-5b8ec6c52626,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Traits can be either dominant or recessive in nature such that in the case of dominant traits conditions manifest in heterozygotes (individuals with just one copy of the mutant allele).,True,Population genetics,,,,
77db951d-f3d8-4f99-bbc9-9db55aac9923,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Recessive traits,False,Recessive traits,,,,
510b7086-651f-4507-9e24-34e1b1e1d73e,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"When speaking of the children of carrier parents, two-thirds of the healthy siblings of an affected child are heterozygous carriers.",True,Recessive traits,,,,
fb5c012a-48b6-464f-8d93-89515a5a489f,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"If an individual with an autosomal recessive disorder has children, a disease-causing mutation will be transmitted to all of them (either of the two mutant alleles). The consequences for the child depends on this individual’s partner. If the partner is homozygous for the normal allele of the respective gene (as in the majority of cases), all offspring will be nonaffected heterozygous carriers. If the partner, however, is a carrier (the likelihood is approximately 0.5 to 1 percent for the more frequent recessive disorders), statistically, half of the offspring will be affected (homozygous or compound heterozygous), and the other half will be carriers. If both partners should have the same recessive disorder (caused by mutations in the same gene), all offspring will be homozygous/compound heterozygous and affected.",True,Recessive traits,,,,
a5bf7239-8c65-4721-89fc-e9cea76b71d3,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,nonaffected,False,nonaffected,,,,
7f551e1b-516f-4e90-925d-3f312be1c340,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Dominant traits,False,Dominant traits,,,,
759c773b-2b84-444e-b7b2-61b57da2d0e2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Semidominance or incomplete dominance,False,Semidominance or incomplete dominance,,,,
e2746187-faad-4e82-b34e-b47946be737a,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"For most disorders inherited as dominant traits, homozygosity for a disease-causing mutation results in a much more severe clinical phenotype than heterozygosity. An example is familial hypercholesterolemia, a genetic disorder resulting from mutations of the low-density lipoprotein (LDL) receptor gene. Individuals with a heterozygous loss-of-function mutation show elevated LDL cholesterol levels (greater than 7 to 10 mmol/ L) and typically suffer their first myocardial infarction in midlife. Homozygous individuals have a much higher LDL cholesterol level (10 to 30 mmol/ L), with the onset of symptoms in early childhood and coronary heart disease as early as school age.",True,Semidominance or incomplete dominance,,,,
3f9e6dbb-fb22-4676-8b9b-08ac69897766,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"In these examples, the phenotype of heterozygotes (Aa) is somewhere in between the phenotypes of wild-type and mutant homozygotes (AA and aa). The inheritance pattern is called semidominant or incompletely dominant, in contrast to complete dominance that is found in very few conditions, such as Huntington’s disease, in which the phenotype of the heterozygous and homozygous mutation carriers is more or less identical. It is worth thinking about reasons why a condition may show complete penetrance. For practical purposes, both types of conditions may be called dominant because the definition rests on the clinical phenotype in the heterozygote, irrespective of what is observed in the homozygote.",True,Semidominance or incomplete dominance,,,,
bf9704df-a6df-4a69-b85b-ed9897ae6982,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Codominance,False,Codominance,,,,
3ffc28af-7fba-43f9-95b4-c7d09341da10,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"There are a few cases in which two alleles of the same gene code for proteins with different specific functions, both of which may be found simultaneously in (compound) heterozygous individuals. Such alleles are said to be codominant to each other. The classic example is the ABO blood group system, in which individuals with genotype AB show phenotypic characteristics of allele A as well as allele B, and there is also a null allele that causes complete loss of protein function.",True,Codominance,,,,
9cc223b0-5445-4ad7-9413-acabeb03fd41,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Sex-linked traits,False,Sex-linked traits,,,,
3f97484e-3b33-4203-8667-f2338f035aee,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"X-linked recessive traits do not typically manifest when there is a normal copy of the gene (e.g., in females). In contrast nearly all X-linked recessive traits are fully evident in males because they only have one copy of the X chromosome, and thus do not have a normal copy of the gene to compensate for the mutant copy. For that same reason, women are rarely affected by X-linked recessive diseases, however, they are affected when they have two copies of the mutant allele.",True,Sex-linked traits,,,,
f5d99446-eb08-41cc-86b4-0be781f61cc5,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,If a man is affected with an X-linked recessive condition:,False,If a man is affected with an X-linked recessive condition:,,,,
ec325fac-e31b-4cc1-9f23-40b87af3c830,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"X-linked dominant disorders clinically manifest when only one copy of the mutant allele is present. There is no transmission from father to son, but there can be transmission from father to daughter (all daughters of an affected male will be affected since the father has only one X chromosome to transmit). Children of an affected woman have a 50 percent chance of inheriting the X chromosome with the mutant allele. Phenotypic presentation of X-linked traits can be influenced by lyonization or X-inactivation. As one X chromosome is randomly expressed in all female cells, the differential patterns of X-inactivation can alter phenotype in female carriers of X-linked recessive disorders and X-linked dominant disorders.",True,If a man is affected with an X-linked recessive condition:,,,,
d8b465dc-bc0b-4e1a-a008-df379e4dfe26,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Calculation of risk,False,Calculation of risk,,,,
462ada91-2a10-4f73-ab1c-ddd993f34c41,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"One of the most important considerations of genetic counseling is calculating risk. Mathematics is only the first step; equally important is communicating the probability that the event will occur. There are a number of ways to say that an event will not occur with absolute certainty. Studies have shown that these terms are understood and evaluated differently by different individuals. Another factor that varies between patients is that events are evaluated according to whether the result will be considered positive or negative and by which consequences they will have. For example, the probability that, beginning at age forty-five, mothers have a 5 percent risk of giving birth to a child with a chromosomal disorder is generally considered a high risk. In cancer, on the other hand, a survival chance of 5 percent is considered low.",True,Calculation of risk,,,,
a18eb162-afd9-4133-a89b-e1e7e321aecd,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Hardy-Weinberg equations,False,Hardy-Weinberg equations,,,,
e61d981e-6d34-4216-8ca6-01d11ca8aa4a,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"The Hardy-Weinberg law rests on the assumption that there are two different alleles at a certain locus; these alleles are named “p” and “q” (i.e., a normal allele [traditionally p] and a variant allele [traditionally q]). Since there are only these two alleles, p + q = 1.",True,Hardy-Weinberg equations,,,,
8a603fda-aa12-436d-91d4-94e865abf852,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"In humans, if the respective gene occurs in two copies on only one autosome, the frequency of the three possible genotypes is calculated from the binominal distribution, which is often represented as:",True,Hardy-Weinberg equations,,,,
4b2ce1d0-2c93-4c89-a962-c7130d61aa82,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,p2 + 2pq + q2 = 1,False,p2 + 2pq + q2 = 1,,,,
d783874f-d16e-4b11-9b5e-9a8a0ef1429f,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,p is the frequency of the ʻAʼ allele,False,p is the frequency of the ʻAʼ allele,,,,
4e3417cb-4555-4fa2-9ef9-792221268d67,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,q is the frequency of the ʻaʼ allele,False,q is the frequency of the ʻaʼ allele,,,,
b8ade5a5-6f8f-4d99-a6c9-46e2440db425,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,p2 = the frequency of the AA genotype,False,p2 = the frequency of the AA genotype,,,,
5b11cd9a-082e-4998-bd20-03d7850ff8ad,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,q2 = the frequency of the aa genotype,False,q2 = the frequency of the aa genotype,,,,
392e0db6-7c3c-4c66-8c56-25bda5a0e4c2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,2pq = the frequency of the Aa genotype,False,2pq = the frequency of the Aa genotype,,,,
42e39642-dd3d-43b6-9e98-fba155e75604,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,The Hardy-Weinberg law only applies to an “ideal population” that meets the following criteria:,True,2pq = the frequency of the Aa genotype,,,,
26a614f4-9ed2-46be-84bb-f4d3f813a4f6,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"The one factor that has practical implications among this group of criteria is random mating, since the Hardy-Weinberg law cannot be applied if there is frequent intermarriage. In such cases, rare recessive disorders occur with much greater frequency than would be expected from the frequency of heterozygosity. The other criteria are more relevant to whether or not the allele or genotype frequencies remain constant or whether the incidence of a disorder changes.",True,2pq = the frequency of the Aa genotype,,,,
bbe9fc07-d2c4-45a1-ba90-13a860a36bc3,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Cystic fibrosis is a recessive condition that affects 1/2,500 births in the Caucasian population:",True,2pq = the frequency of the Aa genotype,,,,
b52b1e79-1b56-4b84-af44-61610ed10a4d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Frequency of the recessive allele:,False,Frequency of the recessive allele:,,,,
66f21237-5e26-427d-850b-72f62725ee24,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"q2 = 1/2,500 = 0.0004",True,Frequency of the recessive allele:,,,,
10f2a2df-88de-4596-8694-ec58f90640f4,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,q = 0.02,True,Frequency of the recessive allele:,,,,
99071944-f62e-4536-9beb-c4891c902a85,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Frequency of the dominant allele:,False,Frequency of the dominant allele:,,,,
be54c1c0-d48c-4e6e-b70a-2d38b0264e3c,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,1 – 0.02 = 0.98 = p,True,Frequency of the dominant allele:,,,,
5a42fa47-3d4f-4243-846c-584e6d905abf,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,14.1 References and resources,True,Frequency of the dominant allele:,,,,
0a4eba50-a570-48fb-a001-f33943a32f9d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Frequency of the dominant allele:,,,,
bb20f14c-13fa-4f83-a2ad-af5b0e15e0d8,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Frequency of the dominant allele:,,,,
8404c287-a247-48cc-af5c-272114a922b2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Frequency of the dominant allele:,,,,
01009b22-6b23-4e98-9f58-9304882e75d4,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
01009b22-6b23-4e98-9f58-9304882e75d4,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
01009b22-6b23-4e98-9f58-9304882e75d4,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
01009b22-6b23-4e98-9f58-9304882e75d4,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
0641d674-7a25-4885-98ff-82b50b5b55d1,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
0641d674-7a25-4885-98ff-82b50b5b55d1,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
0641d674-7a25-4885-98ff-82b50b5b55d1,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
0641d674-7a25-4885-98ff-82b50b5b55d1,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
9a0f8cfc-1791-4960-a262-4c76c6902d1b,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Additional resources,False,Additional resources,,,,
3e62f202-c5e2-435f-9389-114f592682df,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,14.2 Non-Mendelian Inheritance,True,Additional resources,,,,
fe689a68-907a-4613-a4a8-d5ebe8916318,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"The majority of genetic disorders are not inherited in a Mendelian fashion. Even in cases where Mendelian genetics can predict genotype, the disease phenotype may not be displayed or may be variable due to external influences. This section describes some additional factors that influence presentation and inheritance patterns.",True,Additional resources,,,,
bde10d3b-1f79-4c7d-a523-4c92dc7a85c2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
bde10d3b-1f79-4c7d-a523-4c92dc7a85c2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
bde10d3b-1f79-4c7d-a523-4c92dc7a85c2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
bde10d3b-1f79-4c7d-a523-4c92dc7a85c2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
486cbf5e-99e5-4932-be5c-73da78db98b6,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
486cbf5e-99e5-4932-be5c-73da78db98b6,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
486cbf5e-99e5-4932-be5c-73da78db98b6,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
486cbf5e-99e5-4932-be5c-73da78db98b6,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
8ffc74ab-c569-41de-a41e-3664a9a374df,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Extranuclear inheritance,False,Extranuclear inheritance,,,,
f1fd3cc5-58f6-4a34-b07f-5d519173d50d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Mitochondria are unique in that they have multiple copies of a circular chromosome. This DNA is independent of nuclear DNA and inherited from the mother.,True,Extranuclear inheritance,,,,
3c9a8f2f-71ea-4144-aa11-c641f4917eb2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
3c9a8f2f-71ea-4144-aa11-c641f4917eb2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
3c9a8f2f-71ea-4144-aa11-c641f4917eb2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
3c9a8f2f-71ea-4144-aa11-c641f4917eb2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
df459e2b-427d-4eb4-8583-ec90de9603e9,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Heteroplasmy is a term referring to the diversity of the mitochondrial genome within each cell. During cell division, mitochondria are divided randomly between the two daughter cells, and therefore the percentage of affected mitochondrial DNA (mtDNA) will also be variable within the offspring. The mitochondria generate energy for the rest of the cell, therefore disease transmitted through mitochondrial inheritance affects high-energy organs (this is a good example of pleiotropy).",True,Extranuclear inheritance,,,,
00cd124f-caec-43ad-b8c6-896992781d3a,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Genomic imprinting,False,Genomic imprinting,,,,
f2501ae1-05ae-427a-9bbf-f886a698b6f0,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Genetic information is not just stored in the actual code (e.g., ATCG), but also for many genes hereditary information is transmitted with a parental-specific imprint based on whether the gene was transmitted from the father or from the mother. This imprint can be thought of as the font of the genome (e.g., ATCG vs. ATCG vs. ATCG). For these imprinted genes, even though the nucleotide sequence in the maternal and paternal copies is identical, the expression differs depending on the parental imprint. Genomic imprinting is the most well-characterized epigenetic transmission of gene regulation. Often in cases, the imprinting of one allele is essential for a normal phenotype, and loss of imprinting or uniparental disomy (inheritance of both loci from a single parental source) can cause inappropriate expression patterns.",True,Genomic imprinting,,,,
5020306d-8b35-49b0-ba05-b003137443e2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,ATCG,False,ATCG,,,,
3754e7f0-2868-4390-a6b2-c9a2c5706660,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Differential methylation of genomic DNA is a central mechanism in the regulation of the expression of genes. Of special importance is the methylation of cytosine in CpG (cytosine-phosphorus-guanine) dinucleotides. Many genes have numerous “CpG islands” with a large number of CpG dinucleotides located upstream of the transcriptional start. Hypermethylation in this region results in transcriptional silencing, meaning the gene can no longer be read. The methylation pattern of DNA and, consequently, the activity pattern of the genes are generally transmitted as a stable trait in mitosis; however, for imprinted or epigenetically sensitive genes, this “trait” is reset in meiosis.",True,ATCG,,,,
87f5a4e5-f292-455a-b2e3-c57c5511b94d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Trinucleotide repeat disorders,False,Trinucleotide repeat disorders,,,,
9f7fa100-f8a5-4240-afdc-52feb9019fa9,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
9f7fa100-f8a5-4240-afdc-52feb9019fa9,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
9f7fa100-f8a5-4240-afdc-52feb9019fa9,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
9f7fa100-f8a5-4240-afdc-52feb9019fa9,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
cae66ad1-db21-492a-8c6b-04cae2fa10ae,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Triplicate repeat disorders are also characteristic of anticipation where the affected phenotype of individuals becomes progressively worse with each generation. Classic repeat disorders include Fragile X and Huntingtonʼs disease. In the case of Fragile X, the repeated region becomes hypermethylated and the methylation pattern expands into the promoter region for the gene. This will lead to silencing of the transcript. The gene itself, FMR1, is involved in mRNA splicing, and the loss of this gene product has a pleiotropic effect.",True,Trinucleotide repeat disorders,,,,
8b1f562b-317a-43ef-9ef5-4dede21e8540,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,14.2 References and resources,True,Trinucleotide repeat disorders,,,,
86b62291-d846-493f-89b7-3a98b8e38ce0,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Text,False,Text,,,,
05d7be02-c97f-4c9b-8540-1e4aca3570c5,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
05d7be02-c97f-4c9b-8540-1e4aca3570c5,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
05d7be02-c97f-4c9b-8540-1e4aca3570c5,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
05d7be02-c97f-4c9b-8540-1e4aca3570c5,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
2c733af0-853e-4aa5-bbb9-656bee64b196,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
2c733af0-853e-4aa5-bbb9-656bee64b196,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
2c733af0-853e-4aa5-bbb9-656bee64b196,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
2c733af0-853e-4aa5-bbb9-656bee64b196,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
6e9cfde7-29ea-4998-b48b-459f3f706e7d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
6e9cfde7-29ea-4998-b48b-459f3f706e7d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
6e9cfde7-29ea-4998-b48b-459f3f706e7d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
6e9cfde7-29ea-4998-b48b-459f3f706e7d,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
c64f48b3-e4cc-4f63-8db0-61e778bf3b28,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),True,Text,,,,
237526a3-3cb2-462e-b0a4-9441a905d52c,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"There is tremendous interest in finding specific genes that predispose individuals to common disease traits, most of which follow complex inheritance patterns rather than Mendelian (single gene) patterns. Physicians will find frequent references in the medical literature related to the search for genes with high predictive value in common disorders.",True,Text,,,,
16378eda-75e9-426b-8f5e-1f885d761e5a,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"While we know the DNA sequence of the vast majority of the coding regions of the genome, we still do not understand the full function of the majority of genes or how they are involved in human health conditions. There are two major approaches to identifying genetic loci, which contribute to disease presentation: linkage analysis and genome-wide association studies.",True,Text,,,,
e6baf670-a04d-4e87-ae46-b00cefcb0368,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Linkage analysis,False,Linkage analysis,,,,
53dd672c-c5ce-49bf-8d77-2e910142e44f,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Linkage analysis relies on the fact that disease-causing mutations are inherited jointly (linked) with genetic markers located in their immediate vicinity. In order for a gene and a genetic marker to be linked, they must be syntenic, meaning they must be located on the same chromosome. Most genes or markers within the human genome are inherited independently of one another, and therefore are transmitted together 50 percent of the time.",True,Linkage analysis,,,,
92da1e1a-5b4e-492d-8b97-e0f96dbbffdb,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Linkage between two genes means that they tend to be inherited together more often than expected by chance.,True,Linkage analysis,,,,
a3082071-c2d0-4b28-9388-08c9726ed3ca,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"For linkage to occur, two conditions must be met:",False,"For linkage to occur, two conditions must be met:",,,,
f2dc3668-d5b6-4422-a7d1-80e7b28b00db,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Syntenic genes may become detached from one another through crossing over (or recombination). For large chromosomes, crossing over is so common that genes at opposite ends of the chromosome are inherited together no more often than if they resided on entirely different chromosomes.",True,"For linkage to occur, two conditions must be met:",,,,
4ffb6582-95d2-4be2-a3ce-19a294730bc8,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"When markers are close enough together on the same chromosome, crossing over fails to separate them frequently enough for them to be inherited independently of one another. This is evidenced by coinheritance of greater than 50 percent.",True,"For linkage to occur, two conditions must be met:",,,,
f803f40e-6288-4020-a8b4-cd76d6008b93,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"The unit of measure in linkage studies is “centimorgans.” This concept can be confusing because we refer to the “distance” between two traits, but what is measured experimentally is the frequency of coinheritance, not physical distance.",True,"For linkage to occur, two conditions must be met:",,,,
4a59bf47-82e5-44b9-b87d-6a3e1430b428,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
4a59bf47-82e5-44b9-b87d-6a3e1430b428,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
4a59bf47-82e5-44b9-b87d-6a3e1430b428,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
4a59bf47-82e5-44b9-b87d-6a3e1430b428,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
700d2262-d3cc-4c65-b870-2b10a8e7f80b,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"The further apart two genes or markers are on the same chromosome increases the probability of a crossover occurring in between the two markers. Studies to determine linkage require the careful study of large numbers of parents and their offspring. Careful study of the family relationships across three generations allows linkage phases to be determined. In this case, the grandparents’ information is required to determine how the genes are initially linked in the parents, and the grandchildren are studied to determine recombination events (crossing over) that separate the genes or markers during meiosis in the parents.",True,"For linkage to occur, two conditions must be met:",,,,
89f0355f-2ea8-4fbd-b989-810b3fae12a2,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Distance can be expressed in cM as described previously, or in terms of theta (θ), which are proportions. Remember, both are measures of probability, not physical distance. Linkage determinations are based on the fundamental rules of probability and binomial mathematics. Like any probability issue, a ratio greater than one reflects odds in favor (of linkage), and less than one reflects odds against.",True,"For linkage to occur, two conditions must be met:",,,,
ead89eb7-31c5-4a69-9e91-07caa8eb9dd7,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"For linkage studies, each family represents an independent estimate of the odds in favor of (or against) linkage. The property within standard probability laws is the concept of joint probability. To determine joint probability, meaning the chance that BOTH of two events will happen, we use what is often called the “AND rule.” The AND rule applies whenever the probabilities under study are independent of one another.",True,"For linkage to occur, two conditions must be met:",,,,
c0bf70bf-f82f-49a3-ad03-07a50571c029,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Multiplying the results of many families is challenging, and was particularly so before computer resources became readily available. It is simpler mathematically to add numbers. We can move from multiplication to addition if we simply use the log of the probability instead of the probability number itself. Remember that the log of a number that is less than one is a negative number, and for a number greater than one, it is a positive number. Using a log conversion makes it simple to see if the ratio of the odds is favorable (positive) or unfavorable. The term “LOD score” refers to the log (base 10) of the odds of linkage, looking across a series of independent families.",True,"For linkage to occur, two conditions must be met:",,,,
f64ba992-9332-4778-8713-3735d6836434,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,There really are just two things to remember about LOD scores:,True,"For linkage to occur, two conditions must be met:",,,,
f7e9b0e4-1578-4a61-bbb1-f33757b39a5f,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Genome-wide association studies (GWAS),False,Genome-wide association studies (GWAS),,,,
7031fe7b-5195-4a15-afb3-5d27b7a981ea,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Population association is easily confused with the concepts surrounding linkage. These studies look for a statistical association between a marker (often a single nucleotide polymorphism or SNP) and a specific trait. The concept of population association can be exploited to simultaneously study a very large number of detectable genetic markers (SNPs) in patient populations with common disorders.,True,Genome-wide association studies (GWAS),,,,
cf6e1cdd-b7c7-451a-9c9d-212b6b9d5df0,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
cf6e1cdd-b7c7-451a-9c9d-212b6b9d5df0,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
cf6e1cdd-b7c7-451a-9c9d-212b6b9d5df0,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
cf6e1cdd-b7c7-451a-9c9d-212b6b9d5df0,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
b60f55cb-7366-477b-a016-057df458f93a,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"For more information on these types of studies, please see: https://www.genome.gov/20019523/geno…ies-factsheet/.",True,Genome-wide association studies (GWAS),,,,
d9982dc2-5cc5-4d42-a6b5-744262fe6f1e,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,14.3 References and resources,True,Genome-wide association studies (GWAS),,,,
9b8be513-ebe2-4319-9fa0-3ca859a4d438,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Genome-wide association studies (GWAS),,,,
a49b594b-093d-4df7-89c7-6166a512aa0f,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Genome-wide association studies (GWAS),,,,
834304d1-1b9d-4c27-a668-8fca5a0f7447,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Genome-wide association studies (GWAS),,,,
4b3d3238-ae41-4efd-88bc-a41a54b96424,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
4b3d3238-ae41-4efd-88bc-a41a54b96424,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
4b3d3238-ae41-4efd-88bc-a41a54b96424,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
4b3d3238-ae41-4efd-88bc-a41a54b96424,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
56f488e8-0f4a-4552-827e-a639a2a5ca34,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
56f488e8-0f4a-4552-827e-a639a2a5ca34,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
56f488e8-0f4a-4552-827e-a639a2a5ca34,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
56f488e8-0f4a-4552-827e-a639a2a5ca34,https://pressbooks.lib.vt.edu/cellbio/,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/#chapter-96-section-1,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
225a2eef-d2aa-46a2-b41f-d34cc3a23b0e,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Population genetics,False,Population genetics,,,,
0ac7c97b-200c-4e8e-b986-008de7932f40,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"It is important to remember that these inheritance patterns are not characteristic of all genetic traits, and there are many factors that influence an individual’s phenotype.",True,Population genetics,,,,
74e94be8-55c4-461f-9105-0bfe227c0041,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Traits can be either dominant or recessive in nature such that in the case of dominant traits conditions manifest in heterozygotes (individuals with just one copy of the mutant allele).,True,Population genetics,,,,
f09f0857-09e7-44d5-bb8e-8d5a24ea16d3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Recessive traits,False,Recessive traits,,,,
953c99fe-4893-4865-b03d-282105528bbe,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"When speaking of the children of carrier parents, two-thirds of the healthy siblings of an affected child are heterozygous carriers.",True,Recessive traits,,,,
27df1b8a-7651-4356-84bf-0a2c35b04fa4,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"If an individual with an autosomal recessive disorder has children, a disease-causing mutation will be transmitted to all of them (either of the two mutant alleles). The consequences for the child depends on this individual’s partner. If the partner is homozygous for the normal allele of the respective gene (as in the majority of cases), all offspring will be nonaffected heterozygous carriers. If the partner, however, is a carrier (the likelihood is approximately 0.5 to 1 percent for the more frequent recessive disorders), statistically, half of the offspring will be affected (homozygous or compound heterozygous), and the other half will be carriers. If both partners should have the same recessive disorder (caused by mutations in the same gene), all offspring will be homozygous/compound heterozygous and affected.",True,Recessive traits,,,,
1f1053b1-97be-4bd6-ae91-e3de01a77d84,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,nonaffected,False,nonaffected,,,,
9deb5ad0-20d1-4de6-a1ca-0d594e61bcd5,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Dominant traits,False,Dominant traits,,,,
9d654aba-a824-42c7-a986-6f8549c778c6,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Semidominance or incomplete dominance,False,Semidominance or incomplete dominance,,,,
f374e94d-1d35-464c-8443-29bf0a8607b4,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"For most disorders inherited as dominant traits, homozygosity for a disease-causing mutation results in a much more severe clinical phenotype than heterozygosity. An example is familial hypercholesterolemia, a genetic disorder resulting from mutations of the low-density lipoprotein (LDL) receptor gene. Individuals with a heterozygous loss-of-function mutation show elevated LDL cholesterol levels (greater than 7 to 10 mmol/ L) and typically suffer their first myocardial infarction in midlife. Homozygous individuals have a much higher LDL cholesterol level (10 to 30 mmol/ L), with the onset of symptoms in early childhood and coronary heart disease as early as school age.",True,Semidominance or incomplete dominance,,,,
7f7d8a8b-5a6e-417a-832c-78330649c644,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"In these examples, the phenotype of heterozygotes (Aa) is somewhere in between the phenotypes of wild-type and mutant homozygotes (AA and aa). The inheritance pattern is called semidominant or incompletely dominant, in contrast to complete dominance that is found in very few conditions, such as Huntington’s disease, in which the phenotype of the heterozygous and homozygous mutation carriers is more or less identical. It is worth thinking about reasons why a condition may show complete penetrance. For practical purposes, both types of conditions may be called dominant because the definition rests on the clinical phenotype in the heterozygote, irrespective of what is observed in the homozygote.",True,Semidominance or incomplete dominance,,,,
e434b80b-7afb-4993-91a4-eb667cb0a21a,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Codominance,False,Codominance,,,,
9bf680ad-9c28-46c3-aed7-001a005cf2ce,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"There are a few cases in which two alleles of the same gene code for proteins with different specific functions, both of which may be found simultaneously in (compound) heterozygous individuals. Such alleles are said to be codominant to each other. The classic example is the ABO blood group system, in which individuals with genotype AB show phenotypic characteristics of allele A as well as allele B, and there is also a null allele that causes complete loss of protein function.",True,Codominance,,,,
e69912fc-1a60-447e-a2aa-d8af90b1036c,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Sex-linked traits,False,Sex-linked traits,,,,
7d8d2334-5232-4fdc-968f-5a3e1e24eff6,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"X-linked recessive traits do not typically manifest when there is a normal copy of the gene (e.g., in females). In contrast nearly all X-linked recessive traits are fully evident in males because they only have one copy of the X chromosome, and thus do not have a normal copy of the gene to compensate for the mutant copy. For that same reason, women are rarely affected by X-linked recessive diseases, however, they are affected when they have two copies of the mutant allele.",True,Sex-linked traits,,,,
a41510b7-f39a-4f28-9c78-0e9cf789e257,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,If a man is affected with an X-linked recessive condition:,False,If a man is affected with an X-linked recessive condition:,,,,
74609bf9-57b6-4b58-997e-070b36002707,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"X-linked dominant disorders clinically manifest when only one copy of the mutant allele is present. There is no transmission from father to son, but there can be transmission from father to daughter (all daughters of an affected male will be affected since the father has only one X chromosome to transmit). Children of an affected woman have a 50 percent chance of inheriting the X chromosome with the mutant allele. Phenotypic presentation of X-linked traits can be influenced by lyonization or X-inactivation. As one X chromosome is randomly expressed in all female cells, the differential patterns of X-inactivation can alter phenotype in female carriers of X-linked recessive disorders and X-linked dominant disorders.",True,If a man is affected with an X-linked recessive condition:,,,,
1a1d4be4-afff-40ac-b57a-8cc92f70ea9b,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Calculation of risk,False,Calculation of risk,,,,
39f0e1ce-2fad-4d97-b1ca-fcad20dd2df6,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"One of the most important considerations of genetic counseling is calculating risk. Mathematics is only the first step; equally important is communicating the probability that the event will occur. There are a number of ways to say that an event will not occur with absolute certainty. Studies have shown that these terms are understood and evaluated differently by different individuals. Another factor that varies between patients is that events are evaluated according to whether the result will be considered positive or negative and by which consequences they will have. For example, the probability that, beginning at age forty-five, mothers have a 5 percent risk of giving birth to a child with a chromosomal disorder is generally considered a high risk. In cancer, on the other hand, a survival chance of 5 percent is considered low.",True,Calculation of risk,,,,
39e4f96a-1b03-4dae-b9ef-04ba95423ebb,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Hardy-Weinberg equations,False,Hardy-Weinberg equations,,,,
8a657b79-44ca-4c38-9cd1-3c229b27c424,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"The Hardy-Weinberg law rests on the assumption that there are two different alleles at a certain locus; these alleles are named “p” and “q” (i.e., a normal allele [traditionally p] and a variant allele [traditionally q]). Since there are only these two alleles, p + q = 1.",True,Hardy-Weinberg equations,,,,
3e36753b-1c60-425d-b938-57c597b04a47,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"In humans, if the respective gene occurs in two copies on only one autosome, the frequency of the three possible genotypes is calculated from the binominal distribution, which is often represented as:",True,Hardy-Weinberg equations,,,,
812af57d-1f35-4c26-85f4-e80fe199d2a3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,p2 + 2pq + q2 = 1,False,p2 + 2pq + q2 = 1,,,,
053a9cd9-3b4b-4b1b-aea2-079bbcc74556,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,p is the frequency of the ʻAʼ allele,False,p is the frequency of the ʻAʼ allele,,,,
8b4e8d0d-104e-4d21-a21e-e39172737818,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,q is the frequency of the ʻaʼ allele,False,q is the frequency of the ʻaʼ allele,,,,
bc5efc7f-4766-40fb-b765-7fac91d0eed4,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,p2 = the frequency of the AA genotype,False,p2 = the frequency of the AA genotype,,,,
64f2fc21-484b-4bf7-b7f5-fc48e285fa64,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,q2 = the frequency of the aa genotype,False,q2 = the frequency of the aa genotype,,,,
c1dab7d4-fa43-4dbc-94c3-0df02a0115a2,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,2pq = the frequency of the Aa genotype,False,2pq = the frequency of the Aa genotype,,,,
aeb6c914-6e88-4c00-934d-b5e4b908e149,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,The Hardy-Weinberg law only applies to an “ideal population” that meets the following criteria:,True,2pq = the frequency of the Aa genotype,,,,
800acd7d-913a-4f4b-a024-817646f26eff,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"The one factor that has practical implications among this group of criteria is random mating, since the Hardy-Weinberg law cannot be applied if there is frequent intermarriage. In such cases, rare recessive disorders occur with much greater frequency than would be expected from the frequency of heterozygosity. The other criteria are more relevant to whether or not the allele or genotype frequencies remain constant or whether the incidence of a disorder changes.",True,2pq = the frequency of the Aa genotype,,,,
77aa6e0e-0bbf-4028-9373-387b4782ae45,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Cystic fibrosis is a recessive condition that affects 1/2,500 births in the Caucasian population:",True,2pq = the frequency of the Aa genotype,,,,
45d85511-58cf-4a52-92f1-ed334011ce26,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Frequency of the recessive allele:,False,Frequency of the recessive allele:,,,,
27719826-4a15-4a6c-998e-6b3166d37863,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"q2 = 1/2,500 = 0.0004",True,Frequency of the recessive allele:,,,,
7709222b-983f-4787-ae93-c7b82d0a2b3b,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,q = 0.02,True,Frequency of the recessive allele:,,,,
596b7863-4c66-42d9-a138-b539c6caa8fc,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Frequency of the dominant allele:,False,Frequency of the dominant allele:,,,,
7353f112-90fa-46e6-8a41-23735a5f5b8e,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,1 – 0.02 = 0.98 = p,True,Frequency of the dominant allele:,,,,
12290f59-9a22-42c5-8bca-137907d8f6d2,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,14.1 References and resources,True,Frequency of the dominant allele:,,,,
9e094062-3fe0-43fe-b6fe-6d80993f9a61,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Frequency of the dominant allele:,,,,
ead93b24-0f07-4366-b16e-91b14beb9942,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Frequency of the dominant allele:,,,,
0ccc985c-1e34-4f4e-a2fe-ebc31d712074,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Frequency of the dominant allele:,,,,
53bc04d1-b547-455f-a75a-7d590fd985b5,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
53bc04d1-b547-455f-a75a-7d590fd985b5,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
53bc04d1-b547-455f-a75a-7d590fd985b5,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
53bc04d1-b547-455f-a75a-7d590fd985b5,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.1 Punnett square illustrating allelic distribution of recessive traits. 2021. https://archive.org/details/14.1_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.1,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
f6005107-168a-4b94-8b1f-7e99af17d1d1,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
f6005107-168a-4b94-8b1f-7e99af17d1d1,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
f6005107-168a-4b94-8b1f-7e99af17d1d1,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
f6005107-168a-4b94-8b1f-7e99af17d1d1,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.2 Allelic distributions in dominant traits. 2021. https://archive.org/details/14.2_20210926. CC BY 4.0.",True,Frequency of the dominant allele:,Figure 14.2,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
99ca818a-1a9e-4740-95d0-d1e178c8f972,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Additional resources,False,Additional resources,,,,
2b9a8953-4b0f-40f5-9286-890fdf87758b,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,14.2 Non-Mendelian Inheritance,True,Additional resources,,,,
9d8a85e6-9dbe-4f46-af0d-cc8e07e68bbd,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"The majority of genetic disorders are not inherited in a Mendelian fashion. Even in cases where Mendelian genetics can predict genotype, the disease phenotype may not be displayed or may be variable due to external influences. This section describes some additional factors that influence presentation and inheritance patterns.",True,Additional resources,,,,
3d5c5adb-5191-4399-9c76-33582b04381e,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
3d5c5adb-5191-4399-9c76-33582b04381e,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
3d5c5adb-5191-4399-9c76-33582b04381e,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
3d5c5adb-5191-4399-9c76-33582b04381e,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Penetrance refers to the display of any signs or symptoms if you have the genetic abnormality; this does not describe the variety of phenotype. As illustrated in figure 14.3, this refers to the number of “affected (purple)” versus “unaffected (white)” cells in an individual. Individuals with a greater number of purple cells may have a more pronounced phenotype than individuals with greater numbers of white cells.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
99fa6fb9-affe-470a-bc1f-34a9a8ba6944,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
99fa6fb9-affe-470a-bc1f-34a9a8ba6944,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
99fa6fb9-affe-470a-bc1f-34a9a8ba6944,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
99fa6fb9-affe-470a-bc1f-34a9a8ba6944,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Variable phenotypes can present due to changes in expressivity or pleiotropy. These terms refer to the variety of presentations from a single genetic disorder (variable expression). As illustrated in figure 14.3, expressivity can be a range of “purplish” colors, which may give rise to a variable phenotype. In other more complicated genetic cases, both penetrance and expressivity must be considered when making a diagnosis. Pleiotropy of a disorder is best described as a single gene disorder having implications on several different organ systems.",True,Additional resources,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
35d6c06a-1f58-47b6-97f1-36398a225881,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Extranuclear inheritance,False,Extranuclear inheritance,,,,
f37a5c6b-fb47-4451-8489-e90bb523e73c,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Mitochondria are unique in that they have multiple copies of a circular chromosome. This DNA is independent of nuclear DNA and inherited from the mother.,True,Extranuclear inheritance,,,,
3a007c33-fa27-4cab-aa17-fa19b025c3b3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
3a007c33-fa27-4cab-aa17-fa19b025c3b3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
3a007c33-fa27-4cab-aa17-fa19b025c3b3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
3a007c33-fa27-4cab-aa17-fa19b025c3b3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Therefore in this inheritance modality, the females can transmit the trait to all offspring (figure 14.4), however, only female offspring will continue to transmit the disorder. Disease phenotype in mitochondrial disease is extremely variable due to mitochondrial heteroplasmy.",True,Extranuclear inheritance,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
c304a696-e8a5-4047-8274-abdb5817caee,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Heteroplasmy is a term referring to the diversity of the mitochondrial genome within each cell. During cell division, mitochondria are divided randomly between the two daughter cells, and therefore the percentage of affected mitochondrial DNA (mtDNA) will also be variable within the offspring. The mitochondria generate energy for the rest of the cell, therefore disease transmitted through mitochondrial inheritance affects high-energy organs (this is a good example of pleiotropy).",True,Extranuclear inheritance,,,,
5ef2e74a-1ce5-484b-9754-378186daa4b3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Genomic imprinting,False,Genomic imprinting,,,,
43733abc-e23b-4069-bc60-fd12343d0d68,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Genetic information is not just stored in the actual code (e.g., ATCG), but also for many genes hereditary information is transmitted with a parental-specific imprint based on whether the gene was transmitted from the father or from the mother. This imprint can be thought of as the font of the genome (e.g., ATCG vs. ATCG vs. ATCG). For these imprinted genes, even though the nucleotide sequence in the maternal and paternal copies is identical, the expression differs depending on the parental imprint. Genomic imprinting is the most well-characterized epigenetic transmission of gene regulation. Often in cases, the imprinting of one allele is essential for a normal phenotype, and loss of imprinting or uniparental disomy (inheritance of both loci from a single parental source) can cause inappropriate expression patterns.",True,Genomic imprinting,,,,
379d4383-03d2-42d2-8f4f-3b14882c9440,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,ATCG,False,ATCG,,,,
40e8ba67-306c-4c70-8afa-3dd3869eee72,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Differential methylation of genomic DNA is a central mechanism in the regulation of the expression of genes. Of special importance is the methylation of cytosine in CpG (cytosine-phosphorus-guanine) dinucleotides. Many genes have numerous “CpG islands” with a large number of CpG dinucleotides located upstream of the transcriptional start. Hypermethylation in this region results in transcriptional silencing, meaning the gene can no longer be read. The methylation pattern of DNA and, consequently, the activity pattern of the genes are generally transmitted as a stable trait in mitosis; however, for imprinted or epigenetically sensitive genes, this “trait” is reset in meiosis.",True,ATCG,,,,
19441e2d-9892-47ad-abfc-846417bed221,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Trinucleotide repeat disorders,False,Trinucleotide repeat disorders,,,,
5aadb748-98ee-41d2-b38f-e61025051c78,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
5aadb748-98ee-41d2-b38f-e61025051c78,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
5aadb748-98ee-41d2-b38f-e61025051c78,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
5aadb748-98ee-41d2-b38f-e61025051c78,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Disorders in this category are caused by expansion of tandem trinucleotide repeats (figure 14.5). These repetitive regions can be within upstream regulatory elements or within the coding region themselves; typically these repeated regions are of low copy number. In each generation there is the potential for these repetitive sequences to expand, and the expansion will change gene expression.",True,Trinucleotide repeat disorders,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
f740b776-13e6-4b98-9a6d-0708bb23f898,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Triplicate repeat disorders are also characteristic of anticipation where the affected phenotype of individuals becomes progressively worse with each generation. Classic repeat disorders include Fragile X and Huntingtonʼs disease. In the case of Fragile X, the repeated region becomes hypermethylated and the methylation pattern expands into the promoter region for the gene. This will lead to silencing of the transcript. The gene itself, FMR1, is involved in mRNA splicing, and the loss of this gene product has a pleiotropic effect.",True,Trinucleotide repeat disorders,,,,
221ab7ff-2ca0-4193-a1f2-a9e6d9fd6973,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,14.2 References and resources,True,Trinucleotide repeat disorders,,,,
5849b7d8-aca4-4382-91e5-908363ddc03b,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Text,False,Text,,,,
369b5786-823e-41d2-a08d-aad5a264a728,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
369b5786-823e-41d2-a08d-aad5a264a728,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
369b5786-823e-41d2-a08d-aad5a264a728,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
369b5786-823e-41d2-a08d-aad5a264a728,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.3 Graphic representation of penetrance and expressivity. 2021. CC BY4.0. Adapted from Introduction to Genetic Analysis 7th Ed. Figure 4.33 The effects of penetrance and expressivity through a hypothetical character “pigment intensity. From NCBI.",True,Text,Figure 14.3,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
7e81f7bf-fce9-423f-a287-28819546e7df,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
7e81f7bf-fce9-423f-a287-28819546e7df,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
7e81f7bf-fce9-423f-a287-28819546e7df,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
7e81f7bf-fce9-423f-a287-28819546e7df,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.4 Mitochondrial inheritance pattern. 2021. https://archive.org/details/14.4_20210926. CC BY-SA 4.0. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons.",True,Text,Figure 14.4,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
000481c0-d9cc-4707-aa72-b4ced4664ef0,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
000481c0-d9cc-4707-aa72-b4ced4664ef0,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
000481c0-d9cc-4707-aa72-b4ced4664ef0,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
000481c0-d9cc-4707-aa72-b4ced4664ef0,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease. 2021.",True,Text,Figure 14.5,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
e3b70417-9f77-441d-8db3-3b6277816d7b,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),True,Text,,,,
802a9e94-296b-44e4-99d2-4ef4b9d8e038,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"There is tremendous interest in finding specific genes that predispose individuals to common disease traits, most of which follow complex inheritance patterns rather than Mendelian (single gene) patterns. Physicians will find frequent references in the medical literature related to the search for genes with high predictive value in common disorders.",True,Text,,,,
4b235ee6-5bb2-4f50-be9b-a764fc0135f3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"While we know the DNA sequence of the vast majority of the coding regions of the genome, we still do not understand the full function of the majority of genes or how they are involved in human health conditions. There are two major approaches to identifying genetic loci, which contribute to disease presentation: linkage analysis and genome-wide association studies.",True,Text,,,,
fa1f988a-ec09-4297-97ce-1045d2aced58,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Linkage analysis,False,Linkage analysis,,,,
37f3f8c3-6f0f-4513-a51c-5f3328b36e36,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Linkage analysis relies on the fact that disease-causing mutations are inherited jointly (linked) with genetic markers located in their immediate vicinity. In order for a gene and a genetic marker to be linked, they must be syntenic, meaning they must be located on the same chromosome. Most genes or markers within the human genome are inherited independently of one another, and therefore are transmitted together 50 percent of the time.",True,Linkage analysis,,,,
7fbc9017-67ee-4ad2-bf4a-885012ecc552,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Linkage between two genes means that they tend to be inherited together more often than expected by chance.,True,Linkage analysis,,,,
804eb37c-1f81-4a65-af76-aa1e0042b893,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"For linkage to occur, two conditions must be met:",False,"For linkage to occur, two conditions must be met:",,,,
e3b66617-13f9-443a-9f8f-8ee70efc0521,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Syntenic genes may become detached from one another through crossing over (or recombination). For large chromosomes, crossing over is so common that genes at opposite ends of the chromosome are inherited together no more often than if they resided on entirely different chromosomes.",True,"For linkage to occur, two conditions must be met:",,,,
175062d5-6831-4cce-9dc3-d7d1bacc340d,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"When markers are close enough together on the same chromosome, crossing over fails to separate them frequently enough for them to be inherited independently of one another. This is evidenced by coinheritance of greater than 50 percent.",True,"For linkage to occur, two conditions must be met:",,,,
f54d0e55-d75a-4d7c-a3e5-02359098565a,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"The unit of measure in linkage studies is “centimorgans.” This concept can be confusing because we refer to the “distance” between two traits, but what is measured experimentally is the frequency of coinheritance, not physical distance.",True,"For linkage to occur, two conditions must be met:",,,,
6b8ae1af-e1e1-4152-a9ed-13f561f172e7,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
6b8ae1af-e1e1-4152-a9ed-13f561f172e7,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
6b8ae1af-e1e1-4152-a9ed-13f561f172e7,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
6b8ae1af-e1e1-4152-a9ed-13f561f172e7,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"A very small linkage distance means the traits are rarely separated during meiosis. A distance of 0 cM means two traits always stay together, implying that they are extremely close to one another on the same chromosome. If the two traits separate from one another 1 percent of the time during meiosis, they are described as being 1 cM apart; if the two traits separate from one another 5 percent of the time during meiosis, they are described as being 5 cM apart (figure 14.6).",True,"For linkage to occur, two conditions must be met:",Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
23c327ae-e2ae-4f14-ac1c-129666e3b9d9,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"The further apart two genes or markers are on the same chromosome increases the probability of a crossover occurring in between the two markers. Studies to determine linkage require the careful study of large numbers of parents and their offspring. Careful study of the family relationships across three generations allows linkage phases to be determined. In this case, the grandparents’ information is required to determine how the genes are initially linked in the parents, and the grandchildren are studied to determine recombination events (crossing over) that separate the genes or markers during meiosis in the parents.",True,"For linkage to occur, two conditions must be met:",,,,
d6786938-b227-4b69-854c-a3d8d0e88679,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Distance can be expressed in cM as described previously, or in terms of theta (θ), which are proportions. Remember, both are measures of probability, not physical distance. Linkage determinations are based on the fundamental rules of probability and binomial mathematics. Like any probability issue, a ratio greater than one reflects odds in favor (of linkage), and less than one reflects odds against.",True,"For linkage to occur, two conditions must be met:",,,,
4c36ecad-6aa0-4a14-984d-cba04f7e5a27,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"For linkage studies, each family represents an independent estimate of the odds in favor of (or against) linkage. The property within standard probability laws is the concept of joint probability. To determine joint probability, meaning the chance that BOTH of two events will happen, we use what is often called the “AND rule.” The AND rule applies whenever the probabilities under study are independent of one another.",True,"For linkage to occur, two conditions must be met:",,,,
b5aebc4f-a95f-4aec-ba9b-47eba935c16c,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Multiplying the results of many families is challenging, and was particularly so before computer resources became readily available. It is simpler mathematically to add numbers. We can move from multiplication to addition if we simply use the log of the probability instead of the probability number itself. Remember that the log of a number that is less than one is a negative number, and for a number greater than one, it is a positive number. Using a log conversion makes it simple to see if the ratio of the odds is favorable (positive) or unfavorable. The term “LOD score” refers to the log (base 10) of the odds of linkage, looking across a series of independent families.",True,"For linkage to occur, two conditions must be met:",,,,
1a083c63-e20e-40b7-a33d-083a764565ed,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,There really are just two things to remember about LOD scores:,True,"For linkage to occur, two conditions must be met:",,,,
6da52296-206c-4d83-a156-877824d8a738,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Genome-wide association studies (GWAS),False,Genome-wide association studies (GWAS),,,,
9a202a22-ada0-4bd4-a644-4ebf9c5e5b60,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Population association is easily confused with the concepts surrounding linkage. These studies look for a statistical association between a marker (often a single nucleotide polymorphism or SNP) and a specific trait. The concept of population association can be exploited to simultaneously study a very large number of detectable genetic markers (SNPs) in patient populations with common disorders.,True,Genome-wide association studies (GWAS),,,,
84767488-1809-4bb7-b1d1-172e34d6eb87,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
84767488-1809-4bb7-b1d1-172e34d6eb87,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
84767488-1809-4bb7-b1d1-172e34d6eb87,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
84767488-1809-4bb7-b1d1-172e34d6eb87,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,Much of the power of personalized medicine is derived from such associations. There is an abundance of GWAS that appear in the medical literature. This is a highly sophisticated type of case-control study for which careful study design is required to avoid spurious findings. These studies provide information related to common genetic traits but do not help address genetic manifestations of rare traits in a population (figure 14.7).,True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
ef48d4e0-46fc-47a5-b9b7-f2a98468a307,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"For more information on these types of studies, please see: https://www.genome.gov/20019523/geno…ies-factsheet/.",True,Genome-wide association studies (GWAS),,,,
dd74585f-c027-43e3-9eb3-2b3ce3ab75dc,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,14.3 References and resources,True,Genome-wide association studies (GWAS),,,,
79b14852-270a-4c23-aa47-de2e40d4a382,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 12: Mendel’s Experiments and Heridity, Chapter 13: Modern Understandings of Inheritance.",True,Genome-wide association studies (GWAS),,,,
8b06cbcf-99b3-420b-936b-e6a74f20c9fb,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 55–59.",True,Genome-wide association studies (GWAS),,,,
9f74d102-ccc4-4795-a398-e377fb46be77,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 7: Patterns of Single Gene Inheritance, Chapter 9: Genetic Variations in Populations, Chapter 10: Identifying the Genetic Basis for Human Disease.",True,Genome-wide association studies (GWAS),,,,
d18070bf-37a6-4fa1-b1f9-637486c73ba3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
d18070bf-37a6-4fa1-b1f9-637486c73ba3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
d18070bf-37a6-4fa1-b1f9-637486c73ba3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
d18070bf-37a6-4fa1-b1f9-637486c73ba3,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Grey, Kindred, Figure 14.6 Relationship between centimorgans and recombination frequency. 2021. https://archive.org/details/14.6_20210926. CC BY 4.0.",True,Genome-wide association studies (GWAS),Figure 14.6,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
ecf8a263-2e4e-45c0-a2f8-2fbcb20c0049,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.3 Linkage Analysis and Genome-Wide Association Studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
ecf8a263-2e4e-45c0-a2f8-2fbcb20c0049,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.2 Non-Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
ecf8a263-2e4e-45c0-a2f8-2fbcb20c0049,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,14.1 Mendelian Inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
ecf8a263-2e4e-45c0-a2f8-2fbcb20c0049,https://pressbooks.lib.vt.edu/cellbio/,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/cellbio/chapter/linkage-studies-pedigrees-and-population-genetics/,"Tam, V., Patel, N., Turcotte, M. et al. Figure 14.7 Schematic of GWAS study. Adapted under Fair Use from Benefits and limitations of genome-wide association studies. Nat Rev Genet 20, 467–484 (2019). https://pubmed.ncbi.nlm.nih.gov/31068683/. Fig. 1: GWAS study design. Added Mitochondrial inheritance by Domaina, Angelito7 and SUM1. CC BY-SA 4.0. From Wikimedia Commons. Added Genetic similarities between 51 worldwide human populations (Euclidean genetic distance using 289,160 SNPs) by Tiago R. Magalhães, Jillian P. Casey, Judith Conroy, Regina Regan, Darren J. Fitzpatrick, Naisha Shah, João Sobral, Sean Ennis. CC BY 2.5. From Wikimedia Commons. Added Histopathology of adenosquamous carcinoma of the pancreas by Yeung, Vincent; Palmer, Joshua D.; Williams, Noelle; Weinstein, Jonathan C.; Fortuna, Danielle; Sama, Ashwin; Winter, Jordan; Bar-Ad, Voichita. CC BY 4.0. From Wikimedia Commons.",True,Genome-wide association studies (GWAS),Figure 14.7,"14. Linkage Studies, Pedigrees, and Population Genetics",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
a541c570-a5e2-440b-9ec0-c65c9906cb24,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Genetics methodology,False,Genetics methodology,,,,
bad8f8d1-1d3a-43e7-8392-5213c3c48a96,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
bad8f8d1-1d3a-43e7-8392-5213c3c48a96,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
bad8f8d1-1d3a-43e7-8392-5213c3c48a96,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
00d0547a-82e5-4e9e-a593-6b04edc988a8,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Chromosome structure,False,Chromosome structure,,,,
b42eb673-ec33-42c6-8265-56b815cbc845,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
b42eb673-ec33-42c6-8265-56b815cbc845,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
b42eb673-ec33-42c6-8265-56b815cbc845,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
1d6dde61-1836-4348-bdd4-04b37abc709a,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Nondisjunction,False,Nondisjunction,,,,
2d57684c-1779-483e-9269-0ab2600660c9,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
2d57684c-1779-483e-9269-0ab2600660c9,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
2d57684c-1779-483e-9269-0ab2600660c9,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
6be9bb20-9108-413d-a2d4-035d2d8e2402,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Table 13.1: Summary of meiotic and mitotic cell divisions.,True,Nondisjunction,,,,
0f8aaaa5-0a19-4cd6-bd72-8171aba3d86d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"These nondisjunction events can result in unequal distribution of chromosomes rendering a cell with an atypical chromosome number. A cell that is euploid would contain all twenty-three chromosomes, while polyploidy would suggest additional chromosomes within the cell. In humans, aneuploidy of autosomes are the most clinically important abnormalities to address, and the most common cause of this is a nondisjunction event.",True,Nondisjunction,,,,
312dc073-dcc8-4905-8bc8-1776534cee28,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Meiotic nondisjunction,False,Meiotic nondisjunction,,,,
4b2ca528-0100-41c6-8698-cd784fcbcfa2,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Normally, one copy of each chromosome is inherited from each parent; however, when there is nondisjunction at either anaphase I or anaphase II, gametes will contain either two copies or no copies of the chromosome, which failed to disjoin. At fertilization, when the gamete provided by the other parent contributes one copy of each chromosome, the newly formed zygote will instead possess three copies (trisomy) or one copy (monosomy) of the chromosome, which failed to disjoin. Trisomy and monosomy are both examples of aneuploidy, a general term that denotes an abnormality in the number of copies of any given chromosome.",True,Meiotic nondisjunction,,,,
1e1cdff8-54c0-4be4-833a-c7ad36c277e6,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
1e1cdff8-54c0-4be4-833a-c7ad36c277e6,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
1e1cdff8-54c0-4be4-833a-c7ad36c277e6,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
a3566fc6-cd1f-40f3-838b-b641923dd82d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Meiotic nondisjunction is the cause of the most common and clinically significant class of chromosomal abnormalities. This is true for chromosomal abnormalities found in spontaneous abortions where approximately 35 percent of miscarriages have a trisomy or monosomy, in stillbirths with approximately 4 percent being aneuploid, and also in live births with 0.3 percent being affected. Most autosomal trisomies and virtually all autosomal monosomies result in pregnancy failure or spontaneous abortion. Trisomies for chromosomes 13, 18, or 21 can result in the live birth of an infant with birth defects and intellectual disability. Extra copies of the X or Y chromosome are compatible with live birth, as is a small fraction of the conceptions with only a single X chromosome (Turner syndrome).",True,Meiotic nondisjunction,,,,
5086f012-57d7-4e89-bdfd-a98d3a509540,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,monosomies,False,monosomies,,,,
8f64d649-ec27-45b3-a2fa-1507d7d0ad67,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Increasing maternal age is considered a risk factor for increased frequency of nondisjunctional events. This maternal age effect is seen in both meiosis I and meiosis II, with the majority of these events occurring at meiosis I. Only a small proportion of chromosomal aneuploidies are due to errors in male meiosis, and these generally involve the sex chromosomes. Although there is little correlation with increasing paternal age and nondisjunctional events, there is some evidence to suggest that increased paternal age increases risk for other conditions (neurofibromatosis and achondroplasia) and should therefore not be ignored when determining risk.",True,monosomies,,,,
d8fcaea0-87cc-42c2-b894-e631db48e3ed,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Mitotic nondisjunction,False,Mitotic nondisjunction,,,,
d8c269d1-8e17-4d82-bbb3-40dd31c2b2b5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
d8c269d1-8e17-4d82-bbb3-40dd31c2b2b5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
d8c269d1-8e17-4d82-bbb3-40dd31c2b2b5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
804205fc-eb30-43f4-a400-a40a5f8ab05e,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Mosaicism is often found in sex chromosome abnormalities and some autosomal trisomies. Over half of mosaic trisomy 21 cases have been shown to be the result of loss of the extra 21 in subsequent mitotic divisions after a trisomic conception, while trisomy 8 mosaicism typically seems to be acquired during mitotic divisions after a normal conception.",True,Mitotic nondisjunction,,,,
23884c1c-f607-4784-b779-b3004ef05ad7,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Chimaerism is similar to mosaicism in that multiple, genetically distinct cell lines are present in the same individual. Here, however, the cell lines begin as different zygotes rather than arising through changes during mitosis. This can arise naturally from the fusion of closely implanted twins or migration of cells between embryos in multiple gestations, or it can be caused by the transplantation of tissues or organs from donors for medical treatment.",True,Mitotic nondisjunction,,,,
5c4058b8-555d-4705-931b-ff675dd5fe53,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Chimaerism,False,Chimaerism,,,,
915e4835-0383-47b9-b6ea-2c3de3714e16,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Chromosome structural defects,False,Chromosome structural defects,,,,
d92c3981-a1ec-4a08-9a09-1e9a36c6323f,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"In addition to copy number defects, parts of the chromosome may be lost or altered. These rearrangements, regardless of the type, may be balanced or unbalanced (where the rearrangement does not produce a loss or gain).",True,Chromosome structural defects,,,,
f06066d6-0166-441e-9893-411b64a1215d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Deletions and duplications,False,Deletions and duplications,,,,
779f1f86-7f82-4769-b64d-190de0a10fa3,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"A deletion occurs when a chromosome breaks at two sites and the segment between them gets lost. Depending on the size and breakage site, varying numbers of genes can be lost. In rare cases the deletions are large enough to be visible under the light microscope. Smaller deletions have traditionally been identified by molecular cytogenetic (FISH) analyses, although they are now routinely detected with chromosome oligonucleotide arrays. These are called microdeletions, while the resulting pathologies are called microdeletion syndromes.",True,Deletions and duplications,,,,
ee2c0108-b8a6-4f02-b5cb-4c88126d99b5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
ee2c0108-b8a6-4f02-b5cb-4c88126d99b5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
ee2c0108-b8a6-4f02-b5cb-4c88126d99b5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
6def6267-8e27-42a2-aa58-2f147743b535,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Duplications refer to a chromosome segment appearing in two (often sequentially inserted) copies on a single homolog. Most of the time, this is caused by a nonhomologous recombination in the first meiotic division.",True,Deletions and duplications,,,,
b05c571d-5569-4edb-a164-10923635e686,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Inversion,False,Inversion,,,,
c5d22359-57cb-4792-a8fd-cfeed7b0aaf5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
c5d22359-57cb-4792-a8fd-cfeed7b0aaf5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
c5d22359-57cb-4792-a8fd-cfeed7b0aaf5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
f0d8f41c-970c-4c92-8475-eef0d5c125f2,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Isochromosome,False,Isochromosome,,,,
800a1de6-b4c6-43b3-945b-b1fe5c0d127e,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,An isochromosome is a derivative chromosome with two homologous arms after the centromere divided transversely rather than longitudinally. An isochromosome can be thought of as a “mirror image” of either the short arm or the long arm of a given chromosome.,True,Isochromosome,,,,
5207e9cb-26d6-4678-91f3-c778bade5ced,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Ring chromosome,False,Ring chromosome,,,,
0bf34b86-d4c7-4dd4-a6c2-3b12b9bed68a,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Ring chromosomes occur when a chromosome breaks at both ends and the ends join together. They typically become clinically relevant through the loss of chromosomal material distal to the breaks. Ring chromosome X causes 5 percent of Turner syndrome cases.,True,Ring chromosome,,,,
b95f4150-5f46-4274-9e18-1ab0e9ed8ab1,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Translocations,False,Translocations,,,,
44554f7d-4769-457e-8dc3-92de782d954c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
44554f7d-4769-457e-8dc3-92de782d954c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
44554f7d-4769-457e-8dc3-92de782d954c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
8dc1b3d2-9c32-4e04-b128-e2e342b35c61,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Translocations can be classified as either reciprocal or Robertsonian.,False,Translocations can be classified as either reciprocal or Robertsonian.,,,,
8e82a25e-74d4-4412-9ceb-6e3569561d0c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,13.1 References and resources,True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
5ce52b21-1270-4f00-a2a4-2a16f2b7bb00,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 11: Meiosis and Sexual Reproduction, Chapter 13: Modern Understandings of Inheritance, Chapter 17: Biotechnology and Genomics.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
b7b4a880-4845-42d0-a220-1384df7b9d95,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 52–55.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
bea9c47f-2d76-4b3e-9b7f-9c8f9827d769,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"LeClair, R. J., and R. G. Best. “Chromosome Mechanics.” eLS (2016): 1–11. https://onlinelibrary.wiley.com/doi/….a0001441.pub3.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
f472d67b-810e-4501-a8e1-16942e5f20d5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 5: Principles of Clinical Cytogenetics.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
5f48b4d8-87af-4212-acaf-2df3848b79e3,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
5f48b4d8-87af-4212-acaf-2df3848b79e3,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
5f48b4d8-87af-4212-acaf-2df3848b79e3,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
7029f490-3116-4d36-8cae-e27197201056,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
7029f490-3116-4d36-8cae-e27197201056,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
7029f490-3116-4d36-8cae-e27197201056,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
7d967f18-82d6-4930-868b-471e0423d26d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
7d967f18-82d6-4930-868b-471e0423d26d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
7d967f18-82d6-4930-868b-471e0423d26d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
d3cb14e4-9d78-41cb-8d4e-c3d6a8366015,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
d3cb14e4-9d78-41cb-8d4e-c3d6a8366015,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
d3cb14e4-9d78-41cb-8d4e-c3d6a8366015,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
3d760ddc-a5c1-49ea-b61a-87ca01930ce9,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
3d760ddc-a5c1-49ea-b61a-87ca01930ce9,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
3d760ddc-a5c1-49ea-b61a-87ca01930ce9,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
e2cda674-623a-4ced-aa09-e724c849b440,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
e2cda674-623a-4ced-aa09-e724c849b440,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
e2cda674-623a-4ced-aa09-e724c849b440,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
34b87450-83fb-4789-a4ab-40b18d16de8e,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
34b87450-83fb-4789-a4ab-40b18d16de8e,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
34b87450-83fb-4789-a4ab-40b18d16de8e,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
db853414-a1db-4f7c-9168-ffd4d2aaeb7c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,13.2 Biotechnology,True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
2aa207b1-118c-4f90-b1f0-4d549231a90d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Basic techniques to manipulate genetic material (DNA and RNA),False,Basic techniques to manipulate genetic material (DNA and RNA),,,,
d4e7e9ae-5335-4367-8757-ae3d2c38f99a,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"To evaluate genetic disorders a variety of biochemical techniques can be used. The type, kind, and size of the projected genetic variation will determine what approach is taken.",True,Basic techniques to manipulate genetic material (DNA and RNA),,,,
77d3eba5-8982-4a8e-931b-25c995d2bf18,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Following DNA extraction there are a variety of techniques that can be employed. The lowest resolution technique for evaluating the genome is the karyotype followed by high-resolution banding. From here, smaller genomic changes can be observed using comparative genome hybridization, fluorescence in situ hybridization (FISH) analysis, or microarrays. Finally, specific nucleotide changes can be examined by whole genome sequencing.",True,Basic techniques to manipulate genetic material (DNA and RNA),,,,
4dd022c9-2544-4092-a0a8-975a139446ba,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,microarrays,False,microarrays,,,,
4edcaec0-044e-4dc7-84ec-9fbc95d79a5b,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,DNA and RNA extraction,False,DNA and RNA extraction,,,,
dfe65351-1ba7-4fa8-960e-e44770fe1482,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
dfe65351-1ba7-4fa8-960e-e44770fe1482,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
dfe65351-1ba7-4fa8-960e-e44770fe1482,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
5b02dacb-42c0-4396-afa8-1747218bc1ae,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,RNAses,False,RNAses,,,,
95f4295f-9a4f-46e8-92f5-f559a3927ff2,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Scientists perform RNA analysis to study gene expression patterns in cells. RNA is naturally very unstable because RNAses are commonly present in nature and very difficult to inactivate. Similar to DNA, RNA extraction involves using various buffers and enzymes to inactivate macromolecules and preserve the RNA.",True,RNAses,,,,
028b0b3e-fa23-485e-a957-9e97a88422d6,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Karoytype and high-resolution banding,False,Karoytype and high-resolution banding,,,,
d9a33d67-8fa0-42b6-ab41-381586aa92fc,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Karyotyping can be used to look at general chromosome morphology and chromosome number. To do this, cells are harvested and arrested in metaphase allowing for the chromosomes to be fixed, spread on slides, and stained by one of several techniques. Giemsa banding (G banding) is the gold standard for the detection and characterization of structural and numerical genomic abnormalities in clinical diagnostic settings for both constitutional (postnatal or prenatal) and acquired (cancer) disorders.",True,Karoytype and high-resolution banding,,,,
dbc2a865-a717-4143-ab7b-aa16a85baf23,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
dbc2a865-a717-4143-ab7b-aa16a85baf23,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
dbc2a865-a717-4143-ab7b-aa16a85baf23,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
25da1ddc-7789-49cc-8270-b533c3d1227e,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Fluorescence in situ hybridization (FISH),False,Fluorescence in situ hybridization (FISH),,,,
5797abda-a9e8-4dd0-9721-62a1335374a0,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,FISH is a targeted approach using a sequence-specific probe to detect the presence or absence of a particular DNA sequence or for evaluating the number or organization of a chromosome or chromosomal region in situ.,True,Fluorescence in situ hybridization (FISH),,,,
36fe26ea-ff29-4021-873f-38b6d19dfb66,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,This technique has several advantages and can be used to identify a variety of different chromosomal changes:,True,Fluorescence in situ hybridization (FISH),,,,
cb5a77eb-be43-464f-a675-ff13045ae95f,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Microarrays,False,Microarrays,,,,
f1012b21-35f5-4e3d-89f1-d390617a25b5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Although FISH can detect chromosome changes, microarrays can simultaneously query the whole genome to detect relative copy number variations, gains, or losses by hybridizing a control genome to one of a patient. In looking at the results, an excess of sequences from one genome would represent an overrepresentation in a gene locus within an individual (duplication). This technique can also be used to look at single nucleotide polymorphisms to determine allele frequency.",True,Microarrays,,,,
f4af6c4a-cf1b-4ac8-8ab9-c5a404537363,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,DNA sequencing techniques,False,DNA sequencing techniques,,,,
5653a75e-f441-448c-8479-8e3e4d1ed470,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Sanger sequencing is commonly referred to as the dideoxy chain termination method. The method is based on the use of chain terminators, the dideoxynucleotides (ddNTPs). The ddNTPSs differ from the deoxynucleotides by the lack of a free 3′ OH group on the five-carbon sugar. If a ddNTP is added to a growing DNA strand, the chain cannot be extended any further because the free 3′ OH group needed to add another nucleotide is not available. By using a predetermined ratio of deoxyribonucleotides to dideoxynucleotides, it is possible to generate DNA fragments of different sizes.",True,DNA sequencing techniques,,,,
0501f9ea-2fef-439e-be9a-780f14a30814,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
0501f9ea-2fef-439e-be9a-780f14a30814,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
0501f9ea-2fef-439e-be9a-780f14a30814,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
08edf074-447e-4d63-8c21-2dfe4bfca319,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Nucleic acid fragment amplification by polymerase chain reaction (PCR),False,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
a4ad8cba-34e8-4244-b2ab-2b20b1831f99,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
a4ad8cba-34e8-4244-b2ab-2b20b1831f99,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
a4ad8cba-34e8-4244-b2ab-2b20b1831f99,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
e21cf8c4-a95c-42d2-ab65-3b931943cd3f,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Scientists use polymerase chain reaction, or PCR, to amplify a specific DNA sequence. Primers are short pieces of DNA complementary to each end of the target sequence combined with genomic DNA, Taq polymerase, and deoxynucleotides.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
20dae2ab-dea0-4bf5-9340-aa075cdbd381,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Reverse transcriptase PCR (RT-PCR) is similar to PCR, but cDNA is made from an RNA template before PCR begins. DNA fragments can also be amplified from an RNA template in a process called reverse transcriptase PCR (RT-PCR). The first step is to recreate the original DNA template strand (called cDNA) by applying DNA nucleotides to the mRNA. This process is called reverse transcription. This requires the presence of an enzyme called reverse transcriptase. After the cDNA is made, regular PCR can be used to amplify it.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
ae5d6dbd-b700-46e3-9ea5-c7b42cdb47f1,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Gel electrophoresis,False,Gel electrophoresis,,,,
2b599b2f-c189-4fc3-8122-e41f64584620,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Gel electrophoresis is a technique used to separate DNA fragments of different sizes. Usually the gel is made of a chemical called agarose or polyacylamide depending on the sample being used. The DNA has a net negative charge and moves from the negative electrode toward the positive electrode. The electric current is applied for sufficient time to let the DNA separate according to size; the smallest fragments will be farthest from the well (where the DNA was loaded), and the heavier molecular weight fragments will be closest to the well. Once the DNA is separated, the gel is stained with a DNA-specific dye for viewing it.",True,Gel electrophoresis,,,,
af9cfd99-af40-4ff7-a51e-1c9f2d349273,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Hybridization, southern blotting, and northern blotting",False,"Hybridization, southern blotting, and northern blotting",,,,
39d4cfc6-ce04-47b5-98c5-d4c1ab14badd,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Different types of electrophoresis can be used to look at various changes at the level of the DNA (genome), RNA (transcriptome), or protein (proteome). In all cases, a sample (DNA, RNA, protein) is run on a gel (electrophoresis) and is then examined using a probe specific to the sample.",True,"Hybridization, southern blotting, and northern blotting",,,,
4acfe7ef-a0ad-4d50-b52c-c791e0319240,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
4acfe7ef-a0ad-4d50-b52c-c791e0319240,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
4acfe7ef-a0ad-4d50-b52c-c791e0319240,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
571d2bed-0971-44cb-a251-73c8cd57b305,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Northern blots are designed to examine changes in RNA. RNA is probed with a DNA probe complementary to the transcript of interest. This will detect changes in gene expression.,True,"Hybridization, southern blotting, and northern blotting",,,,
031a0f8f-c5e9-4c3c-9765-046de41e93f2,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,Western blots are designed to examine changes in protein size and amount. Cell lysates or protein isolates are probed with an antibody specific to the protein of interest. This will detect changes in protein expression.,True,"Hybridization, southern blotting, and northern blotting",,,,
d549bc4e-7163-4272-9347-ceb25f5ae2e0,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,13.2 References and resources,True,"Hybridization, southern blotting, and northern blotting",,,,
ce0e78f6-1c1f-4e06-b174-1aee893ba25c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
ce0e78f6-1c1f-4e06-b174-1aee893ba25c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
ce0e78f6-1c1f-4e06-b174-1aee893ba25c,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
d3078451-4861-4d2d-9981-918de812962d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
d3078451-4861-4d2d-9981-918de812962d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
d3078451-4861-4d2d-9981-918de812962d,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
07a28833-f49d-4e50-90ba-18f94a3ceea0,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
07a28833-f49d-4e50-90ba-18f94a3ceea0,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
07a28833-f49d-4e50-90ba-18f94a3ceea0,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
19b8358b-71ca-4e78-8147-e5e8b16a93f5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
19b8358b-71ca-4e78-8147-e5e8b16a93f5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
19b8358b-71ca-4e78-8147-e5e8b16a93f5,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
455d3428-bedc-45f5-9469-ad3db59bacba,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
455d3428-bedc-45f5-9469-ad3db59bacba,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
455d3428-bedc-45f5-9469-ad3db59bacba,https://pressbooks.lib.vt.edu/cellbio/,13.2 Biotechnology,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-2,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
b5bb7527-2670-437f-af78-f567282dac9e,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Genetics methodology,False,Genetics methodology,,,,
96247fb2-2cf1-46a4-840a-953466d8e720,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
96247fb2-2cf1-46a4-840a-953466d8e720,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
96247fb2-2cf1-46a4-840a-953466d8e720,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
87aeec03-5762-4972-ad0e-b6425549170e,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Chromosome structure,False,Chromosome structure,,,,
041cde78-82e3-4595-a113-7a6d19f5c8fd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
041cde78-82e3-4595-a113-7a6d19f5c8fd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
041cde78-82e3-4595-a113-7a6d19f5c8fd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
e554adbd-dac6-43c0-8483-36f74c6154b8,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Nondisjunction,False,Nondisjunction,,,,
7bc4d965-2f7d-4268-835b-5f3a4c13e9e3,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
7bc4d965-2f7d-4268-835b-5f3a4c13e9e3,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
7bc4d965-2f7d-4268-835b-5f3a4c13e9e3,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
1fbeadc0-71dc-4cf7-8edb-c61db99b74be,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Table 13.1: Summary of meiotic and mitotic cell divisions.,True,Nondisjunction,,,,
aeab70b9-36a9-404c-97a8-68262112a656,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"These nondisjunction events can result in unequal distribution of chromosomes rendering a cell with an atypical chromosome number. A cell that is euploid would contain all twenty-three chromosomes, while polyploidy would suggest additional chromosomes within the cell. In humans, aneuploidy of autosomes are the most clinically important abnormalities to address, and the most common cause of this is a nondisjunction event.",True,Nondisjunction,,,,
0339183f-c439-4123-887f-871db7d7051f,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Meiotic nondisjunction,False,Meiotic nondisjunction,,,,
e18c41d3-4dc7-4828-a489-b700ee8d6ac3,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Normally, one copy of each chromosome is inherited from each parent; however, when there is nondisjunction at either anaphase I or anaphase II, gametes will contain either two copies or no copies of the chromosome, which failed to disjoin. At fertilization, when the gamete provided by the other parent contributes one copy of each chromosome, the newly formed zygote will instead possess three copies (trisomy) or one copy (monosomy) of the chromosome, which failed to disjoin. Trisomy and monosomy are both examples of aneuploidy, a general term that denotes an abnormality in the number of copies of any given chromosome.",True,Meiotic nondisjunction,,,,
bba75b1f-2bb7-406f-81af-2ce39b6db9ee,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
bba75b1f-2bb7-406f-81af-2ce39b6db9ee,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
bba75b1f-2bb7-406f-81af-2ce39b6db9ee,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
ff9d811d-2801-457e-9d89-a89e5e10b61b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Meiotic nondisjunction is the cause of the most common and clinically significant class of chromosomal abnormalities. This is true for chromosomal abnormalities found in spontaneous abortions where approximately 35 percent of miscarriages have a trisomy or monosomy, in stillbirths with approximately 4 percent being aneuploid, and also in live births with 0.3 percent being affected. Most autosomal trisomies and virtually all autosomal monosomies result in pregnancy failure or spontaneous abortion. Trisomies for chromosomes 13, 18, or 21 can result in the live birth of an infant with birth defects and intellectual disability. Extra copies of the X or Y chromosome are compatible with live birth, as is a small fraction of the conceptions with only a single X chromosome (Turner syndrome).",True,Meiotic nondisjunction,,,,
7a52b3da-2204-44c2-8b7f-b41f2c5af896,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,monosomies,False,monosomies,,,,
dd5f5e0d-8e2b-4f10-9f8d-711791198104,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Increasing maternal age is considered a risk factor for increased frequency of nondisjunctional events. This maternal age effect is seen in both meiosis I and meiosis II, with the majority of these events occurring at meiosis I. Only a small proportion of chromosomal aneuploidies are due to errors in male meiosis, and these generally involve the sex chromosomes. Although there is little correlation with increasing paternal age and nondisjunctional events, there is some evidence to suggest that increased paternal age increases risk for other conditions (neurofibromatosis and achondroplasia) and should therefore not be ignored when determining risk.",True,monosomies,,,,
d3ce6fac-95ba-42b6-9ab5-5c3b7ce4b214,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Mitotic nondisjunction,False,Mitotic nondisjunction,,,,
bdc633fd-5b53-4965-bffa-7660d8a90904,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
bdc633fd-5b53-4965-bffa-7660d8a90904,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
bdc633fd-5b53-4965-bffa-7660d8a90904,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
6b266038-36cf-4beb-8022-d6014fa0cf20,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Mosaicism is often found in sex chromosome abnormalities and some autosomal trisomies. Over half of mosaic trisomy 21 cases have been shown to be the result of loss of the extra 21 in subsequent mitotic divisions after a trisomic conception, while trisomy 8 mosaicism typically seems to be acquired during mitotic divisions after a normal conception.",True,Mitotic nondisjunction,,,,
c39076a6-7577-4bed-86b2-e6c2b89eebff,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Chimaerism is similar to mosaicism in that multiple, genetically distinct cell lines are present in the same individual. Here, however, the cell lines begin as different zygotes rather than arising through changes during mitosis. This can arise naturally from the fusion of closely implanted twins or migration of cells between embryos in multiple gestations, or it can be caused by the transplantation of tissues or organs from donors for medical treatment.",True,Mitotic nondisjunction,,,,
edff2625-994a-4a0f-b970-dbaeb3d04f0f,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Chimaerism,False,Chimaerism,,,,
faf5a52e-8f65-41f9-938a-a678900d46a7,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Chromosome structural defects,False,Chromosome structural defects,,,,
2a6bdb72-553e-4c66-96b5-790bbba0d28d,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"In addition to copy number defects, parts of the chromosome may be lost or altered. These rearrangements, regardless of the type, may be balanced or unbalanced (where the rearrangement does not produce a loss or gain).",True,Chromosome structural defects,,,,
e6eb970c-f5a7-48cf-9c56-31afbc284fed,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Deletions and duplications,False,Deletions and duplications,,,,
0b25977f-dc10-4c56-8441-6413e7aa5d5b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"A deletion occurs when a chromosome breaks at two sites and the segment between them gets lost. Depending on the size and breakage site, varying numbers of genes can be lost. In rare cases the deletions are large enough to be visible under the light microscope. Smaller deletions have traditionally been identified by molecular cytogenetic (FISH) analyses, although they are now routinely detected with chromosome oligonucleotide arrays. These are called microdeletions, while the resulting pathologies are called microdeletion syndromes.",True,Deletions and duplications,,,,
ce754cfb-8256-4be6-9e11-18bb25abaaa2,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
ce754cfb-8256-4be6-9e11-18bb25abaaa2,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
ce754cfb-8256-4be6-9e11-18bb25abaaa2,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
19d192a9-1b7e-42f7-baa2-36bc1dac26eb,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Duplications refer to a chromosome segment appearing in two (often sequentially inserted) copies on a single homolog. Most of the time, this is caused by a nonhomologous recombination in the first meiotic division.",True,Deletions and duplications,,,,
2efaabda-7c75-4515-8910-77172d183a1b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Inversion,False,Inversion,,,,
f80f10e7-92ca-40db-9adf-a1af24c38b7c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
f80f10e7-92ca-40db-9adf-a1af24c38b7c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
f80f10e7-92ca-40db-9adf-a1af24c38b7c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
5c84df1b-e936-4a44-8886-96c3bb85dc8c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Isochromosome,False,Isochromosome,,,,
8d7c6d13-580f-4e6b-a6b0-77e51af7145e,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,An isochromosome is a derivative chromosome with two homologous arms after the centromere divided transversely rather than longitudinally. An isochromosome can be thought of as a “mirror image” of either the short arm or the long arm of a given chromosome.,True,Isochromosome,,,,
81083d9e-f738-434b-aa7a-8b5305aa802c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Ring chromosome,False,Ring chromosome,,,,
53f7a95f-d7ef-4980-a656-48f1e2860b96,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Ring chromosomes occur when a chromosome breaks at both ends and the ends join together. They typically become clinically relevant through the loss of chromosomal material distal to the breaks. Ring chromosome X causes 5 percent of Turner syndrome cases.,True,Ring chromosome,,,,
96b1d274-1443-4aec-a068-d282d8d0abcd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Translocations,False,Translocations,,,,
2ad32881-f2ca-46fb-83fa-93366a3158b0,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
2ad32881-f2ca-46fb-83fa-93366a3158b0,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
2ad32881-f2ca-46fb-83fa-93366a3158b0,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
0e8992d2-af51-4a60-bf50-a446721ca421,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Translocations can be classified as either reciprocal or Robertsonian.,False,Translocations can be classified as either reciprocal or Robertsonian.,,,,
9d8c2d10-be6e-40bb-9f7b-d919dd4238be,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,13.1 References and resources,True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
eea486fc-8acd-43f5-9b7c-27fe6606fc93,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 11: Meiosis and Sexual Reproduction, Chapter 13: Modern Understandings of Inheritance, Chapter 17: Biotechnology and Genomics.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
ae470323-97f6-458a-9fd2-e91b1005cf0a,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 52–55.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
963bb069-12be-4fa2-b682-738b58bd3d14,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"LeClair, R. J., and R. G. Best. “Chromosome Mechanics.” eLS (2016): 1–11. https://onlinelibrary.wiley.com/doi/….a0001441.pub3.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
b981cad1-fa4e-4a35-9086-ae7895729174,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 5: Principles of Clinical Cytogenetics.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
340c24de-14c7-4504-9bc6-6175f5bde3ca,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
340c24de-14c7-4504-9bc6-6175f5bde3ca,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
340c24de-14c7-4504-9bc6-6175f5bde3ca,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
3cb2c247-f06f-4671-bba8-33ac986afa28,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
3cb2c247-f06f-4671-bba8-33ac986afa28,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
3cb2c247-f06f-4671-bba8-33ac986afa28,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
2f8e40ee-749a-4d98-b0a2-7c2c6bc80a72,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
2f8e40ee-749a-4d98-b0a2-7c2c6bc80a72,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
2f8e40ee-749a-4d98-b0a2-7c2c6bc80a72,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
8df3fd5a-bfe8-42b6-a0bf-5a11f416c8e8,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
8df3fd5a-bfe8-42b6-a0bf-5a11f416c8e8,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
8df3fd5a-bfe8-42b6-a0bf-5a11f416c8e8,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
b349aed1-2018-4102-91ed-75e618cfec1b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
b349aed1-2018-4102-91ed-75e618cfec1b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
b349aed1-2018-4102-91ed-75e618cfec1b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
b14c5379-a21f-4a8a-97eb-020ab7842622,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
b14c5379-a21f-4a8a-97eb-020ab7842622,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
b14c5379-a21f-4a8a-97eb-020ab7842622,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
1168b457-4be6-4559-b1a5-eed62ec1a4bd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
1168b457-4be6-4559-b1a5-eed62ec1a4bd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
1168b457-4be6-4559-b1a5-eed62ec1a4bd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
fa7fb9d5-258d-43f3-a17a-3fd65ac1ff77,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,13.2 Biotechnology,True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
d8e652d0-bdd3-49eb-9b28-0041d560d49a,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Basic techniques to manipulate genetic material (DNA and RNA),False,Basic techniques to manipulate genetic material (DNA and RNA),,,,
447626bf-c09f-4e12-b51a-701f4a9733ab,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"To evaluate genetic disorders a variety of biochemical techniques can be used. The type, kind, and size of the projected genetic variation will determine what approach is taken.",True,Basic techniques to manipulate genetic material (DNA and RNA),,,,
deef2d7c-31c2-440b-a1dc-ee0b9015ccb2,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Following DNA extraction there are a variety of techniques that can be employed. The lowest resolution technique for evaluating the genome is the karyotype followed by high-resolution banding. From here, smaller genomic changes can be observed using comparative genome hybridization, fluorescence in situ hybridization (FISH) analysis, or microarrays. Finally, specific nucleotide changes can be examined by whole genome sequencing.",True,Basic techniques to manipulate genetic material (DNA and RNA),,,,
fb4597eb-b4a0-4923-beed-eb1e24143e29,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,microarrays,False,microarrays,,,,
c5144c33-1515-4e7a-8b6a-49782c84597f,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,DNA and RNA extraction,False,DNA and RNA extraction,,,,
9b35c89c-5486-42f7-b3f4-af209cfaf781,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
9b35c89c-5486-42f7-b3f4-af209cfaf781,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
9b35c89c-5486-42f7-b3f4-af209cfaf781,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
aa4a9b0d-a9b6-4e41-8474-dec09d987335,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,RNAses,False,RNAses,,,,
459674bb-7f01-44bd-954e-042cf63bf689,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Scientists perform RNA analysis to study gene expression patterns in cells. RNA is naturally very unstable because RNAses are commonly present in nature and very difficult to inactivate. Similar to DNA, RNA extraction involves using various buffers and enzymes to inactivate macromolecules and preserve the RNA.",True,RNAses,,,,
96e94f94-8057-455c-a711-046eb72d764a,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Karoytype and high-resolution banding,False,Karoytype and high-resolution banding,,,,
3dfd13d5-41d9-455a-936e-29e52d6e95e8,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Karyotyping can be used to look at general chromosome morphology and chromosome number. To do this, cells are harvested and arrested in metaphase allowing for the chromosomes to be fixed, spread on slides, and stained by one of several techniques. Giemsa banding (G banding) is the gold standard for the detection and characterization of structural and numerical genomic abnormalities in clinical diagnostic settings for both constitutional (postnatal or prenatal) and acquired (cancer) disorders.",True,Karoytype and high-resolution banding,,,,
5f06974f-a70f-4a65-a9da-e3df4b26c1a5,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
5f06974f-a70f-4a65-a9da-e3df4b26c1a5,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
5f06974f-a70f-4a65-a9da-e3df4b26c1a5,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
6e83adfc-d4e4-4631-b9f8-63700324da24,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Fluorescence in situ hybridization (FISH),False,Fluorescence in situ hybridization (FISH),,,,
029fe3ee-f41c-4a1b-8a0f-dfd4397b8528,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,FISH is a targeted approach using a sequence-specific probe to detect the presence or absence of a particular DNA sequence or for evaluating the number or organization of a chromosome or chromosomal region in situ.,True,Fluorescence in situ hybridization (FISH),,,,
1f93e158-ef57-4d2f-9e8b-c54d7ff7b40d,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,This technique has several advantages and can be used to identify a variety of different chromosomal changes:,True,Fluorescence in situ hybridization (FISH),,,,
3c13bcfa-cd67-46ef-a421-149eddce9501,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Microarrays,False,Microarrays,,,,
da0b9764-30c8-47d2-9d26-dc98053eb40f,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Although FISH can detect chromosome changes, microarrays can simultaneously query the whole genome to detect relative copy number variations, gains, or losses by hybridizing a control genome to one of a patient. In looking at the results, an excess of sequences from one genome would represent an overrepresentation in a gene locus within an individual (duplication). This technique can also be used to look at single nucleotide polymorphisms to determine allele frequency.",True,Microarrays,,,,
924a323d-f42d-4a09-98ec-bd5902655bce,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,DNA sequencing techniques,False,DNA sequencing techniques,,,,
6b198483-23ef-48fb-abbf-94c0cb0e7105,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Sanger sequencing is commonly referred to as the dideoxy chain termination method. The method is based on the use of chain terminators, the dideoxynucleotides (ddNTPs). The ddNTPSs differ from the deoxynucleotides by the lack of a free 3′ OH group on the five-carbon sugar. If a ddNTP is added to a growing DNA strand, the chain cannot be extended any further because the free 3′ OH group needed to add another nucleotide is not available. By using a predetermined ratio of deoxyribonucleotides to dideoxynucleotides, it is possible to generate DNA fragments of different sizes.",True,DNA sequencing techniques,,,,
420eb335-699f-4340-b05b-6e54661ae26b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
420eb335-699f-4340-b05b-6e54661ae26b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
420eb335-699f-4340-b05b-6e54661ae26b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
bd5df36d-73a0-41cb-b106-5582cce7c6e0,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Nucleic acid fragment amplification by polymerase chain reaction (PCR),False,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
19be3958-7271-450c-a126-90e8aedd051c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
19be3958-7271-450c-a126-90e8aedd051c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
19be3958-7271-450c-a126-90e8aedd051c,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
97ab0aec-7bd4-47ab-9544-06120932cbdd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Scientists use polymerase chain reaction, or PCR, to amplify a specific DNA sequence. Primers are short pieces of DNA complementary to each end of the target sequence combined with genomic DNA, Taq polymerase, and deoxynucleotides.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
ff84af38-ae5b-4447-be1f-2580fd6c72cd,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Reverse transcriptase PCR (RT-PCR) is similar to PCR, but cDNA is made from an RNA template before PCR begins. DNA fragments can also be amplified from an RNA template in a process called reverse transcriptase PCR (RT-PCR). The first step is to recreate the original DNA template strand (called cDNA) by applying DNA nucleotides to the mRNA. This process is called reverse transcription. This requires the presence of an enzyme called reverse transcriptase. After the cDNA is made, regular PCR can be used to amplify it.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
09888627-9c35-4569-bb00-d2731ab87414,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Gel electrophoresis,False,Gel electrophoresis,,,,
5187233b-4c9d-4f1a-9385-1d677da51acf,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Gel electrophoresis is a technique used to separate DNA fragments of different sizes. Usually the gel is made of a chemical called agarose or polyacylamide depending on the sample being used. The DNA has a net negative charge and moves from the negative electrode toward the positive electrode. The electric current is applied for sufficient time to let the DNA separate according to size; the smallest fragments will be farthest from the well (where the DNA was loaded), and the heavier molecular weight fragments will be closest to the well. Once the DNA is separated, the gel is stained with a DNA-specific dye for viewing it.",True,Gel electrophoresis,,,,
49b7f9b2-24d8-4d66-81ac-5d1a29332190,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Hybridization, southern blotting, and northern blotting",False,"Hybridization, southern blotting, and northern blotting",,,,
24f85619-d61b-4905-8eb5-aca54f9b5c49,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Different types of electrophoresis can be used to look at various changes at the level of the DNA (genome), RNA (transcriptome), or protein (proteome). In all cases, a sample (DNA, RNA, protein) is run on a gel (electrophoresis) and is then examined using a probe specific to the sample.",True,"Hybridization, southern blotting, and northern blotting",,,,
184ff9da-a174-48fc-a67d-9da739e5291a,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
184ff9da-a174-48fc-a67d-9da739e5291a,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
184ff9da-a174-48fc-a67d-9da739e5291a,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
826ce5f1-4ec3-4d29-99ba-e9bb5e6ac0c0,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Northern blots are designed to examine changes in RNA. RNA is probed with a DNA probe complementary to the transcript of interest. This will detect changes in gene expression.,True,"Hybridization, southern blotting, and northern blotting",,,,
77a9206a-59c4-46c2-92b4-74edc324fa5f,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,Western blots are designed to examine changes in protein size and amount. Cell lysates or protein isolates are probed with an antibody specific to the protein of interest. This will detect changes in protein expression.,True,"Hybridization, southern blotting, and northern blotting",,,,
47c81a76-2aac-4392-be20-7fc00861095e,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,13.2 References and resources,True,"Hybridization, southern blotting, and northern blotting",,,,
14b95297-1f86-4267-9f12-93572c12900b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
14b95297-1f86-4267-9f12-93572c12900b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
14b95297-1f86-4267-9f12-93572c12900b,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
4d6b85d5-113c-405d-bdc5-acf333a3abcc,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
4d6b85d5-113c-405d-bdc5-acf333a3abcc,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
4d6b85d5-113c-405d-bdc5-acf333a3abcc,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
630128ad-2aa5-45d6-87bf-f6d64591a0de,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
630128ad-2aa5-45d6-87bf-f6d64591a0de,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
630128ad-2aa5-45d6-87bf-f6d64591a0de,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
5a864d6c-bf0a-41e2-a3d3-8cae66973146,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
5a864d6c-bf0a-41e2-a3d3-8cae66973146,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
5a864d6c-bf0a-41e2-a3d3-8cae66973146,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
3e9c3394-6aa1-45b0-8e33-65fb18d438f6,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
3e9c3394-6aa1-45b0-8e33-65fb18d438f6,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
3e9c3394-6aa1-45b0-8e33-65fb18d438f6,https://pressbooks.lib.vt.edu/cellbio/,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/#chapter-93-section-1,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
72832e62-825a-46be-9f7b-0e184560e99a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Genetics methodology,False,Genetics methodology,,,,
f9ecb674-9f4d-49b8-8875-0419f7b0ba8a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
f9ecb674-9f4d-49b8-8875-0419f7b0ba8a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
f9ecb674-9f4d-49b8-8875-0419f7b0ba8a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Chromosomes can be analyzed from living tissue and arranged in a karyotype (figure 13.1). Chromosomes can be sorted into the autosomal pairs (twenty-two) and sex chromosomes and classified to determine any abnormalities. A normal karyotype for a female is 46,XX, and a male is 46,XY. Deviations from this patterning can result in chromosomal abnormalities, which may or may not produce viable offspring.",True,Genetics methodology,Figure 13.1,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
e25a2ec5-09fd-448f-9316-d4fb9a1d4ce1,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Chromosome structure,False,Chromosome structure,,,,
28ebd085-81f4-4d16-a119-0b3ba347e752,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
28ebd085-81f4-4d16-a119-0b3ba347e752,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
28ebd085-81f4-4d16-a119-0b3ba347e752,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Each chromosome is made up of a p and q arm held together by the centromere. The position of the centromere is a distinguishing characteristic and can be classified as metacentric, submetacentric, or acrocentric. The position of the centromere plays a key role in mitotic and meiotic division as chromosomes with skewed centromeres are more likely to be involved in nondisjunction events (figure 13.2).",True,Chromosome structure,Figure 13.2,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
55bd2a36-3bcd-4795-a42b-8940dd89b829,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Nondisjunction,False,Nondisjunction,,,,
e4b36115-bd10-444a-91bf-2fd4a3cea660,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
e4b36115-bd10-444a-91bf-2fd4a3cea660,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
e4b36115-bd10-444a-91bf-2fd4a3cea660,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The precise pairing and segregation during the two meiotic divisions ensures the equal division of the somatic diploid set of chromosomes into the four resulting haploid cells (figure 13.3). Nondisjunction is the term used when the two homologous chromosomes in the first division or the two sister chromatids in the second do not segregate from each other at anaphase, but instead move together into the same daughter cell. This term may also be used for the same occurrence in mitotic cell divisions when the sister chromatids fail to segregate properly.",True,Nondisjunction,Figure 13.3,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
9f9ec451-07b2-4259-b453-dbed28a9c051,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Table 13.1: Summary of meiotic and mitotic cell divisions.,True,Nondisjunction,,,,
c68d4f56-7bda-494e-bb3c-877548591a89,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"These nondisjunction events can result in unequal distribution of chromosomes rendering a cell with an atypical chromosome number. A cell that is euploid would contain all twenty-three chromosomes, while polyploidy would suggest additional chromosomes within the cell. In humans, aneuploidy of autosomes are the most clinically important abnormalities to address, and the most common cause of this is a nondisjunction event.",True,Nondisjunction,,,,
de45f5a4-4358-4114-9d0a-36cefd4c21a8,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Meiotic nondisjunction,False,Meiotic nondisjunction,,,,
0debeef2-dc53-46de-830d-16a4acc9fe4a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Normally, one copy of each chromosome is inherited from each parent; however, when there is nondisjunction at either anaphase I or anaphase II, gametes will contain either two copies or no copies of the chromosome, which failed to disjoin. At fertilization, when the gamete provided by the other parent contributes one copy of each chromosome, the newly formed zygote will instead possess three copies (trisomy) or one copy (monosomy) of the chromosome, which failed to disjoin. Trisomy and monosomy are both examples of aneuploidy, a general term that denotes an abnormality in the number of copies of any given chromosome.",True,Meiotic nondisjunction,,,,
0f876833-9a49-4409-8ecf-c774f3f7f15c,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
0f876833-9a49-4409-8ecf-c774f3f7f15c,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
0f876833-9a49-4409-8ecf-c774f3f7f15c,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Chromosomal trisomies caused by nondisjunction at meiosis I can be distinguished from those occurring at meiosis II by examining the inheritance patterns of polymorphic markers near the centromere in cells obtained from the trisomic offspring (figure 13.4).,True,Meiotic nondisjunction,Figure 13.4,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
40683c1a-421a-4db3-ba77-c6b8b9c281e0,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Meiotic nondisjunction is the cause of the most common and clinically significant class of chromosomal abnormalities. This is true for chromosomal abnormalities found in spontaneous abortions where approximately 35 percent of miscarriages have a trisomy or monosomy, in stillbirths with approximately 4 percent being aneuploid, and also in live births with 0.3 percent being affected. Most autosomal trisomies and virtually all autosomal monosomies result in pregnancy failure or spontaneous abortion. Trisomies for chromosomes 13, 18, or 21 can result in the live birth of an infant with birth defects and intellectual disability. Extra copies of the X or Y chromosome are compatible with live birth, as is a small fraction of the conceptions with only a single X chromosome (Turner syndrome).",True,Meiotic nondisjunction,,,,
36d70c2f-06dc-4686-ac81-6dc47a5ed1ca,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,monosomies,False,monosomies,,,,
f81c5b81-0999-4663-82db-b31e13890578,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Increasing maternal age is considered a risk factor for increased frequency of nondisjunctional events. This maternal age effect is seen in both meiosis I and meiosis II, with the majority of these events occurring at meiosis I. Only a small proportion of chromosomal aneuploidies are due to errors in male meiosis, and these generally involve the sex chromosomes. Although there is little correlation with increasing paternal age and nondisjunctional events, there is some evidence to suggest that increased paternal age increases risk for other conditions (neurofibromatosis and achondroplasia) and should therefore not be ignored when determining risk.",True,monosomies,,,,
de83a3bc-80dc-42e0-8f62-edce4fb1ea0a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Mitotic nondisjunction,False,Mitotic nondisjunction,,,,
815dc1c4-6ef1-4074-9025-36d76f84bd79,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
815dc1c4-6ef1-4074-9025-36d76f84bd79,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
815dc1c4-6ef1-4074-9025-36d76f84bd79,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Mitotic nondisjunction occurs after zygote formation and may be the result of misdivision of a cell after a normal conception with gain (or loss) of a chromosome during embryogenesis. This typically results in mosaicism (figure 13.5), the presence of multiple and genetically distinct cell populations in the same individual. The timing of mitotic nondisjunction events determines the ratio of aneuploid to normal cells and the types of tissues affected. For example, if the nondisjunction occurs early in development, the majority of cells and tissues would carry this aneuploidy, which would result in an increased clinical severity.",True,Mitotic nondisjunction,Figure 13.5,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
53b79796-1e3f-4060-a852-25141d5cb9c9,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Mosaicism is often found in sex chromosome abnormalities and some autosomal trisomies. Over half of mosaic trisomy 21 cases have been shown to be the result of loss of the extra 21 in subsequent mitotic divisions after a trisomic conception, while trisomy 8 mosaicism typically seems to be acquired during mitotic divisions after a normal conception.",True,Mitotic nondisjunction,,,,
10743a66-d2df-4992-a630-fcfcbbb52202,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Chimaerism is similar to mosaicism in that multiple, genetically distinct cell lines are present in the same individual. Here, however, the cell lines begin as different zygotes rather than arising through changes during mitosis. This can arise naturally from the fusion of closely implanted twins or migration of cells between embryos in multiple gestations, or it can be caused by the transplantation of tissues or organs from donors for medical treatment.",True,Mitotic nondisjunction,,,,
da9dbb93-7b53-4716-a709-700f4b9f10cc,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Chimaerism,False,Chimaerism,,,,
8da80441-55e4-4cb0-b0a6-bd628bd76fe2,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Chromosome structural defects,False,Chromosome structural defects,,,,
5c48fcf0-1fc9-4f9e-9dd4-b8df490e5cf5,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"In addition to copy number defects, parts of the chromosome may be lost or altered. These rearrangements, regardless of the type, may be balanced or unbalanced (where the rearrangement does not produce a loss or gain).",True,Chromosome structural defects,,,,
aa284489-ff61-421c-81bc-234d3f646fcf,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Deletions and duplications,False,Deletions and duplications,,,,
6306d142-622d-49e8-be07-7ba714c3cf61,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"A deletion occurs when a chromosome breaks at two sites and the segment between them gets lost. Depending on the size and breakage site, varying numbers of genes can be lost. In rare cases the deletions are large enough to be visible under the light microscope. Smaller deletions have traditionally been identified by molecular cytogenetic (FISH) analyses, although they are now routinely detected with chromosome oligonucleotide arrays. These are called microdeletions, while the resulting pathologies are called microdeletion syndromes.",True,Deletions and duplications,,,,
079c4484-1387-4cd1-b70a-106a3fde2fa1,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
079c4484-1387-4cd1-b70a-106a3fde2fa1,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
079c4484-1387-4cd1-b70a-106a3fde2fa1,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"An example of this is Prader-Willi syndrome, a rare disorder due to the deletion or loss of expression from the paternal chromosome 15. This short region of genes is subject to maternal imprinting and typically only expressed from a single chromosomal loci. In these individuals, loss of expressivity from the paternal allele (either through a microdeletion or loss of chromosome 15) and imprinting of the maternal allele leads to this presentation. If both copies of the region are inherited from the paternal allele the result is the presentation of Angelman syndrome (figure 13.6).",True,Deletions and duplications,Figure 13.6,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
95803b91-5bce-4633-a44f-8747b3aa418e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Duplications refer to a chromosome segment appearing in two (often sequentially inserted) copies on a single homolog. Most of the time, this is caused by a nonhomologous recombination in the first meiotic division.",True,Deletions and duplications,,,,
93cd14bf-147b-450a-95b9-4df362aae142,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Inversion,False,Inversion,,,,
bd7d0820-b037-44b8-8869-ec997592e8da,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
bd7d0820-b037-44b8-8869-ec997592e8da,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
bd7d0820-b037-44b8-8869-ec997592e8da,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Inversion occurs when a chromosome segment between two breaks is rotated 180 degrees before reinsertion. The gene copy number remains the same; clinical symptoms may arise if there is an additional deletion or duplication, if the breaks occur within the coding region of a gene, or if the regulation of a gene is altered. Like other balanced chromosomal aberrations, inversions may cause infertility, recurrent miscarriages, or an unbalanced chromosome complement in a child (figure 13.7).",True,Inversion,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
b1e0c43a-62a5-4f3f-a2c6-9d4e23e57fac,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Isochromosome,False,Isochromosome,,,,
46010809-ac49-47fd-9bfe-b2772b4b2ca8,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,An isochromosome is a derivative chromosome with two homologous arms after the centromere divided transversely rather than longitudinally. An isochromosome can be thought of as a “mirror image” of either the short arm or the long arm of a given chromosome.,True,Isochromosome,,,,
93cc7c24-72e8-4bb0-9fdb-ec85f9664da1,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Ring chromosome,False,Ring chromosome,,,,
31564071-2d89-4cd8-8cb6-56874b7a1891,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Ring chromosomes occur when a chromosome breaks at both ends and the ends join together. They typically become clinically relevant through the loss of chromosomal material distal to the breaks. Ring chromosome X causes 5 percent of Turner syndrome cases.,True,Ring chromosome,,,,
8454e84b-bbc9-4a9e-a6e4-71431978576e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Translocations,False,Translocations,,,,
386f60e0-37c1-408a-8053-1c6f9081e277,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
386f60e0-37c1-408a-8053-1c6f9081e277,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
386f60e0-37c1-408a-8053-1c6f9081e277,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Translocations occur most often during meiosis if unequal crossing over occurs. Additionally, translocations (interchange of genetic material between nonhomologous chromosomes) can be another source of chromosomal abnormality (figure 13.7).",True,Translocations,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
abba14fd-eeeb-4d9a-8492-5a79018cdd7b,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Translocations can be classified as either reciprocal or Robertsonian.,False,Translocations can be classified as either reciprocal or Robertsonian.,,,,
3b790a92-98d4-4d3e-a3a4-2dd88dbde590,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,13.1 References and resources,True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
3c3acca9-d39d-4084-b8ff-eda3e59c4390,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 11: Meiosis and Sexual Reproduction, Chapter 13: Modern Understandings of Inheritance, Chapter 17: Biotechnology and Genomics.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
6ba9295f-b163-48a4-941d-0576e3752b07,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 52–55.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
68dc1470-44ac-4a51-950a-fca5b1677b19,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"LeClair, R. J., and R. G. Best. “Chromosome Mechanics.” eLS (2016): 1–11. https://onlinelibrary.wiley.com/doi/….a0001441.pub3.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
4cfe801e-da6e-4692-badb-c2e2c2e2df58,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 5: Principles of Clinical Cytogenetics.",True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
1ac7c3a9-eb50-4956-aaeb-10cb14c75bf8,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
1ac7c3a9-eb50-4956-aaeb-10cb14c75bf8,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
1ac7c3a9-eb50-4956-aaeb-10cb14c75bf8,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Bolzer A, Kreth G, Solovei I, et al. Figure 13.1 Representative karyotype illustrating 22 pairs of autosomes and one pair of sex chromosomes. PLoSBiol3.5.Fig7ChromosomesAluFish. CC BY 2.5. From WIkimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.1,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
90f4ae7e-f172-4963-86a6-1712806a4317,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
90f4ae7e-f172-4963-86a6-1712806a4317,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
90f4ae7e-f172-4963-86a6-1712806a4317,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Csink AK, Henikoff S. Figure 13.6 Genetic basis of Prader-Willi (PWS) and Angelman syndrome(AS). Adapted under Fair Use from Trends in Genetics. Volume 14, Issue 5, 1 May 1998, pp 194-200. Figure 2. Prader-Willi and Angelman syndromes.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.6,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
567ea980-7a8b-4dff-b58f-664ccc23c521,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
567ea980-7a8b-4dff-b58f-664ccc23c521,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
567ea980-7a8b-4dff-b58f-664ccc23c521,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.2 Basics of chromosome structure. 2021. https://archive.org/details/13.2_20210926. CC BY 4.0. Added Karyotype (normal) by National Cancer Institute. Public domain. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.2,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
3b074800-e731-4d71-99b7-a94ac3365128,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
3b074800-e731-4d71-99b7-a94ac3365128,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
3b074800-e731-4d71-99b7-a94ac3365128,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.3 Summary of meiotic and mitotic cell divisions. 2021. https://archive.org/details/13.3_20210926. CC BY 4.0. Adapted from Figure 1. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.3,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
af62cc02-3960-4864-b94f-21d8d3075a6f,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
af62cc02-3960-4864-b94f-21d8d3075a6f,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
af62cc02-3960-4864-b94f-21d8d3075a6f,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.4 Comparison on nondisjunction in meiosis I vs. meiosis II. 2021. https://archive.org/details/13.4_20210926. CC BY 4.0. Adapted from Figure 8. CC BY 4.0. From Open Oregon.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.4,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
d837695b-53fa-4975-b2f5-8e9ab904cc7e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
d837695b-53fa-4975-b2f5-8e9ab904cc7e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
d837695b-53fa-4975-b2f5-8e9ab904cc7e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.5 Mosaicism resulting in cells with differing genetics across the body. 2021. CC BY SA 3.0. Added Sperm by Amit Hazra from the Noun Project and Woman surface diagram ahead-behind dark skin by Jmarchn. CC BY-SA 3.0. From Wikimedia Commons.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.5,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
14d4cb52-10c1-4289-96e3-d6ec56a16502,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
14d4cb52-10c1-4289-96e3-d6ec56a16502,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
14d4cb52-10c1-4289-96e3-d6ec56a16502,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.7 Example of a chromosome inversion and translocation. 2021. https://archive.org/details/13.7_20210926. CC BY 4.0.",True,Translocations can be classified as either reciprocal or Robertsonian.,Figure 13.7,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
a8999d60-4f68-4c12-a3ad-a08db57620d6,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,13.2 Biotechnology,True,Translocations can be classified as either reciprocal or Robertsonian.,,,,
4d80a288-0e62-4418-a4cf-51ad7fea846a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Basic techniques to manipulate genetic material (DNA and RNA),False,Basic techniques to manipulate genetic material (DNA and RNA),,,,
8833529f-82e6-4a24-ba42-f6fb2cd2ad04,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"To evaluate genetic disorders a variety of biochemical techniques can be used. The type, kind, and size of the projected genetic variation will determine what approach is taken.",True,Basic techniques to manipulate genetic material (DNA and RNA),,,,
7b5f7abe-0cce-48fb-9dd7-2d686f169e84,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Following DNA extraction there are a variety of techniques that can be employed. The lowest resolution technique for evaluating the genome is the karyotype followed by high-resolution banding. From here, smaller genomic changes can be observed using comparative genome hybridization, fluorescence in situ hybridization (FISH) analysis, or microarrays. Finally, specific nucleotide changes can be examined by whole genome sequencing.",True,Basic techniques to manipulate genetic material (DNA and RNA),,,,
b9b5ac76-6102-4f2b-8ae5-54f9ca7078a6,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,microarrays,False,microarrays,,,,
1d35951f-e7d8-4bbb-b9a3-e4ba3231299f,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,DNA and RNA extraction,False,DNA and RNA extraction,,,,
23edce44-b6a1-43f8-bd55-a075ae1ae77a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
23edce44-b6a1-43f8-bd55-a075ae1ae77a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
23edce44-b6a1-43f8-bd55-a075ae1ae77a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"To study or manipulate nucleic acids, one must first isolate or extract the DNA or RNA from the cells. Most nucleic acid extraction techniques involve steps to break open the cell and use enzymatic reactions to destroy all macromolecules that are not desired. Enzymes such as proteases that break down proteins inactivate macromolecules, and ribonucleases (RNAses) that break down RNA are inhibited to ensure sample stability. Using alcohol precipitates the DNA. Human genomic DNA is usually visible as a gelatinous, white mass. One can store the DNA samples frozen at ‒80°C for several years (figure 13.8).",True,DNA and RNA extraction,Figure 13.8,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
9b1199db-3ef9-438e-980b-757a79eeee2e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,RNAses,False,RNAses,,,,
f63c273f-cdc6-46a0-9e73-4787942612b3,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Scientists perform RNA analysis to study gene expression patterns in cells. RNA is naturally very unstable because RNAses are commonly present in nature and very difficult to inactivate. Similar to DNA, RNA extraction involves using various buffers and enzymes to inactivate macromolecules and preserve the RNA.",True,RNAses,,,,
b871e65a-79be-4b00-be67-1ee1cc444192,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Karoytype and high-resolution banding,False,Karoytype and high-resolution banding,,,,
ab8f7d09-90f7-47a8-bf4a-1c173d63abe7,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Karyotyping can be used to look at general chromosome morphology and chromosome number. To do this, cells are harvested and arrested in metaphase allowing for the chromosomes to be fixed, spread on slides, and stained by one of several techniques. Giemsa banding (G banding) is the gold standard for the detection and characterization of structural and numerical genomic abnormalities in clinical diagnostic settings for both constitutional (postnatal or prenatal) and acquired (cancer) disorders.",True,Karoytype and high-resolution banding,,,,
aa26752d-cdea-4fb7-ab26-dcb5f69d1c51,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
aa26752d-cdea-4fb7-ab26-dcb5f69d1c51,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
aa26752d-cdea-4fb7-ab26-dcb5f69d1c51,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The pattern of light and dark bands on each chromosome is numbered on each arm from the centromere to the telomere, and comparison of a patient sample to a standard map can be used to precisely identify changes in chromosome structure. Microdeletion syndromes can be detected with this technique (figure 13.9).",True,Karoytype and high-resolution banding,Figure 13.9,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
37069341-2de3-49df-8a27-f37939e8d843,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Fluorescence in situ hybridization (FISH),False,Fluorescence in situ hybridization (FISH),,,,
5eae620c-21d9-4ea7-895f-2d96c7551ff3,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,FISH is a targeted approach using a sequence-specific probe to detect the presence or absence of a particular DNA sequence or for evaluating the number or organization of a chromosome or chromosomal region in situ.,True,Fluorescence in situ hybridization (FISH),,,,
f0809d8a-948d-4ac9-8bbc-cd6dd8ffc508,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,This technique has several advantages and can be used to identify a variety of different chromosomal changes:,True,Fluorescence in situ hybridization (FISH),,,,
16abc03c-c68b-4b12-80f2-45e04a8adc48,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Microarrays,False,Microarrays,,,,
9aa38909-c1ed-40da-aa8e-d34bd5ad2ee4,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Although FISH can detect chromosome changes, microarrays can simultaneously query the whole genome to detect relative copy number variations, gains, or losses by hybridizing a control genome to one of a patient. In looking at the results, an excess of sequences from one genome would represent an overrepresentation in a gene locus within an individual (duplication). This technique can also be used to look at single nucleotide polymorphisms to determine allele frequency.",True,Microarrays,,,,
bc44fb05-7bcd-4596-9f5f-3658d0c94299,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,DNA sequencing techniques,False,DNA sequencing techniques,,,,
afeeba53-d533-44ab-94c3-37097b589501,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Sanger sequencing is commonly referred to as the dideoxy chain termination method. The method is based on the use of chain terminators, the dideoxynucleotides (ddNTPs). The ddNTPSs differ from the deoxynucleotides by the lack of a free 3′ OH group on the five-carbon sugar. If a ddNTP is added to a growing DNA strand, the chain cannot be extended any further because the free 3′ OH group needed to add another nucleotide is not available. By using a predetermined ratio of deoxyribonucleotides to dideoxynucleotides, it is possible to generate DNA fragments of different sizes.",True,DNA sequencing techniques,,,,
cea0c97f-c59e-4ab3-91c8-853ec03703d2,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
cea0c97f-c59e-4ab3-91c8-853ec03703d2,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
cea0c97f-c59e-4ab3-91c8-853ec03703d2,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"The DNA sample to be sequenced is denatured (separated into two strands by heating it to high temperatures). The DNA is divided into four tubes in which a primer, DNA polymerase, and all four nucleoside triphosphates (A, T, G, and C) are added. In addition, limited quantities of one of the four dideoxynucleoside triphosphates (ddCTP, ddATP, ddGTP, and ddTTP) are added to each tube respectively. The tubes are labeled as A, T, G, and C according to the ddNTP added. For detection purposes, each of the four dideoxynucleotides carries a different fluorescent label. Chain elongation continues until a fluorescent dideoxy nucleotide is incorporated, after which no further elongation takes place. After the reaction is over, electrophoresis is performed. Even a difference in length of a single base can be detected (figure 13.10).",True,DNA sequencing techniques,Figure 13.10,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
6e306eb7-f528-41c8-a44e-0abc9c7d3734,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Nucleic acid fragment amplification by polymerase chain reaction (PCR),False,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
eee57f21-f7a1-492a-b7ab-09a39b4d3908,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
eee57f21-f7a1-492a-b7ab-09a39b4d3908,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
eee57f21-f7a1-492a-b7ab-09a39b4d3908,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"DNA analysis often requires focusing on one or more specific genome regions. Polymerase chain reaction (PCR) is a technique that scientists use to amplify specific DNA regions for further analysis (figure 13.11). Researchers use PCR for many purposes in laboratories, such as cloning gene fragments to analyze genetic diseases, identifying contaminant foreign DNA in a sample, and amplifying DNA for sequencing. More practical applications include determining paternity and detecting genetic diseases.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),Figure 13.11,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
a53a6627-be2a-44a2-9eda-96f1e726935d,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Scientists use polymerase chain reaction, or PCR, to amplify a specific DNA sequence. Primers are short pieces of DNA complementary to each end of the target sequence combined with genomic DNA, Taq polymerase, and deoxynucleotides.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
a35f673c-370d-4688-8bb8-634b9d2319e5,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Reverse transcriptase PCR (RT-PCR) is similar to PCR, but cDNA is made from an RNA template before PCR begins. DNA fragments can also be amplified from an RNA template in a process called reverse transcriptase PCR (RT-PCR). The first step is to recreate the original DNA template strand (called cDNA) by applying DNA nucleotides to the mRNA. This process is called reverse transcription. This requires the presence of an enzyme called reverse transcriptase. After the cDNA is made, regular PCR can be used to amplify it.",True,Nucleic acid fragment amplification by polymerase chain reaction (PCR),,,,
cb0ed28f-3140-456c-afdf-ff1f2b8d0f25,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Gel electrophoresis,False,Gel electrophoresis,,,,
3096c57b-c054-44f8-b3d8-c0387603bb56,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Gel electrophoresis is a technique used to separate DNA fragments of different sizes. Usually the gel is made of a chemical called agarose or polyacylamide depending on the sample being used. The DNA has a net negative charge and moves from the negative electrode toward the positive electrode. The electric current is applied for sufficient time to let the DNA separate according to size; the smallest fragments will be farthest from the well (where the DNA was loaded), and the heavier molecular weight fragments will be closest to the well. Once the DNA is separated, the gel is stained with a DNA-specific dye for viewing it.",True,Gel electrophoresis,,,,
89ed6a9b-3a48-4c38-9618-149f92b1740c,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Hybridization, southern blotting, and northern blotting",False,"Hybridization, southern blotting, and northern blotting",,,,
94c76fd5-c10b-4cf8-bd54-978cb624670e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Different types of electrophoresis can be used to look at various changes at the level of the DNA (genome), RNA (transcriptome), or protein (proteome). In all cases, a sample (DNA, RNA, protein) is run on a gel (electrophoresis) and is then examined using a probe specific to the sample.",True,"Hybridization, southern blotting, and northern blotting",,,,
78dc4dc4-366e-4071-b2d5-0d872edf319b,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
78dc4dc4-366e-4071-b2d5-0d872edf319b,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
78dc4dc4-366e-4071-b2d5-0d872edf319b,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Southern blots are designed to examine changes in DNA. DNA, typically genomic DNA, is probed with a DNA probe complementary to the region of interest in the genome (figure 13.12).",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
ef3bb760-83ad-41e0-ae11-5225bf35d6e2,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Northern blots are designed to examine changes in RNA. RNA is probed with a DNA probe complementary to the transcript of interest. This will detect changes in gene expression.,True,"Hybridization, southern blotting, and northern blotting",,,,
8df4f69c-8abf-45ab-9e91-b09e7f62f006,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,Western blots are designed to examine changes in protein size and amount. Cell lysates or protein isolates are probed with an antibody specific to the protein of interest. This will detect changes in protein expression.,True,"Hybridization, southern blotting, and northern blotting",,,,
060ee25c-d406-4ffe-9c89-f475d4d651db,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,13.2 References and resources,True,"Hybridization, southern blotting, and northern blotting",,,,
55f04b2f-df75-4a0a-850f-b45d9cbc032e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
55f04b2f-df75-4a0a-850f-b45d9cbc032e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
55f04b2f-df75-4a0a-850f-b45d9cbc032e,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.8 Basic process for DNA extraction. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.3 This diagram shows the basic method of DNA extraction.CC BY 4.0. From OpenStax. Added Test Tube by Victoria Codes from the Noun Project.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.8,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
3aecb2b2-fc48-4386-9441-cc628d32d26a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
3aecb2b2-fc48-4386-9441-cc628d32d26a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
3aecb2b2-fc48-4386-9441-cc628d32d26a,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.10 Schematic of Sanger sequencing technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.14 This figure illustrates Frederick Sanger’s dideoxy chain termination method. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.10,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
863562c8-d928-4d05-8cc7-8fd616c806ed,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
863562c8-d928-4d05-8cc7-8fd616c806ed,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
863562c8-d928-4d05-8cc7-8fd616c806ed,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Grey, Kindred, Figure 13.12 Schematic of Southern Blotting technique. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 17.6 Scientists use Southern blotting to find a particular sequence in a DNA sample. CC BY 4.0. From OpenStax.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.12,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
6556226b-8a91-474a-9699-1acd0e2ea9e6,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
6556226b-8a91-474a-9699-1acd0e2ea9e6,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
6556226b-8a91-474a-9699-1acd0e2ea9e6,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,"Lieberman M, Peet A. Figure 13.11 Overview of polymerase chain reaction. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 329. Figure 17.10 Polymerase chain reaction (PCR). 2017.",True,"Hybridization, southern blotting, and northern blotting",Figure 13.11,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
d925822e-68cb-487c-b6dc-4474f0ff381d,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13.2 Biotechnology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
d925822e-68cb-487c-b6dc-4474f0ff381d,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13.1 Chromosomal Structure and Cytogenetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
d925822e-68cb-487c-b6dc-4474f0ff381d,https://pressbooks.lib.vt.edu/cellbio/,13. Human Genetics,https://pressbooks.lib.vt.edu/cellbio/chapter/human-genetics/,National Cancer Institute. Figure 13.9 Male karyotype with G-banding patterns. Karyotype (normal). Public domain. From Wikimedia Commons.,True,"Hybridization, southern blotting, and northern blotting",Figure 13.9,13. Human Genetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
33f8d57d-33e6-4e6d-8074-027b7d7b4364,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Some genes (the so-called “house-keeping genes”) are likely (constitutively) expressed in all cell types since certain proteins (and RNAs) are involved in the basic metabolic processes common to all cell types. Other genes are expressed in one cell type but not another (e.g., certain immune cells normally synthesize antibodies, but neurons do not). Thus, different cell types arise because of differential gene expression, and the RNA and protein content of different cell types shows considerable variation.",True,"Hybridization, southern blotting, and northern blotting",,,,
af521ffa-f57b-46d6-a124-40bf570ffc65,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Changes to DNA content and rearrangement are addressed elsewhere. Briefly, DNA of different cell types does not vary in either amount or type. However, highly specialized cases are known to exist where DNA loss, rearrangement, and amplification profoundly influence gene expression in isolated situations.",True,"Hybridization, southern blotting, and northern blotting",,,,
93b89dcf-96dd-43c9-b39f-925faa1e5280,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,This section will focus on changes in gene expression.,False,This section will focus on changes in gene expression.,,,,
4919721a-cb1d-4049-b652-69dd417f3f5f,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Regulation is known to occur at several different points of a multistep gene expression pathway. Four main levels of control include:,True,This section will focus on changes in gene expression.,,,,
016da556-375c-4e28-b115-1cfcf298fe17,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"1. Transcriptional control: Determines if, how much, and when an mRNA is made.",True,This section will focus on changes in gene expression.,,,,
f430facd-a4b0-4ddf-ab3f-a3eaf4ceea7a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"2. Processing or post-transcriptional control: Determines if, how much, and when an mRNA is available for translation into a protein.",True,This section will focus on changes in gene expression.,,,,
cc073bf5-fcd2-4e27-9f6f-643a59645bc6,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"3. Translational control: Determines if, how much, and when a protein is made.",True,This section will focus on changes in gene expression.,,,,
0148cfbc-9494-4524-aa59-b1ac66bc349a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"4. Post-translational control: Determines if, how much, and when a protein is functional.",True,This section will focus on changes in gene expression.,,,,
4200372e-54b7-45c1-b35e-90e4dabb83e7,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Transcriptional control,False,Transcriptional control,,,,
8b7da794-28e6-4af4-af30-215c83639998,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Control of transcriptional initiation is a primary means used to regulate gene expression in eukaryotic organisms. Most eukaryotic genes are controlled at the level of transcription by proteins (trans-acting factors) that interact with specific gene sequences (cis-acting regulatory sequences).,True,Transcriptional control,,,,
0a8e0553-7ded-4201-bc25-9b9f35b6c11d,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Transcription factors: Enhancers,False,Transcription factors: Enhancers,,,,
367061fe-4d87-4a4d-b72b-297167a2fefc,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Along with general transcription factors, there are additional regions that help increase or enhance transcription. These regions, called enhancers, are not necessarily close to the genes they enhance. They can be located upstream of a gene, within the coding region of the gene, downstream of a gene, or thousands of nucleotides away.",True,Transcription factors: Enhancers,,,,
d5b65959-dc71-4f4e-8bb0-4a151b1b235a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
d5b65959-dc71-4f4e-8bb0-4a151b1b235a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
d5b65959-dc71-4f4e-8bb0-4a151b1b235a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
d5b65959-dc71-4f4e-8bb0-4a151b1b235a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
685814b8-4deb-40f5-afbe-cef4baf1830d,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Transcription factors: Repressors,False,Transcription factors: Repressors,,,,
6a3c0cfe-dbda-4ee9-8e2d-0b2c326af860,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6a3c0cfe-dbda-4ee9-8e2d-0b2c326af860,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6a3c0cfe-dbda-4ee9-8e2d-0b2c326af860,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6a3c0cfe-dbda-4ee9-8e2d-0b2c326af860,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
accccd04-a334-40f1-9729-ded7542a6a88,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Transcription factors: Structure and function,False,Transcription factors: Structure and function,,,,
a022a82e-54e6-499b-ba54-bfdd54a06938,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Structurally, transcription factors share similar characteristics but can take on very different secondary structures. Common examples of transcription factors include: Zn fingers, helix-loop-helixs, and leucine zippers. Regardless of structure, common characteristics include:",True,Transcription factors: Structure and function,,,,
6dca7235-56cb-43f1-9546-f97a92560741,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6dca7235-56cb-43f1-9546-f97a92560741,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6dca7235-56cb-43f1-9546-f97a92560741,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6dca7235-56cb-43f1-9546-f97a92560741,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
a8e49ddf-bd6f-4e8a-9fa6-3e41768bad44,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Processing or post/cotranscription,False,Processing or post/cotranscription,,,,
c401a277-9ba9-472b-a5d2-97727fecb737,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Alternative RNA splicing,False,Alternative RNA splicing,,,,
d6169e44-138e-4b82-a4fd-9cec550e51c5,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
d6169e44-138e-4b82-a4fd-9cec550e51c5,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
d6169e44-138e-4b82-a4fd-9cec550e51c5,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
d6169e44-138e-4b82-a4fd-9cec550e51c5,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
d65b68b9-44c4-4a98-81cd-1ae884edb312,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Translational control,False,Translational control,,,,
9e097e38-8dcd-49f1-88f8-8b0a58f953f2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Like transcription, translation is controlled by proteins that bind and initiate the process, restrict access to the mRNA, or control the localization of the transcript itself.",True,Translational control,,,,
2e45e955-a476-4e33-be99-b0e07fca97ed,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Localization,False,Localization,,,,
443c0cdd-107e-430a-ada3-615505f5de22,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,One fundamental way in which translation is controlled is physically by where the mRNA is located within the cell or organism. This is extremely important in development where restriction of a transcript to one side of a cell can influence the phenotype of a localized cellular region. This is largely mediated by interactions with the 5ʼ untranslated region (UTR).,True,Localization,,,,
aba73cc2-1dcf-4fa0-813d-c614ea0f1e20,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Translational initiation,False,Translational initiation,,,,
37bdb907-a86b-4f97-ab65-584c9710c87a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"In translation, the complex that assembles to start the process is referred to as the translation initiation complex, and similar to transcription, this complex can be activated or inhibited. In eukaryotes, translation is initiated by binding the initiating met-tRNAi to the 40S ribosome.",True,Translational initiation,,,,
926b42ec-c92b-44c7-97f6-44e2479f1895,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Initially the met-tRNAi is brought to the 40S ribosome by a protein initiation factor, eukaryotic initiation factor-2 (eIF-2). The eIF-2 protein binds to the high-energy molecule guanosine triphosphate (GTP), and the tRNA-eIF2-GTP complex then binds to the 40S ribosome.",True,Translational initiation,,,,
770b9711-0232-40e8-ab64-40ee0d174bd2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The cap-binding protein eIF4F brings the mRNA complex together with the 40S ribosome complex. The ribosome then scans along the mRNA until it finds a start codon AUG. When the anticodon of the initiator tRNA and the start codon are aligned, the GTP is hydrolyzed, the initiation factors are released, and the large 60S ribosomal subunit binds to form the translation complex. Insulin increases the efficiency of formation of the cap-binding complex, therefore increasing the rate of protein synthesis.",True,Translational initiation,,,,
6688d9da-2c39-4d8d-be5d-63939d208064,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
6688d9da-2c39-4d8d-be5d-63939d208064,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
6688d9da-2c39-4d8d-be5d-63939d208064,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
6688d9da-2c39-4d8d-be5d-63939d208064,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
457442d7-5171-457c-9e5c-05c7bf133402,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"When eIF-2 remains unphosphorylated, the initiation complex can form normally, and translation can continue.",True,Translational initiation,,,,
50f3d55e-c6bf-45de-9fad-36c322aa8b7a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Control of RNA stability,False,Control of RNA stability,,,,
5f51ed24-838f-44cb-b50a-b26b039520d4,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Before the mRNA leaves the nucleus, it is given two protective “caps” that prevent the ends of the strand from degrading during its journey. These changes protect the two ends of the RNA from exonuclease attack.",True,Control of RNA stability,,,,
d7d98aa6-b4b7-4b73-97d1-9259938be6c2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Once the RNA is transported to the cytoplasm, the length of time that the RNA resides there can be controlled. Each RNA molecule has a defined lifespan and decays at a specific rate. This rate of decay can influence how much protein is in the cell.",True,Control of RNA stability,,,,
c9089e4f-c894-4e4e-981e-0bbd35112417,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,RNA-binding proteins,False,RNA-binding proteins,,,,
ce0224fe-9431-43d0-8e14-e455e1c61d46,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
ce0224fe-9431-43d0-8e14-e455e1c61d46,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
ce0224fe-9431-43d0-8e14-e455e1c61d46,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
ce0224fe-9431-43d0-8e14-e455e1c61d46,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
c29ed357-a44d-45fb-a8c0-a3f782fea4db,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,One classic example of this is the regulation of transferrin receptor (TR) and ferritin levels in response to iron.,True,RNA-binding proteins,,,,
6a6b6098-3a61-4814-9c84-8ea1bc1a4d25,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,microRNAs,False,microRNAs,,,,
8f959f3d-c469-4a6d-b63f-178b429014d3,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"In addition to RBPs that bind to and control (increase or decrease) RNA stability, other elements called microRNAs can bind to the RNA molecule. These microRNAs, or miRNAs, are short RNA molecules that are only twenty-one to twenty-four nucleotides in length. The miRNAs are made in the nucleus as longer pre-miRNAs.",True,microRNAs,,,,
c01b4801-a7ea-4c68-8b99-f95a372fdecc,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"These pre-miRNAs are chopped into mature miRNAs by a protein called dicer. Like transcription factors and RBPs, mature miRNAs recognize a specific sequence and bind to the RNA; however, miRNAs also associate with a ribonucleoprotein complex called the RNA-induced silencing complex (RISC). The RNA component of the RISC base-pairs with complementary sequences on an mRNA and either impede translation of the message or lead to the degradation of the mRNA.",True,microRNAs,,,,
923619b1-db8d-40a5-8b2c-a268464a31e9,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Post-translation regulation,False,Post-translation regulation,,,,
6b3833c8-81cf-414e-8228-49bef96665c2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Chemical modifications,False,Chemical modifications,,,,
603fa7a9-237b-4431-9e2a-944fc3425c63,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Proteins can be chemically modified with the addition of groups including methyl, phosphate, acetyl, and ubiquitin groups.",True,Chemical modifications,,,,
0fef1d2b-ba12-42b0-8d07-3868869c4caa,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,The addition or removal of these groups from proteins can have many effects and can be in response to many cellular changes. For example:,True,Chemical modifications,,,,
ab14c964-07df-4939-8fd9-d0a5dd1aaa46,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"This is an efficient way for the cell to rapidly change the levels of specific proteins in response to the environment. Because proteins are involved in every stage of gene regulation, the phosphorylation of a protein (depending on the protein that is modified) can alter accessibility to the chromosome, can alter translation (by altering transcription factor binding or function), can change nuclear shuttling (by influencing modifications to the nuclear pore complex), can alter RNA stability (by binding or not binding to the RNA to regulate its stability), can modify translation (increase or decrease), or can change post-translational modifications (add or remove phosphates or other chemical modifications).",True,Chemical modifications,,,,
258d0094-5a9d-464c-9afd-b07b6ddf9308,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Protein degradation,False,Protein degradation,,,,
3794a3e3-c6cf-4f6c-b61d-3e19dd563d82,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
3794a3e3-c6cf-4f6c-b61d-3e19dd563d82,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
3794a3e3-c6cf-4f6c-b61d-3e19dd563d82,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
3794a3e3-c6cf-4f6c-b61d-3e19dd563d82,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
c45d42b4-b37d-4e09-9420-5e386f5ad9f7,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,12.1 References and resources,True,Protein degradation,,,,
8e38faa2-ffa1-42b4-b361-79ee84222f9a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 11: Meiosis and Sexual Reproduction, Chapter 16: Gene Expression.",True,Protein degradation,,,,
a1cc2d91-1fbd-4776-b83f-a5aa5a2a02f8,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 11: Gene Expression: From Transcription to Translation, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication and Repair, Chapter 14: Cellular Reproduction.",True,Protein degradation,,,,
84c40167-03c9-4bbb-ad15-47c2d5d6bc7e,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 41–43, 46.",True,Protein degradation,,,,
7281b61b-11c4-44a4-8b85-a842014f125b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 3: The Human Genome: Gene Structure and Function.",True,Protein degradation,,,,
931b53d2-cb69-4104-96a0-f802f533d303,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
931b53d2-cb69-4104-96a0-f802f533d303,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
931b53d2-cb69-4104-96a0-f802f533d303,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
931b53d2-cb69-4104-96a0-f802f533d303,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
d6c68435-2b6b-436d-bef6-9de190488161,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
d6c68435-2b6b-436d-bef6-9de190488161,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
d6c68435-2b6b-436d-bef6-9de190488161,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
d6c68435-2b6b-436d-bef6-9de190488161,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
63c3b683-e45a-4d65-8b52-213ac67bfaf2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
63c3b683-e45a-4d65-8b52-213ac67bfaf2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
63c3b683-e45a-4d65-8b52-213ac67bfaf2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
63c3b683-e45a-4d65-8b52-213ac67bfaf2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
b45042c5-36e6-4d51-a1d7-d0e449f7f0c8,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
b45042c5-36e6-4d51-a1d7-d0e449f7f0c8,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
b45042c5-36e6-4d51-a1d7-d0e449f7f0c8,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
b45042c5-36e6-4d51-a1d7-d0e449f7f0c8,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
a6bfc2b0-7fae-4331-993d-b6e0ec27cf23,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
a6bfc2b0-7fae-4331-993d-b6e0ec27cf23,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
a6bfc2b0-7fae-4331-993d-b6e0ec27cf23,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
a6bfc2b0-7fae-4331-993d-b6e0ec27cf23,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
7a2fc746-978b-4cab-b62e-0cf020a0cc85,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
7a2fc746-978b-4cab-b62e-0cf020a0cc85,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
7a2fc746-978b-4cab-b62e-0cf020a0cc85,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
7a2fc746-978b-4cab-b62e-0cf020a0cc85,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
bf948ae2-98a1-4320-98c4-9598b5e1e1db,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,12.2 Cell Cycle,True,Protein degradation,,,,
0cb860e9-a345-4ad5-943a-d712442cd199,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Checkpoints are the most critical, and the full summary of mitosis is for background.",True,Protein degradation,,,,
6509939a-9391-4994-814f-948222d62374,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6509939a-9391-4994-814f-948222d62374,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6509939a-9391-4994-814f-948222d62374,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6509939a-9391-4994-814f-948222d62374,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
99b98f46-60d1-4416-96c7-29b60ed5eb96,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Interphase,False,Interphase,,,,
105b3d64-6bb0-4cf4-938f-e426286e18da,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During interphase, the cell undergoes normal processes while also preparing for cell division. For a cell to move from interphase to the mitotic phase, many internal and external conditions must be met. The three stages of interphase are called G1, S, and G2.",True,Interphase,,,,
e25275c6-2011-4667-92f3-b7e25b965e37,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,G1 phase,False,G1 phase,,,,
1c2925e5-4138-4918-9836-c936481e48ab,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The first stage of interphase is called the G1 phase, or first gap, because little change is visible. However, during the G1 stage, the cell is quite active at the biochemical level. The cell is accumulating the building blocks of chromosomal DNA and the associated proteins, as well as accumulating enough energy reserves to complete the task of replicating each chromosome in the nucleus.",True,G1 phase,,,,
a6c53fea-a82e-4e4d-a3ab-1ce6b1b7d2e3,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,S phase,False,S phase,,,,
0b82a5bf-7dcc-4af8-b5da-e8b27bc3d705,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Throughout interphase, nuclear DNA remains in a semicondensed chromatin configuration. In the S phase (synthesis phase), DNA replication results in the formation of two identical copies of each chromosome (sister chromatids) that are firmly attached at the centromere region. At this stage, each chromosome is made of two sister chromatids and is a duplicated chromosome. The centrosome is duplicated during the S phase. The two centrosomes will give rise to the mitotic spindle, the apparatus that orchestrates the movement of chromosomes during mitosis. The centrosome consists of a pair of rod-like centrioles at right angles to each other. Centrioles help organize cell division.",True,S phase,,,,
d407796d-ffb2-4ce4-8545-674667397be1,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,semicondensed,False,semicondensed,,,,
60b0d740-5f51-43a0-8680-0ea49bdea8c2,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,G2 phase,False,G2 phase,,,,
bd64bebc-3339-4fdc-bc03-a077f29e85b5,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"In the G2 phase, or second gap, the cell replenishes its energy stores and synthesizes the proteins necessary for chromosome manipulation. Some cell organelles are duplicated, and the cytoskeleton is dismantled to provide resources for the mitotic spindle. The final preparations for the mitotic phase must be completed before the cell is able to enter the first stage of mitosis.",True,G2 phase,,,,
26dd9eec-4474-4635-9d37-658ba10ddf26,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,The mitotic phase,False,The mitotic phase,,,,
8edbac20-35c4-4c26-98c8-9c7ae612807b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
8edbac20-35c4-4c26-98c8-9c7ae612807b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
8edbac20-35c4-4c26-98c8-9c7ae612807b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
8edbac20-35c4-4c26-98c8-9c7ae612807b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
08de86c7-21a8-4db0-858f-89c7af66f42e,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Mitosis,False,Mitosis,,,,
5e1592ed-3c7f-4ab2-88c1-933406ae20e4,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
5e1592ed-3c7f-4ab2-88c1-933406ae20e4,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
5e1592ed-3c7f-4ab2-88c1-933406ae20e4,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
5e1592ed-3c7f-4ab2-88c1-933406ae20e4,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
6d23414b-b6e8-49a5-aebc-69cb7b88dbae,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During prophase, the “first phase,” several events must occur to provide access to the chromosomes in the nucleus. The nuclear envelope starts to break into small vesicles, and the Golgi apparatus and endoplasmic reticulum fragment and disperse to the periphery of the cell. The nucleolus disappears. The centrosomes begin to move to opposite poles of the cell. The microtubules that form the basis of the mitotic spindle extend between the centrosomes, pushing them farther apart as the microtubule fibers lengthen. The sister chromatids begin to coil more tightly and become visible under a light microscope.",True,Mitosis,,,,
df5b2100-6271-4eb4-afc7-6a20a3fd09b5,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During prometaphase, many processes that were begun in prophase continue to advance and culminate in the formation of a connection between the chromosomes and cytoskeleton. The remnants of the nuclear envelope disappear. The mitotic spindle continues to develop as more microtubules assemble and stretch across the length of the former nuclear area. Chromosomes become more condensed and visually discrete. Each sister chromatid attaches to spindle microtubules at the centromere via a protein complex called the kinetochore.",True,Mitosis,,,,
dbd33494-e584-45e0-a1c3-8d37c4e40577,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During metaphase, all the chromosomes are aligned in a plane called the metaphase plate, or the equatorial plane, midway between the two poles of the cell. The sister chromatids are still tightly attached to each other. At this time, the chromosomes are maximally condensed.",True,Mitosis,,,,
bcceb08f-4e7a-418c-811e-cb84e7086a0c,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During anaphase, the sister chromatids at the equatorial plane are split apart at the centromere. Each chromatid, now called a chromosome, is pulled rapidly toward the centrosome to which its microtubule was attached. The cell becomes visibly elongated as the nonkinetochore microtubules slide against each other at the metaphase plate where they overlap.",True,Mitosis,,,,
fb4cab6f-e65d-4230-99d9-c5ddea8e0da5,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During telophase, all the events that set up the duplicated chromosomes for mitosis during the first three phases are reversed. The chromosomes reach the opposite poles and begin to decondense (unravel). The mitotic spindles are broken down into monomers that will be used to assemble cytoskeleton components for each daughter cell. Nuclear envelopes form around chromosomes.",True,Mitosis,,,,
510c92e0-2e29-4413-a255-56e3ad3d5968,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Control of the cell cycle,False,Control of the cell cycle,,,,
35ed8f4e-a1e1-426f-af7a-272531415e77,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,There are three key checkpoints in the cell cycle that provide regulation oversight:,True,Control of the cell cycle,,,,
a068935c-a4a5-453a-be41-6e328c1d4e74,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Progress through these checkpoints is regulated by a family of cyclin dependent kinases (CDKs). These proteins are constitutive (always present) and inactive. CDKs bind specific cyclin activators, which are required for activity of the kinase. CDKs are present throughout the cell cycle, but expression of the cyclins is restricted to certain times in the cycle, and they are rapidly degraded as the cells progress through the checkpoints. Through binding of cyclins and negative regulation by phosphorylation by CDK inhibitors (CKIs), the cycle is tightly regulated in a restricted manner.",True,Control of the cell cycle,,,,
c86c0c7f-5445-46c3-a1ca-dea804ea9599,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,The cyclin and CDK complex can be produced from a combination of different cyclins (A‒D) and different CDKs (1‒6).,True,Control of the cell cycle,,,,
a0fa624b-a128-4299-a30f-edd569bc18a4,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Rb-protein,False,Rb-protein,,,,
4d18c87e-8476-448f-9447-f9ef4dac3054,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Rb-protein (pRb, retinoblastoma protein) is an important substrate of the G1/S‒CDK complexes. During the G0 and G1 phases, Rb is present in an unphosphorylated (hypophosphorylationed) form, which binds to the transcription factor E2F and thereby blocks it from initiating transcription. When the cycle moves into the S1 phase, pRb becomes phosphorylated (by the CyclinD/CDK4/6 active complex), which allows for the release of E2F.",True,Rb-protein,,,,
9c41e7b5-6787-451d-9505-767c5bac67b8,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,DNA damage,False,DNA damage,,,,
55f18151-12f7-40ec-8f7f-1b148f9ef178,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During the process of DNA replication, DNA damage will halt the process until it can be repaired. Likewise, extrinsic damaging factors can trigger a DNA repair process. Protein p53 is commonly known for its role in DNA repair mechanisms. Under nonstressful conditions it is bound to mdm2 within the cytosol. In response to stress and DNA damage, it is activated, through ATM- or ATR-mediated phosphorylation. Once active, it functions as a transcription factor and induces the synthesis of protein p21.",True,DNA damage,,,,
f2e8c384-0600-4e06-9b4b-327a15ae0718,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
f2e8c384-0600-4e06-9b4b-327a15ae0718,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
f2e8c384-0600-4e06-9b4b-327a15ae0718,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
f2e8c384-0600-4e06-9b4b-327a15ae0718,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7f75fdd9-ee93-43b0-ad35-38b63dc7deea,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7f75fdd9-ee93-43b0-ad35-38b63dc7deea,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7f75fdd9-ee93-43b0-ad35-38b63dc7deea,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7f75fdd9-ee93-43b0-ad35-38b63dc7deea,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
5ef01268-bfdf-490c-9ceb-d7b97ace660d,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,12.2 References and resources,True,DNA damage,,,,
eccfb1bb-d75a-4cca-8013-59343ed72b45,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Text,False,Text,,,,
96fae94d-06c7-468a-a01c-e148dcbf5543,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
96fae94d-06c7-468a-a01c-e148dcbf5543,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
96fae94d-06c7-468a-a01c-e148dcbf5543,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
96fae94d-06c7-468a-a01c-e148dcbf5543,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
39913e28-bff0-4f38-b1bf-88370fa3cb10,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
39913e28-bff0-4f38-b1bf-88370fa3cb10,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
39913e28-bff0-4f38-b1bf-88370fa3cb10,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
39913e28-bff0-4f38-b1bf-88370fa3cb10,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
ee072d43-688e-48dd-83be-f6c023c37c12,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
ee072d43-688e-48dd-83be-f6c023c37c12,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
ee072d43-688e-48dd-83be-f6c023c37c12,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
ee072d43-688e-48dd-83be-f6c023c37c12,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
25559ec4-a7fc-462d-80b4-4ad8c36492fc,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,12.3 Meiosis,True,Text,,,,
9a28540c-770e-4d36-8678-b8278223e355,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The twenty-three chromosome pairs in humans accounts for all the genetic information needed to survive. For most of the components within the cell, only an approximation of division is needed during cell replication, however, with respect to division of DNA, this duplication and segregation must be exact. The integrity of the genetic information within the cell is critical for the well-being of the organisms and its offspring, so these processes are clearly controlled.",True,Text,,,,
6ad6a192-a3c3-4c94-baf1-9e85513f7b41,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Within the cell cycle, the process of mitosis is largely responsible for this intricate chromosomal division of the somatic (body) cells by which two identical diploid daughter cells are produced through deoxyribonucleic acid (DNA) replication and cytoplasmic division.",True,Text,,,,
da75e659-0020-4de3-afe1-eea1197d5a94,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"In contrast, meiosis is a specialized process of the germline (sperm and eggs) that involves one round of DNA replication followed by two cell divisions to produce four haploid germ cells. Unlike mitosis, the resulting germ cells differ in males and females.",True,Text,,,,
b42ff3d7-8c5d-4659-b637-9b2d0f1d2f15,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Male meiosis results in the production of four equally sized, functional spermatozoa, while female meiosis results in a single large functional ovum and three small nonfunctional polar bodies. Abnormalities in these processes include chromosomal nondisjunction, which results in the loss or gain of one or more chromosomes, and chromosomal breakage due to unrepaired DNA damage, which results in the formation of abnormal chromosomes and an increased risk for neoplasia.",True,Text,,,,
62227dc9-1bd2-4aa7-99cc-5881edfac36e,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Meiosis,False,Meiosis,,,,
27fbc03c-b817-48ce-a612-3ec33ef8793b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
27fbc03c-b817-48ce-a612-3ec33ef8793b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
27fbc03c-b817-48ce-a612-3ec33ef8793b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
27fbc03c-b817-48ce-a612-3ec33ef8793b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
84719ee6-9306-4492-ac68-64dea5296121,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,reductional,False,reductional,,,,
ae41e1a0-9b6e-4a1e-8a02-9cc106044a99,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,equational,False,equational,,,,
0e2d0410-8bda-4bbe-a41c-42c4ec5e97ea,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Meiosis I: Reductional division,False,Meiosis I: Reductional division,,,,
506c343e-d8a4-4f72-baef-d3e3551748ba,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Before meiosis, gametic stem cells replicate through mitosis. At the very beginning of meiosis, the last G1 phase of the diploid stem cells is followed by chromosome replication during S phase and G2, ending the last somatic interphase. Thus, each cell enters meiosis with two copies of the diploid genome (2n, 2c). At this point, the spermatogonium (male somatic cell) enlarges to become a primary spermatocyte, and the oogonium (female somatic cell) enlarges to become a primary oocyte.",True,Meiosis I: Reductional division,,,,
5f0925e0-53e2-43af-8eae-cd7e40d24184,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"These cells then enter prophase I, which is subdivided into five stages: leptotene, zygotene, pachytene, diplotene, and diakinesis. In female meiosis, there is an additional stage following diplotene called dictyotene in which the oocyte remains from early fetal gestation until ovulation when diakinesis occurs.",True,Meiosis I: Reductional division,,,,
4253ac3b-887e-48f7-ae46-fc1578ebb7ea,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Prophase I,False,Prophase I,,,,
10f38a4e-4226-4698-8f80-ea38ac80c29b,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"During prophase I, homologous chromosomes pair and undergo recombination through crossing over. This is visualized by the presence of X-shaped connections between homologues, called chiasmata, as the homologues begin to repel each other. These chiasmata will aid in the proper segregation of the chromosomes and become more prominent during diplotene. This is where the synaptoneal complex dissolves, allowing for chromosomal condensation to continue and for the repulsion of homologous chromosomes. The separation of the homologous chromosomes causes the chiasmata to appear. Individual chromatids can be visualized during this stage. (The dictyotene stage is unique to female meiosis in which there is a decondensation of chromosomal bivalents. The oocyte remains in this state for many years until follicle maturation and ovulation.)",True,Prophase I,,,,
bdb6b745-1727-4044-808a-b7386f3fb073,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,synaptoneal,False,synaptoneal,,,,
f89e7146-6dd0-4c73-a650-ac491cf9cf28,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,decondensation,False,decondensation,,,,
6819f41a-5045-408f-a96f-31d073b7bfd8,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"At diakinesis, chromosomal condensation is completed. The chiasmata on each arm of the chromosomes move distally toward the telomeres. Each bivalent contains four chromatids, and pairs of sister chromatids are linked at the centromeres.",True,decondensation,,,,
bc459fcf-d528-4c50-aede-f49776364c23,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Metaphase I,False,Metaphase I,,,,
b57fb932-de3e-4f21-a9f4-d4cb3aa2e322,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The spindle forms, and the nuclear membrane disappears. Bivalents align on the metaphase plate still held together by the chiasmata. The centromeres of the two homologous chromosomes are separate, aligning on either side of the equatorial plate.",True,Metaphase I,,,,
cccbe06a-17eb-4957-bfa9-eab90bf54652,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Anaphase I,False,Anaphase I,,,,
aa55585f-6446-4ed0-b518-d78cf0ac1287,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Homologous chromosomes separate from each other by final terminalization of the chiasmata. They move to opposite poles, pulled by the centromere, which is attached to spindle fibers.",True,Anaphase I,,,,
99d6a865-38b4-4e1a-8cc3-b3c0f372513d,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Telophase I,False,Telophase I,,,,
20e4e682-7ddc-4d3c-86d0-26066857094e,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The chromosomes reach the poles, a nuclear membrane is formed, and cell division occurs. In male meiosis, the cytoplasm is divided equally, and the two resulting cells become secondary spermatocytes. In female meiosis, the division is unequal; most of the cytoplasm is retained in the secondary oocyte, while very little is retained by the first polar body. This period is very brief, and chromosomes move immediately to the second meiotic division. Each cell at this stage is haploid (1n) but with each chromosome formed of sister chromatids (2c). The sister chromatids may be unique due to recombination during the two homologues in prophase I.",True,Telophase I,,,,
71fa4314-4fe2-4d50-97c1-7eef3039a932,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Meiosis II: Equational division,False,Meiosis II: Equational division,,,,
3e4ac15e-8183-45f4-b16c-72735b913a5a,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"This division is similar to mitosis in that individual chromosomes align on the metaphase plate, and sister chromatids separate and move to opposite poles at anaphase. The single copy (1c) of each chromosome is represented by one sister chromatid in the spermatids or mature ova.",True,Meiosis II: Equational division,,,,
7dfcb110-3420-47d9-ad26-b14d71313d08,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Male meiosis,False,Male meiosis,,,,
8c48d5e5-7238-4733-8245-819cbdf179aa,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"In humans, the male is the heterogametic sex, producing two kinds of normal sperm: 23,X and 23,Y. Spermatogenesis is a constant event beginning at puberty and continuing throughout life to produce four functional spermatids from each primary gametocyte. At puberty, the number of spermatogonia (diploid stem cells) increases. These develop into primary spermatocytes after several mitotic divisions. Each primary spermatocyte undergoes the first meiotic division to become two secondary spermatocytes. These cells then undergo the second meiotic division to become four spermatids of equal size with a haploid set of chromosomes. Spermiogenesis then transforms the spermatids into mature spermatozoa by elimination of the cytoplasm, elongation of the head of the sperm, and formation of a tail. The entire process from the enlargement of the spermatogonium to formation of the mature spermatozoa takes approximately sixty-four days.",True,Male meiosis,,,,
608e578b-cdd6-46fe-8c5d-67f97140b6bb,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Female meiosis,False,Female meiosis,,,,
79c6561c-6540-40ff-9e66-06da1fbebf90,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"This is in contrast to meiosis in females, which begins before birth and produces only a single type of normal ovum: 23,X. The precursors to the germ cells are oogonia; these increase in number through mitosis, reaching a maximum number of approximately 7 million. Each individual oogonium enlarges to form a primary oocyte, which becomes surrounded by ovarian stromal cells to form a primary follicle. The vast majority of primary oocytes are formed during the third and fourth months of fetal life.",True,Female meiosis,,,,
f2a219d7-e3cc-452a-b52f-05cf8e6a3506,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"The primary oocyte begins the first meiotic division to become a secondary oocyte with the extrusion of a small polar body as the follicle matures and completes metaphase I with expulsion from the mature follicle at ovulation. The secondary oocyte does not complete the second meiotic division until fertilization, when a second polar body is extruded to form a mature ovum with a haploid set of chromosomes. Thus, each primary oocyte produces one functional gamete, the mature ovum, and three polar bodies. A nuclear membrane forms a pronucleus around the haploid set of maternal chromosomes, while a second pronucleus forms from the haploid set of chromosomes from the sperm head. These two pronuclei then fuse to begin the first mitotic division.",True,Female meiosis,,,,
2db043d8-a739-4b20-98d1-59ce22e7714c,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,Meiotic pairing,False,Meiotic pairing,,,,
3d3fdbc3-4e5d-443b-b93a-a6eda82d7d56,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Homologous pairing is unique to meiosis and plays two important roles: genetic recombination and chromosomal stabilization. While it has long been believed that the former is the most important, the latter is now accepted as the primary significance of meiotic recombination. During meiosis I, the pairing of homologues facilitates recombination, which is initiated by programed double-stranded breaks occurring at synaptic initiation sites (SISs). A subset of these breaks will resolve into the formation of the synaptonemal complex. When pairing is completed, synapsis occurs between the homologues, which completes the crossing over event. Each crossover event forms chasmata, which play an analogous role to the centromere and stabilize the maternal and paternal chromosomes. The stabilization of the metaphase chromosomes using this mechanism is key to normal chromosomal alignment and maintenance of an intact genome. Without recombination, the total number of unique gametic combinations of genes for each parent would be just over 8 million. However, crossing over greatly increases the total number of possible gene combinations such that the likelihood of either parent producing identical gametes is vanishingly small.",True,Meiotic pairing,,,,
1309681f-3c8e-49d6-ba7a-c59a43252048,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,12.3 References and resources,True,Meiotic pairing,,,,
e6f78724-5964-484b-b67a-c9d2e3ded76f,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
e6f78724-5964-484b-b67a-c9d2e3ded76f,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
e6f78724-5964-484b-b67a-c9d2e3ded76f,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
e6f78724-5964-484b-b67a-c9d2e3ded76f,https://pressbooks.lib.vt.edu/cellbio/,12.3 Meiosis,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-3,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
23e988cb-f2bd-47f4-91db-be5f545d8c9e,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Some genes (the so-called “house-keeping genes”) are likely (constitutively) expressed in all cell types since certain proteins (and RNAs) are involved in the basic metabolic processes common to all cell types. Other genes are expressed in one cell type but not another (e.g., certain immune cells normally synthesize antibodies, but neurons do not). Thus, different cell types arise because of differential gene expression, and the RNA and protein content of different cell types shows considerable variation.",True,Meiotic pairing,,,,
fcd32db9-30cb-4734-9c73-7ce548a6c35b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Changes to DNA content and rearrangement are addressed elsewhere. Briefly, DNA of different cell types does not vary in either amount or type. However, highly specialized cases are known to exist where DNA loss, rearrangement, and amplification profoundly influence gene expression in isolated situations.",True,Meiotic pairing,,,,
68b22356-a6a3-4399-a469-b9e1c9836f69,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,This section will focus on changes in gene expression.,False,This section will focus on changes in gene expression.,,,,
f611aa6e-7ab2-453e-bb69-376e85d7411d,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Regulation is known to occur at several different points of a multistep gene expression pathway. Four main levels of control include:,True,This section will focus on changes in gene expression.,,,,
6586749d-c0be-48d8-84a7-dd3bd5ffee42,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"1. Transcriptional control: Determines if, how much, and when an mRNA is made.",True,This section will focus on changes in gene expression.,,,,
5e4cf4da-e8ab-4e7e-a545-8066ab7bc00a,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"2. Processing or post-transcriptional control: Determines if, how much, and when an mRNA is available for translation into a protein.",True,This section will focus on changes in gene expression.,,,,
de4afdef-3484-47c2-9428-73f9f852e372,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"3. Translational control: Determines if, how much, and when a protein is made.",True,This section will focus on changes in gene expression.,,,,
4450dfe9-6657-45b4-b4c5-ea4c2f0df531,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"4. Post-translational control: Determines if, how much, and when a protein is functional.",True,This section will focus on changes in gene expression.,,,,
c647a6af-b7a6-4003-af51-1069fd787481,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Transcriptional control,False,Transcriptional control,,,,
a296bfa2-1a2b-434a-b6bd-bdd1fb694925,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Control of transcriptional initiation is a primary means used to regulate gene expression in eukaryotic organisms. Most eukaryotic genes are controlled at the level of transcription by proteins (trans-acting factors) that interact with specific gene sequences (cis-acting regulatory sequences).,True,Transcriptional control,,,,
0057801f-cbd7-47d4-a4da-215eae201bf6,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Transcription factors: Enhancers,False,Transcription factors: Enhancers,,,,
d5c3ebbc-648e-43df-a6c7-ed674b50c114,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Along with general transcription factors, there are additional regions that help increase or enhance transcription. These regions, called enhancers, are not necessarily close to the genes they enhance. They can be located upstream of a gene, within the coding region of the gene, downstream of a gene, or thousands of nucleotides away.",True,Transcription factors: Enhancers,,,,
4d7c237b-3880-454f-8d2c-5d7542d45428,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
4d7c237b-3880-454f-8d2c-5d7542d45428,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
4d7c237b-3880-454f-8d2c-5d7542d45428,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
4d7c237b-3880-454f-8d2c-5d7542d45428,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
aa4197ad-e562-4760-88cb-651a45b6c721,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Transcription factors: Repressors,False,Transcription factors: Repressors,,,,
10c7b9b7-0a3e-4a84-96d9-dcf9c52a55f7,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
10c7b9b7-0a3e-4a84-96d9-dcf9c52a55f7,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
10c7b9b7-0a3e-4a84-96d9-dcf9c52a55f7,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
10c7b9b7-0a3e-4a84-96d9-dcf9c52a55f7,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
667a6c20-802e-4697-b360-7a6be7ee8e9b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Transcription factors: Structure and function,False,Transcription factors: Structure and function,,,,
04ac9810-1118-4fa4-9bb2-cd0980205184,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Structurally, transcription factors share similar characteristics but can take on very different secondary structures. Common examples of transcription factors include: Zn fingers, helix-loop-helixs, and leucine zippers. Regardless of structure, common characteristics include:",True,Transcription factors: Structure and function,,,,
344f8f78-da14-48d5-baa5-b229b90a68e1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
344f8f78-da14-48d5-baa5-b229b90a68e1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
344f8f78-da14-48d5-baa5-b229b90a68e1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
344f8f78-da14-48d5-baa5-b229b90a68e1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6df55e1a-7072-48c4-a926-229addf7474a,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Processing or post/cotranscription,False,Processing or post/cotranscription,,,,
d6eb473a-63cd-4a4b-9b0d-55e2d0ff1acf,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Alternative RNA splicing,False,Alternative RNA splicing,,,,
65fbb8c8-35c4-451c-9531-4ce4d1b84b1f,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
65fbb8c8-35c4-451c-9531-4ce4d1b84b1f,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
65fbb8c8-35c4-451c-9531-4ce4d1b84b1f,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
65fbb8c8-35c4-451c-9531-4ce4d1b84b1f,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
6fc29a30-4c5c-4f2b-baa8-d4628d271c1a,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Translational control,False,Translational control,,,,
c8dee7a0-0026-4ffb-814f-eaf26196d583,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Like transcription, translation is controlled by proteins that bind and initiate the process, restrict access to the mRNA, or control the localization of the transcript itself.",True,Translational control,,,,
998f149a-f31f-4bff-a39e-fadb56ebee77,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Localization,False,Localization,,,,
954ea118-4783-440b-affd-72eeca23d462,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,One fundamental way in which translation is controlled is physically by where the mRNA is located within the cell or organism. This is extremely important in development where restriction of a transcript to one side of a cell can influence the phenotype of a localized cellular region. This is largely mediated by interactions with the 5ʼ untranslated region (UTR).,True,Localization,,,,
e8b6321d-e543-4315-bce9-2713640fd549,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Translational initiation,False,Translational initiation,,,,
74346ce4-b4fa-44da-a58a-051532b89c9e,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"In translation, the complex that assembles to start the process is referred to as the translation initiation complex, and similar to transcription, this complex can be activated or inhibited. In eukaryotes, translation is initiated by binding the initiating met-tRNAi to the 40S ribosome.",True,Translational initiation,,,,
1224958d-2b19-4057-9ff7-00b6c020cb58,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Initially the met-tRNAi is brought to the 40S ribosome by a protein initiation factor, eukaryotic initiation factor-2 (eIF-2). The eIF-2 protein binds to the high-energy molecule guanosine triphosphate (GTP), and the tRNA-eIF2-GTP complex then binds to the 40S ribosome.",True,Translational initiation,,,,
4eed397c-b1da-4640-a1ce-7df46bc1f294,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The cap-binding protein eIF4F brings the mRNA complex together with the 40S ribosome complex. The ribosome then scans along the mRNA until it finds a start codon AUG. When the anticodon of the initiator tRNA and the start codon are aligned, the GTP is hydrolyzed, the initiation factors are released, and the large 60S ribosomal subunit binds to form the translation complex. Insulin increases the efficiency of formation of the cap-binding complex, therefore increasing the rate of protein synthesis.",True,Translational initiation,,,,
bab2213a-5326-4a2c-9254-855f2cf83e14,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
bab2213a-5326-4a2c-9254-855f2cf83e14,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
bab2213a-5326-4a2c-9254-855f2cf83e14,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
bab2213a-5326-4a2c-9254-855f2cf83e14,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
911ff25a-bd02-4bfb-aaac-d80817c02bad,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"When eIF-2 remains unphosphorylated, the initiation complex can form normally, and translation can continue.",True,Translational initiation,,,,
7bc3da47-a4e3-4af3-b805-2f203e178e91,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Control of RNA stability,False,Control of RNA stability,,,,
0a070d3f-9ba4-445f-838f-b49304df243a,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Before the mRNA leaves the nucleus, it is given two protective “caps” that prevent the ends of the strand from degrading during its journey. These changes protect the two ends of the RNA from exonuclease attack.",True,Control of RNA stability,,,,
d74dfba6-898d-453e-bb94-5ad64165c1f4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Once the RNA is transported to the cytoplasm, the length of time that the RNA resides there can be controlled. Each RNA molecule has a defined lifespan and decays at a specific rate. This rate of decay can influence how much protein is in the cell.",True,Control of RNA stability,,,,
2d2fcbbb-6456-451d-b1c9-49dd0962540e,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,RNA-binding proteins,False,RNA-binding proteins,,,,
5b40a6f8-53c3-4d02-8eb2-306c35c5919c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
5b40a6f8-53c3-4d02-8eb2-306c35c5919c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
5b40a6f8-53c3-4d02-8eb2-306c35c5919c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
5b40a6f8-53c3-4d02-8eb2-306c35c5919c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
a26396e5-cc9e-4c8c-a0b5-fd012e5c6f7a,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,One classic example of this is the regulation of transferrin receptor (TR) and ferritin levels in response to iron.,True,RNA-binding proteins,,,,
4bd0e201-1131-4acd-9ab2-9732091fe7c1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,microRNAs,False,microRNAs,,,,
0114fecc-1a06-48fa-9a61-2c694e44a166,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"In addition to RBPs that bind to and control (increase or decrease) RNA stability, other elements called microRNAs can bind to the RNA molecule. These microRNAs, or miRNAs, are short RNA molecules that are only twenty-one to twenty-four nucleotides in length. The miRNAs are made in the nucleus as longer pre-miRNAs.",True,microRNAs,,,,
74b6f2f0-f873-4255-8b6f-f64851445369,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"These pre-miRNAs are chopped into mature miRNAs by a protein called dicer. Like transcription factors and RBPs, mature miRNAs recognize a specific sequence and bind to the RNA; however, miRNAs also associate with a ribonucleoprotein complex called the RNA-induced silencing complex (RISC). The RNA component of the RISC base-pairs with complementary sequences on an mRNA and either impede translation of the message or lead to the degradation of the mRNA.",True,microRNAs,,,,
a5e38c46-feff-4526-bf81-637dd48ece0d,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Post-translation regulation,False,Post-translation regulation,,,,
cfaca258-60b4-40ea-aab0-dfa8004ed173,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Chemical modifications,False,Chemical modifications,,,,
ffbcd641-2d46-4c75-9ef2-0e595170da6f,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Proteins can be chemically modified with the addition of groups including methyl, phosphate, acetyl, and ubiquitin groups.",True,Chemical modifications,,,,
944cdff5-140c-494c-8aab-f7af61c8178e,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,The addition or removal of these groups from proteins can have many effects and can be in response to many cellular changes. For example:,True,Chemical modifications,,,,
939f73bc-429f-4727-9368-c8efc53be437,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"This is an efficient way for the cell to rapidly change the levels of specific proteins in response to the environment. Because proteins are involved in every stage of gene regulation, the phosphorylation of a protein (depending on the protein that is modified) can alter accessibility to the chromosome, can alter translation (by altering transcription factor binding or function), can change nuclear shuttling (by influencing modifications to the nuclear pore complex), can alter RNA stability (by binding or not binding to the RNA to regulate its stability), can modify translation (increase or decrease), or can change post-translational modifications (add or remove phosphates or other chemical modifications).",True,Chemical modifications,,,,
8d787dab-bd2f-4ead-bf83-c14831293fd5,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Protein degradation,False,Protein degradation,,,,
11a873d4-29cc-427f-8257-022179543972,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
11a873d4-29cc-427f-8257-022179543972,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
11a873d4-29cc-427f-8257-022179543972,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
11a873d4-29cc-427f-8257-022179543972,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
150c275f-85f7-4103-afbf-0c20d7c61d68,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,12.1 References and resources,True,Protein degradation,,,,
8a5e633c-d07c-4fdc-a24b-c23765c0f4d2,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 11: Meiosis and Sexual Reproduction, Chapter 16: Gene Expression.",True,Protein degradation,,,,
4c0a4bab-497e-4f15-8989-11de9a8cc093,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 11: Gene Expression: From Transcription to Translation, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication and Repair, Chapter 14: Cellular Reproduction.",True,Protein degradation,,,,
fb99844a-8486-4be2-bda9-a1d770711cae,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 41–43, 46.",True,Protein degradation,,,,
0875bc34-47b9-4b2d-a22a-86b0ec3c39b1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 3: The Human Genome: Gene Structure and Function.",True,Protein degradation,,,,
f3eba175-dd63-454c-8abe-91b1742e5e41,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
f3eba175-dd63-454c-8abe-91b1742e5e41,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
f3eba175-dd63-454c-8abe-91b1742e5e41,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
f3eba175-dd63-454c-8abe-91b1742e5e41,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
8a4092e5-659d-43cb-9086-c97bb48d589c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
8a4092e5-659d-43cb-9086-c97bb48d589c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
8a4092e5-659d-43cb-9086-c97bb48d589c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
8a4092e5-659d-43cb-9086-c97bb48d589c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
7dea9efa-589f-4a44-9e41-cbf15a5af753,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
7dea9efa-589f-4a44-9e41-cbf15a5af753,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
7dea9efa-589f-4a44-9e41-cbf15a5af753,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
7dea9efa-589f-4a44-9e41-cbf15a5af753,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
3e6ea70f-2878-4eae-a4dc-b096b9ab5aed,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
3e6ea70f-2878-4eae-a4dc-b096b9ab5aed,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
3e6ea70f-2878-4eae-a4dc-b096b9ab5aed,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
3e6ea70f-2878-4eae-a4dc-b096b9ab5aed,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
e51b9a5a-7e85-4b46-a5ef-a8da13f0df16,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
e51b9a5a-7e85-4b46-a5ef-a8da13f0df16,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
e51b9a5a-7e85-4b46-a5ef-a8da13f0df16,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
e51b9a5a-7e85-4b46-a5ef-a8da13f0df16,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
4ab09ec8-4aeb-4162-a3e7-9e2b24fbf919,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
4ab09ec8-4aeb-4162-a3e7-9e2b24fbf919,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
4ab09ec8-4aeb-4162-a3e7-9e2b24fbf919,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
4ab09ec8-4aeb-4162-a3e7-9e2b24fbf919,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
3071698b-fd21-47f4-a2b8-b775ed571e4b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,12.2 Cell Cycle,True,Protein degradation,,,,
70427791-813f-4ab2-bcb6-027c6b49ffad,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Checkpoints are the most critical, and the full summary of mitosis is for background.",True,Protein degradation,,,,
6020208d-e1c6-42aa-8850-0537d79a983b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6020208d-e1c6-42aa-8850-0537d79a983b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6020208d-e1c6-42aa-8850-0537d79a983b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6020208d-e1c6-42aa-8850-0537d79a983b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
ac3c4896-0d5b-4a1b-be4e-c69e02a8396d,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Interphase,False,Interphase,,,,
2fc85cfe-3fff-40a9-b3cb-bf3c072dbcf2,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During interphase, the cell undergoes normal processes while also preparing for cell division. For a cell to move from interphase to the mitotic phase, many internal and external conditions must be met. The three stages of interphase are called G1, S, and G2.",True,Interphase,,,,
5df135d3-9928-453d-8c36-d6c1125e0e61,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,G1 phase,False,G1 phase,,,,
338d4557-978a-4f4e-bac6-b9251847ed29,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The first stage of interphase is called the G1 phase, or first gap, because little change is visible. However, during the G1 stage, the cell is quite active at the biochemical level. The cell is accumulating the building blocks of chromosomal DNA and the associated proteins, as well as accumulating enough energy reserves to complete the task of replicating each chromosome in the nucleus.",True,G1 phase,,,,
a4b25793-b643-437a-9342-e184314e84eb,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,S phase,False,S phase,,,,
77067ce0-18be-4011-b006-6ebcdc56ce1c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Throughout interphase, nuclear DNA remains in a semicondensed chromatin configuration. In the S phase (synthesis phase), DNA replication results in the formation of two identical copies of each chromosome (sister chromatids) that are firmly attached at the centromere region. At this stage, each chromosome is made of two sister chromatids and is a duplicated chromosome. The centrosome is duplicated during the S phase. The two centrosomes will give rise to the mitotic spindle, the apparatus that orchestrates the movement of chromosomes during mitosis. The centrosome consists of a pair of rod-like centrioles at right angles to each other. Centrioles help organize cell division.",True,S phase,,,,
8af768e6-2b7f-47f5-9f1c-60983e1dd09b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,semicondensed,False,semicondensed,,,,
c9fe0bf6-ea84-49b2-88f3-56e4e0566c8b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,G2 phase,False,G2 phase,,,,
b97d394a-cbc4-470c-a80f-b64c40546720,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"In the G2 phase, or second gap, the cell replenishes its energy stores and synthesizes the proteins necessary for chromosome manipulation. Some cell organelles are duplicated, and the cytoskeleton is dismantled to provide resources for the mitotic spindle. The final preparations for the mitotic phase must be completed before the cell is able to enter the first stage of mitosis.",True,G2 phase,,,,
3a9861a7-5f54-49f7-96f1-959181c6104d,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,The mitotic phase,False,The mitotic phase,,,,
76304aa1-4406-4dc0-9df1-3b90180bd708,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
76304aa1-4406-4dc0-9df1-3b90180bd708,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
76304aa1-4406-4dc0-9df1-3b90180bd708,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
76304aa1-4406-4dc0-9df1-3b90180bd708,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
520dd68e-452c-4fd9-bb2a-c595bbbc291a,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Mitosis,False,Mitosis,,,,
1db38312-af33-4ca9-808d-2106cdff4016,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
1db38312-af33-4ca9-808d-2106cdff4016,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
1db38312-af33-4ca9-808d-2106cdff4016,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
1db38312-af33-4ca9-808d-2106cdff4016,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
97f31855-a1bc-4105-914e-3655a529033f,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During prophase, the “first phase,” several events must occur to provide access to the chromosomes in the nucleus. The nuclear envelope starts to break into small vesicles, and the Golgi apparatus and endoplasmic reticulum fragment and disperse to the periphery of the cell. The nucleolus disappears. The centrosomes begin to move to opposite poles of the cell. The microtubules that form the basis of the mitotic spindle extend between the centrosomes, pushing them farther apart as the microtubule fibers lengthen. The sister chromatids begin to coil more tightly and become visible under a light microscope.",True,Mitosis,,,,
4ace6e1f-7c4e-47c4-b4ff-28a0e2c6f092,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During prometaphase, many processes that were begun in prophase continue to advance and culminate in the formation of a connection between the chromosomes and cytoskeleton. The remnants of the nuclear envelope disappear. The mitotic spindle continues to develop as more microtubules assemble and stretch across the length of the former nuclear area. Chromosomes become more condensed and visually discrete. Each sister chromatid attaches to spindle microtubules at the centromere via a protein complex called the kinetochore.",True,Mitosis,,,,
4ab8f333-3546-4bb6-8199-148d50fe754b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During metaphase, all the chromosomes are aligned in a plane called the metaphase plate, or the equatorial plane, midway between the two poles of the cell. The sister chromatids are still tightly attached to each other. At this time, the chromosomes are maximally condensed.",True,Mitosis,,,,
b19e7338-a9d8-4b52-b8ed-2a89db1ee899,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During anaphase, the sister chromatids at the equatorial plane are split apart at the centromere. Each chromatid, now called a chromosome, is pulled rapidly toward the centrosome to which its microtubule was attached. The cell becomes visibly elongated as the nonkinetochore microtubules slide against each other at the metaphase plate where they overlap.",True,Mitosis,,,,
a29b266e-19f3-4623-b796-53bb621ebbc8,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During telophase, all the events that set up the duplicated chromosomes for mitosis during the first three phases are reversed. The chromosomes reach the opposite poles and begin to decondense (unravel). The mitotic spindles are broken down into monomers that will be used to assemble cytoskeleton components for each daughter cell. Nuclear envelopes form around chromosomes.",True,Mitosis,,,,
36bbcd69-09fd-4f3c-a9aa-30d68d6b0ee6,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Control of the cell cycle,False,Control of the cell cycle,,,,
28bdcbf5-7c7c-4423-8002-215d7f31c915,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,There are three key checkpoints in the cell cycle that provide regulation oversight:,True,Control of the cell cycle,,,,
68061fe8-f6c7-4d59-a6f7-27f9a06b90e4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Progress through these checkpoints is regulated by a family of cyclin dependent kinases (CDKs). These proteins are constitutive (always present) and inactive. CDKs bind specific cyclin activators, which are required for activity of the kinase. CDKs are present throughout the cell cycle, but expression of the cyclins is restricted to certain times in the cycle, and they are rapidly degraded as the cells progress through the checkpoints. Through binding of cyclins and negative regulation by phosphorylation by CDK inhibitors (CKIs), the cycle is tightly regulated in a restricted manner.",True,Control of the cell cycle,,,,
1ae525b3-cd84-4597-9b07-0aea4256cca1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,The cyclin and CDK complex can be produced from a combination of different cyclins (A‒D) and different CDKs (1‒6).,True,Control of the cell cycle,,,,
b78202c1-dabd-4372-9a76-6dcba2db424d,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Rb-protein,False,Rb-protein,,,,
0e41da0b-2710-4d89-bca6-4fee910649a1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Rb-protein (pRb, retinoblastoma protein) is an important substrate of the G1/S‒CDK complexes. During the G0 and G1 phases, Rb is present in an unphosphorylated (hypophosphorylationed) form, which binds to the transcription factor E2F and thereby blocks it from initiating transcription. When the cycle moves into the S1 phase, pRb becomes phosphorylated (by the CyclinD/CDK4/6 active complex), which allows for the release of E2F.",True,Rb-protein,,,,
b7f33b2f-b2ac-47b3-a7a3-7d795b3daa99,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,DNA damage,False,DNA damage,,,,
4173de2d-6a1a-4ee5-904e-f4cdd66d5517,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During the process of DNA replication, DNA damage will halt the process until it can be repaired. Likewise, extrinsic damaging factors can trigger a DNA repair process. Protein p53 is commonly known for its role in DNA repair mechanisms. Under nonstressful conditions it is bound to mdm2 within the cytosol. In response to stress and DNA damage, it is activated, through ATM- or ATR-mediated phosphorylation. Once active, it functions as a transcription factor and induces the synthesis of protein p21.",True,DNA damage,,,,
d0d3314e-96c6-4467-9de9-cb38ae095fbc,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
d0d3314e-96c6-4467-9de9-cb38ae095fbc,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
d0d3314e-96c6-4467-9de9-cb38ae095fbc,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
d0d3314e-96c6-4467-9de9-cb38ae095fbc,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
da93c859-0f97-40c0-9e43-cd766558e392,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
da93c859-0f97-40c0-9e43-cd766558e392,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
da93c859-0f97-40c0-9e43-cd766558e392,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
da93c859-0f97-40c0-9e43-cd766558e392,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
088082c8-1e5b-4fbe-bc53-7875c97bfaf8,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,12.2 References and resources,True,DNA damage,,,,
5537b88f-28ee-4704-9197-5e4934b31788,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Text,False,Text,,,,
9af8f18d-d465-41ce-a540-8af04548954c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
9af8f18d-d465-41ce-a540-8af04548954c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
9af8f18d-d465-41ce-a540-8af04548954c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
9af8f18d-d465-41ce-a540-8af04548954c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6047ea4a-06af-4288-80aa-0b2f6c1c78cd,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
6047ea4a-06af-4288-80aa-0b2f6c1c78cd,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
6047ea4a-06af-4288-80aa-0b2f6c1c78cd,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
6047ea4a-06af-4288-80aa-0b2f6c1c78cd,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
ce33b3a0-f764-4f83-b10b-f1aac3c2cc72,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
ce33b3a0-f764-4f83-b10b-f1aac3c2cc72,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
ce33b3a0-f764-4f83-b10b-f1aac3c2cc72,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
ce33b3a0-f764-4f83-b10b-f1aac3c2cc72,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
9408b206-45de-41d6-b89e-88d186c5d780,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,12.3 Meiosis,True,Text,,,,
d9726cd2-6dcb-4202-987c-a38fab73f1db,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The twenty-three chromosome pairs in humans accounts for all the genetic information needed to survive. For most of the components within the cell, only an approximation of division is needed during cell replication, however, with respect to division of DNA, this duplication and segregation must be exact. The integrity of the genetic information within the cell is critical for the well-being of the organisms and its offspring, so these processes are clearly controlled.",True,Text,,,,
58b51a30-c3ef-420f-a658-8ec333c327a4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Within the cell cycle, the process of mitosis is largely responsible for this intricate chromosomal division of the somatic (body) cells by which two identical diploid daughter cells are produced through deoxyribonucleic acid (DNA) replication and cytoplasmic division.",True,Text,,,,
ab39e74a-0a58-4afd-ad3a-5192a9882339,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"In contrast, meiosis is a specialized process of the germline (sperm and eggs) that involves one round of DNA replication followed by two cell divisions to produce four haploid germ cells. Unlike mitosis, the resulting germ cells differ in males and females.",True,Text,,,,
192b849c-15b0-40a5-9627-97b1c3047ecd,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Male meiosis results in the production of four equally sized, functional spermatozoa, while female meiosis results in a single large functional ovum and three small nonfunctional polar bodies. Abnormalities in these processes include chromosomal nondisjunction, which results in the loss or gain of one or more chromosomes, and chromosomal breakage due to unrepaired DNA damage, which results in the formation of abnormal chromosomes and an increased risk for neoplasia.",True,Text,,,,
a18d9a35-f93d-4b20-b6f9-0bc36ff20a8b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Meiosis,False,Meiosis,,,,
eb66a954-3f2d-4766-ac5d-67e1259c4aa5,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
eb66a954-3f2d-4766-ac5d-67e1259c4aa5,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
eb66a954-3f2d-4766-ac5d-67e1259c4aa5,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
eb66a954-3f2d-4766-ac5d-67e1259c4aa5,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
a1e84586-ec57-48d5-b2c3-4cfed54108b8,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,reductional,False,reductional,,,,
484e09dd-29e2-43bf-a522-f9100f9fe451,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,equational,False,equational,,,,
0e92a4b7-5296-4994-a865-0c639c39d0eb,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Meiosis I: Reductional division,False,Meiosis I: Reductional division,,,,
11ae79ae-8d8f-43c3-a356-9dadee71685c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Before meiosis, gametic stem cells replicate through mitosis. At the very beginning of meiosis, the last G1 phase of the diploid stem cells is followed by chromosome replication during S phase and G2, ending the last somatic interphase. Thus, each cell enters meiosis with two copies of the diploid genome (2n, 2c). At this point, the spermatogonium (male somatic cell) enlarges to become a primary spermatocyte, and the oogonium (female somatic cell) enlarges to become a primary oocyte.",True,Meiosis I: Reductional division,,,,
b637b9ad-083b-4f39-9bd3-ff3fb2d7fd05,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"These cells then enter prophase I, which is subdivided into five stages: leptotene, zygotene, pachytene, diplotene, and diakinesis. In female meiosis, there is an additional stage following diplotene called dictyotene in which the oocyte remains from early fetal gestation until ovulation when diakinesis occurs.",True,Meiosis I: Reductional division,,,,
9d40d6de-8e07-40d1-b84f-13909305aca4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Prophase I,False,Prophase I,,,,
2814aa4a-680c-4685-81f1-33f7eb45d5d7,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"During prophase I, homologous chromosomes pair and undergo recombination through crossing over. This is visualized by the presence of X-shaped connections between homologues, called chiasmata, as the homologues begin to repel each other. These chiasmata will aid in the proper segregation of the chromosomes and become more prominent during diplotene. This is where the synaptoneal complex dissolves, allowing for chromosomal condensation to continue and for the repulsion of homologous chromosomes. The separation of the homologous chromosomes causes the chiasmata to appear. Individual chromatids can be visualized during this stage. (The dictyotene stage is unique to female meiosis in which there is a decondensation of chromosomal bivalents. The oocyte remains in this state for many years until follicle maturation and ovulation.)",True,Prophase I,,,,
e7e140a6-429a-4b84-8ed7-e793c4db8ad5,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,synaptoneal,False,synaptoneal,,,,
eb3c43fe-c730-4ce5-993e-af89b9ad459b,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,decondensation,False,decondensation,,,,
ec50a37d-5e41-45d0-93b3-dbdddb22d3b1,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"At diakinesis, chromosomal condensation is completed. The chiasmata on each arm of the chromosomes move distally toward the telomeres. Each bivalent contains four chromatids, and pairs of sister chromatids are linked at the centromeres.",True,decondensation,,,,
a34b3c7e-bbd0-4e9e-bea5-d74b0de318dc,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Metaphase I,False,Metaphase I,,,,
8d695087-1de6-4199-8c2e-65c25102f181,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The spindle forms, and the nuclear membrane disappears. Bivalents align on the metaphase plate still held together by the chiasmata. The centromeres of the two homologous chromosomes are separate, aligning on either side of the equatorial plate.",True,Metaphase I,,,,
8fc418d0-1787-42c8-bca4-6b10fe3d2858,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Anaphase I,False,Anaphase I,,,,
c28ac672-e273-4215-8025-3e0b939f67e8,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Homologous chromosomes separate from each other by final terminalization of the chiasmata. They move to opposite poles, pulled by the centromere, which is attached to spindle fibers.",True,Anaphase I,,,,
681bc3fe-c481-4428-88e5-9909cd131aa4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Telophase I,False,Telophase I,,,,
0a97b0d9-90fd-41d0-9d59-202acdfcfcec,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The chromosomes reach the poles, a nuclear membrane is formed, and cell division occurs. In male meiosis, the cytoplasm is divided equally, and the two resulting cells become secondary spermatocytes. In female meiosis, the division is unequal; most of the cytoplasm is retained in the secondary oocyte, while very little is retained by the first polar body. This period is very brief, and chromosomes move immediately to the second meiotic division. Each cell at this stage is haploid (1n) but with each chromosome formed of sister chromatids (2c). The sister chromatids may be unique due to recombination during the two homologues in prophase I.",True,Telophase I,,,,
809cae5e-60a0-4d29-89b7-466cd8ae569f,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Meiosis II: Equational division,False,Meiosis II: Equational division,,,,
56bc1ffd-9800-4b71-98d7-f100f36fb762,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"This division is similar to mitosis in that individual chromosomes align on the metaphase plate, and sister chromatids separate and move to opposite poles at anaphase. The single copy (1c) of each chromosome is represented by one sister chromatid in the spermatids or mature ova.",True,Meiosis II: Equational division,,,,
b5bb71b2-8d5f-4e62-8b8e-ab8c590941da,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Male meiosis,False,Male meiosis,,,,
952e277d-ee47-469c-b38a-0ad2344c4047,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"In humans, the male is the heterogametic sex, producing two kinds of normal sperm: 23,X and 23,Y. Spermatogenesis is a constant event beginning at puberty and continuing throughout life to produce four functional spermatids from each primary gametocyte. At puberty, the number of spermatogonia (diploid stem cells) increases. These develop into primary spermatocytes after several mitotic divisions. Each primary spermatocyte undergoes the first meiotic division to become two secondary spermatocytes. These cells then undergo the second meiotic division to become four spermatids of equal size with a haploid set of chromosomes. Spermiogenesis then transforms the spermatids into mature spermatozoa by elimination of the cytoplasm, elongation of the head of the sperm, and formation of a tail. The entire process from the enlargement of the spermatogonium to formation of the mature spermatozoa takes approximately sixty-four days.",True,Male meiosis,,,,
f445ffda-6e07-41c4-82e3-81e8ad17edad,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Female meiosis,False,Female meiosis,,,,
4c97e731-ebb6-430b-8f37-b6dd7d0eedc9,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"This is in contrast to meiosis in females, which begins before birth and produces only a single type of normal ovum: 23,X. The precursors to the germ cells are oogonia; these increase in number through mitosis, reaching a maximum number of approximately 7 million. Each individual oogonium enlarges to form a primary oocyte, which becomes surrounded by ovarian stromal cells to form a primary follicle. The vast majority of primary oocytes are formed during the third and fourth months of fetal life.",True,Female meiosis,,,,
277163fa-88c6-4a41-ab1a-375707c31945,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"The primary oocyte begins the first meiotic division to become a secondary oocyte with the extrusion of a small polar body as the follicle matures and completes metaphase I with expulsion from the mature follicle at ovulation. The secondary oocyte does not complete the second meiotic division until fertilization, when a second polar body is extruded to form a mature ovum with a haploid set of chromosomes. Thus, each primary oocyte produces one functional gamete, the mature ovum, and three polar bodies. A nuclear membrane forms a pronucleus around the haploid set of maternal chromosomes, while a second pronucleus forms from the haploid set of chromosomes from the sperm head. These two pronuclei then fuse to begin the first mitotic division.",True,Female meiosis,,,,
70208c18-333f-4830-b1e0-9f3e8f6da05c,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,Meiotic pairing,False,Meiotic pairing,,,,
68ba4edb-8265-4d8b-8ebe-a9a744d82bd6,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Homologous pairing is unique to meiosis and plays two important roles: genetic recombination and chromosomal stabilization. While it has long been believed that the former is the most important, the latter is now accepted as the primary significance of meiotic recombination. During meiosis I, the pairing of homologues facilitates recombination, which is initiated by programed double-stranded breaks occurring at synaptic initiation sites (SISs). A subset of these breaks will resolve into the formation of the synaptonemal complex. When pairing is completed, synapsis occurs between the homologues, which completes the crossing over event. Each crossover event forms chasmata, which play an analogous role to the centromere and stabilize the maternal and paternal chromosomes. The stabilization of the metaphase chromosomes using this mechanism is key to normal chromosomal alignment and maintenance of an intact genome. Without recombination, the total number of unique gametic combinations of genes for each parent would be just over 8 million. However, crossing over greatly increases the total number of possible gene combinations such that the likelihood of either parent producing identical gametes is vanishingly small.",True,Meiotic pairing,,,,
1c0ab38a-ce36-41a9-a368-aa4c4a03f181,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,12.3 References and resources,True,Meiotic pairing,,,,
6aaa9b31-290e-407c-ac75-d81aca50a9a4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
6aaa9b31-290e-407c-ac75-d81aca50a9a4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
6aaa9b31-290e-407c-ac75-d81aca50a9a4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
6aaa9b31-290e-407c-ac75-d81aca50a9a4,https://pressbooks.lib.vt.edu/cellbio/,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-2,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
8af273ad-481d-4e3a-a01c-bb126e8b2375,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Some genes (the so-called “house-keeping genes”) are likely (constitutively) expressed in all cell types since certain proteins (and RNAs) are involved in the basic metabolic processes common to all cell types. Other genes are expressed in one cell type but not another (e.g., certain immune cells normally synthesize antibodies, but neurons do not). Thus, different cell types arise because of differential gene expression, and the RNA and protein content of different cell types shows considerable variation.",True,Meiotic pairing,,,,
78ed1b99-a6a8-4e39-b285-70b51450955a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Changes to DNA content and rearrangement are addressed elsewhere. Briefly, DNA of different cell types does not vary in either amount or type. However, highly specialized cases are known to exist where DNA loss, rearrangement, and amplification profoundly influence gene expression in isolated situations.",True,Meiotic pairing,,,,
e88d404c-a680-4b55-bba9-3cd1b272392a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,This section will focus on changes in gene expression.,False,This section will focus on changes in gene expression.,,,,
48f1acf6-c0bc-43c4-8f67-e0dc7961b743,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Regulation is known to occur at several different points of a multistep gene expression pathway. Four main levels of control include:,True,This section will focus on changes in gene expression.,,,,
84afec7d-69a4-427c-b9f0-85b5f705d00e,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"1. Transcriptional control: Determines if, how much, and when an mRNA is made.",True,This section will focus on changes in gene expression.,,,,
98888c80-7e92-40fd-a974-49c21b48eda6,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"2. Processing or post-transcriptional control: Determines if, how much, and when an mRNA is available for translation into a protein.",True,This section will focus on changes in gene expression.,,,,
f3b21712-71bc-4b3d-9bc1-93de082f8634,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"3. Translational control: Determines if, how much, and when a protein is made.",True,This section will focus on changes in gene expression.,,,,
04e466a9-9b72-4e5a-a9ed-22b04abd9bd5,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"4. Post-translational control: Determines if, how much, and when a protein is functional.",True,This section will focus on changes in gene expression.,,,,
a671bf4a-ce2a-4b44-8bbf-4ba54249357d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Transcriptional control,False,Transcriptional control,,,,
e5720506-cf72-4189-8db8-9523b858ef74,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Control of transcriptional initiation is a primary means used to regulate gene expression in eukaryotic organisms. Most eukaryotic genes are controlled at the level of transcription by proteins (trans-acting factors) that interact with specific gene sequences (cis-acting regulatory sequences).,True,Transcriptional control,,,,
fb925e25-62e5-4bce-823d-5b866ca37598,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Transcription factors: Enhancers,False,Transcription factors: Enhancers,,,,
1d00394b-6951-4761-bfbe-bff2062d0cc9,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Along with general transcription factors, there are additional regions that help increase or enhance transcription. These regions, called enhancers, are not necessarily close to the genes they enhance. They can be located upstream of a gene, within the coding region of the gene, downstream of a gene, or thousands of nucleotides away.",True,Transcription factors: Enhancers,,,,
99f0e06b-035a-40b0-82fe-dc366037a258,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
99f0e06b-035a-40b0-82fe-dc366037a258,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
99f0e06b-035a-40b0-82fe-dc366037a258,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
99f0e06b-035a-40b0-82fe-dc366037a258,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
d2bf2740-2c85-402c-a04d-30496b3d962a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Transcription factors: Repressors,False,Transcription factors: Repressors,,,,
67d046eb-67b7-4254-8b4d-ff41f5c640a8,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
67d046eb-67b7-4254-8b4d-ff41f5c640a8,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
67d046eb-67b7-4254-8b4d-ff41f5c640a8,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
67d046eb-67b7-4254-8b4d-ff41f5c640a8,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
8551bb1f-6ad4-4d0d-885e-c166e37da4f4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Transcription factors: Structure and function,False,Transcription factors: Structure and function,,,,
4eb6fdd2-cba1-4c32-aea6-34d5b3219746,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Structurally, transcription factors share similar characteristics but can take on very different secondary structures. Common examples of transcription factors include: Zn fingers, helix-loop-helixs, and leucine zippers. Regardless of structure, common characteristics include:",True,Transcription factors: Structure and function,,,,
fc017764-214a-40e9-83ad-57be7d71a577,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
fc017764-214a-40e9-83ad-57be7d71a577,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
fc017764-214a-40e9-83ad-57be7d71a577,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
fc017764-214a-40e9-83ad-57be7d71a577,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
cc3840a3-19b9-42ef-b12f-7dcf360fe2f1,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Processing or post/cotranscription,False,Processing or post/cotranscription,,,,
d9913fc4-afd4-4ce0-a36b-8f7f4169c783,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Alternative RNA splicing,False,Alternative RNA splicing,,,,
b6fdb752-1d72-447b-975b-f399e04db5eb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
b6fdb752-1d72-447b-975b-f399e04db5eb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
b6fdb752-1d72-447b-975b-f399e04db5eb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
b6fdb752-1d72-447b-975b-f399e04db5eb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
f8d24986-5017-47d8-bb43-f69123684786,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Translational control,False,Translational control,,,,
ebfaada1-bbfd-4196-863f-2311d2b3929b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Like transcription, translation is controlled by proteins that bind and initiate the process, restrict access to the mRNA, or control the localization of the transcript itself.",True,Translational control,,,,
591f14c7-a863-4d8b-98d3-aa7312347097,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Localization,False,Localization,,,,
4817e47e-bd69-44c0-8678-7ea210e67f98,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,One fundamental way in which translation is controlled is physically by where the mRNA is located within the cell or organism. This is extremely important in development where restriction of a transcript to one side of a cell can influence the phenotype of a localized cellular region. This is largely mediated by interactions with the 5ʼ untranslated region (UTR).,True,Localization,,,,
e1c46ec2-1137-46de-bea9-0c5fcc0cccb2,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Translational initiation,False,Translational initiation,,,,
19555e3b-5a2a-44bc-8a2f-4bd3bb7a6122,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"In translation, the complex that assembles to start the process is referred to as the translation initiation complex, and similar to transcription, this complex can be activated or inhibited. In eukaryotes, translation is initiated by binding the initiating met-tRNAi to the 40S ribosome.",True,Translational initiation,,,,
29e11c7e-07c6-49c4-bd41-4c37948ed900,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Initially the met-tRNAi is brought to the 40S ribosome by a protein initiation factor, eukaryotic initiation factor-2 (eIF-2). The eIF-2 protein binds to the high-energy molecule guanosine triphosphate (GTP), and the tRNA-eIF2-GTP complex then binds to the 40S ribosome.",True,Translational initiation,,,,
5ac5e98e-a1a2-4a27-aa14-950ce85088c9,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The cap-binding protein eIF4F brings the mRNA complex together with the 40S ribosome complex. The ribosome then scans along the mRNA until it finds a start codon AUG. When the anticodon of the initiator tRNA and the start codon are aligned, the GTP is hydrolyzed, the initiation factors are released, and the large 60S ribosomal subunit binds to form the translation complex. Insulin increases the efficiency of formation of the cap-binding complex, therefore increasing the rate of protein synthesis.",True,Translational initiation,,,,
4af143f7-0014-44d0-8585-f194cb402524,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
4af143f7-0014-44d0-8585-f194cb402524,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
4af143f7-0014-44d0-8585-f194cb402524,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
4af143f7-0014-44d0-8585-f194cb402524,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
b181a2cf-0340-4ac9-b3b3-101b2dc5882e,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"When eIF-2 remains unphosphorylated, the initiation complex can form normally, and translation can continue.",True,Translational initiation,,,,
ec5c35da-b93c-445a-88a5-50cdf9ff60cd,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Control of RNA stability,False,Control of RNA stability,,,,
2769a0d7-34c4-4ece-aafe-aee171256ac4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Before the mRNA leaves the nucleus, it is given two protective “caps” that prevent the ends of the strand from degrading during its journey. These changes protect the two ends of the RNA from exonuclease attack.",True,Control of RNA stability,,,,
58880c2a-7b86-45bd-9b2e-ec4e2084bd21,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Once the RNA is transported to the cytoplasm, the length of time that the RNA resides there can be controlled. Each RNA molecule has a defined lifespan and decays at a specific rate. This rate of decay can influence how much protein is in the cell.",True,Control of RNA stability,,,,
1c298c25-a4a2-45d0-a7ab-4690a51ecac1,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,RNA-binding proteins,False,RNA-binding proteins,,,,
bed87477-c7af-4e13-9d8d-9b92db17a7d4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
bed87477-c7af-4e13-9d8d-9b92db17a7d4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
bed87477-c7af-4e13-9d8d-9b92db17a7d4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
bed87477-c7af-4e13-9d8d-9b92db17a7d4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
efa9cf9a-db07-4e1c-8e2b-ef09c7c4d05d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,One classic example of this is the regulation of transferrin receptor (TR) and ferritin levels in response to iron.,True,RNA-binding proteins,,,,
c8a2b94a-8901-40d2-98a6-f8c3dfa70ce8,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,microRNAs,False,microRNAs,,,,
d8e72efe-4250-45cd-a5c9-843073c4ce30,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"In addition to RBPs that bind to and control (increase or decrease) RNA stability, other elements called microRNAs can bind to the RNA molecule. These microRNAs, or miRNAs, are short RNA molecules that are only twenty-one to twenty-four nucleotides in length. The miRNAs are made in the nucleus as longer pre-miRNAs.",True,microRNAs,,,,
b43f7893-0b17-459d-bd76-337616851bc0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"These pre-miRNAs are chopped into mature miRNAs by a protein called dicer. Like transcription factors and RBPs, mature miRNAs recognize a specific sequence and bind to the RNA; however, miRNAs also associate with a ribonucleoprotein complex called the RNA-induced silencing complex (RISC). The RNA component of the RISC base-pairs with complementary sequences on an mRNA and either impede translation of the message or lead to the degradation of the mRNA.",True,microRNAs,,,,
17ae6658-d26d-4580-80f0-5c067d6cd8bb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Post-translation regulation,False,Post-translation regulation,,,,
9b15e804-1a2c-401a-adb0-dcad959bd793,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Chemical modifications,False,Chemical modifications,,,,
7f4648d1-b171-4d80-9177-09e095012b4b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Proteins can be chemically modified with the addition of groups including methyl, phosphate, acetyl, and ubiquitin groups.",True,Chemical modifications,,,,
6b935d2c-8bbd-48be-a16e-dcb59a849e97,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,The addition or removal of these groups from proteins can have many effects and can be in response to many cellular changes. For example:,True,Chemical modifications,,,,
606b821d-487f-4778-b32f-5783d9288607,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"This is an efficient way for the cell to rapidly change the levels of specific proteins in response to the environment. Because proteins are involved in every stage of gene regulation, the phosphorylation of a protein (depending on the protein that is modified) can alter accessibility to the chromosome, can alter translation (by altering transcription factor binding or function), can change nuclear shuttling (by influencing modifications to the nuclear pore complex), can alter RNA stability (by binding or not binding to the RNA to regulate its stability), can modify translation (increase or decrease), or can change post-translational modifications (add or remove phosphates or other chemical modifications).",True,Chemical modifications,,,,
7664bb76-65a4-4cca-b8de-83cad8d26270,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Protein degradation,False,Protein degradation,,,,
015c7e8b-35df-493b-81cf-e509637d21d6,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
015c7e8b-35df-493b-81cf-e509637d21d6,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
015c7e8b-35df-493b-81cf-e509637d21d6,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
015c7e8b-35df-493b-81cf-e509637d21d6,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
232340d9-c2bc-4f06-8b53-a3ad1f0d5592,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,12.1 References and resources,True,Protein degradation,,,,
eba133c8-c59a-4d79-838f-67966c79cf91,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 11: Meiosis and Sexual Reproduction, Chapter 16: Gene Expression.",True,Protein degradation,,,,
4f3dc6a3-f383-40f2-a854-c541fc61bf6f,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 11: Gene Expression: From Transcription to Translation, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication and Repair, Chapter 14: Cellular Reproduction.",True,Protein degradation,,,,
b2e2b0a0-be13-4f2d-94b6-2a86dfc094c7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 41–43, 46.",True,Protein degradation,,,,
0f458c7d-e110-4b27-9f43-fdbe250d08f2,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 3: The Human Genome: Gene Structure and Function.",True,Protein degradation,,,,
65cdbcaf-adc8-48e5-833f-e06d6589709c,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
65cdbcaf-adc8-48e5-833f-e06d6589709c,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
65cdbcaf-adc8-48e5-833f-e06d6589709c,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
65cdbcaf-adc8-48e5-833f-e06d6589709c,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
c5a73a44-ce6d-4bd4-b983-93852a6ae1fb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
c5a73a44-ce6d-4bd4-b983-93852a6ae1fb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
c5a73a44-ce6d-4bd4-b983-93852a6ae1fb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
c5a73a44-ce6d-4bd4-b983-93852a6ae1fb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
a46b0578-942f-419b-9d70-1d9eb60ef2a7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
a46b0578-942f-419b-9d70-1d9eb60ef2a7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
a46b0578-942f-419b-9d70-1d9eb60ef2a7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
a46b0578-942f-419b-9d70-1d9eb60ef2a7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
be6e389d-540e-4755-abe4-96e4086730bd,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
be6e389d-540e-4755-abe4-96e4086730bd,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
be6e389d-540e-4755-abe4-96e4086730bd,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
be6e389d-540e-4755-abe4-96e4086730bd,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
9bac47ea-6123-4ab8-a5c7-5e925d1aaa2d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
9bac47ea-6123-4ab8-a5c7-5e925d1aaa2d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
9bac47ea-6123-4ab8-a5c7-5e925d1aaa2d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
9bac47ea-6123-4ab8-a5c7-5e925d1aaa2d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
0e240582-676c-4432-b101-939d699ebef0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
0e240582-676c-4432-b101-939d699ebef0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
0e240582-676c-4432-b101-939d699ebef0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
0e240582-676c-4432-b101-939d699ebef0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
a8f1c41d-7ef9-47fc-a0d3-df483dd57d79,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,12.2 Cell Cycle,True,Protein degradation,,,,
485b26d2-e407-49e0-81e0-81d5cc62b43f,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Checkpoints are the most critical, and the full summary of mitosis is for background.",True,Protein degradation,,,,
07058df6-a5f6-4068-be57-78fff888a400,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
07058df6-a5f6-4068-be57-78fff888a400,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
07058df6-a5f6-4068-be57-78fff888a400,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
07058df6-a5f6-4068-be57-78fff888a400,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
d74d8ad7-d04f-48ea-8e23-bad43e645008,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Interphase,False,Interphase,,,,
ef57c0a7-70c0-41fc-a484-f056a6ae6297,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During interphase, the cell undergoes normal processes while also preparing for cell division. For a cell to move from interphase to the mitotic phase, many internal and external conditions must be met. The three stages of interphase are called G1, S, and G2.",True,Interphase,,,,
4f550ee5-c4d2-4a5a-a112-cc55f9beddae,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,G1 phase,False,G1 phase,,,,
51f35c99-c0a2-4527-b608-3d49fee4215c,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The first stage of interphase is called the G1 phase, or first gap, because little change is visible. However, during the G1 stage, the cell is quite active at the biochemical level. The cell is accumulating the building blocks of chromosomal DNA and the associated proteins, as well as accumulating enough energy reserves to complete the task of replicating each chromosome in the nucleus.",True,G1 phase,,,,
93dba437-3d9e-410a-bd64-1c66450046ad,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,S phase,False,S phase,,,,
53a0cbd1-f76d-4e14-bc92-0465b3f68a20,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Throughout interphase, nuclear DNA remains in a semicondensed chromatin configuration. In the S phase (synthesis phase), DNA replication results in the formation of two identical copies of each chromosome (sister chromatids) that are firmly attached at the centromere region. At this stage, each chromosome is made of two sister chromatids and is a duplicated chromosome. The centrosome is duplicated during the S phase. The two centrosomes will give rise to the mitotic spindle, the apparatus that orchestrates the movement of chromosomes during mitosis. The centrosome consists of a pair of rod-like centrioles at right angles to each other. Centrioles help organize cell division.",True,S phase,,,,
5dac7426-e5f0-42c7-adba-14b8bba48719,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,semicondensed,False,semicondensed,,,,
2823cb78-df6f-40a3-ab3a-60cd196485e0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,G2 phase,False,G2 phase,,,,
c6c1fbbe-1b2a-4d2e-badd-9c1c3fc2b4aa,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"In the G2 phase, or second gap, the cell replenishes its energy stores and synthesizes the proteins necessary for chromosome manipulation. Some cell organelles are duplicated, and the cytoskeleton is dismantled to provide resources for the mitotic spindle. The final preparations for the mitotic phase must be completed before the cell is able to enter the first stage of mitosis.",True,G2 phase,,,,
ed6f3e34-a587-470e-99d3-6dd5a39c6e69,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,The mitotic phase,False,The mitotic phase,,,,
e8eb7072-6df7-4ad6-9a66-21287b4fd13d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
e8eb7072-6df7-4ad6-9a66-21287b4fd13d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
e8eb7072-6df7-4ad6-9a66-21287b4fd13d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
e8eb7072-6df7-4ad6-9a66-21287b4fd13d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
50826c92-688c-4667-8af1-de71c33f232e,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Mitosis,False,Mitosis,,,,
f63cbb67-ee2f-4f1d-8f5e-4ecc9c5f8f01,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
f63cbb67-ee2f-4f1d-8f5e-4ecc9c5f8f01,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
f63cbb67-ee2f-4f1d-8f5e-4ecc9c5f8f01,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
f63cbb67-ee2f-4f1d-8f5e-4ecc9c5f8f01,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
e4b7ea18-9290-46e9-a460-5a796027d89f,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During prophase, the “first phase,” several events must occur to provide access to the chromosomes in the nucleus. The nuclear envelope starts to break into small vesicles, and the Golgi apparatus and endoplasmic reticulum fragment and disperse to the periphery of the cell. The nucleolus disappears. The centrosomes begin to move to opposite poles of the cell. The microtubules that form the basis of the mitotic spindle extend between the centrosomes, pushing them farther apart as the microtubule fibers lengthen. The sister chromatids begin to coil more tightly and become visible under a light microscope.",True,Mitosis,,,,
381e3895-5a55-410f-8b0c-5289ac398f07,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During prometaphase, many processes that were begun in prophase continue to advance and culminate in the formation of a connection between the chromosomes and cytoskeleton. The remnants of the nuclear envelope disappear. The mitotic spindle continues to develop as more microtubules assemble and stretch across the length of the former nuclear area. Chromosomes become more condensed and visually discrete. Each sister chromatid attaches to spindle microtubules at the centromere via a protein complex called the kinetochore.",True,Mitosis,,,,
8558fd12-bfc5-4bfe-9f57-eee9f1d52706,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During metaphase, all the chromosomes are aligned in a plane called the metaphase plate, or the equatorial plane, midway between the two poles of the cell. The sister chromatids are still tightly attached to each other. At this time, the chromosomes are maximally condensed.",True,Mitosis,,,,
024ad5f6-1f9a-4116-9ee6-3fd4263635f5,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During anaphase, the sister chromatids at the equatorial plane are split apart at the centromere. Each chromatid, now called a chromosome, is pulled rapidly toward the centrosome to which its microtubule was attached. The cell becomes visibly elongated as the nonkinetochore microtubules slide against each other at the metaphase plate where they overlap.",True,Mitosis,,,,
cbbacc31-0722-4870-b60a-c6026740fcc8,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During telophase, all the events that set up the duplicated chromosomes for mitosis during the first three phases are reversed. The chromosomes reach the opposite poles and begin to decondense (unravel). The mitotic spindles are broken down into monomers that will be used to assemble cytoskeleton components for each daughter cell. Nuclear envelopes form around chromosomes.",True,Mitosis,,,,
fdbc0230-c5f4-41e7-9617-08a082a5e730,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Control of the cell cycle,False,Control of the cell cycle,,,,
68b5b8f7-d501-47d7-b79c-ae40a6a5f429,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,There are three key checkpoints in the cell cycle that provide regulation oversight:,True,Control of the cell cycle,,,,
fcea966a-0a42-46e0-acb4-a8ac0f1e4287,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Progress through these checkpoints is regulated by a family of cyclin dependent kinases (CDKs). These proteins are constitutive (always present) and inactive. CDKs bind specific cyclin activators, which are required for activity of the kinase. CDKs are present throughout the cell cycle, but expression of the cyclins is restricted to certain times in the cycle, and they are rapidly degraded as the cells progress through the checkpoints. Through binding of cyclins and negative regulation by phosphorylation by CDK inhibitors (CKIs), the cycle is tightly regulated in a restricted manner.",True,Control of the cell cycle,,,,
984a7d48-e98d-4b1e-8803-3010d2b9b185,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,The cyclin and CDK complex can be produced from a combination of different cyclins (A‒D) and different CDKs (1‒6).,True,Control of the cell cycle,,,,
79af68ab-67ad-4540-9907-3754c43fe253,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Rb-protein,False,Rb-protein,,,,
bc012a30-466a-4513-908b-ff60a1061214,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Rb-protein (pRb, retinoblastoma protein) is an important substrate of the G1/S‒CDK complexes. During the G0 and G1 phases, Rb is present in an unphosphorylated (hypophosphorylationed) form, which binds to the transcription factor E2F and thereby blocks it from initiating transcription. When the cycle moves into the S1 phase, pRb becomes phosphorylated (by the CyclinD/CDK4/6 active complex), which allows for the release of E2F.",True,Rb-protein,,,,
0796d9b7-b295-4cca-9b9a-65b9922d2e0a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,DNA damage,False,DNA damage,,,,
a1554cdc-6ac1-46ad-8f6b-0b502b4357ee,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During the process of DNA replication, DNA damage will halt the process until it can be repaired. Likewise, extrinsic damaging factors can trigger a DNA repair process. Protein p53 is commonly known for its role in DNA repair mechanisms. Under nonstressful conditions it is bound to mdm2 within the cytosol. In response to stress and DNA damage, it is activated, through ATM- or ATR-mediated phosphorylation. Once active, it functions as a transcription factor and induces the synthesis of protein p21.",True,DNA damage,,,,
54a7dbb4-c8b4-4463-bf53-0ee99fedfaa0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
54a7dbb4-c8b4-4463-bf53-0ee99fedfaa0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
54a7dbb4-c8b4-4463-bf53-0ee99fedfaa0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
54a7dbb4-c8b4-4463-bf53-0ee99fedfaa0,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
39575b0c-3985-44e9-adda-9a7daaff7b23,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
39575b0c-3985-44e9-adda-9a7daaff7b23,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
39575b0c-3985-44e9-adda-9a7daaff7b23,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
39575b0c-3985-44e9-adda-9a7daaff7b23,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7f612aa6-bc58-4825-b7ba-4b0fb646ad0b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,12.2 References and resources,True,DNA damage,,,,
600aaf6c-098e-49f7-b531-c3a75368e967,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Text,False,Text,,,,
a0873442-3a84-4b8c-bb7d-58f2ebdaf2d9,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
a0873442-3a84-4b8c-bb7d-58f2ebdaf2d9,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
a0873442-3a84-4b8c-bb7d-58f2ebdaf2d9,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
a0873442-3a84-4b8c-bb7d-58f2ebdaf2d9,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
4db6fc21-4376-4b77-a32b-7a169b5d378b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
4db6fc21-4376-4b77-a32b-7a169b5d378b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
4db6fc21-4376-4b77-a32b-7a169b5d378b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
4db6fc21-4376-4b77-a32b-7a169b5d378b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
7c51d87c-8421-4353-a35f-58ff1794cec4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7c51d87c-8421-4353-a35f-58ff1794cec4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7c51d87c-8421-4353-a35f-58ff1794cec4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
7c51d87c-8421-4353-a35f-58ff1794cec4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
79ac0e8d-0c2c-4a06-81dd-15c9c434382d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,12.3 Meiosis,True,Text,,,,
332a0a76-9d8f-483a-82f0-18f33b589eb7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The twenty-three chromosome pairs in humans accounts for all the genetic information needed to survive. For most of the components within the cell, only an approximation of division is needed during cell replication, however, with respect to division of DNA, this duplication and segregation must be exact. The integrity of the genetic information within the cell is critical for the well-being of the organisms and its offspring, so these processes are clearly controlled.",True,Text,,,,
4a4d72ba-09d0-4b39-bfe7-c5d87fb2f9a7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Within the cell cycle, the process of mitosis is largely responsible for this intricate chromosomal division of the somatic (body) cells by which two identical diploid daughter cells are produced through deoxyribonucleic acid (DNA) replication and cytoplasmic division.",True,Text,,,,
980fd451-1445-48a8-91ee-2e5dfeae13e4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"In contrast, meiosis is a specialized process of the germline (sperm and eggs) that involves one round of DNA replication followed by two cell divisions to produce four haploid germ cells. Unlike mitosis, the resulting germ cells differ in males and females.",True,Text,,,,
7133f455-d625-4a04-b797-512651134ae4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Male meiosis results in the production of four equally sized, functional spermatozoa, while female meiosis results in a single large functional ovum and three small nonfunctional polar bodies. Abnormalities in these processes include chromosomal nondisjunction, which results in the loss or gain of one or more chromosomes, and chromosomal breakage due to unrepaired DNA damage, which results in the formation of abnormal chromosomes and an increased risk for neoplasia.",True,Text,,,,
3aeb643a-ae6a-4f02-b854-62764e18a942,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Meiosis,False,Meiosis,,,,
82ea2549-f80e-4739-80bb-d6948350038a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
82ea2549-f80e-4739-80bb-d6948350038a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
82ea2549-f80e-4739-80bb-d6948350038a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
82ea2549-f80e-4739-80bb-d6948350038a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
cb06ff2a-cbce-43aa-90e1-6bce82f39e70,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,reductional,False,reductional,,,,
ce7c8d6b-24f8-4608-8125-c3cf4e9a1379,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,equational,False,equational,,,,
6a81b8ae-7129-4ff9-9691-5677c1273ad5,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Meiosis I: Reductional division,False,Meiosis I: Reductional division,,,,
a4e00cac-9966-4fa2-9d71-bb2641e46fb1,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Before meiosis, gametic stem cells replicate through mitosis. At the very beginning of meiosis, the last G1 phase of the diploid stem cells is followed by chromosome replication during S phase and G2, ending the last somatic interphase. Thus, each cell enters meiosis with two copies of the diploid genome (2n, 2c). At this point, the spermatogonium (male somatic cell) enlarges to become a primary spermatocyte, and the oogonium (female somatic cell) enlarges to become a primary oocyte.",True,Meiosis I: Reductional division,,,,
4911f920-a8c4-4e29-bb9a-0cb081999021,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"These cells then enter prophase I, which is subdivided into five stages: leptotene, zygotene, pachytene, diplotene, and diakinesis. In female meiosis, there is an additional stage following diplotene called dictyotene in which the oocyte remains from early fetal gestation until ovulation when diakinesis occurs.",True,Meiosis I: Reductional division,,,,
6b525ff9-f5ed-4706-a3c1-b6549ec8d5df,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Prophase I,False,Prophase I,,,,
d81a9760-5caf-40da-a656-3bcd4bb1bbd5,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"During prophase I, homologous chromosomes pair and undergo recombination through crossing over. This is visualized by the presence of X-shaped connections between homologues, called chiasmata, as the homologues begin to repel each other. These chiasmata will aid in the proper segregation of the chromosomes and become more prominent during diplotene. This is where the synaptoneal complex dissolves, allowing for chromosomal condensation to continue and for the repulsion of homologous chromosomes. The separation of the homologous chromosomes causes the chiasmata to appear. Individual chromatids can be visualized during this stage. (The dictyotene stage is unique to female meiosis in which there is a decondensation of chromosomal bivalents. The oocyte remains in this state for many years until follicle maturation and ovulation.)",True,Prophase I,,,,
351b9d5a-d251-4b41-b98a-fa6e2a556572,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,synaptoneal,False,synaptoneal,,,,
521029fe-96ff-470d-8702-488915cc6cec,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,decondensation,False,decondensation,,,,
3e3898f1-38ee-4e75-bf4a-77a1d30a20bb,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"At diakinesis, chromosomal condensation is completed. The chiasmata on each arm of the chromosomes move distally toward the telomeres. Each bivalent contains four chromatids, and pairs of sister chromatids are linked at the centromeres.",True,decondensation,,,,
1566f72d-902b-4f47-8649-1a44ad8e1a80,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Metaphase I,False,Metaphase I,,,,
bfecdc72-ff9f-40f7-ae22-f7deea71d382,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The spindle forms, and the nuclear membrane disappears. Bivalents align on the metaphase plate still held together by the chiasmata. The centromeres of the two homologous chromosomes are separate, aligning on either side of the equatorial plate.",True,Metaphase I,,,,
5b294ae1-7b0d-4d83-bd46-74fa8eeb1a3b,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Anaphase I,False,Anaphase I,,,,
d5178a93-81e5-40bc-89ef-24cb94cb8df7,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Homologous chromosomes separate from each other by final terminalization of the chiasmata. They move to opposite poles, pulled by the centromere, which is attached to spindle fibers.",True,Anaphase I,,,,
041a9c5a-db30-4bb4-bc9d-bed43ab8fe91,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Telophase I,False,Telophase I,,,,
6f2fe6c5-5517-407f-bddc-ca99902a9c44,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The chromosomes reach the poles, a nuclear membrane is formed, and cell division occurs. In male meiosis, the cytoplasm is divided equally, and the two resulting cells become secondary spermatocytes. In female meiosis, the division is unequal; most of the cytoplasm is retained in the secondary oocyte, while very little is retained by the first polar body. This period is very brief, and chromosomes move immediately to the second meiotic division. Each cell at this stage is haploid (1n) but with each chromosome formed of sister chromatids (2c). The sister chromatids may be unique due to recombination during the two homologues in prophase I.",True,Telophase I,,,,
7203b003-5346-4387-8034-d623f13b6fc4,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Meiosis II: Equational division,False,Meiosis II: Equational division,,,,
fe02959f-71b2-46ab-9050-27870668b26a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"This division is similar to mitosis in that individual chromosomes align on the metaphase plate, and sister chromatids separate and move to opposite poles at anaphase. The single copy (1c) of each chromosome is represented by one sister chromatid in the spermatids or mature ova.",True,Meiosis II: Equational division,,,,
aeeb9610-8c1e-4b13-ab6b-3eafc204c09a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Male meiosis,False,Male meiosis,,,,
61931ae7-af29-4cd4-aaa0-c86da0756cef,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"In humans, the male is the heterogametic sex, producing two kinds of normal sperm: 23,X and 23,Y. Spermatogenesis is a constant event beginning at puberty and continuing throughout life to produce four functional spermatids from each primary gametocyte. At puberty, the number of spermatogonia (diploid stem cells) increases. These develop into primary spermatocytes after several mitotic divisions. Each primary spermatocyte undergoes the first meiotic division to become two secondary spermatocytes. These cells then undergo the second meiotic division to become four spermatids of equal size with a haploid set of chromosomes. Spermiogenesis then transforms the spermatids into mature spermatozoa by elimination of the cytoplasm, elongation of the head of the sperm, and formation of a tail. The entire process from the enlargement of the spermatogonium to formation of the mature spermatozoa takes approximately sixty-four days.",True,Male meiosis,,,,
ff10e93a-2673-4ee3-9918-5f702589adfc,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Female meiosis,False,Female meiosis,,,,
19dae53e-d874-4329-b650-33db682bc035,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"This is in contrast to meiosis in females, which begins before birth and produces only a single type of normal ovum: 23,X. The precursors to the germ cells are oogonia; these increase in number through mitosis, reaching a maximum number of approximately 7 million. Each individual oogonium enlarges to form a primary oocyte, which becomes surrounded by ovarian stromal cells to form a primary follicle. The vast majority of primary oocytes are formed during the third and fourth months of fetal life.",True,Female meiosis,,,,
3a6d7227-4d9e-485f-a30a-40f8728b813f,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"The primary oocyte begins the first meiotic division to become a secondary oocyte with the extrusion of a small polar body as the follicle matures and completes metaphase I with expulsion from the mature follicle at ovulation. The secondary oocyte does not complete the second meiotic division until fertilization, when a second polar body is extruded to form a mature ovum with a haploid set of chromosomes. Thus, each primary oocyte produces one functional gamete, the mature ovum, and three polar bodies. A nuclear membrane forms a pronucleus around the haploid set of maternal chromosomes, while a second pronucleus forms from the haploid set of chromosomes from the sperm head. These two pronuclei then fuse to begin the first mitotic division.",True,Female meiosis,,,,
fb545449-4e7a-44b6-8f8d-db7e199ccab9,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,Meiotic pairing,False,Meiotic pairing,,,,
bb3ee6b9-fb80-42bd-8d74-3cd3e00d9d6f,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Homologous pairing is unique to meiosis and plays two important roles: genetic recombination and chromosomal stabilization. While it has long been believed that the former is the most important, the latter is now accepted as the primary significance of meiotic recombination. During meiosis I, the pairing of homologues facilitates recombination, which is initiated by programed double-stranded breaks occurring at synaptic initiation sites (SISs). A subset of these breaks will resolve into the formation of the synaptonemal complex. When pairing is completed, synapsis occurs between the homologues, which completes the crossing over event. Each crossover event forms chasmata, which play an analogous role to the centromere and stabilize the maternal and paternal chromosomes. The stabilization of the metaphase chromosomes using this mechanism is key to normal chromosomal alignment and maintenance of an intact genome. Without recombination, the total number of unique gametic combinations of genes for each parent would be just over 8 million. However, crossing over greatly increases the total number of possible gene combinations such that the likelihood of either parent producing identical gametes is vanishingly small.",True,Meiotic pairing,,,,
92b3a709-c67d-406a-8578-a3e14c3c176d,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,12.3 References and resources,True,Meiotic pairing,,,,
160d03f5-ee95-430f-89f3-7870615b0a9a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
160d03f5-ee95-430f-89f3-7870615b0a9a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
160d03f5-ee95-430f-89f3-7870615b0a9a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
160d03f5-ee95-430f-89f3-7870615b0a9a,https://pressbooks.lib.vt.edu/cellbio/,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/#chapter-91-section-1,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
0440c53f-21f4-4de7-81b2-ec05b4ddeca6,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Some genes (the so-called “house-keeping genes”) are likely (constitutively) expressed in all cell types since certain proteins (and RNAs) are involved in the basic metabolic processes common to all cell types. Other genes are expressed in one cell type but not another (e.g., certain immune cells normally synthesize antibodies, but neurons do not). Thus, different cell types arise because of differential gene expression, and the RNA and protein content of different cell types shows considerable variation.",True,Meiotic pairing,,,,
0f1e3e6b-0021-4ebc-b45d-7d71371f308a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Changes to DNA content and rearrangement are addressed elsewhere. Briefly, DNA of different cell types does not vary in either amount or type. However, highly specialized cases are known to exist where DNA loss, rearrangement, and amplification profoundly influence gene expression in isolated situations.",True,Meiotic pairing,,,,
853533bf-0971-451f-ab78-d8dad781609e,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,This section will focus on changes in gene expression.,False,This section will focus on changes in gene expression.,,,,
1fb98c97-4493-4ecb-90b2-95a6e6e2c401,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Regulation is known to occur at several different points of a multistep gene expression pathway. Four main levels of control include:,True,This section will focus on changes in gene expression.,,,,
33697cae-54ab-461e-98ed-4cac1e580310,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"1. Transcriptional control: Determines if, how much, and when an mRNA is made.",True,This section will focus on changes in gene expression.,,,,
a8339a02-cd97-42e2-b6bd-b5155ed80cdd,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"2. Processing or post-transcriptional control: Determines if, how much, and when an mRNA is available for translation into a protein.",True,This section will focus on changes in gene expression.,,,,
1341ec0f-c8d7-48c0-b5f7-90fbd56fa57a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"3. Translational control: Determines if, how much, and when a protein is made.",True,This section will focus on changes in gene expression.,,,,
33611aa4-da56-4240-8887-032d8b0f3741,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"4. Post-translational control: Determines if, how much, and when a protein is functional.",True,This section will focus on changes in gene expression.,,,,
ec300964-558b-4fdb-b996-02a84d54034d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Transcriptional control,False,Transcriptional control,,,,
5b6fa18d-d810-4070-9de5-0e2159f6f758,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Control of transcriptional initiation is a primary means used to regulate gene expression in eukaryotic organisms. Most eukaryotic genes are controlled at the level of transcription by proteins (trans-acting factors) that interact with specific gene sequences (cis-acting regulatory sequences).,True,Transcriptional control,,,,
6d4b1573-ae70-4c76-a7b9-cd52f065def4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Transcription factors: Enhancers,False,Transcription factors: Enhancers,,,,
4827ded2-f98b-4763-964f-0b69fa872c4a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Along with general transcription factors, there are additional regions that help increase or enhance transcription. These regions, called enhancers, are not necessarily close to the genes they enhance. They can be located upstream of a gene, within the coding region of the gene, downstream of a gene, or thousands of nucleotides away.",True,Transcription factors: Enhancers,,,,
36c5fa75-7d4a-457c-830c-2bfa503a4f96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
36c5fa75-7d4a-457c-830c-2bfa503a4f96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
36c5fa75-7d4a-457c-830c-2bfa503a4f96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
36c5fa75-7d4a-457c-830c-2bfa503a4f96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Enhancer regions are binding sequences, or sites, for specific transcription factors. When a protein transcription factor binds to its enhancer sequence, the shape of the protein changes, allowing it to interact with proteins at the promotor site. However, since the enhancer region may be distant from the promoter, the DNA must bend to allow the proteins at the two sites to come into contact. DNA-bending proteins help bend the DNA and bring the enhancer and promoter regions together (figure 12.1). This shape change allows for the interaction of the specific activator proteins bound to the enhancers with the general transcription factors bound to the promoter region and the RNA polymerase. Two different genes may have the same promoter but different distal control elements, enabling differential gene expression.",True,Transcription factors: Enhancers,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
24a40943-04df-4cbb-960f-43c9bbdc084e,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Transcription factors: Repressors,False,Transcription factors: Repressors,,,,
69642ef6-39b0-40ba-bdc4-4675da8ae961,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
69642ef6-39b0-40ba-bdc4-4675da8ae961,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
69642ef6-39b0-40ba-bdc4-4675da8ae961,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
69642ef6-39b0-40ba-bdc4-4675da8ae961,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Like prokaryotic cells, eukaryotic cells also have mechanisms to prevent transcription. Transcriptional repressors can bind to promoter or enhancer regions and block transcription. Like the transcriptional activators, repressors respond to external stimuli preventing the binding of activating transcription factors. This is often done by histone deacetylation, which increases the interaction of DNA and histones (figure 12.2).",True,Transcription factors: Repressors,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
89344a3e-e13a-40cc-bcb7-f3b64ad0bf44,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Transcription factors: Structure and function,False,Transcription factors: Structure and function,,,,
68135870-f176-4a80-9c70-24bb3e9b1c97,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Structurally, transcription factors share similar characteristics but can take on very different secondary structures. Common examples of transcription factors include: Zn fingers, helix-loop-helixs, and leucine zippers. Regardless of structure, common characteristics include:",True,Transcription factors: Structure and function,,,,
4a086922-975e-4c5e-a1d2-387884898381,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
4a086922-975e-4c5e-a1d2-387884898381,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
4a086922-975e-4c5e-a1d2-387884898381,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
4a086922-975e-4c5e-a1d2-387884898381,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"As noted above, one of the major roles of transcription factors is to bend or remodel the DNA in a way to allow for interactions of transcription factors and their binding sites. Chromatin remodeling by modifications of the histones (through acetylation or shifting) is common (figure 12.2).",True,Transcription factors: Structure and function,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
6099c639-d576-4a61-97ee-b891bc88699f,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Processing or post/cotranscription,False,Processing or post/cotranscription,,,,
690494dc-f74e-4cd3-ad22-a1d6213f4cc1,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Alternative RNA splicing,False,Alternative RNA splicing,,,,
199b99db-342d-43d5-aab3-a51d29bc78cf,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
199b99db-342d-43d5-aab3-a51d29bc78cf,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
199b99db-342d-43d5-aab3-a51d29bc78cf,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
199b99db-342d-43d5-aab3-a51d29bc78cf,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Alternative RNA splicing is a mechanism that allows different protein products to be produced from one gene when different combinations of exons are combined to form the mRNA. This alternative splicing can be haphazard, but more often it is controlled and acts as a mechanism of gene regulation, with the frequency of different splicing alternatives controlled by the cell as a way to control the production of different protein products in different cells or at different stages of development. Alternative splicing is a common mechanism of gene regulation in eukaryotes; according to one estimate, 70 percent of genes in humans are expressed as multiple proteins through alternative splicing. Although there are multiple ways to alternatively splice RNA transcripts, the original 5′-3′ order of the exons is always conserved. That is, a transcript with exons 1 2 3 4 5 6 7 might be spliced 1 2 4 5 6 7 or 1 2 3 6 7, but never 1 2 5 4 3 6 7 (figure 12.3).",True,Alternative RNA splicing,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
b8e7d679-dcbc-4064-9dbd-996f6ea65ac5,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Translational control,False,Translational control,,,,
05ddcca8-ec02-4969-a427-854a489730f2,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Like transcription, translation is controlled by proteins that bind and initiate the process, restrict access to the mRNA, or control the localization of the transcript itself.",True,Translational control,,,,
63b036e2-5ca8-4b1b-ae3d-32a06f7f76d6,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Localization,False,Localization,,,,
77db1aee-0299-4f09-8e8b-27874c15de3c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,One fundamental way in which translation is controlled is physically by where the mRNA is located within the cell or organism. This is extremely important in development where restriction of a transcript to one side of a cell can influence the phenotype of a localized cellular region. This is largely mediated by interactions with the 5ʼ untranslated region (UTR).,True,Localization,,,,
3d93f4af-aaba-4d90-b2c6-2a317d383df9,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Translational initiation,False,Translational initiation,,,,
41627638-b460-490e-a06a-52889b639bb2,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"In translation, the complex that assembles to start the process is referred to as the translation initiation complex, and similar to transcription, this complex can be activated or inhibited. In eukaryotes, translation is initiated by binding the initiating met-tRNAi to the 40S ribosome.",True,Translational initiation,,,,
a8a804a4-9fee-4ed7-836e-f6182afde9f0,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Initially the met-tRNAi is brought to the 40S ribosome by a protein initiation factor, eukaryotic initiation factor-2 (eIF-2). The eIF-2 protein binds to the high-energy molecule guanosine triphosphate (GTP), and the tRNA-eIF2-GTP complex then binds to the 40S ribosome.",True,Translational initiation,,,,
7a0359cb-4301-4498-80c5-a8ddad924675,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The cap-binding protein eIF4F brings the mRNA complex together with the 40S ribosome complex. The ribosome then scans along the mRNA until it finds a start codon AUG. When the anticodon of the initiator tRNA and the start codon are aligned, the GTP is hydrolyzed, the initiation factors are released, and the large 60S ribosomal subunit binds to form the translation complex. Insulin increases the efficiency of formation of the cap-binding complex, therefore increasing the rate of protein synthesis.",True,Translational initiation,,,,
47b8c429-0939-476e-a6a5-ca08d8f3b32c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
47b8c429-0939-476e-a6a5-ca08d8f3b32c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
47b8c429-0939-476e-a6a5-ca08d8f3b32c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
47b8c429-0939-476e-a6a5-ca08d8f3b32c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly, and translation is impeded (figure 12.4).",True,Translational initiation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
f84c361f-07d6-4822-88f0-220ab2a2d279,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"When eIF-2 remains unphosphorylated, the initiation complex can form normally, and translation can continue.",True,Translational initiation,,,,
3ef66dc3-fd4e-4a65-af17-6a3611148826,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Control of RNA stability,False,Control of RNA stability,,,,
480ba0e6-1fed-4dc7-9b28-d1f4da36a454,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Before the mRNA leaves the nucleus, it is given two protective “caps” that prevent the ends of the strand from degrading during its journey. These changes protect the two ends of the RNA from exonuclease attack.",True,Control of RNA stability,,,,
aa4b45bc-4833-46c6-bb43-510d1a13c155,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Once the RNA is transported to the cytoplasm, the length of time that the RNA resides there can be controlled. Each RNA molecule has a defined lifespan and decays at a specific rate. This rate of decay can influence how much protein is in the cell.",True,Control of RNA stability,,,,
79962411-a82c-49f0-91b4-71c27a9840f6,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,RNA-binding proteins,False,RNA-binding proteins,,,,
563c2eaa-22ea-4524-a111-52ed6c244a96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
563c2eaa-22ea-4524-a111-52ed6c244a96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
563c2eaa-22ea-4524-a111-52ed6c244a96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
563c2eaa-22ea-4524-a111-52ed6c244a96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Binding of proteins to the RNA can also influence its stability. Proteins called RNA-binding proteins, or RBPs, can bind to the regions of the mRNA just upstream or downstream of the protein-coding region. These regions in the RNA that are not translated into protein are called the untranslated regions, or UTRs (figure 12.5). They are not introns (those have been removed in the nucleus). Rather, these are regions that regulate mRNA localization, stability, and protein translation. The region just before the protein-coding region is called the 5′ UTR, whereas the region after the coding region is called the 3′ UTR. The binding of RBPs to these regions can increase or decrease the stability of an RNA molecule, depending on the specific RBP that binds.",True,RNA-binding proteins,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
bdcf0537-0c35-4913-b8ca-f2fc8133aeee,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,One classic example of this is the regulation of transferrin receptor (TR) and ferritin levels in response to iron.,True,RNA-binding proteins,,,,
fe007db0-3703-49dc-89a8-aa6646cba333,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,microRNAs,False,microRNAs,,,,
30571d8c-db3d-4edf-bb80-a2ed78d2efee,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"In addition to RBPs that bind to and control (increase or decrease) RNA stability, other elements called microRNAs can bind to the RNA molecule. These microRNAs, or miRNAs, are short RNA molecules that are only twenty-one to twenty-four nucleotides in length. The miRNAs are made in the nucleus as longer pre-miRNAs.",True,microRNAs,,,,
2e343864-d1f3-4871-a058-fad43850631a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"These pre-miRNAs are chopped into mature miRNAs by a protein called dicer. Like transcription factors and RBPs, mature miRNAs recognize a specific sequence and bind to the RNA; however, miRNAs also associate with a ribonucleoprotein complex called the RNA-induced silencing complex (RISC). The RNA component of the RISC base-pairs with complementary sequences on an mRNA and either impede translation of the message or lead to the degradation of the mRNA.",True,microRNAs,,,,
421be0e8-08cc-4940-a4cf-3d713b5381b1,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Post-translation regulation,False,Post-translation regulation,,,,
d519a3ff-1da5-4d67-b5bc-bbf5391d631e,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Chemical modifications,False,Chemical modifications,,,,
bb1dde32-42f0-4941-8e67-6b71c8fd04cb,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Proteins can be chemically modified with the addition of groups including methyl, phosphate, acetyl, and ubiquitin groups.",True,Chemical modifications,,,,
8c837e89-224b-4860-b307-28d9bd8a8e79,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,The addition or removal of these groups from proteins can have many effects and can be in response to many cellular changes. For example:,True,Chemical modifications,,,,
753a2289-85fc-4ad6-aad4-3acf00afaf40,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"This is an efficient way for the cell to rapidly change the levels of specific proteins in response to the environment. Because proteins are involved in every stage of gene regulation, the phosphorylation of a protein (depending on the protein that is modified) can alter accessibility to the chromosome, can alter translation (by altering transcription factor binding or function), can change nuclear shuttling (by influencing modifications to the nuclear pore complex), can alter RNA stability (by binding or not binding to the RNA to regulate its stability), can modify translation (increase or decrease), or can change post-translational modifications (add or remove phosphates or other chemical modifications).",True,Chemical modifications,,,,
bab667de-e914-43d4-a3c5-fc3db832be8f,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Protein degradation,False,Protein degradation,,,,
b4219d52-9ff1-4a3d-bf91-010cf3045892,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
b4219d52-9ff1-4a3d-bf91-010cf3045892,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
b4219d52-9ff1-4a3d-bf91-010cf3045892,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
b4219d52-9ff1-4a3d-bf91-010cf3045892,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome, an organelle that functions to remove proteins, to be degraded. One way to control gene expression, therefore, is to alter the longevity of the protein (figure 12.6).",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
4ce2ff28-474f-4cb6-a0cc-4cda41596736,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,12.1 References and resources,True,Protein degradation,,,,
94d6fe95-1e3a-4872-af09-56e9352053ae,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 10: Cell Reproduction, Chapter 11: Meiosis and Sexual Reproduction, Chapter 16: Gene Expression.",True,Protein degradation,,,,
b84427c2-0102-4926-9b91-d8fb1386b300,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 11: Gene Expression: From Transcription to Translation, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication and Repair, Chapter 14: Cellular Reproduction.",True,Protein degradation,,,,
2575c2af-689d-4280-9653-a47f51ffb7a0,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 41–43, 46.",True,Protein degradation,,,,
b2e26a8c-0e93-45fc-a05d-343134749289,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 3: The Human Genome: Gene Structure and Function.",True,Protein degradation,,,,
a1c556da-f65f-4681-976a-a9eb8d76af7d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
a1c556da-f65f-4681-976a-a9eb8d76af7d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
a1c556da-f65f-4681-976a-a9eb8d76af7d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
a1c556da-f65f-4681-976a-a9eb8d76af7d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.1 Example of transcriptional complex involving two separate genes. 2021. CC BY 4.0. Adapted from Biology 2e Figure 16.10 Interaction between proteins at the promoter and enhancer sites. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.1,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
e0a62949-9570-451b-afa6-7590c1e09cbb,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
e0a62949-9570-451b-afa6-7590c1e09cbb,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
e0a62949-9570-451b-afa6-7590c1e09cbb,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
e0a62949-9570-451b-afa6-7590c1e09cbb,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.2 Modification of DNA and histones can alter DNA accessibility and therefore transcription. 2021. CC BY 4.0. Adapted from Biology 2e. Figure 16.8 Nucleosomes can slide along DNA. CC BY 4.0. From OpenStax.",True,Protein degradation,Figure 12.2,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
3788927c-d223-4024-9412-80ac468c1623,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
3788927c-d223-4024-9412-80ac468c1623,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
3788927c-d223-4024-9412-80ac468c1623,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
3788927c-d223-4024-9412-80ac468c1623,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.3 Five common modes of alternative splicing. 2021. https://archive.org/details/12.3_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.3,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
c7aac1e0-8285-4a04-9f8b-9aada030f21d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
c7aac1e0-8285-4a04-9f8b-9aada030f21d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
c7aac1e0-8285-4a04-9f8b-9aada030f21d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
c7aac1e0-8285-4a04-9f8b-9aada030f21d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.4 Regulation of translational initiation. 2021. https://archive.org/details/12.4_20210926. CC BY 4.0.",True,Protein degradation,Figure 12.4,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
e59c92fc-37ea-41c9-ad4e-f8c4527d76ea,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
e59c92fc-37ea-41c9-ad4e-f8c4527d76ea,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
e59c92fc-37ea-41c9-ad4e-f8c4527d76ea,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
e59c92fc-37ea-41c9-ad4e-f8c4527d76ea,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.5 RNA Binding proteins can increase stability of the transcript. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 16.21 Translational regulation of ferritin synthesis. 2017.",True,Protein degradation,Figure 12.5,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
b4045a40-786c-4f32-9217-58dbbd693754,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
b4045a40-786c-4f32-9217-58dbbd693754,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
b4045a40-786c-4f32-9217-58dbbd693754,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
b4045a40-786c-4f32-9217-58dbbd693754,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Lieberman M, Peet A. Figure 12.6 Proteasome mediated degradation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 312. Figure 35.6 The proteasome and regulatory proteins. 2017.",True,Protein degradation,Figure 12.6,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
63cabced-3ab3-4cae-b5f2-1ee069ebeb8f,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,12.2 Cell Cycle,True,Protein degradation,,,,
1edf5b45-dd28-4dee-8131-359d028ff2bf,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Checkpoints are the most critical, and the full summary of mitosis is for background.",True,Protein degradation,,,,
e0fdff5b-fefa-4371-b5db-b2563ea300d2,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
e0fdff5b-fefa-4371-b5db-b2563ea300d2,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
e0fdff5b-fefa-4371-b5db-b2563ea300d2,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
e0fdff5b-fefa-4371-b5db-b2563ea300d2,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The cycle is divided into four distinct phases, G1, S, G2, and M (mitosis), and for most mammalian cells in culture this process takes about twenty-four hours to complete. The majority of differentiated cells in the body are not dividing, retained in a resting state or Go (figure 12.7).",True,Protein degradation,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
6fdb4e97-8f84-4e0c-87c3-158d9cdac89f,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Interphase,False,Interphase,,,,
a3527ea0-815a-4a05-b964-9967ddcc331e,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During interphase, the cell undergoes normal processes while also preparing for cell division. For a cell to move from interphase to the mitotic phase, many internal and external conditions must be met. The three stages of interphase are called G1, S, and G2.",True,Interphase,,,,
879a45ab-097d-4b70-b216-950c3a5f820d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,G1 phase,False,G1 phase,,,,
5d1a403b-2804-4938-84ad-0454599f1cb4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The first stage of interphase is called the G1 phase, or first gap, because little change is visible. However, during the G1 stage, the cell is quite active at the biochemical level. The cell is accumulating the building blocks of chromosomal DNA and the associated proteins, as well as accumulating enough energy reserves to complete the task of replicating each chromosome in the nucleus.",True,G1 phase,,,,
c66ac80b-3c16-4dd2-9c2d-ba68bbb13b2d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,S phase,False,S phase,,,,
2bb3f539-7e33-4eba-8f41-870778ad34a4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Throughout interphase, nuclear DNA remains in a semicondensed chromatin configuration. In the S phase (synthesis phase), DNA replication results in the formation of two identical copies of each chromosome (sister chromatids) that are firmly attached at the centromere region. At this stage, each chromosome is made of two sister chromatids and is a duplicated chromosome. The centrosome is duplicated during the S phase. The two centrosomes will give rise to the mitotic spindle, the apparatus that orchestrates the movement of chromosomes during mitosis. The centrosome consists of a pair of rod-like centrioles at right angles to each other. Centrioles help organize cell division.",True,S phase,,,,
30d80ced-5dfd-4af5-a03b-0e5d99987d96,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,semicondensed,False,semicondensed,,,,
7a2e8ef8-cece-43df-95b5-9b01157ba57d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,G2 phase,False,G2 phase,,,,
334470af-ee88-4998-884d-c825cda8e1aa,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"In the G2 phase, or second gap, the cell replenishes its energy stores and synthesizes the proteins necessary for chromosome manipulation. Some cell organelles are duplicated, and the cytoskeleton is dismantled to provide resources for the mitotic spindle. The final preparations for the mitotic phase must be completed before the cell is able to enter the first stage of mitosis.",True,G2 phase,,,,
03490070-d1a3-4681-81f7-dfd66b89014e,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,The mitotic phase,False,The mitotic phase,,,,
9c99b018-9e59-43dc-8f0b-70efb8412dd4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
9c99b018-9e59-43dc-8f0b-70efb8412dd4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
9c99b018-9e59-43dc-8f0b-70efb8412dd4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
9c99b018-9e59-43dc-8f0b-70efb8412dd4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"To make two daughter cells, the contents of the nucleus and the cytoplasm must be divided. The mitotic phase is a multistep process during which the duplicated chromosomes are aligned, separated, and moved to opposite poles of the cell, and then the cell is divided into two new identical daughter cells. The first portion of the mitotic phase, mitosis, is composed of five stages, which accomplish nuclear division. The second portion of the mitotic phase, called cytokinesis, is the physical separation of the cytoplasmic components into two daughter cells (figure 12.8).",True,The mitotic phase,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
ec35a8ba-0373-43a4-858b-458581a39949,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Mitosis,False,Mitosis,,,,
c08b3d13-ceed-4f43-b6cd-8383806e235a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
c08b3d13-ceed-4f43-b6cd-8383806e235a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
c08b3d13-ceed-4f43-b6cd-8383806e235a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
c08b3d13-ceed-4f43-b6cd-8383806e235a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Mitosis is divided into a series of phases — prophase, prometaphase, metaphase, anaphase, and telophase — that result in the division of the cell nucleus (figure 12.8).",True,Mitosis,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
b667a9c8-10ed-443b-b2eb-d6bccfbe6e02,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During prophase, the “first phase,” several events must occur to provide access to the chromosomes in the nucleus. The nuclear envelope starts to break into small vesicles, and the Golgi apparatus and endoplasmic reticulum fragment and disperse to the periphery of the cell. The nucleolus disappears. The centrosomes begin to move to opposite poles of the cell. The microtubules that form the basis of the mitotic spindle extend between the centrosomes, pushing them farther apart as the microtubule fibers lengthen. The sister chromatids begin to coil more tightly and become visible under a light microscope.",True,Mitosis,,,,
4e03f4f8-7596-4729-9a6a-acbd2a8ba1e6,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During prometaphase, many processes that were begun in prophase continue to advance and culminate in the formation of a connection between the chromosomes and cytoskeleton. The remnants of the nuclear envelope disappear. The mitotic spindle continues to develop as more microtubules assemble and stretch across the length of the former nuclear area. Chromosomes become more condensed and visually discrete. Each sister chromatid attaches to spindle microtubules at the centromere via a protein complex called the kinetochore.",True,Mitosis,,,,
5f6deb30-b73b-4213-82e7-588f330c4f9c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During metaphase, all the chromosomes are aligned in a plane called the metaphase plate, or the equatorial plane, midway between the two poles of the cell. The sister chromatids are still tightly attached to each other. At this time, the chromosomes are maximally condensed.",True,Mitosis,,,,
e5c0837a-19fa-407f-a9f6-30f4ee7f86c8,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During anaphase, the sister chromatids at the equatorial plane are split apart at the centromere. Each chromatid, now called a chromosome, is pulled rapidly toward the centrosome to which its microtubule was attached. The cell becomes visibly elongated as the nonkinetochore microtubules slide against each other at the metaphase plate where they overlap.",True,Mitosis,,,,
cc14c950-f4ba-4aab-a346-45cc0552d6c8,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During telophase, all the events that set up the duplicated chromosomes for mitosis during the first three phases are reversed. The chromosomes reach the opposite poles and begin to decondense (unravel). The mitotic spindles are broken down into monomers that will be used to assemble cytoskeleton components for each daughter cell. Nuclear envelopes form around chromosomes.",True,Mitosis,,,,
c5c17ffb-4e18-4df4-b376-86a61c4bded1,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Control of the cell cycle,False,Control of the cell cycle,,,,
c0905174-c81c-45e0-a68a-15d516cd804e,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,There are three key checkpoints in the cell cycle that provide regulation oversight:,True,Control of the cell cycle,,,,
76b6ef5f-efd6-4be6-aa84-eb0cd2f151b1,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Progress through these checkpoints is regulated by a family of cyclin dependent kinases (CDKs). These proteins are constitutive (always present) and inactive. CDKs bind specific cyclin activators, which are required for activity of the kinase. CDKs are present throughout the cell cycle, but expression of the cyclins is restricted to certain times in the cycle, and they are rapidly degraded as the cells progress through the checkpoints. Through binding of cyclins and negative regulation by phosphorylation by CDK inhibitors (CKIs), the cycle is tightly regulated in a restricted manner.",True,Control of the cell cycle,,,,
910292f1-1a0c-4a19-acc6-f068ebdf7771,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,The cyclin and CDK complex can be produced from a combination of different cyclins (A‒D) and different CDKs (1‒6).,True,Control of the cell cycle,,,,
9ce6a93c-1844-4c31-b575-78f6540d6697,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Rb-protein,False,Rb-protein,,,,
7039606b-0169-4cf7-87ec-b4f18fc3c79a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Rb-protein (pRb, retinoblastoma protein) is an important substrate of the G1/S‒CDK complexes. During the G0 and G1 phases, Rb is present in an unphosphorylated (hypophosphorylationed) form, which binds to the transcription factor E2F and thereby blocks it from initiating transcription. When the cycle moves into the S1 phase, pRb becomes phosphorylated (by the CyclinD/CDK4/6 active complex), which allows for the release of E2F.",True,Rb-protein,,,,
beba0445-0673-43f7-b8d2-a6249c02cba1,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,DNA damage,False,DNA damage,,,,
9e80814d-f81d-4172-a003-0a676eb6993a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During the process of DNA replication, DNA damage will halt the process until it can be repaired. Likewise, extrinsic damaging factors can trigger a DNA repair process. Protein p53 is commonly known for its role in DNA repair mechanisms. Under nonstressful conditions it is bound to mdm2 within the cytosol. In response to stress and DNA damage, it is activated, through ATM- or ATR-mediated phosphorylation. Once active, it functions as a transcription factor and induces the synthesis of protein p21.",True,DNA damage,,,,
e15ad2b5-98f7-476f-b486-271179795e1d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
e15ad2b5-98f7-476f-b486-271179795e1d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
e15ad2b5-98f7-476f-b486-271179795e1d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
e15ad2b5-98f7-476f-b486-271179795e1d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"p21 will then act as a CDK inhibitor (Cip/Kip family) and blocks the action of the G1‒CDK complex. This will halt the cell cycle at the transition to the S1 phase, and the DNA can be repaired at leisure (figure 12.9). When this has been successfully completed, p53 is dephosphorylated, ubiquitinylated, and passed on to the proteasome. Thus, p53 does not accumulate in normal cells.",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
becee9ec-3bdb-48a8-8186-04addb26298a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
becee9ec-3bdb-48a8-8186-04addb26298a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
becee9ec-3bdb-48a8-8186-04addb26298a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
becee9ec-3bdb-48a8-8186-04addb26298a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"If the DNA repair systems do not succeed in eliminating the DNA damage, a steady increase in the concentration of phosphorylated p53 finally drives the cell into apoptosis. Proteins pRb and p53 are products of tumor suppressor genes. Complete absence of them, due to mutations, leads to accelerated cell division, a typical feature of tumors. In fact, somatic mutations in pRb and p53 have been found in more than half of all human tumors (figure 12.9).",True,DNA damage,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
6201eba9-b2b9-41a8-b9f1-80f7d7314f28,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,12.2 References and resources,True,DNA damage,,,,
4173cc95-dcd4-4ccf-af83-57b462f95663,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Text,False,Text,,,,
b247da83-3221-4488-b90f-350b1702ef3b,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
b247da83-3221-4488-b90f-350b1702ef3b,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
b247da83-3221-4488-b90f-350b1702ef3b,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
b247da83-3221-4488-b90f-350b1702ef3b,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.7 Overview of the cell cycle. 2021. https://archive.org/details/12.7_20210926. CC BY 4.0.",True,Text,Figure 12.7,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
1840adc9-875d-4798-8254-a541737f02fc,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
1840adc9-875d-4798-8254-a541737f02fc,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
1840adc9-875d-4798-8254-a541737f02fc,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
1840adc9-875d-4798-8254-a541737f02fc,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.8 Summary of the mitotic phase. 2021. https://archive.org/details/12.8_20210926. CC BY 4.0. Added Mitosis cells sequence by LadyofHats. Public domain. From Wikimedia Commons. And Figure 2. CC BY 4.0. From Lumen.",True,Text,Figure 12.8,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
30d60a5b-66b9-4fbb-bd0d-c689d91a05b4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
30d60a5b-66b9-4fbb-bd0d-c689d91a05b4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
30d60a5b-66b9-4fbb-bd0d-c689d91a05b4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
30d60a5b-66b9-4fbb-bd0d-c689d91a05b4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.9 Summary of cell cycle checkpoints and role of CDK inhibitors in halting cell cycle progress. 2021. https://archive.org/details/12.9_20210926. CC BY 4.0.",True,Text,Figure 12.9,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
14ae32ba-f265-4b0c-bde2-29baa199eef7,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,12.3 Meiosis,True,Text,,,,
70150dd6-4983-40a1-a397-c4255b1e1b70,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The twenty-three chromosome pairs in humans accounts for all the genetic information needed to survive. For most of the components within the cell, only an approximation of division is needed during cell replication, however, with respect to division of DNA, this duplication and segregation must be exact. The integrity of the genetic information within the cell is critical for the well-being of the organisms and its offspring, so these processes are clearly controlled.",True,Text,,,,
1423a8f9-7e03-4670-9828-d01539e10def,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Within the cell cycle, the process of mitosis is largely responsible for this intricate chromosomal division of the somatic (body) cells by which two identical diploid daughter cells are produced through deoxyribonucleic acid (DNA) replication and cytoplasmic division.",True,Text,,,,
1bdb9063-0ac3-4ac4-a993-b938f27cc442,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"In contrast, meiosis is a specialized process of the germline (sperm and eggs) that involves one round of DNA replication followed by two cell divisions to produce four haploid germ cells. Unlike mitosis, the resulting germ cells differ in males and females.",True,Text,,,,
d0bc7867-01dc-48c4-9fe8-021079009978,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Male meiosis results in the production of four equally sized, functional spermatozoa, while female meiosis results in a single large functional ovum and three small nonfunctional polar bodies. Abnormalities in these processes include chromosomal nondisjunction, which results in the loss or gain of one or more chromosomes, and chromosomal breakage due to unrepaired DNA damage, which results in the formation of abnormal chromosomes and an increased risk for neoplasia.",True,Text,,,,
8aeaba71-732a-4fc1-a609-695eeed66fe3,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Meiosis,False,Meiosis,,,,
bc3f2242-ab05-48b1-9634-cd4f4818d072,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
bc3f2242-ab05-48b1-9634-cd4f4818d072,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
bc3f2242-ab05-48b1-9634-cd4f4818d072,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
bc3f2242-ab05-48b1-9634-cd4f4818d072,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Meiosis is composed of two distinctive cell divisions, meiosis I and meiosis II, which are found only in the germline. Through these two divisions, haploid gametes are formed from diploid somatic cells. There is only one replication of the DNA, but there are two divisions of the chromosomes. The first division differs from the second in that there is pairing and recombination between homologous chromosomes resulting in variation in the genetic makeup of the gametes. Segregation of the homologues occurs during the first meiotic (reductional) division, reducing the forty-six chromosomes to twenty-three, one from each homologous pair. The second (equational) division is similar to mitosis with segregation of sister chromatids into daughter cells (figure 12.10).",True,Meiosis,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
9fad7f64-5b00-4e1a-a63a-2922e3272a1b,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,reductional,False,reductional,,,,
026fe10c-7cf0-4630-85b6-b515a4338a74,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,equational,False,equational,,,,
1d0c7fa5-01d1-4bf1-ab68-197771bb8807,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Meiosis I: Reductional division,False,Meiosis I: Reductional division,,,,
9c090041-d55e-4c84-aaca-868f2169633b,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Before meiosis, gametic stem cells replicate through mitosis. At the very beginning of meiosis, the last G1 phase of the diploid stem cells is followed by chromosome replication during S phase and G2, ending the last somatic interphase. Thus, each cell enters meiosis with two copies of the diploid genome (2n, 2c). At this point, the spermatogonium (male somatic cell) enlarges to become a primary spermatocyte, and the oogonium (female somatic cell) enlarges to become a primary oocyte.",True,Meiosis I: Reductional division,,,,
94db5055-7314-4c60-b4c5-f5a9a8c7bfef,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"These cells then enter prophase I, which is subdivided into five stages: leptotene, zygotene, pachytene, diplotene, and diakinesis. In female meiosis, there is an additional stage following diplotene called dictyotene in which the oocyte remains from early fetal gestation until ovulation when diakinesis occurs.",True,Meiosis I: Reductional division,,,,
4b38a519-f4c6-4846-9725-797188d6275c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Prophase I,False,Prophase I,,,,
36d50b66-3ff0-4e04-9e6b-c2cadde57da4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"During prophase I, homologous chromosomes pair and undergo recombination through crossing over. This is visualized by the presence of X-shaped connections between homologues, called chiasmata, as the homologues begin to repel each other. These chiasmata will aid in the proper segregation of the chromosomes and become more prominent during diplotene. This is where the synaptoneal complex dissolves, allowing for chromosomal condensation to continue and for the repulsion of homologous chromosomes. The separation of the homologous chromosomes causes the chiasmata to appear. Individual chromatids can be visualized during this stage. (The dictyotene stage is unique to female meiosis in which there is a decondensation of chromosomal bivalents. The oocyte remains in this state for many years until follicle maturation and ovulation.)",True,Prophase I,,,,
364402a3-a7bb-43ef-bba4-89a61308eff6,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,synaptoneal,False,synaptoneal,,,,
e83719a4-6dfd-4e14-864a-b67420848835,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,decondensation,False,decondensation,,,,
c0ecbf32-efca-46e4-966f-61d272d0768c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"At diakinesis, chromosomal condensation is completed. The chiasmata on each arm of the chromosomes move distally toward the telomeres. Each bivalent contains four chromatids, and pairs of sister chromatids are linked at the centromeres.",True,decondensation,,,,
077fcd8f-2a4e-4c40-ad2e-71a5c663452c,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Metaphase I,False,Metaphase I,,,,
0e01b5b7-754c-46f2-b93c-ecdb323700cd,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The spindle forms, and the nuclear membrane disappears. Bivalents align on the metaphase plate still held together by the chiasmata. The centromeres of the two homologous chromosomes are separate, aligning on either side of the equatorial plate.",True,Metaphase I,,,,
84c0cf25-6d40-4ee9-acab-e341861b0e62,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Anaphase I,False,Anaphase I,,,,
f1f71012-d371-4b5a-bf8e-fcc56c16ba94,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Homologous chromosomes separate from each other by final terminalization of the chiasmata. They move to opposite poles, pulled by the centromere, which is attached to spindle fibers.",True,Anaphase I,,,,
f04d7ebe-58c9-496f-b7d9-b5b0890ae720,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Telophase I,False,Telophase I,,,,
39618981-0c64-44c2-a2c0-3e6f08566482,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The chromosomes reach the poles, a nuclear membrane is formed, and cell division occurs. In male meiosis, the cytoplasm is divided equally, and the two resulting cells become secondary spermatocytes. In female meiosis, the division is unequal; most of the cytoplasm is retained in the secondary oocyte, while very little is retained by the first polar body. This period is very brief, and chromosomes move immediately to the second meiotic division. Each cell at this stage is haploid (1n) but with each chromosome formed of sister chromatids (2c). The sister chromatids may be unique due to recombination during the two homologues in prophase I.",True,Telophase I,,,,
15fca2e4-4be5-42e1-8ae6-078e6bb42f2f,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Meiosis II: Equational division,False,Meiosis II: Equational division,,,,
8dd3afd3-99cf-4f66-a71a-3b65a9451555,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"This division is similar to mitosis in that individual chromosomes align on the metaphase plate, and sister chromatids separate and move to opposite poles at anaphase. The single copy (1c) of each chromosome is represented by one sister chromatid in the spermatids or mature ova.",True,Meiosis II: Equational division,,,,
386f1db4-0a05-4108-a7c0-4a34306a5a3d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Male meiosis,False,Male meiosis,,,,
02f0db07-215d-48ff-8583-2b04f3090de9,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"In humans, the male is the heterogametic sex, producing two kinds of normal sperm: 23,X and 23,Y. Spermatogenesis is a constant event beginning at puberty and continuing throughout life to produce four functional spermatids from each primary gametocyte. At puberty, the number of spermatogonia (diploid stem cells) increases. These develop into primary spermatocytes after several mitotic divisions. Each primary spermatocyte undergoes the first meiotic division to become two secondary spermatocytes. These cells then undergo the second meiotic division to become four spermatids of equal size with a haploid set of chromosomes. Spermiogenesis then transforms the spermatids into mature spermatozoa by elimination of the cytoplasm, elongation of the head of the sperm, and formation of a tail. The entire process from the enlargement of the spermatogonium to formation of the mature spermatozoa takes approximately sixty-four days.",True,Male meiosis,,,,
5540d0e0-df1e-4b7e-b042-cda2c150c9e4,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Female meiosis,False,Female meiosis,,,,
f45d0357-7b90-491f-9826-86b68c07358f,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"This is in contrast to meiosis in females, which begins before birth and produces only a single type of normal ovum: 23,X. The precursors to the germ cells are oogonia; these increase in number through mitosis, reaching a maximum number of approximately 7 million. Each individual oogonium enlarges to form a primary oocyte, which becomes surrounded by ovarian stromal cells to form a primary follicle. The vast majority of primary oocytes are formed during the third and fourth months of fetal life.",True,Female meiosis,,,,
c0fda880-87c8-4adf-a675-257fce09e5dd,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"The primary oocyte begins the first meiotic division to become a secondary oocyte with the extrusion of a small polar body as the follicle matures and completes metaphase I with expulsion from the mature follicle at ovulation. The secondary oocyte does not complete the second meiotic division until fertilization, when a second polar body is extruded to form a mature ovum with a haploid set of chromosomes. Thus, each primary oocyte produces one functional gamete, the mature ovum, and three polar bodies. A nuclear membrane forms a pronucleus around the haploid set of maternal chromosomes, while a second pronucleus forms from the haploid set of chromosomes from the sperm head. These two pronuclei then fuse to begin the first mitotic division.",True,Female meiosis,,,,
64b77d03-7040-4a82-9b75-5a532710590a,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,Meiotic pairing,False,Meiotic pairing,,,,
1678359b-cc9c-44ab-b770-29e862d08b75,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Homologous pairing is unique to meiosis and plays two important roles: genetic recombination and chromosomal stabilization. While it has long been believed that the former is the most important, the latter is now accepted as the primary significance of meiotic recombination. During meiosis I, the pairing of homologues facilitates recombination, which is initiated by programed double-stranded breaks occurring at synaptic initiation sites (SISs). A subset of these breaks will resolve into the formation of the synaptonemal complex. When pairing is completed, synapsis occurs between the homologues, which completes the crossing over event. Each crossover event forms chasmata, which play an analogous role to the centromere and stabilize the maternal and paternal chromosomes. The stabilization of the metaphase chromosomes using this mechanism is key to normal chromosomal alignment and maintenance of an intact genome. Without recombination, the total number of unique gametic combinations of genes for each parent would be just over 8 million. However, crossing over greatly increases the total number of possible gene combinations such that the likelihood of either parent producing identical gametes is vanishingly small.",True,Meiotic pairing,,,,
e08600a3-0011-47cf-a36e-c1c49d1ade30,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,12.3 References and resources,True,Meiotic pairing,,,,
cad14772-5a27-4239-bd88-9803801eb23d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.3 Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
cad14772-5a27-4239-bd88-9803801eb23d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.2 Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
cad14772-5a27-4239-bd88-9803801eb23d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12.1 Eukaryotic Gene Regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
cad14772-5a27-4239-bd88-9803801eb23d,https://pressbooks.lib.vt.edu/cellbio/,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/gene-regulation-and-the-cell-cycle/,"Grey, Kindred, Figure 12.10 Overview of Meiosis. 2021. https://archive.org/details/12.10_202109. CC BY 4.0. Added Meiosis Stages by Ali Zifan. CC BY 4.0. From Wikimedia Commons.",True,Meiotic pairing,Figure 12.10,12. Gene Regulation and the Cell Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
f94bb9f9-35c2-47d4-9adc-5e0573663a03,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The translation to protein is a bit more complex because three mRNA nucleotides correspond to one amino acid in the polypeptide sequence. However, the translation to protein is still systematic and colinear.",True,Meiotic pairing,,,,
bacb30d7-c65a-42d7-879f-ddc599879b5c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,5ʼ,False,5ʼ,,,,
820e77ec-a910-4a44-a5f9-3c5f08ca2987,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,3ʼ,False,3ʼ,,,,
503ea02e-ea44-4e3d-934f-4b2312af9142,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,nontemplate,False,nontemplate,,,,
43079a3b-d7a6-4d0d-bf91-2638f1e8bac1,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Gene structure,False,Gene structure,,,,
0e27dfb9-0315-4a9d-9e41-735d2af819bf,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
0e27dfb9-0315-4a9d-9e41-735d2af819bf,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
0e27dfb9-0315-4a9d-9e41-735d2af819bf,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
35f47e1d-6b9a-4c55-a578-7102e6bdf1b5,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,The regulatory or promoter region is upstream of the transcriptional start and contains regulatory elements such as:,True,Gene structure,,,,
4fca3a38-aaa7-4277-81ba-b4ad4ea96cff,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"In eukaryotes, a single gene will produce one gene product as all genes are regulated independently. This is in contrast to prokaryotes, which regulate genes in an operon structure where one mRNA may be polycistronic and encode for multiple protein products.",True,Gene structure,,,,
52097e55-a349-4766-b636-2850554b4d58,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Types of RNA polymerase,False,Types of RNA polymerase,,,,
097f448d-c804-4f16-8d2e-505e548aae4c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"RNA polymerase I is located in the nucleolus, a specialized nuclear substructure in which ribosomal RNA (rRNA) is transcribed, processed, and assembled into ribosomes. RNA polymerase I synthesizes all the rRNAs from the tandemly duplicated set of 18S, 5.8S, and 28S ribosomal genes. (Note that the “S” designation applies to “Svedberg” units, a nonadditive value that characterizes the speed at which a particle sediments during centrifugation.)",True,Types of RNA polymerase,,,,
ea25eeb0-7933-44e4-b91e-bc6b7c22e760,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,tandemly,False,tandemly,,,,
a692a6c4-6dc3-48bc-9d77-00a7c69fd8b1,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,18S,False,18S,,,,
c035ab33-74d9-4f85-bd8b-ab7f40903264,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,28S,False,28S,,,,
a9bf787b-d0e9-4c2d-81e7-b563234b0e35,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,RNA polymerase II is located in the nucleus and synthesizes all protein-coding nuclear pre-mRNAs. Eukaryotic pre-mRNAs undergo extensive processing after transcription but before translation.,True,28S,,,,
fce8cad4-409e-499c-941d-175179206375,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"RNA polymerase II is responsible for transcribing the overwhelming majority of eukaryotic genes. RNA polymerase III is also located in the nucleus. This polymerase transcribes a variety of structural RNAs that includes the 5S pre-rRNA, transfer pre-RNAs (pre-tRNAs), and small nuclear pre-RNAs. The tRNAs have a critical role in translation; they serve as the “adaptor molecules” between the mRNA template and the growing polypeptide chain. Small nuclear RNAs have a variety of functions, including “splicing” pre-mRNAs and regulating transcription factors.",True,28S,,,,
bef621c6-e404-4fc8-9f2d-e5b8a85fb907,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",False,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",,,,
5a5d717b-d481-49eb-ba3d-e112d25f4f4d,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Table 11.1: Locations, products, and sensitivities of the three eukaryotic RNA polymerases.",True,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",,,,
f79f7f1a-acf1-435a-9954-4686609300fd,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Transcription,False,Transcription,,,,
0d7eb573-213d-4ce7-a4b3-34e946047b19,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Initiation,False,Initiation,,,,
e1552d45-0186-433a-aa7a-aec1e8f1cbf0,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Eukaryotes assemble a complex of transcription factors required to recruit RNA polymerase II to a protein coding gene.,True,Initiation,,,,
e40aab1b-ac80-40cd-af2e-44681ecda242,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
e40aab1b-ac80-40cd-af2e-44681ecda242,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
e40aab1b-ac80-40cd-af2e-44681ecda242,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
949751dd-86ff-4c0f-823d-3d6a3850fc2c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Some eukaryotic promoters also have a conserved CAAT box (GGCCAATCT) at approximately -80. Further upstream of the TATA box, eukaryotic promoters may also contain one or more GC-rich boxes (GGCG) or octamer boxes (ATTTGCAT). These elements bind cellular factors that increase the efficiency of transcription initiation and are often identified in more “active” genes that are constantly being expressed by the cell. Other regulatory elements within the promoter region will be discussed in section 12.1.",True,Initiation,,,,
56590132-ea8e-4049-ad83-95d03105ef25,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Elongation,False,Elongation,,,,
38a1d0d3-1efa-4b62-9e79-f223a8ab90be,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Following the formation of the pre-initiation complex, the polymerase is released from the other transcription factors, and elongation is allowed to proceed with the polymerase synthesizing pre-mRNA in the 5′ to 3′ direction.",True,Elongation,,,,
db20c842-71ee-45ad-b6fe-5b50c587e5c2,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Termination,False,Termination,,,,
0741daea-32f9-4bd7-9dc6-69af2d87447d,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The termination of transcription is different for the different polymerases. Unlike in prokaryotes, elongation by RNA polymerase II in eukaryotes takes place 1,000 to 2,000 nucleotides beyond the end of the gene being transcribed. This pre-mRNA tail is subsequently removed by cleavage during mRNA processing. Alternatively, RNA polymerases I and III require termination signals. Genes transcribed by RNA polymerase I contain a specific eighteen-nucleotide sequence that is recognized by a termination protein. The process of termination in RNA polymerase III involves an mRNA hairpin similar to rho-independent termination of transcription in prokaryotes.",True,Termination,,,,
dd2d23db-19e4-4aa4-ba7a-9806608fe400,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Types of RNA,False,Types of RNA,,,,
20cc6626-ac31-45a2-b482-6c3fe7e4210e,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"RNA is found in three different forms in the cell, and each is used for specific aspects of translation. Not all RNA that is transcribed is translated into a protein product; some transcribed RNA (rRNA and tRNA) is fully functional in the RNA form. mRNA (messenger RNA) is transcribed by RNA pol II.",True,Types of RNA,,,,
a230adbd-095b-41b4-ae14-e509bc879194,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,mRNA,False,mRNA,,,,
b44be84e-566e-4fc4-b080-080a6cf6f45f,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
b44be84e-566e-4fc4-b080-080a6cf6f45f,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
b44be84e-566e-4fc4-b080-080a6cf6f45f,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
f6be0f92-36d2-4858-9605-8073fe52e152,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
f6be0f92-36d2-4858-9605-8073fe52e152,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
f6be0f92-36d2-4858-9605-8073fe52e152,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
47f32687-a09e-485a-8230-8d31948b7ac5,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,tRNA,False,tRNA,,,,
f18f99fa-80b2-4922-9b54-2c5bd4e6b97b,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"tRNA, transfer RNA, is transcribed by RNA pol III, and like mRNA it requires maturation including:",True,tRNA,,,,
b075a68e-39f8-47f8-bf86-c215fa7b89af,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"tRNAs also are typical of base modifications generating nonconventional bases allowing base-pairing to several codons. This duplicity of binding is usually due to wobble in the third base pair. tRNA primarily functions to bring amino acids to the ribosome during protein translation. The anticodon on tRNA pairs with the codon on mRNA, and this determines which amino acid is added to the growing polypeptide chain.",True,tRNA,,,,
9394b2f5-13a6-428c-a761-188d78c55b61,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,rRNA,False,rRNA,,,,
d8bdf8ec-8eb5-4ca6-81e4-7d47bce1ff0a,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"rRNA, ribosomal RNA, is transcribed by RNA poly I and III and requires maturation that is slightly different from mRNA and tRNA. This RNA product is not translated but rather requires methylation and is incorporated into the protein as structural support. The 18S RNA is incorporated into the 40S ribosomal subunit, and the 28S, 5.8S, and 5S is incorporated into the 60S ribosomal subunit. These combine to make the full 80S ribosome required for protein translation.",True,rRNA,,,,
52437ade-a313-4fab-999b-96ba69ac2c34,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,11.1 References and resources,True,rRNA,,,,
eefc5cd9-c0fa-4183-baaf-7780657ec74b,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 15: Genes and Proteins.",True,rRNA,,,,
a9ed0c94-6c1c-4844-a636-4550a0f102f2,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 11: Gene Expression: From Transcription to Translation.",True,rRNA,,,,
bef1408e-e37f-4905-995a-37aa725ea289,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 39, 41–45.",True,rRNA,,,,
4c334747-b7fe-440b-b617-79c86c67808c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 3: The Human Genome: Gene Structure and Function.",True,rRNA,,,,
6df088c2-3775-4365-ba1f-b4862e16f4e1,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
6df088c2-3775-4365-ba1f-b4862e16f4e1,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
6df088c2-3775-4365-ba1f-b4862e16f4e1,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
ed0bb0ad-1ddf-4425-aff7-cacd8bd8fae5,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
ed0bb0ad-1ddf-4425-aff7-cacd8bd8fae5,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
ed0bb0ad-1ddf-4425-aff7-cacd8bd8fae5,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
9e0a996e-dcfb-4af4-8889-1a13a7c7fc2f,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
9e0a996e-dcfb-4af4-8889-1a13a7c7fc2f,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
9e0a996e-dcfb-4af4-8889-1a13a7c7fc2f,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
ac84efbe-8779-466d-b0aa-55ea56c58b2c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
ac84efbe-8779-466d-b0aa-55ea56c58b2c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
ac84efbe-8779-466d-b0aa-55ea56c58b2c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
1cbf6cbb-3711-48d8-938b-f95db474684a,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
1cbf6cbb-3711-48d8-938b-f95db474684a,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
1cbf6cbb-3711-48d8-938b-f95db474684a,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
8d4cb77f-7f72-4b2a-be0c-d69ce210a1bc,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,11.2 Protein Translation,True,rRNA,,,,
966dd498-fc0e-412c-9c85-196e7ce837b9,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Translation is the process by which mRNAs are converted into protein products through the interactions of mRNA, tRNA, and rRNA. Even before an mRNA is translated, a cell must invest energy to build each of its ribosomes, a complex macromolecule composed of structural and catalytic rRNAs, and many distinct polypeptides. In eukaryotes, the nucleolus is completely specialized for the synthesis and assembly of rRNAs.",True,rRNA,,,,
3808c5de-4ff8-4647-8c5f-e05e084f6753,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Ribosomes exist in the cytoplasm and rough endoplasmic reticulum of eukaryotes. Ribosomes dissociate into large and small subunits when they are not synthesizing proteins and reassociate during the initiation of translation.,True,rRNA,,,,
8b79b097-d0ac-4a62-b605-e236e472f0bc,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Each mRNA molecule is simultaneously translated by many ribosomes, all synthesizing protein in the same direction: reading the mRNA from 5′ to 3′ and synthesizing the polypeptide from the N terminus to the C terminus. The complete mRNA/poly-ribosome structure is called a polysome.",True,rRNA,,,,
b8fd9e01-d82b-4840-80ea-f69392fa0b64,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,tRNA synthetases,False,tRNA synthetases,,,,
4ef0ec0d-6710-412b-9f89-fef0d0a005b0,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"mRNAs are read three base pairs at a time (codon), and the reading frame will start with the first AUG (figures 11.6 and 11.7). Translation requires the formation of an aminoacyl-tRNA where tRNA is charged with the correct amino acid and brought to the translational machinery. Through the process of tRNA “charging,” each tRNA molecule is linked to its correct amino acid by one of a group of enzymes called aminoacyl tRNA synthetases.",True,tRNA synthetases,,,,
4445fa99-64d0-42f1-9305-05be60d399e1,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"At least one type of aminoacyl tRNA synthetase exists for each of the twenty amino acids; the exact number of aminoacyl tRNA synthetases varies by species. These enzymes first bind and hydrolyze ATP to catalyze a high-energy bond between an amino acid and adenosine monophosphate (AMP). The activated amino acid is then transferred to the tRNA, and AMP is released. The term “charging” is appropriate, since the high-energy bond that attaches an amino acid to its tRNA is later used to drive the formation of the peptide bond. Each tRNA is named for its amino acid.",True,tRNA synthetases,,,,
cfe91714-8c54-4671-a29d-2ab90dd4eda7,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Translational initiation,False,Translational initiation,,,,
2e4603d9-00fc-4d15-bf97-3255dbe2b61c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
2e4603d9-00fc-4d15-bf97-3255dbe2b61c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
2e4603d9-00fc-4d15-bf97-3255dbe2b61c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
2b7c6ea3-6af3-45b4-8567-a18e2a063432,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,40S,False,40S,,,,
27541b4f-ebb4-4f4d-a4c1-10e8c4e5dfd1,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,60S,False,60S,,,,
235b8179-4ee4-490e-82d0-37a10d01a07c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,tRNAi,False,tRNAi,,,,
215d7c59-c117-492e-8a19-7675829075be,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Translation elongation,False,Translation elongation,,,,
87489772-7067-4758-a8fe-316a9b7495c9,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The ribosome has three locations for tRNA binding: A, P, and E sites.",True,Translation elongation,,,,
2df1ec5a-7e99-46a9-9b66-91b15ecd5d7f,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Translation elongation requires energy in the form of GTP, and additional elongation factors (EFs) are required for this process. Elongation proceeds with charged tRNAs sequentially entering and leaving the ribosome as each new amino acid is added to the polypeptide chain. Movement of a tRNA from A to P to E sites is induced by conformational changes that advance the ribosome by three bases in the 3′ direction. GTP energy is required both for the binding of a new aminoacyl-tRNA to the A site and for its translocation to the P site after formation of the peptide bond.",True,Translation elongation,,,,
98418d94-72ff-4f75-b28b-368aa72cb3b9,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Peptide bonds form between the amino group of the amino acid attached to the A-site tRNA and the carboxyl group of the amino acid attached to the P-site tRNA. A new tRNA with the corresponding amino acid coded for by the mRNA will enter into the A site of the ribosome.,True,Translation elongation,,,,
10e585d1-c464-4f24-8631-3004e2902b9b,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
10e585d1-c464-4f24-8631-3004e2902b9b,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
10e585d1-c464-4f24-8631-3004e2902b9b,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
243b0b81-ac96-435f-8230-738a469fd766,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,Translational termination,False,Translational termination,,,,
1feb638e-77f1-4422-8c1b-0ab29c5c020b,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Termination of translation occurs when a nonsense codon (UAA, UAG, or UGA) is encountered. Upon aligning with the A site, these nonsense codons are recognized by protein release factors that resemble tRNAs.",True,Translational termination,,,,
fb58528e-c6a3-4364-8d37-9990b16d3531,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The release factors in both prokaryotes and eukaryotes instruct peptidyl transferase to add a water molecule to the carboxyl end of the P-site amino acid. This reaction forces the P-site amino acid to detach from its tRNA, and the newly made protein is released.",True,Translational termination,,,,
a03e10d4-1a16-471f-86b4-fd7ae851a0c3,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"The small and large ribosomal subunits dissociate from the mRNA and from each other; they are recruited almost immediately into another translation initiation complex. After many ribosomes have completed translation, the mRNA is degraded so the nucleotides can be reused in another transcription reaction.",True,Translational termination,,,,
2b71cef6-e1c8-4083-b72b-3ed555b8bdb9,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,11.2 References and resources,True,Translational termination,,,,
2682944b-920b-4cec-98e6-1835affc4754,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
2682944b-920b-4cec-98e6-1835affc4754,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
2682944b-920b-4cec-98e6-1835affc4754,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
190c6b1f-14f5-4aa0-a7f1-d4a119118887,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
190c6b1f-14f5-4aa0-a7f1-d4a119118887,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
190c6b1f-14f5-4aa0-a7f1-d4a119118887,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
a4cd4a8f-b3ab-46a5-a380-2288e4bed48c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
a4cd4a8f-b3ab-46a5-a380-2288e4bed48c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
a4cd4a8f-b3ab-46a5-a380-2288e4bed48c,https://pressbooks.lib.vt.edu/cellbio/,11.2 Protein Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-2,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
db1dd789-284a-4611-bf94-d065f0253d8e,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The translation to protein is a bit more complex because three mRNA nucleotides correspond to one amino acid in the polypeptide sequence. However, the translation to protein is still systematic and colinear.",True,Translational termination,,,,
6ea4aa9d-2013-4521-a438-404b5f271399,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,5ʼ,False,5ʼ,,,,
12c2c783-eb96-4e08-8ada-88031b8e5fbb,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,3ʼ,False,3ʼ,,,,
ca4819b9-404a-46ee-bf45-043bd0b653d8,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,nontemplate,False,nontemplate,,,,
519c7bed-7c22-4486-bc00-e3acc65eb602,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Gene structure,False,Gene structure,,,,
061fc8a3-7469-414a-a8f7-8ff79bdadbfe,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
061fc8a3-7469-414a-a8f7-8ff79bdadbfe,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
061fc8a3-7469-414a-a8f7-8ff79bdadbfe,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
474fb5f5-74a4-4f51-a4ca-7cf35948c040,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,The regulatory or promoter region is upstream of the transcriptional start and contains regulatory elements such as:,True,Gene structure,,,,
bde5f2df-3eaa-4e74-8c1e-af50833fea87,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"In eukaryotes, a single gene will produce one gene product as all genes are regulated independently. This is in contrast to prokaryotes, which regulate genes in an operon structure where one mRNA may be polycistronic and encode for multiple protein products.",True,Gene structure,,,,
ed6542c6-1c4b-4fd1-bbb5-7b26c5f6b768,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Types of RNA polymerase,False,Types of RNA polymerase,,,,
7ea0884e-4c4a-44f5-9d7c-d93c52ba54fa,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"RNA polymerase I is located in the nucleolus, a specialized nuclear substructure in which ribosomal RNA (rRNA) is transcribed, processed, and assembled into ribosomes. RNA polymerase I synthesizes all the rRNAs from the tandemly duplicated set of 18S, 5.8S, and 28S ribosomal genes. (Note that the “S” designation applies to “Svedberg” units, a nonadditive value that characterizes the speed at which a particle sediments during centrifugation.)",True,Types of RNA polymerase,,,,
d398fa0b-fe68-4226-a1ca-d169e3e7ca25,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,tandemly,False,tandemly,,,,
a50a040c-9c7a-4ad0-ab5e-6dad04d22bf0,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,18S,False,18S,,,,
1ff6caa6-ebc1-4343-b51f-51a059771290,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,28S,False,28S,,,,
7c053511-0360-4970-9751-97a8f2b0cba9,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,RNA polymerase II is located in the nucleus and synthesizes all protein-coding nuclear pre-mRNAs. Eukaryotic pre-mRNAs undergo extensive processing after transcription but before translation.,True,28S,,,,
e8af8724-755e-4345-be9f-4858c1f905f0,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"RNA polymerase II is responsible for transcribing the overwhelming majority of eukaryotic genes. RNA polymerase III is also located in the nucleus. This polymerase transcribes a variety of structural RNAs that includes the 5S pre-rRNA, transfer pre-RNAs (pre-tRNAs), and small nuclear pre-RNAs. The tRNAs have a critical role in translation; they serve as the “adaptor molecules” between the mRNA template and the growing polypeptide chain. Small nuclear RNAs have a variety of functions, including “splicing” pre-mRNAs and regulating transcription factors.",True,28S,,,,
aa9eec22-7e64-454d-9d0e-826928af045d,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",False,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",,,,
ac838727-a497-4d50-b8ec-83fc2c97e528,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Table 11.1: Locations, products, and sensitivities of the three eukaryotic RNA polymerases.",True,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",,,,
1237e782-6370-49a4-8793-be53a9e3d09e,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Transcription,False,Transcription,,,,
44ed7d4a-6b46-432c-88e0-8a298f13ee90,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Initiation,False,Initiation,,,,
5dcf5c56-2da1-4968-8484-f854105d087c,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Eukaryotes assemble a complex of transcription factors required to recruit RNA polymerase II to a protein coding gene.,True,Initiation,,,,
a1d1710f-d473-4102-b75b-8990e968b04b,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
a1d1710f-d473-4102-b75b-8990e968b04b,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
a1d1710f-d473-4102-b75b-8990e968b04b,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
a0423cd1-5f94-4519-9685-a4b0fdb5d075,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Some eukaryotic promoters also have a conserved CAAT box (GGCCAATCT) at approximately -80. Further upstream of the TATA box, eukaryotic promoters may also contain one or more GC-rich boxes (GGCG) or octamer boxes (ATTTGCAT). These elements bind cellular factors that increase the efficiency of transcription initiation and are often identified in more “active” genes that are constantly being expressed by the cell. Other regulatory elements within the promoter region will be discussed in section 12.1.",True,Initiation,,,,
ea3b93c2-eff6-4c84-9221-b865fbea1cdd,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Elongation,False,Elongation,,,,
63bbef7c-d2e2-4942-8d86-8c54890ca610,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Following the formation of the pre-initiation complex, the polymerase is released from the other transcription factors, and elongation is allowed to proceed with the polymerase synthesizing pre-mRNA in the 5′ to 3′ direction.",True,Elongation,,,,
f724b175-5fef-4358-b739-44185b6c52e5,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Termination,False,Termination,,,,
44227894-7787-4f3d-a0c0-1cfbb24bd470,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The termination of transcription is different for the different polymerases. Unlike in prokaryotes, elongation by RNA polymerase II in eukaryotes takes place 1,000 to 2,000 nucleotides beyond the end of the gene being transcribed. This pre-mRNA tail is subsequently removed by cleavage during mRNA processing. Alternatively, RNA polymerases I and III require termination signals. Genes transcribed by RNA polymerase I contain a specific eighteen-nucleotide sequence that is recognized by a termination protein. The process of termination in RNA polymerase III involves an mRNA hairpin similar to rho-independent termination of transcription in prokaryotes.",True,Termination,,,,
ce3278ca-0961-4fde-8989-62ffac9d1717,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Types of RNA,False,Types of RNA,,,,
9813821d-6343-4104-ae4a-883af0e27275,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"RNA is found in three different forms in the cell, and each is used for specific aspects of translation. Not all RNA that is transcribed is translated into a protein product; some transcribed RNA (rRNA and tRNA) is fully functional in the RNA form. mRNA (messenger RNA) is transcribed by RNA pol II.",True,Types of RNA,,,,
f8c20594-60e8-4a6a-bdcc-56d7632e1ec3,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,mRNA,False,mRNA,,,,
80c4bacf-c2bc-4f31-9857-e0802c25f463,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
80c4bacf-c2bc-4f31-9857-e0802c25f463,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
80c4bacf-c2bc-4f31-9857-e0802c25f463,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
f459f902-2164-484d-93bf-8a76d9371ab6,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
f459f902-2164-484d-93bf-8a76d9371ab6,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
f459f902-2164-484d-93bf-8a76d9371ab6,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
6dd95fc6-e1a9-4fa2-8a86-c1addaf2c206,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,tRNA,False,tRNA,,,,
279ae3a6-927c-445c-9227-101262094eac,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"tRNA, transfer RNA, is transcribed by RNA pol III, and like mRNA it requires maturation including:",True,tRNA,,,,
5dd5f8b0-2de0-439a-a4fe-9fb146c6a786,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"tRNAs also are typical of base modifications generating nonconventional bases allowing base-pairing to several codons. This duplicity of binding is usually due to wobble in the third base pair. tRNA primarily functions to bring amino acids to the ribosome during protein translation. The anticodon on tRNA pairs with the codon on mRNA, and this determines which amino acid is added to the growing polypeptide chain.",True,tRNA,,,,
f293f2c6-8969-4733-b1bb-b18139043cc2,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,rRNA,False,rRNA,,,,
03a0d027-b101-49a2-bd09-c7ce4dfd48da,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"rRNA, ribosomal RNA, is transcribed by RNA poly I and III and requires maturation that is slightly different from mRNA and tRNA. This RNA product is not translated but rather requires methylation and is incorporated into the protein as structural support. The 18S RNA is incorporated into the 40S ribosomal subunit, and the 28S, 5.8S, and 5S is incorporated into the 60S ribosomal subunit. These combine to make the full 80S ribosome required for protein translation.",True,rRNA,,,,
85863eb4-bdac-498e-b015-ddd3d3057b43,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,11.1 References and resources,True,rRNA,,,,
c31565de-d6b6-4efa-8029-037b7753c170,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 15: Genes and Proteins.",True,rRNA,,,,
7b383db6-b53f-4c09-b24c-0c3a72ec3ce5,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 11: Gene Expression: From Transcription to Translation.",True,rRNA,,,,
a16ef64b-051e-4259-b866-2049626104ff,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 39, 41–45.",True,rRNA,,,,
5ab33c0a-ff74-4fe2-8293-36381c64a7ba,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 3: The Human Genome: Gene Structure and Function.",True,rRNA,,,,
bd01c5b0-aa70-4fc4-bd65-39d00930e655,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
bd01c5b0-aa70-4fc4-bd65-39d00930e655,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
bd01c5b0-aa70-4fc4-bd65-39d00930e655,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
85b89526-2870-4a74-b564-0ed736e9ce57,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
85b89526-2870-4a74-b564-0ed736e9ce57,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
85b89526-2870-4a74-b564-0ed736e9ce57,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
8853597d-b4b7-422f-8b1c-03559bde5783,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
8853597d-b4b7-422f-8b1c-03559bde5783,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
8853597d-b4b7-422f-8b1c-03559bde5783,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
8d599b72-e169-422c-bac8-0d9a0002efc3,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
8d599b72-e169-422c-bac8-0d9a0002efc3,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
8d599b72-e169-422c-bac8-0d9a0002efc3,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
b54234e0-bfdd-4878-824f-1317acf9e412,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
b54234e0-bfdd-4878-824f-1317acf9e412,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
b54234e0-bfdd-4878-824f-1317acf9e412,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
c969d5a2-d7d9-4294-9d62-7f255851a307,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,11.2 Protein Translation,True,rRNA,,,,
25041323-0ad1-42a7-a573-80ec48a673ea,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Translation is the process by which mRNAs are converted into protein products through the interactions of mRNA, tRNA, and rRNA. Even before an mRNA is translated, a cell must invest energy to build each of its ribosomes, a complex macromolecule composed of structural and catalytic rRNAs, and many distinct polypeptides. In eukaryotes, the nucleolus is completely specialized for the synthesis and assembly of rRNAs.",True,rRNA,,,,
b1f2e8f2-d928-4f88-a606-37238bca8421,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Ribosomes exist in the cytoplasm and rough endoplasmic reticulum of eukaryotes. Ribosomes dissociate into large and small subunits when they are not synthesizing proteins and reassociate during the initiation of translation.,True,rRNA,,,,
547b7fe3-c1e9-4489-ba11-41cc64633b4f,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Each mRNA molecule is simultaneously translated by many ribosomes, all synthesizing protein in the same direction: reading the mRNA from 5′ to 3′ and synthesizing the polypeptide from the N terminus to the C terminus. The complete mRNA/poly-ribosome structure is called a polysome.",True,rRNA,,,,
d9c048e2-a0ae-4b62-9ee5-d3e50c133a3b,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,tRNA synthetases,False,tRNA synthetases,,,,
670163ed-56d5-4d56-86e1-6a6a8f952be5,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"mRNAs are read three base pairs at a time (codon), and the reading frame will start with the first AUG (figures 11.6 and 11.7). Translation requires the formation of an aminoacyl-tRNA where tRNA is charged with the correct amino acid and brought to the translational machinery. Through the process of tRNA “charging,” each tRNA molecule is linked to its correct amino acid by one of a group of enzymes called aminoacyl tRNA synthetases.",True,tRNA synthetases,,,,
02cb9c77-8008-4468-ba8c-6d48f4bc11e6,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"At least one type of aminoacyl tRNA synthetase exists for each of the twenty amino acids; the exact number of aminoacyl tRNA synthetases varies by species. These enzymes first bind and hydrolyze ATP to catalyze a high-energy bond between an amino acid and adenosine monophosphate (AMP). The activated amino acid is then transferred to the tRNA, and AMP is released. The term “charging” is appropriate, since the high-energy bond that attaches an amino acid to its tRNA is later used to drive the formation of the peptide bond. Each tRNA is named for its amino acid.",True,tRNA synthetases,,,,
6cb9fd92-3e6b-47c6-ad41-8f8b2b31fa43,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Translational initiation,False,Translational initiation,,,,
acc734c3-488e-4ce5-92bc-779c1ff1cd87,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
acc734c3-488e-4ce5-92bc-779c1ff1cd87,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
acc734c3-488e-4ce5-92bc-779c1ff1cd87,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
070d160d-32ed-4f41-ad5c-b56d088452b1,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,40S,False,40S,,,,
a703d49c-a031-413c-a7b5-aca9351c761d,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,60S,False,60S,,,,
bea9ada8-7436-4a31-9bb1-bb9a6182fc3a,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,tRNAi,False,tRNAi,,,,
9bf29dc1-fc1b-492a-a9bd-8865903aa49e,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Translation elongation,False,Translation elongation,,,,
968c1a2d-d6c6-41ce-99ed-d95344683ff3,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The ribosome has three locations for tRNA binding: A, P, and E sites.",True,Translation elongation,,,,
0b65740a-edd5-46d4-b317-a8ee98f2eb5a,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Translation elongation requires energy in the form of GTP, and additional elongation factors (EFs) are required for this process. Elongation proceeds with charged tRNAs sequentially entering and leaving the ribosome as each new amino acid is added to the polypeptide chain. Movement of a tRNA from A to P to E sites is induced by conformational changes that advance the ribosome by three bases in the 3′ direction. GTP energy is required both for the binding of a new aminoacyl-tRNA to the A site and for its translocation to the P site after formation of the peptide bond.",True,Translation elongation,,,,
5680b02f-5972-4231-819a-d37f8ea6fe74,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Peptide bonds form between the amino group of the amino acid attached to the A-site tRNA and the carboxyl group of the amino acid attached to the P-site tRNA. A new tRNA with the corresponding amino acid coded for by the mRNA will enter into the A site of the ribosome.,True,Translation elongation,,,,
424abd9f-9535-4d74-824f-2828af9f0197,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
424abd9f-9535-4d74-824f-2828af9f0197,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
424abd9f-9535-4d74-824f-2828af9f0197,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
50547a43-7157-4b31-adc4-738c6189aa51,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,Translational termination,False,Translational termination,,,,
482d7f29-22b6-44aa-b45f-bd0dd8879ada,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Termination of translation occurs when a nonsense codon (UAA, UAG, or UGA) is encountered. Upon aligning with the A site, these nonsense codons are recognized by protein release factors that resemble tRNAs.",True,Translational termination,,,,
01a52642-cfe9-48c9-bfa1-0e723746fd59,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The release factors in both prokaryotes and eukaryotes instruct peptidyl transferase to add a water molecule to the carboxyl end of the P-site amino acid. This reaction forces the P-site amino acid to detach from its tRNA, and the newly made protein is released.",True,Translational termination,,,,
57cb5fc7-49b0-42c1-b872-76fcbfac9e41,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"The small and large ribosomal subunits dissociate from the mRNA and from each other; they are recruited almost immediately into another translation initiation complex. After many ribosomes have completed translation, the mRNA is degraded so the nucleotides can be reused in another transcription reaction.",True,Translational termination,,,,
94cae716-e9a9-4799-b2d7-281784487f1f,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,11.2 References and resources,True,Translational termination,,,,
51d2751d-3f1d-48f8-a904-c2ced7871d22,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
51d2751d-3f1d-48f8-a904-c2ced7871d22,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
51d2751d-3f1d-48f8-a904-c2ced7871d22,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
62ae23e6-cd0d-4f9c-89c2-b2b320393b5c,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
62ae23e6-cd0d-4f9c-89c2-b2b320393b5c,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
62ae23e6-cd0d-4f9c-89c2-b2b320393b5c,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
ed505383-606e-4384-843a-a765530a8c9b,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
ed505383-606e-4384-843a-a765530a8c9b,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
ed505383-606e-4384-843a-a765530a8c9b,https://pressbooks.lib.vt.edu/cellbio/,11.1 Transcription,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/#chapter-88-section-1,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
fc8ef1cc-87e3-4509-9651-3fe151832b2e,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The translation to protein is a bit more complex because three mRNA nucleotides correspond to one amino acid in the polypeptide sequence. However, the translation to protein is still systematic and colinear.",True,Translational termination,,,,
b8a65e8b-3c7e-40d7-b6d6-7f4c61d0e690,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,5ʼ,False,5ʼ,,,,
50aceea2-38c4-4fa1-b0ed-7acfaf25d385,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,3ʼ,False,3ʼ,,,,
5984a01d-61f3-475f-bd62-a415e19f81ed,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,nontemplate,False,nontemplate,,,,
6fbed646-9e6c-417c-8056-348eccd4d09b,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Gene structure,False,Gene structure,,,,
4261a378-98cb-40d6-813b-be6ee44412b5,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
4261a378-98cb-40d6-813b-be6ee44412b5,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
4261a378-98cb-40d6-813b-be6ee44412b5,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The chromosome is organized into functional units call genes. These are specific locations on a chromosome that are composed of a transcribed region and a regulatory (or promoter) region. The transcribed region is typically (but not always) downstream of the transcriptional start and contains the following DNA elements: a 5ʼ cap site (required for maturation of mRNA), translational start (AUG), introns and exons, and the polyadenylation site (figure 11.2).",True,Gene structure,Figure 11.2,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
2ccb4daf-9646-43dd-b787-fecde19cad90,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,The regulatory or promoter region is upstream of the transcriptional start and contains regulatory elements such as:,True,Gene structure,,,,
1d29855d-c16f-4a3a-b64c-afe34cf4e0c3,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"In eukaryotes, a single gene will produce one gene product as all genes are regulated independently. This is in contrast to prokaryotes, which regulate genes in an operon structure where one mRNA may be polycistronic and encode for multiple protein products.",True,Gene structure,,,,
8ecd30b1-17ff-48f3-94c8-37508ea18030,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Types of RNA polymerase,False,Types of RNA polymerase,,,,
ebf6c56f-4ddc-4614-a08d-7fce7a2e084b,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"RNA polymerase I is located in the nucleolus, a specialized nuclear substructure in which ribosomal RNA (rRNA) is transcribed, processed, and assembled into ribosomes. RNA polymerase I synthesizes all the rRNAs from the tandemly duplicated set of 18S, 5.8S, and 28S ribosomal genes. (Note that the “S” designation applies to “Svedberg” units, a nonadditive value that characterizes the speed at which a particle sediments during centrifugation.)",True,Types of RNA polymerase,,,,
12b7ab8f-8629-4075-8057-9f753a08456d,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,tandemly,False,tandemly,,,,
4e2f725a-dcb2-4438-a023-96a7543f293e,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,18S,False,18S,,,,
41e873a1-2484-46b4-9db8-96d5775b96a6,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,28S,False,28S,,,,
545c5dc4-92e1-4120-8d85-56bb333125b1,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,RNA polymerase II is located in the nucleus and synthesizes all protein-coding nuclear pre-mRNAs. Eukaryotic pre-mRNAs undergo extensive processing after transcription but before translation.,True,28S,,,,
b68bee27-e849-4fdc-a31c-9312d3c23b58,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"RNA polymerase II is responsible for transcribing the overwhelming majority of eukaryotic genes. RNA polymerase III is also located in the nucleus. This polymerase transcribes a variety of structural RNAs that includes the 5S pre-rRNA, transfer pre-RNAs (pre-tRNAs), and small nuclear pre-RNAs. The tRNAs have a critical role in translation; they serve as the “adaptor molecules” between the mRNA template and the growing polypeptide chain. Small nuclear RNAs have a variety of functions, including “splicing” pre-mRNAs and regulating transcription factors.",True,28S,,,,
fca5a991-c5fa-4222-bea2-16d541042332,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",False,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",,,,
587a0d6d-48b0-43b2-bd4f-1e40f41395de,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Table 11.1: Locations, products, and sensitivities of the three eukaryotic RNA polymerases.",True,"Locations, products, and sensitivities of the three eukaryotic RNA polymerases",,,,
4c01d14d-be23-4c9a-bb1c-dde589ba9813,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Transcription,False,Transcription,,,,
50e10589-99ff-4ffd-aae6-ae9e41094b39,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Initiation,False,Initiation,,,,
b55d2014-3238-4c7c-9301-28f21f85bb37,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Eukaryotes assemble a complex of transcription factors required to recruit RNA polymerase II to a protein coding gene.,True,Initiation,,,,
7e328734-b44b-43b2-a33f-38f4bf4c473c,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
7e328734-b44b-43b2-a33f-38f4bf4c473c,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
7e328734-b44b-43b2-a33f-38f4bf4c473c,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Transcription factors that bind to the promoter are called basal transcription factors. These basal factors are all called TFII (for transcription factor/polymerase II) plus an additional letter (A–J). The core complex is TFIID, which includes a TATA-binding protein (TBP). The other transcription factors systematically fall into place on the DNA template, with each one further stabilizing the pre-initiation complex and contributing to the recruitment of RNA polymerase II (figure 11.3).",True,Initiation,Figure 11.3,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
fb74d476-1d79-4dd2-8067-9f3810627784,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Some eukaryotic promoters also have a conserved CAAT box (GGCCAATCT) at approximately -80. Further upstream of the TATA box, eukaryotic promoters may also contain one or more GC-rich boxes (GGCG) or octamer boxes (ATTTGCAT). These elements bind cellular factors that increase the efficiency of transcription initiation and are often identified in more “active” genes that are constantly being expressed by the cell. Other regulatory elements within the promoter region will be discussed in section 12.1.",True,Initiation,,,,
03d0053f-a98d-456d-81f8-c5cf33110f47,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Elongation,False,Elongation,,,,
2b428e97-164a-4c08-bb78-449e70592218,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Following the formation of the pre-initiation complex, the polymerase is released from the other transcription factors, and elongation is allowed to proceed with the polymerase synthesizing pre-mRNA in the 5′ to 3′ direction.",True,Elongation,,,,
5254515c-1c11-4e28-80c9-ff4825aef681,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Termination,False,Termination,,,,
b890d946-0b54-4460-bd54-a74963e00432,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The termination of transcription is different for the different polymerases. Unlike in prokaryotes, elongation by RNA polymerase II in eukaryotes takes place 1,000 to 2,000 nucleotides beyond the end of the gene being transcribed. This pre-mRNA tail is subsequently removed by cleavage during mRNA processing. Alternatively, RNA polymerases I and III require termination signals. Genes transcribed by RNA polymerase I contain a specific eighteen-nucleotide sequence that is recognized by a termination protein. The process of termination in RNA polymerase III involves an mRNA hairpin similar to rho-independent termination of transcription in prokaryotes.",True,Termination,,,,
73bd6ed5-2267-493a-9d54-65bf8c94f613,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Types of RNA,False,Types of RNA,,,,
9415c314-baef-49cf-9637-e9216b82185e,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"RNA is found in three different forms in the cell, and each is used for specific aspects of translation. Not all RNA that is transcribed is translated into a protein product; some transcribed RNA (rRNA and tRNA) is fully functional in the RNA form. mRNA (messenger RNA) is transcribed by RNA pol II.",True,Types of RNA,,,,
4e425f22-de2b-4ee8-b5cd-3438666923eb,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,mRNA,False,mRNA,,,,
55a415b4-f98b-4469-9043-c93dabe08dad,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
55a415b4-f98b-4469-9043-c93dabe08dad,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
55a415b4-f98b-4469-9043-c93dabe08dad,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"In eukaryotes, pre-mRNA requires maturation before use in translation including (figure 11.4):",True,mRNA,Figure 11.4,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
13c17512-089e-4c7a-8c56-0fa333002e46,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
13c17512-089e-4c7a-8c56-0fa333002e46,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
13c17512-089e-4c7a-8c56-0fa333002e46,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Splicing is a complex process mediated by a large protein RNA-associated complex called the spliceosome. The structure contains both proteins and small nuclear (sn)RNA. (Note antibodies to snRNAs are specific for systemic lupus.) Intronic sequences usually have GU at their 5′ end and AG at their 3′ end. An adenosine (A) is typically found at the branching point within the intron sequence. Small nuclear ribonucleoproteins (snRNPs) of the spliceosome recognize intron‒exon junctions and splice out the intron as a “lariat” structure. Splicing starts with an autocatalytic cleavage of the 5ʼ end of the intron leading to the formation of a circular or lariat where a 5′ UG sequence pairs with an internal adenine (A) or branch site. Finally the 3ʼ end of the intron is cleaved, and the intron is released as a lariat, and the right side of the exon is spliced to the left side. Alternative splicing of introns and exons generates protein variation from a single mRNA (figure 11.5).",True,mRNA,Figure 11.5,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
961e905f-41cd-4f3d-8ed4-da2d543992b0,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,tRNA,False,tRNA,,,,
73d3decd-285d-4ed9-aa33-cceb951991b6,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"tRNA, transfer RNA, is transcribed by RNA pol III, and like mRNA it requires maturation including:",True,tRNA,,,,
e35c3cc2-dfb7-45c6-bcb7-1aa21c778fb3,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"tRNAs also are typical of base modifications generating nonconventional bases allowing base-pairing to several codons. This duplicity of binding is usually due to wobble in the third base pair. tRNA primarily functions to bring amino acids to the ribosome during protein translation. The anticodon on tRNA pairs with the codon on mRNA, and this determines which amino acid is added to the growing polypeptide chain.",True,tRNA,,,,
e886acc4-7fb9-479a-af49-370cb15a275f,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,rRNA,False,rRNA,,,,
6257915b-9da9-4943-80b7-149fc4216eba,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"rRNA, ribosomal RNA, is transcribed by RNA poly I and III and requires maturation that is slightly different from mRNA and tRNA. This RNA product is not translated but rather requires methylation and is incorporated into the protein as structural support. The 18S RNA is incorporated into the 40S ribosomal subunit, and the 28S, 5.8S, and 5S is incorporated into the 60S ribosomal subunit. These combine to make the full 80S ribosome required for protein translation.",True,rRNA,,,,
43a0754c-1fb7-4f94-bc45-cd6c25fc3cc9,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,11.1 References and resources,True,rRNA,,,,
54eaa3cd-5612-4d68-b70a-888c4c4a15c4,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 15: Genes and Proteins.",True,rRNA,,,,
cf498f57-b747-4d1e-a59f-45b403437b06,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 11: Gene Expression: From Transcription to Translation.",True,rRNA,,,,
52a74e12-58d6-4a74-8e08-dd589822804b,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 39, 41–45.",True,rRNA,,,,
702de702-6ef4-489f-8426-61368ad1b634,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 3: The Human Genome: Gene Structure and Function.",True,rRNA,,,,
d48c2586-8c9e-49b4-8de0-f8c5141c979a,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
d48c2586-8c9e-49b4-8de0-f8c5141c979a,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
d48c2586-8c9e-49b4-8de0-f8c5141c979a,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.3 Transcription initiation. 2021. https://archive.org/details/11.3_20210926. CC BY 4.0.",True,rRNA,Figure 11.3,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
bfdbb9d6-297a-4ca6-a070-5c5f0d8a9f45,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
bfdbb9d6-297a-4ca6-a070-5c5f0d8a9f45,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
bfdbb9d6-297a-4ca6-a070-5c5f0d8a9f45,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.4 Overview of mRNA processing involving the removal of introns (splicing), addition of a 5’ cap and 3’ tail. 2021. https://archive.org/details/11.4_20210926. CC BY 4.0.",True,rRNA,Figure 11.4,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
afc03485-ee8c-463b-9a8d-a5936d34dd69,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
afc03485-ee8c-463b-9a8d-a5936d34dd69,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
afc03485-ee8c-463b-9a8d-a5936d34dd69,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.5 Summary of mRNA splicing. 2021. https://archive.org/details/11.5_20210926. CC BY 4.0.",True,rRNA,Figure 11.5,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
ac34910b-360c-4a32-8333-d7c0569ef9b6,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
ac34910b-360c-4a32-8333-d7c0569ef9b6,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
ac34910b-360c-4a32-8333-d7c0569ef9b6,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Lieberman M, Peet A. Figure 11.1 Co-linearity of DNA and RNA. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 277. Figure 15.3 Reading frame of messenger RNA (mRNA). 2017.",True,rRNA,Figure 11.1,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
8ae789cf-dff7-4b5c-9e5a-66eb2ab2d455,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
8ae789cf-dff7-4b5c-9e5a-66eb2ab2d455,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
8ae789cf-dff7-4b5c-9e5a-66eb2ab2d455,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Lieberman M, Peet A. Figure 11.2 Schematic view of a eukaryotic gene structure. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 255. Figure 14.4 A schematic view of a eukarytoic gene, and steps required to produce a protein product. 2017. Added Myoglobin by AzaToth. Public domain. From Wikimedia Commons.",True,rRNA,Figure 11.2,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
bd3a51ce-dbb3-4acc-8135-cb58b80acc77,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,11.2 Protein Translation,True,rRNA,,,,
959f7d30-43cf-4be7-9f5c-f1f2c15067df,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Translation is the process by which mRNAs are converted into protein products through the interactions of mRNA, tRNA, and rRNA. Even before an mRNA is translated, a cell must invest energy to build each of its ribosomes, a complex macromolecule composed of structural and catalytic rRNAs, and many distinct polypeptides. In eukaryotes, the nucleolus is completely specialized for the synthesis and assembly of rRNAs.",True,rRNA,,,,
07eb5e11-7078-40b2-8850-44fc97dc9f87,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Ribosomes exist in the cytoplasm and rough endoplasmic reticulum of eukaryotes. Ribosomes dissociate into large and small subunits when they are not synthesizing proteins and reassociate during the initiation of translation.,True,rRNA,,,,
42b7f238-c914-40c5-956a-8b50cb335899,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Each mRNA molecule is simultaneously translated by many ribosomes, all synthesizing protein in the same direction: reading the mRNA from 5′ to 3′ and synthesizing the polypeptide from the N terminus to the C terminus. The complete mRNA/poly-ribosome structure is called a polysome.",True,rRNA,,,,
9e81325f-6861-4c2d-8af0-96763eb601ee,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,tRNA synthetases,False,tRNA synthetases,,,,
dbb1d85a-1da7-4151-88bc-d452a8866819,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"mRNAs are read three base pairs at a time (codon), and the reading frame will start with the first AUG (figures 11.6 and 11.7). Translation requires the formation of an aminoacyl-tRNA where tRNA is charged with the correct amino acid and brought to the translational machinery. Through the process of tRNA “charging,” each tRNA molecule is linked to its correct amino acid by one of a group of enzymes called aminoacyl tRNA synthetases.",True,tRNA synthetases,,,,
1d952da0-7bd0-48a8-a1a3-c12206a1a960,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"At least one type of aminoacyl tRNA synthetase exists for each of the twenty amino acids; the exact number of aminoacyl tRNA synthetases varies by species. These enzymes first bind and hydrolyze ATP to catalyze a high-energy bond between an amino acid and adenosine monophosphate (AMP). The activated amino acid is then transferred to the tRNA, and AMP is released. The term “charging” is appropriate, since the high-energy bond that attaches an amino acid to its tRNA is later used to drive the formation of the peptide bond. Each tRNA is named for its amino acid.",True,tRNA synthetases,,,,
dbb18044-32e3-4974-aa7d-6af59deaec45,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Translational initiation,False,Translational initiation,,,,
040891bc-ce3d-4e87-8692-529fc9f19474,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
040891bc-ce3d-4e87-8692-529fc9f19474,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
040891bc-ce3d-4e87-8692-529fc9f19474,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Translation is initiated by the assembly of the small ribosomal subunit (40S) with initiation factors (IF), which recognize the 5ʼ cap of the mRNA. This is referred to as the cap-binding complex, and this will scan the mRNA for the initial AUG needed to start translation. Once at the cap, the initiation complex tracks along the mRNA in the 5′ to 3′ direction, searching for the AUG start codon. Many eukaryotic mRNAs are translated from the first AUG, but this is not always the case. Once the appropriate AUG is identified, the other proteins and CBP dissociate, and the 60S subunit binds to the complex of Met-tRNAi, mRNA, and the 40S subunit. This step completes the initiation of translation in eukaryotes (figure 11.8).",True,Translational initiation,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
6fc51f65-361c-4ac6-ae0f-e239bac2fd66,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,40S,False,40S,,,,
4b4dad53-12f2-49ac-954d-14dfdc10db46,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,60S,False,60S,,,,
17fde464-ea8a-49e9-b98d-342a953e91db,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,tRNAi,False,tRNAi,,,,
3e449ee7-4df7-47c8-b33a-bba0a4a0c1d6,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Translation elongation,False,Translation elongation,,,,
aaff4e5f-dfbb-4484-977c-7c6513058308,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The ribosome has three locations for tRNA binding: A, P, and E sites.",True,Translation elongation,,,,
1b909c3f-cc41-4fcc-8e47-ee2a5fe65bae,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Translation elongation requires energy in the form of GTP, and additional elongation factors (EFs) are required for this process. Elongation proceeds with charged tRNAs sequentially entering and leaving the ribosome as each new amino acid is added to the polypeptide chain. Movement of a tRNA from A to P to E sites is induced by conformational changes that advance the ribosome by three bases in the 3′ direction. GTP energy is required both for the binding of a new aminoacyl-tRNA to the A site and for its translocation to the P site after formation of the peptide bond.",True,Translation elongation,,,,
b3e666de-99e4-4bec-9bca-1ceb2cda8d77,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Peptide bonds form between the amino group of the amino acid attached to the A-site tRNA and the carboxyl group of the amino acid attached to the P-site tRNA. A new tRNA with the corresponding amino acid coded for by the mRNA will enter into the A site of the ribosome.,True,Translation elongation,,,,
6def6ba5-5a61-45b3-b274-f28fe9d00b64,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
6def6ba5-5a61-45b3-b274-f28fe9d00b64,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
6def6ba5-5a61-45b3-b274-f28fe9d00b64,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The amino acid attached to the tRNA in the P site will be transferred to the tRNA in the A site; this is referred to as the peptidyl transferase react ion. The tRNAs will slide such that the tRNA in the P site will move to the E site and the tRNA in the A site will move to the P site. The tRNA in the E site will be released, and a new tRNA will enter into the A site, and the process will continue with the addition of tRNAs in the manner until the full message is transcribed (figure 11.8).",True,Translation elongation,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
b184df61-df8e-42d6-8984-0e5d058a19b7,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,Translational termination,False,Translational termination,,,,
a8357fe1-c0ae-48f3-9544-8a98d2b1b948,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Termination of translation occurs when a nonsense codon (UAA, UAG, or UGA) is encountered. Upon aligning with the A site, these nonsense codons are recognized by protein release factors that resemble tRNAs.",True,Translational termination,,,,
4c115f48-f5f0-4660-b519-64461d194298,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The release factors in both prokaryotes and eukaryotes instruct peptidyl transferase to add a water molecule to the carboxyl end of the P-site amino acid. This reaction forces the P-site amino acid to detach from its tRNA, and the newly made protein is released.",True,Translational termination,,,,
6a24a918-c67b-44c9-906b-6dbc08258fcc,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"The small and large ribosomal subunits dissociate from the mRNA and from each other; they are recruited almost immediately into another translation initiation complex. After many ribosomes have completed translation, the mRNA is degraded so the nucleotides can be reused in another transcription reaction.",True,Translational termination,,,,
9efa4e7d-4cdd-467e-8cc1-1940b989aa93,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,11.2 References and resources,True,Translational termination,,,,
4acf5081-eddd-4a5d-bc68-e2035e890494,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
4acf5081-eddd-4a5d-bc68-e2035e890494,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
4acf5081-eddd-4a5d-bc68-e2035e890494,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.6 Genetic code, each codons is 3 nucleotides corresponding to a specific amino acid. The code is degenerate meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered. 2021. https://archive.org/details/11.6_20210926. CC BY 4.0.",True,Translational termination,Figure 11.6,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
c4370327-c1c5-4f17-8e51-c093966312f7,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
c4370327-c1c5-4f17-8e51-c093966312f7,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
c4370327-c1c5-4f17-8e51-c093966312f7,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.7: Summary of translational initiation. 2021. CC BY SA 3.0. Adapted from Eukaryotic Translation Initiation by Chewie. CC BY SA 3.0. From Wikimedia Commons.",True,Translational termination,Figure 11.7,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
dff7d7d8-4ef1-47f9-8a8a-5956acc2822c,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11.2 Protein Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
dff7d7d8-4ef1-47f9-8a8a-5956acc2822c,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11.1 Transcription,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
dff7d7d8-4ef1-47f9-8a8a-5956acc2822c,https://pressbooks.lib.vt.edu/cellbio/,11. Transcription and Translation,https://pressbooks.lib.vt.edu/cellbio/chapter/transcription-and-translation/,"Grey, Kindred, Figure 11.8 Summary of translational elongation. 2021. CC BY 4.0.",True,Translational termination,Figure 11.8,11. Transcription and Translation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
b2b3db9a-3db9-4320-a793-5ff260163367,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Nucleotides and basic DNA structure,False,Nucleotides and basic DNA structure,,,,
3f30ee6e-ffd0-40c8-9885-8e80cea49da2,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The nucleotides combine with each other to produce phosphodiester bonds. The phosphate residue attached to the 5′ carbon of the sugar of one nucleotide forms a second ester linkage with the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, thereby forming a 5′-3′ phosphodiester bond. In a polynucleotide, one end of the chain has a free 5′ phosphate, and the other end has a free 3′-OH. These are called the 5′ and 3′ ends of the chain.",True,Nucleotides and basic DNA structure,,,,
0b055861-5c47-4297-8ad1-353a0950fefc,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Base-pairing takes place between a purine and pyrimidine on opposite strands, so that adenine and thymine are complementary base pairs, and cytosine and guanine are also complementary base pairs. The base pairs are stabilized by hydrogen bonds: adenine and thymine form two hydrogen bonds, and cytosine and guanine form three hydrogen bonds. The two strands are anti-parallel in nature; that is, the 3′ end of one strand faces the 5′ end of the other strand. The sugar and phosphate of the nucleotides form the backbone of the structure, whereas the nitrogenous bases are stacked inside, like the rungs of a ladder. The twisting of the two strands around each other results in the formation of uniformly spaced major and minor grooves.",True,Nucleotides and basic DNA structure,,,,
405cb74b-2ed3-429a-9423-9437a8b52280,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
405cb74b-2ed3-429a-9423-9437a8b52280,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
405cb74b-2ed3-429a-9423-9437a8b52280,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
405cb74b-2ed3-429a-9423-9437a8b52280,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
b5360b59-b8a2-434f-82e5-6b0671e7202a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,DNA packaging and organization,False,DNA packaging and organization,,,,
1bf2c3c1-b4e9-45d9-a41d-c56bacd8ccb4,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Eukaryotic chromosomes consist of a linear DNA molecule complexed with protein (histones); this complex is called chromatin. Histones are evolutionarily conserved proteins that are rich in basic amino acids and form an octamer composed of two molecules of each of four different histones.,True,DNA packaging and organization,,,,
cde557b8-26ab-43e0-ab5b-935bcdd02d9a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
cde557b8-26ab-43e0-ab5b-935bcdd02d9a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
cde557b8-26ab-43e0-ab5b-935bcdd02d9a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
cde557b8-26ab-43e0-ab5b-935bcdd02d9a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
72738197-56e2-4a37-98c5-30962c2676ff,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"In interphase, eukaryotic chromosomes have two distinct regions that can be distinguished by staining. The tightly packaged region is known as heterochromatin, and the less dense region is known as euchromatin.",True,DNA packaging and organization,,,,
9171b2ea-08b5-4d27-aedb-64a9f91a5a9c,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Heterochromatin usually contains genes that are not expressed and is found in the regions of the centromere and telomeres.,True,DNA packaging and organization,,,,
d63eea7e-edcb-4e55-ab24-a9a677064c4b,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The euchromatin usually contains genes that are transcribed, with DNA packaged around nucleosomes but not further compacted.",True,DNA packaging and organization,,,,
2c4513a4-2a86-4cf9-8931-6cdeb52dbedd,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Histone tails can be modified through both methylation and acetylation, which will alter the histone:DNA interaction. Histone methylation can have variable impacts on a given gene locus leading to a change in transcription. Histone acetylation relaxes the interactions of histones and DNA by removing the positive charge on lysine residues allowing the DNA to be transcriptionally accessible (euchromatin). DNA methylation, specifically to CpG islands, globally represses transcription. These modifications on histones and DNA can result in epigenetic influences that have an impact on many biological processes.",True,DNA packaging and organization,,,,
032ca653-9837-4376-bb42-169f4567c217,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Across the three billion base pair genome, genes are organized into clusters with only a fraction of the DNA coding for translated products. The remaining DNA was historically considered “junk,” however, more recently there is a new appreciation for the roles of noncoding DNA regions. Only half of the genome is unique DNA sequence, and only 1.5 percent codes for mRNA (~20,000 protein-coding genes). The remaining sequence can be categorized as:",True,DNA packaging and organization,,,,
85d55426-c44f-426c-9ed9-bac98d6dd169,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,10.1 References and resources,True,DNA packaging and organization,,,,
e94b1cab-3161-4850-9e0c-731242929910,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 14: DNA Structure and Function.",True,DNA packaging and organization,,,,
32a0fa07-bed4-42f6-94c2-6184c6996692,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 10: The Nature of the Gene and the Genome, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication.",True,DNA packaging and organization,,,,
c88b2c4c-3b5e-4b38-8c5a-67684644b5b9,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 34, 38–40.",True,DNA packaging and organization,,,,
5cd1ab88-84e4-441e-be49-47194df0ea17,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 2: The Introduction to the Human Genome.",True,DNA packaging and organization,,,,
0e6d2db8-e8e9-4477-ac17-b81cca516919,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
0e6d2db8-e8e9-4477-ac17-b81cca516919,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
0e6d2db8-e8e9-4477-ac17-b81cca516919,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
0e6d2db8-e8e9-4477-ac17-b81cca516919,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
124e1da2-fbd1-4155-b75b-06ad6399b7f1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
124e1da2-fbd1-4155-b75b-06ad6399b7f1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
124e1da2-fbd1-4155-b75b-06ad6399b7f1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
124e1da2-fbd1-4155-b75b-06ad6399b7f1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
6d64efe5-48e9-470a-bf42-de7e8903ffae,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
6d64efe5-48e9-470a-bf42-de7e8903ffae,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
6d64efe5-48e9-470a-bf42-de7e8903ffae,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
6d64efe5-48e9-470a-bf42-de7e8903ffae,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
f8622bfc-ebd5-4816-94f5-920340c2cc61,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
f8622bfc-ebd5-4816-94f5-920340c2cc61,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
f8622bfc-ebd5-4816-94f5-920340c2cc61,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
f8622bfc-ebd5-4816-94f5-920340c2cc61,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
720ababc-cfc4-41b0-8650-0e79cccf3fcf,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,10.2 DNA Repair,True,DNA packaging and organization,,,,
3b87f707-c0e5-42f9-94bf-1fd8a4ebebab,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"DNA replication is a highly accurate process, but mistakes can occasionally occur, such as a DNA polymerase (DNA pol) inserting a wrong base. Uncorrected mistakes may sometimes lead to serious consequences, such as cancer. Repair mechanisms correct the mistakes. In rare cases, mistakes are not corrected, leading to mutations; in other cases, repair enzymes are themselves mutated or defective.",True,DNA packaging and organization,,,,
77129dfc-e395-4ef2-ae0b-848536a15460,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
77129dfc-e395-4ef2-ae0b-848536a15460,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
77129dfc-e395-4ef2-ae0b-848536a15460,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
77129dfc-e395-4ef2-ae0b-848536a15460,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4b38941b-f244-45cf-adcc-e4588c868ff9,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Mismatch repair,False,Mismatch repair,,,,
054d60a2-fbc6-409b-a40f-109f3eeff57a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
054d60a2-fbc6-409b-a40f-109f3eeff57a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
054d60a2-fbc6-409b-a40f-109f3eeff57a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
054d60a2-fbc6-409b-a40f-109f3eeff57a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
255a66a8-e09c-4440-858e-497d3ace5bab,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,mispaired,False,mispaired,,,,
c3230f23-9f8d-4609-8a1a-32554806627e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"In prokaryotes, the parental strand is determined by the methyl groups on adenine bases, while the newly synthesized strand lacks them. Thus, DNA polymerase is able to remove the wrongly incorporated bases from the newly synthesized, non-methylated strand.",True,mispaired,,,,
618d8182-16b9-404f-94ab-daf24e5087ec,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"In eukaryotes, the mechanism is not very well understood, but it is believed to involve recognition of unsealed nicks in the new strand, as well as a short-term continuing association of some of the replication proteins with the new daughter strand after replication has completed.",True,mispaired,,,,
16957b8a-29ab-46a2-b8e9-5d6d488ecbae,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Errors during DNA replication are not the only reason why mutations arise in DNA. Mutations, variations in the nucleotide sequence of a genome, can also occur because of damage to DNA. Such mutations may be of two types: induced or spontaneous. Induced mutations are those that result from an exposure to chemicals, UV rays, X-rays, or some other environmental agent. Spontaneous mutations occur without any exposure to any environmental agent; they are a result of natural reactions taking place within the body.",True,mispaired,,,,
82355a71-c2af-487a-845b-8ff8a3931e24,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Nucleotide excision repair (NER),False,Nucleotide excision repair (NER),,,,
4c748d6b-84ff-48d7-9b25-6ff0511c51c1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4c748d6b-84ff-48d7-9b25-6ff0511c51c1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4c748d6b-84ff-48d7-9b25-6ff0511c51c1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4c748d6b-84ff-48d7-9b25-6ff0511c51c1,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a52185d6-3939-40ad-9a8c-947eaea82106,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"This repair mechanism is often employed when UV exposure causes the formation of pyrimidine dimers (thymine dimers). When exposed to UV light, thymines lying next to each other can form thymine dimers. In normal cells, they are excised and replaced. Xeroderma pigmentosa is a condition in which thymine dimerization from exposure to UV light is not repaired.",True,Nucleotide excision repair (NER),,,,
1df36bc9-5ec2-4ae2-891f-56a293b3511a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Base excision repair (BER),False,Base excision repair (BER),,,,
d30bcc8b-7428-4537-b5e8-c55fabd567c7,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
d30bcc8b-7428-4537-b5e8-c55fabd567c7,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
d30bcc8b-7428-4537-b5e8-c55fabd567c7,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
d30bcc8b-7428-4537-b5e8-c55fabd567c7,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
9ab73015-c288-4d23-8bad-c8d05b47d669,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,BER,False,BER,,,,
d7f8d397-d9f7-4687-9220-73c2369b6ddc,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,NER,False,NER,,,,
fb89c502-f9eb-4159-8342-faa5fa6e4ccd,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Double-stranded break repair,False,Double-stranded break repair,,,,
bb12ea63-1240-4890-87c8-d3a3278c3926,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Double-stranded breaks are caused by ionizing radiation, such as X-rays or radioactive particles. This can be repaired through two processes: nonhomologous end-joining and homologous recombination. The major difference between these two processes is in nonhomologous end-joining there is direct ligation of the two ends without the need for a DNA template. This can result in some DNA being lost in the process. In contrast, homologous recombination requires a DNA template to repair the break. This allows for restoration of the duplex without a loss of nucleotides.",True,Double-stranded break repair,,,,
acf27e34-f0e2-4f70-8d3b-be20a9e5b6c0,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,10.2 References and resources,True,Double-stranded break repair,,,,
9cac2149-f07a-464b-a9f7-216b267aab27,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
9cac2149-f07a-464b-a9f7-216b267aab27,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
9cac2149-f07a-464b-a9f7-216b267aab27,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
9cac2149-f07a-464b-a9f7-216b267aab27,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
f4da37a4-4c97-44db-a83f-0edcbc47613c,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
f4da37a4-4c97-44db-a83f-0edcbc47613c,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
f4da37a4-4c97-44db-a83f-0edcbc47613c,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
f4da37a4-4c97-44db-a83f-0edcbc47613c,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
4a9b3ed2-d06c-49ce-9ff5-0368c2ceeae9,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,10.3 DNA Replication,True,Double-stranded break repair,,,,
6485cc26-11dd-4010-a90b-5df7c1e88ca2,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,The process of DNA replication can be summarized as follows:,False,The process of DNA replication can be summarized as follows:,,,,
3d707f6c-3e66-4c32-b477-822ccdd6f55b,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,DNA replication,False,DNA replication,,,,
129bc654-a75a-40e4-91d7-6ceb1715f4fd,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The essential steps of replication are the same for both prokaryotes and eukaryotes. Before replication can start, the DNA has to be made available as a template. Eukaryotic DNA is bound to basic proteins known as histones to form structures called nucleosomes. Histones must be removed and then replaced during the replication process, which helps account for the lower replication rate in eukaryotes. The chromatin (the complex between DNA and proteins) may undergo some chemical modifications, so that the DNA may be able to slide off the proteins or be accessible to the enzymes of the DNA replication machinery.",True,DNA replication,,,,
8153ead0-7deb-4b39-b314-df923ba30944,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"One of the key players in DNA replication is the enzyme DNA polymerase, also known as DNA pol, which adds nucleotides one-by-one to the growing DNA chain that is complementary to the template strand.",True,DNA replication,,,,
e156cf96-fcf6-422e-99d3-ae01a2b29bab,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"In prokaryotes, three main types of polymerases are known: DNA pol I, DNA pol II, and DNA pol III.",True,DNA replication,,,,
dc4cf395-c134-454e-9820-e18f6322dafa,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"In eukaryotes there are fourteen are known polymerases, of which five are known to have major roles during replication and have been well studied. They are known as pol α, pol β, pol γ, pol δ, and pol ε.",True,DNA replication,,,,
125a4c36-b94f-447e-8e5e-cfb29b273d60,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,How does the replication machinery know where to begin?,False,How does the replication machinery know where to begin?,,,,
fdb9cbff-e827-46dc-b573-33ae4b6f83b9,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"There are specific nucleotide sequences called origins of replication where replication begins. In prokaryotes, there is typically a single origin of replication on its one chromosome, and this is in contrast to eukaryotes that have many origins of replication across the chromosomes.",True,How does the replication machinery know where to begin?,,,,
b9683302-b920-434c-9520-1d46b80ad4c9,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The origin of replication is recognized by certain proteins that bind to this site. An enzyme called helicase unwinds the DNA by breaking the hydrogen bonds between the nitrogenous base pairs. ATP hydrolysis is required for this process. As the DNA opens up, Y-shaped structures called replication forks are formed. Two replication forks are formed at the origin of replication, and these get extended bidirectionally as replication continues. Single-strand binding proteins coat the single strands of DNA near the replication fork to prevent the single-stranded DNA from winding back into a double helix.",True,How does the replication machinery know where to begin?,,,,
b347f9c6-1976-4720-9a0e-81dedf382f28,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"DNA polymerase has two important restrictions. First, it is able to add nucleotides only in the 5′ to 3′ direction (a new DNA strand can be only extended in this direction). Second, it also requires a free 3′-OH group to which it can add nucleotides by forming a phosphodiester bond between the 3′-OH end and the 5′ phosphate of the next nucleotide. This essentially means that it cannot add nucleotides if a free 3′-OH group is not available.",True,How does the replication machinery know where to begin?,,,,
42ea6481-6ade-4346-ac54-76f3ce6d80a5,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Then how does it add the first nucleotide? The problem is solved with the help of a primer that provides the free 3′-OH end. RNA primase synthesizes an RNA segment that is about five to ten nucleotides long and complementary to the template DNA. Because this sequence primes the DNA synthesis, it is appropriately called the primer. DNA polymerase can now extend this RNA primer, adding nucleotides one-by-one that are complementary to the template strand.",True,How does the replication machinery know where to begin?,,,,
a335b0f9-1f99-4ea6-96a9-2f59feceea24,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The DNA tends to become more highly coiled ahead of the replication fork. Topoisomerase breaks and reforms DNAʼs phosphate backbone ahead of the replication fork, thereby relieving the pressure that results from this “supercoiling.” Single-strand binding proteins bind to the single-stranded DNA to prevent the helix from re-forming.",True,How does the replication machinery know where to begin?,,,,
7b400538-8966-4c98-b200-f4ebc3fb6ad8,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Because DNA polymerase can only extend in the 5′ to 3′ direction, and because the DNA double helix is antiparallel, there is a problem at the replication fork. The two template DNA strands have opposing orientations: one strand is in the 5′ to 3′ direction, and the other is oriented in the 3′ to 5′ direction. Only one new DNA strand, the one that is complementary to the 3′ to 5′ parental DNA strand, can be synthesized continuously toward the replication fork. This continuously synthesized strand is known as the leading strand. The other strand, complementary to the 5′ to 3′ parental DNA, is extended away from the replication fork in small fragments known as Okazaki fragments, each requiring a primer to start the synthesis. New primer segments are laid down in the direction of the replication fork, but each pointing away from it.",True,How does the replication machinery know where to begin?,,,,
2b80081d-bfbd-4386-b160-3d1d7f5855ca,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The overall direction of the lagging strand will be 3′ to 5′, and that of the leading strand 5′ to 3′. A protein called the sliding clamp holds the DNA polymerase in place as it continues to add nucleotides. The sliding clamp is a ring-shaped protein that binds to the DNA and holds the polymerase in place. As synthesis continues, the RNA primers are removed by the exonuclease activity of DNA pol I, which uses DNA behind the RNA as its own primer and fills in the gaps left by removal of the RNA nucleotides by the addition of DNA nucleotides. The nicks that remain between the newly synthesized DNA (that replaced the RNA primer) and the previously synthesized DNA are sealed by the enzyme DNA ligase, which catalyzes the formation of phosphodiester linkages between the 3′-OH end of one nucleotide and the 5′ phosphate end of the other fragment.",True,How does the replication machinery know where to begin?,,,,
46640836-8f78-4604-884c-8f56bd91de2b,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Once the chromosome has been completely replicated, the two DNA copies move into two different cells during cell division.",True,How does the replication machinery know where to begin?,,,,
50378ed2-e483-4fe2-922d-eacd99cc186d,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Telomere replication,False,Telomere replication,,,,
b836338a-30b9-467d-b839-6febbd9b8b38,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"In eukaryotes, leading strand synthesis continues until the end of the chromosome is reached. On the lagging strand, DNA is synthesized in short stretches, each of which is initiated by a separate primer. When the replication fork reaches the end of the linear chromosome, there is no way to replace the primer on the 5ʼ end of the lagging strand.",True,Telomere replication,,,,
1ecb96a2-a064-417a-907b-3b398a45a465,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"The DNA at the ends of the chromosome thus remains unpaired, and over time these ends, called telomeres, may get progressively shorter as cells continue to divide.",True,Telomere replication,,,,
0c4d05cf-3151-4d2b-a1ea-cdaa10e72b2e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
0c4d05cf-3151-4d2b-a1ea-cdaa10e72b2e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
0c4d05cf-3151-4d2b-a1ea-cdaa10e72b2e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
0c4d05cf-3151-4d2b-a1ea-cdaa10e72b2e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
18bfb410-5b44-49a3-8858-d9809a310f4f,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Table 10.1: Prokaryotic DNA replication: enzymes and their function.,True,Telomere replication,,,,
421c5f70-1cd3-4aa0-83f5-91a8ea5c419d,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Table 10.2: Difference between prokaryotic and eukaryotic replication.,True,Telomere replication,,,,
65bcb211-b8e5-49d4-a875-0ba5420fb5f3,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,10.3 References and resources,True,Telomere replication,,,,
14971eef-965f-4467-baa3-514734c937f7,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,Text,False,Text,,,,
febff3fd-d7b7-4d11-9dc8-eacf1663e73e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
febff3fd-d7b7-4d11-9dc8-eacf1663e73e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
febff3fd-d7b7-4d11-9dc8-eacf1663e73e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
febff3fd-d7b7-4d11-9dc8-eacf1663e73e,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
837e5974-b4e9-4b04-b3ef-a7bbdd7aee6a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
837e5974-b4e9-4b04-b3ef-a7bbdd7aee6a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
837e5974-b4e9-4b04-b3ef-a7bbdd7aee6a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
837e5974-b4e9-4b04-b3ef-a7bbdd7aee6a,https://pressbooks.lib.vt.edu/cellbio/,10.3 DNA Replication,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-3,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
051187df-9b4f-468c-8025-6bb79a95256b,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Nucleotides and basic DNA structure,False,Nucleotides and basic DNA structure,,,,
fa3d89cd-a784-46ca-9fb4-34b05a733352,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The nucleotides combine with each other to produce phosphodiester bonds. The phosphate residue attached to the 5′ carbon of the sugar of one nucleotide forms a second ester linkage with the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, thereby forming a 5′-3′ phosphodiester bond. In a polynucleotide, one end of the chain has a free 5′ phosphate, and the other end has a free 3′-OH. These are called the 5′ and 3′ ends of the chain.",True,Nucleotides and basic DNA structure,,,,
4c7b4343-525c-4569-91bb-4ad46fa1a51b,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Base-pairing takes place between a purine and pyrimidine on opposite strands, so that adenine and thymine are complementary base pairs, and cytosine and guanine are also complementary base pairs. The base pairs are stabilized by hydrogen bonds: adenine and thymine form two hydrogen bonds, and cytosine and guanine form three hydrogen bonds. The two strands are anti-parallel in nature; that is, the 3′ end of one strand faces the 5′ end of the other strand. The sugar and phosphate of the nucleotides form the backbone of the structure, whereas the nitrogenous bases are stacked inside, like the rungs of a ladder. The twisting of the two strands around each other results in the formation of uniformly spaced major and minor grooves.",True,Nucleotides and basic DNA structure,,,,
583ca155-997f-4e0a-9115-4145849d0222,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
583ca155-997f-4e0a-9115-4145849d0222,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
583ca155-997f-4e0a-9115-4145849d0222,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
583ca155-997f-4e0a-9115-4145849d0222,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
55e1bffd-8b61-4d6a-9912-2774c5722571,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,DNA packaging and organization,False,DNA packaging and organization,,,,
c45b6f9e-b717-4955-9c8f-e4914377c91c,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Eukaryotic chromosomes consist of a linear DNA molecule complexed with protein (histones); this complex is called chromatin. Histones are evolutionarily conserved proteins that are rich in basic amino acids and form an octamer composed of two molecules of each of four different histones.,True,DNA packaging and organization,,,,
ae0ed45c-150c-4506-aebd-e20fdfae20fb,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
ae0ed45c-150c-4506-aebd-e20fdfae20fb,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
ae0ed45c-150c-4506-aebd-e20fdfae20fb,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
ae0ed45c-150c-4506-aebd-e20fdfae20fb,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
6aa2675c-021d-4e10-b1b4-c8ce454ed39b,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"In interphase, eukaryotic chromosomes have two distinct regions that can be distinguished by staining. The tightly packaged region is known as heterochromatin, and the less dense region is known as euchromatin.",True,DNA packaging and organization,,,,
3684fdb2-b558-4eaa-81cb-b6f749c1b2ff,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Heterochromatin usually contains genes that are not expressed and is found in the regions of the centromere and telomeres.,True,DNA packaging and organization,,,,
9fb71f6e-4063-44b6-b44e-54baf3003729,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The euchromatin usually contains genes that are transcribed, with DNA packaged around nucleosomes but not further compacted.",True,DNA packaging and organization,,,,
815388fb-bc87-4e53-90af-879ba8a3d5f5,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Histone tails can be modified through both methylation and acetylation, which will alter the histone:DNA interaction. Histone methylation can have variable impacts on a given gene locus leading to a change in transcription. Histone acetylation relaxes the interactions of histones and DNA by removing the positive charge on lysine residues allowing the DNA to be transcriptionally accessible (euchromatin). DNA methylation, specifically to CpG islands, globally represses transcription. These modifications on histones and DNA can result in epigenetic influences that have an impact on many biological processes.",True,DNA packaging and organization,,,,
a89cd586-70e3-4e2d-a403-f826eb8112a4,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Across the three billion base pair genome, genes are organized into clusters with only a fraction of the DNA coding for translated products. The remaining DNA was historically considered “junk,” however, more recently there is a new appreciation for the roles of noncoding DNA regions. Only half of the genome is unique DNA sequence, and only 1.5 percent codes for mRNA (~20,000 protein-coding genes). The remaining sequence can be categorized as:",True,DNA packaging and organization,,,,
6f2917d2-a0b2-4748-b2f4-4f21af46e26d,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,10.1 References and resources,True,DNA packaging and organization,,,,
ba4be7ff-fedc-49bc-97d7-8508a483d9c7,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 14: DNA Structure and Function.",True,DNA packaging and organization,,,,
7e3b57b0-9992-4df7-81d6-5c8bbb2f509e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 10: The Nature of the Gene and the Genome, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication.",True,DNA packaging and organization,,,,
41f2b3e5-51ad-44f5-8853-75bdd417bea2,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 34, 38–40.",True,DNA packaging and organization,,,,
bc97731d-e8c2-44d3-9b8c-8678a1dfe0bc,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 2: The Introduction to the Human Genome.",True,DNA packaging and organization,,,,
ba0665ab-4958-43a8-be37-8cfb9aec2330,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
ba0665ab-4958-43a8-be37-8cfb9aec2330,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
ba0665ab-4958-43a8-be37-8cfb9aec2330,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
ba0665ab-4958-43a8-be37-8cfb9aec2330,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
e928a532-e9a4-473b-a98d-c42fd24be707,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
e928a532-e9a4-473b-a98d-c42fd24be707,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
e928a532-e9a4-473b-a98d-c42fd24be707,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
e928a532-e9a4-473b-a98d-c42fd24be707,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
3f6a0375-cbe2-4977-9ba8-65886658e4ab,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
3f6a0375-cbe2-4977-9ba8-65886658e4ab,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
3f6a0375-cbe2-4977-9ba8-65886658e4ab,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
3f6a0375-cbe2-4977-9ba8-65886658e4ab,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
dfe77b32-83c8-4cde-985a-aab88d857ffc,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
dfe77b32-83c8-4cde-985a-aab88d857ffc,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
dfe77b32-83c8-4cde-985a-aab88d857ffc,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
dfe77b32-83c8-4cde-985a-aab88d857ffc,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
14c910bb-47fa-4b0e-a7a3-ceae3687e97d,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,10.2 DNA Repair,True,DNA packaging and organization,,,,
744bfdb3-dbf2-4081-9a84-e30e68244983,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"DNA replication is a highly accurate process, but mistakes can occasionally occur, such as a DNA polymerase (DNA pol) inserting a wrong base. Uncorrected mistakes may sometimes lead to serious consequences, such as cancer. Repair mechanisms correct the mistakes. In rare cases, mistakes are not corrected, leading to mutations; in other cases, repair enzymes are themselves mutated or defective.",True,DNA packaging and organization,,,,
a6d94d3a-ab03-4fd7-a462-aa54d7c9074d,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a6d94d3a-ab03-4fd7-a462-aa54d7c9074d,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a6d94d3a-ab03-4fd7-a462-aa54d7c9074d,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a6d94d3a-ab03-4fd7-a462-aa54d7c9074d,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
11822858-c83c-44c1-91e7-b9dc765d4ffb,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Mismatch repair,False,Mismatch repair,,,,
79a01638-5258-405d-97a6-cf458b0ac151,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
79a01638-5258-405d-97a6-cf458b0ac151,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
79a01638-5258-405d-97a6-cf458b0ac151,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
79a01638-5258-405d-97a6-cf458b0ac151,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
e7dc1393-30cd-4c6e-8c06-3ce50d02303a,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,mispaired,False,mispaired,,,,
ebd7ccee-f9bf-49d2-8869-fbfcd550d884,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"In prokaryotes, the parental strand is determined by the methyl groups on adenine bases, while the newly synthesized strand lacks them. Thus, DNA polymerase is able to remove the wrongly incorporated bases from the newly synthesized, non-methylated strand.",True,mispaired,,,,
b5f1e49c-111b-4313-ac29-81afe325428b,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"In eukaryotes, the mechanism is not very well understood, but it is believed to involve recognition of unsealed nicks in the new strand, as well as a short-term continuing association of some of the replication proteins with the new daughter strand after replication has completed.",True,mispaired,,,,
ad37d39e-f88f-44a3-b72d-fdf29d0981db,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Errors during DNA replication are not the only reason why mutations arise in DNA. Mutations, variations in the nucleotide sequence of a genome, can also occur because of damage to DNA. Such mutations may be of two types: induced or spontaneous. Induced mutations are those that result from an exposure to chemicals, UV rays, X-rays, or some other environmental agent. Spontaneous mutations occur without any exposure to any environmental agent; they are a result of natural reactions taking place within the body.",True,mispaired,,,,
cbca19f4-eeb2-4855-9fa0-79c4641eadad,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Nucleotide excision repair (NER),False,Nucleotide excision repair (NER),,,,
c8f09291-f89b-44d0-9d3e-ce8b670432d4,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
c8f09291-f89b-44d0-9d3e-ce8b670432d4,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
c8f09291-f89b-44d0-9d3e-ce8b670432d4,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
c8f09291-f89b-44d0-9d3e-ce8b670432d4,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
256bbf6a-3074-47fe-9ceb-a41ea171b31e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"This repair mechanism is often employed when UV exposure causes the formation of pyrimidine dimers (thymine dimers). When exposed to UV light, thymines lying next to each other can form thymine dimers. In normal cells, they are excised and replaced. Xeroderma pigmentosa is a condition in which thymine dimerization from exposure to UV light is not repaired.",True,Nucleotide excision repair (NER),,,,
a0be640a-d1a6-484d-b5fc-5043c14eb030,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Base excision repair (BER),False,Base excision repair (BER),,,,
32573fa1-684c-4a4c-bbbb-896a7b52af9e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
32573fa1-684c-4a4c-bbbb-896a7b52af9e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
32573fa1-684c-4a4c-bbbb-896a7b52af9e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
32573fa1-684c-4a4c-bbbb-896a7b52af9e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
2a2ec106-d01c-4524-af3b-2a3b2dd0500e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,BER,False,BER,,,,
8f5e596b-d5c5-4d48-a3e6-edcc227805d8,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,NER,False,NER,,,,
c88ffffc-2f3b-4cc8-94c1-a83cb179db81,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Double-stranded break repair,False,Double-stranded break repair,,,,
fdb3b06f-139c-4f35-8e9b-9af4651fa0c2,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Double-stranded breaks are caused by ionizing radiation, such as X-rays or radioactive particles. This can be repaired through two processes: nonhomologous end-joining and homologous recombination. The major difference between these two processes is in nonhomologous end-joining there is direct ligation of the two ends without the need for a DNA template. This can result in some DNA being lost in the process. In contrast, homologous recombination requires a DNA template to repair the break. This allows for restoration of the duplex without a loss of nucleotides.",True,Double-stranded break repair,,,,
e946d12a-5358-426d-bfd1-f22c643471e5,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,10.2 References and resources,True,Double-stranded break repair,,,,
4c3a60a1-c105-47a2-b678-54a97f0d5e71,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4c3a60a1-c105-47a2-b678-54a97f0d5e71,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4c3a60a1-c105-47a2-b678-54a97f0d5e71,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4c3a60a1-c105-47a2-b678-54a97f0d5e71,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a1956520-989e-4bb9-9706-29acbc85e137,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
a1956520-989e-4bb9-9706-29acbc85e137,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
a1956520-989e-4bb9-9706-29acbc85e137,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
a1956520-989e-4bb9-9706-29acbc85e137,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
0a94cdd7-970c-4ad3-98ae-c33bcb67f155,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,10.3 DNA Replication,True,Double-stranded break repair,,,,
fb7a5186-9049-44c1-8711-42a09468aebc,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,The process of DNA replication can be summarized as follows:,False,The process of DNA replication can be summarized as follows:,,,,
4ba94f3c-c79e-4408-aa26-6da637d2149e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,DNA replication,False,DNA replication,,,,
7f528342-06a5-4d46-93b5-618d3fdae85a,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The essential steps of replication are the same for both prokaryotes and eukaryotes. Before replication can start, the DNA has to be made available as a template. Eukaryotic DNA is bound to basic proteins known as histones to form structures called nucleosomes. Histones must be removed and then replaced during the replication process, which helps account for the lower replication rate in eukaryotes. The chromatin (the complex between DNA and proteins) may undergo some chemical modifications, so that the DNA may be able to slide off the proteins or be accessible to the enzymes of the DNA replication machinery.",True,DNA replication,,,,
dd0e2386-51fb-44cb-8b0b-f0f1486d842a,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"One of the key players in DNA replication is the enzyme DNA polymerase, also known as DNA pol, which adds nucleotides one-by-one to the growing DNA chain that is complementary to the template strand.",True,DNA replication,,,,
f1d0e159-2514-47e1-8cbf-e28559ed42ef,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"In prokaryotes, three main types of polymerases are known: DNA pol I, DNA pol II, and DNA pol III.",True,DNA replication,,,,
badba314-d48e-4ebd-ba0d-1afeca9d328c,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"In eukaryotes there are fourteen are known polymerases, of which five are known to have major roles during replication and have been well studied. They are known as pol α, pol β, pol γ, pol δ, and pol ε.",True,DNA replication,,,,
ce5de9cb-362e-480a-8656-92f8f194c1ce,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,How does the replication machinery know where to begin?,False,How does the replication machinery know where to begin?,,,,
be555a26-50cf-43be-b9c4-c3b77baf8b26,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"There are specific nucleotide sequences called origins of replication where replication begins. In prokaryotes, there is typically a single origin of replication on its one chromosome, and this is in contrast to eukaryotes that have many origins of replication across the chromosomes.",True,How does the replication machinery know where to begin?,,,,
ab3bf50c-5d75-4b40-80a4-e78b9f06c21b,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The origin of replication is recognized by certain proteins that bind to this site. An enzyme called helicase unwinds the DNA by breaking the hydrogen bonds between the nitrogenous base pairs. ATP hydrolysis is required for this process. As the DNA opens up, Y-shaped structures called replication forks are formed. Two replication forks are formed at the origin of replication, and these get extended bidirectionally as replication continues. Single-strand binding proteins coat the single strands of DNA near the replication fork to prevent the single-stranded DNA from winding back into a double helix.",True,How does the replication machinery know where to begin?,,,,
cec4cec1-f8e3-4d86-a6fb-1778e0a4c563,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"DNA polymerase has two important restrictions. First, it is able to add nucleotides only in the 5′ to 3′ direction (a new DNA strand can be only extended in this direction). Second, it also requires a free 3′-OH group to which it can add nucleotides by forming a phosphodiester bond between the 3′-OH end and the 5′ phosphate of the next nucleotide. This essentially means that it cannot add nucleotides if a free 3′-OH group is not available.",True,How does the replication machinery know where to begin?,,,,
123c44d7-6dfa-4dfb-8fcf-5e8a584b4d3e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Then how does it add the first nucleotide? The problem is solved with the help of a primer that provides the free 3′-OH end. RNA primase synthesizes an RNA segment that is about five to ten nucleotides long and complementary to the template DNA. Because this sequence primes the DNA synthesis, it is appropriately called the primer. DNA polymerase can now extend this RNA primer, adding nucleotides one-by-one that are complementary to the template strand.",True,How does the replication machinery know where to begin?,,,,
0f9e0564-2ff1-4652-aaad-397a2fba7aea,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The DNA tends to become more highly coiled ahead of the replication fork. Topoisomerase breaks and reforms DNAʼs phosphate backbone ahead of the replication fork, thereby relieving the pressure that results from this “supercoiling.” Single-strand binding proteins bind to the single-stranded DNA to prevent the helix from re-forming.",True,How does the replication machinery know where to begin?,,,,
b1ba4cef-8111-47fe-87f6-843ec3238ad0,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Because DNA polymerase can only extend in the 5′ to 3′ direction, and because the DNA double helix is antiparallel, there is a problem at the replication fork. The two template DNA strands have opposing orientations: one strand is in the 5′ to 3′ direction, and the other is oriented in the 3′ to 5′ direction. Only one new DNA strand, the one that is complementary to the 3′ to 5′ parental DNA strand, can be synthesized continuously toward the replication fork. This continuously synthesized strand is known as the leading strand. The other strand, complementary to the 5′ to 3′ parental DNA, is extended away from the replication fork in small fragments known as Okazaki fragments, each requiring a primer to start the synthesis. New primer segments are laid down in the direction of the replication fork, but each pointing away from it.",True,How does the replication machinery know where to begin?,,,,
7850c433-23cf-4fb1-b84b-f8a8edb6c55e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The overall direction of the lagging strand will be 3′ to 5′, and that of the leading strand 5′ to 3′. A protein called the sliding clamp holds the DNA polymerase in place as it continues to add nucleotides. The sliding clamp is a ring-shaped protein that binds to the DNA and holds the polymerase in place. As synthesis continues, the RNA primers are removed by the exonuclease activity of DNA pol I, which uses DNA behind the RNA as its own primer and fills in the gaps left by removal of the RNA nucleotides by the addition of DNA nucleotides. The nicks that remain between the newly synthesized DNA (that replaced the RNA primer) and the previously synthesized DNA are sealed by the enzyme DNA ligase, which catalyzes the formation of phosphodiester linkages between the 3′-OH end of one nucleotide and the 5′ phosphate end of the other fragment.",True,How does the replication machinery know where to begin?,,,,
9f96c1f4-8e39-4df2-9684-c41455eb5489,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Once the chromosome has been completely replicated, the two DNA copies move into two different cells during cell division.",True,How does the replication machinery know where to begin?,,,,
359d5552-9adc-498f-9819-a368a77436e4,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Telomere replication,False,Telomere replication,,,,
4617dad9-4331-433e-b982-fe7edbadee9e,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"In eukaryotes, leading strand synthesis continues until the end of the chromosome is reached. On the lagging strand, DNA is synthesized in short stretches, each of which is initiated by a separate primer. When the replication fork reaches the end of the linear chromosome, there is no way to replace the primer on the 5ʼ end of the lagging strand.",True,Telomere replication,,,,
35cf4b13-4792-4955-b71d-bb447f639bde,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"The DNA at the ends of the chromosome thus remains unpaired, and over time these ends, called telomeres, may get progressively shorter as cells continue to divide.",True,Telomere replication,,,,
c387fdb0-af90-402d-b075-5756fd3cfff3,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
c387fdb0-af90-402d-b075-5756fd3cfff3,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
c387fdb0-af90-402d-b075-5756fd3cfff3,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
c387fdb0-af90-402d-b075-5756fd3cfff3,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
65894511-3910-4b07-a41a-fd8078604b16,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Table 10.1: Prokaryotic DNA replication: enzymes and their function.,True,Telomere replication,,,,
2bc8d558-f94f-47b0-a802-138229e02655,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Table 10.2: Difference between prokaryotic and eukaryotic replication.,True,Telomere replication,,,,
6c25e43c-bc53-4b90-8107-d08f2090aecb,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,10.3 References and resources,True,Telomere replication,,,,
b6860fc2-b5a7-48bd-b5f3-1978d564a251,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,Text,False,Text,,,,
076634cf-6eb4-4c66-874a-0a8551c539f2,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
076634cf-6eb4-4c66-874a-0a8551c539f2,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
076634cf-6eb4-4c66-874a-0a8551c539f2,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
076634cf-6eb4-4c66-874a-0a8551c539f2,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
ce2a3b25-8994-4095-bfb1-959ae9a77806,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
ce2a3b25-8994-4095-bfb1-959ae9a77806,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
ce2a3b25-8994-4095-bfb1-959ae9a77806,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
ce2a3b25-8994-4095-bfb1-959ae9a77806,https://pressbooks.lib.vt.edu/cellbio/,10.2 DNA Repair,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-2,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
e90f02b3-a5f0-4924-8c5a-b031399b824b,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Nucleotides and basic DNA structure,False,Nucleotides and basic DNA structure,,,,
4fc3d3a2-c40a-4fdf-be51-2d46f924c90b,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The nucleotides combine with each other to produce phosphodiester bonds. The phosphate residue attached to the 5′ carbon of the sugar of one nucleotide forms a second ester linkage with the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, thereby forming a 5′-3′ phosphodiester bond. In a polynucleotide, one end of the chain has a free 5′ phosphate, and the other end has a free 3′-OH. These are called the 5′ and 3′ ends of the chain.",True,Nucleotides and basic DNA structure,,,,
8464d885-4fae-4475-bc03-ab20e4b64cd5,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Base-pairing takes place between a purine and pyrimidine on opposite strands, so that adenine and thymine are complementary base pairs, and cytosine and guanine are also complementary base pairs. The base pairs are stabilized by hydrogen bonds: adenine and thymine form two hydrogen bonds, and cytosine and guanine form three hydrogen bonds. The two strands are anti-parallel in nature; that is, the 3′ end of one strand faces the 5′ end of the other strand. The sugar and phosphate of the nucleotides form the backbone of the structure, whereas the nitrogenous bases are stacked inside, like the rungs of a ladder. The twisting of the two strands around each other results in the formation of uniformly spaced major and minor grooves.",True,Nucleotides and basic DNA structure,,,,
7e7a86f1-4e9e-4f5e-95cf-d2e3202aeca7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
7e7a86f1-4e9e-4f5e-95cf-d2e3202aeca7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
7e7a86f1-4e9e-4f5e-95cf-d2e3202aeca7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
7e7a86f1-4e9e-4f5e-95cf-d2e3202aeca7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
c336ad0b-1ffd-4df3-b163-90a9bd402b90,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,DNA packaging and organization,False,DNA packaging and organization,,,,
43dc0429-20f8-46a0-adca-0c4bcf8c18db,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Eukaryotic chromosomes consist of a linear DNA molecule complexed with protein (histones); this complex is called chromatin. Histones are evolutionarily conserved proteins that are rich in basic amino acids and form an octamer composed of two molecules of each of four different histones.,True,DNA packaging and organization,,,,
ca973dd5-7ac4-4073-898a-2d951f9beb25,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
ca973dd5-7ac4-4073-898a-2d951f9beb25,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
ca973dd5-7ac4-4073-898a-2d951f9beb25,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
ca973dd5-7ac4-4073-898a-2d951f9beb25,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
64fa50fa-8f1e-4b30-9938-362132e5432c,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"In interphase, eukaryotic chromosomes have two distinct regions that can be distinguished by staining. The tightly packaged region is known as heterochromatin, and the less dense region is known as euchromatin.",True,DNA packaging and organization,,,,
c4d1c3eb-cea7-45a2-9b3b-5b4c2083fc8a,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Heterochromatin usually contains genes that are not expressed and is found in the regions of the centromere and telomeres.,True,DNA packaging and organization,,,,
3e2af0aa-75c2-46ca-af28-bfb4608fe3b1,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The euchromatin usually contains genes that are transcribed, with DNA packaged around nucleosomes but not further compacted.",True,DNA packaging and organization,,,,
4aec9e91-4337-4f48-a19c-71e2bf538adf,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Histone tails can be modified through both methylation and acetylation, which will alter the histone:DNA interaction. Histone methylation can have variable impacts on a given gene locus leading to a change in transcription. Histone acetylation relaxes the interactions of histones and DNA by removing the positive charge on lysine residues allowing the DNA to be transcriptionally accessible (euchromatin). DNA methylation, specifically to CpG islands, globally represses transcription. These modifications on histones and DNA can result in epigenetic influences that have an impact on many biological processes.",True,DNA packaging and organization,,,,
b7529a33-fb52-4b65-ad82-2dcdeeed8d97,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Across the three billion base pair genome, genes are organized into clusters with only a fraction of the DNA coding for translated products. The remaining DNA was historically considered “junk,” however, more recently there is a new appreciation for the roles of noncoding DNA regions. Only half of the genome is unique DNA sequence, and only 1.5 percent codes for mRNA (~20,000 protein-coding genes). The remaining sequence can be categorized as:",True,DNA packaging and organization,,,,
8e20e616-3b54-4df0-936e-e697a4a72866,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,10.1 References and resources,True,DNA packaging and organization,,,,
6ceee620-3607-4572-bf08-9815e19b4c48,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 14: DNA Structure and Function.",True,DNA packaging and organization,,,,
2d3a05fb-0912-4ad3-be40-23f59835707b,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 10: The Nature of the Gene and the Genome, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication.",True,DNA packaging and organization,,,,
50eede7a-0f29-4994-9020-1f7eeb71ce2e,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 34, 38–40.",True,DNA packaging and organization,,,,
c0f76774-d217-4c13-8a17-59829257b456,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 2: The Introduction to the Human Genome.",True,DNA packaging and organization,,,,
54477034-8aaa-4663-bb2e-07c9f71d8ed0,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
54477034-8aaa-4663-bb2e-07c9f71d8ed0,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
54477034-8aaa-4663-bb2e-07c9f71d8ed0,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
54477034-8aaa-4663-bb2e-07c9f71d8ed0,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
b0d29305-8e1a-4abd-a13f-c1becefe5f39,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
b0d29305-8e1a-4abd-a13f-c1becefe5f39,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
b0d29305-8e1a-4abd-a13f-c1becefe5f39,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
b0d29305-8e1a-4abd-a13f-c1becefe5f39,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
00a7066e-8bca-468e-bd0a-24d9732bf814,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
00a7066e-8bca-468e-bd0a-24d9732bf814,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
00a7066e-8bca-468e-bd0a-24d9732bf814,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
00a7066e-8bca-468e-bd0a-24d9732bf814,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
e012f133-317a-4371-a59b-75c68a9756f4,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
e012f133-317a-4371-a59b-75c68a9756f4,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
e012f133-317a-4371-a59b-75c68a9756f4,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
e012f133-317a-4371-a59b-75c68a9756f4,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
43645df7-1e3f-410b-9987-b50d28534f81,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,10.2 DNA Repair,True,DNA packaging and organization,,,,
a04a7f01-2f9a-4f6c-8e69-67d409c5b650,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"DNA replication is a highly accurate process, but mistakes can occasionally occur, such as a DNA polymerase (DNA pol) inserting a wrong base. Uncorrected mistakes may sometimes lead to serious consequences, such as cancer. Repair mechanisms correct the mistakes. In rare cases, mistakes are not corrected, leading to mutations; in other cases, repair enzymes are themselves mutated or defective.",True,DNA packaging and organization,,,,
24e36e30-b54a-45bb-9499-c06c53b8167e,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
24e36e30-b54a-45bb-9499-c06c53b8167e,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
24e36e30-b54a-45bb-9499-c06c53b8167e,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
24e36e30-b54a-45bb-9499-c06c53b8167e,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
487f1cfa-f305-43eb-8603-02e6fcb8fad1,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Mismatch repair,False,Mismatch repair,,,,
e4749deb-eb44-498b-8beb-cb117c1429d7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
e4749deb-eb44-498b-8beb-cb117c1429d7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
e4749deb-eb44-498b-8beb-cb117c1429d7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
e4749deb-eb44-498b-8beb-cb117c1429d7,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
663c7f69-be0d-4afd-a812-58d388192c08,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,mispaired,False,mispaired,,,,
24a94ed1-d25a-493d-ad67-3d904197eb29,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"In prokaryotes, the parental strand is determined by the methyl groups on adenine bases, while the newly synthesized strand lacks them. Thus, DNA polymerase is able to remove the wrongly incorporated bases from the newly synthesized, non-methylated strand.",True,mispaired,,,,
e83de8ee-3afa-4e39-a0b3-21f367db9e16,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"In eukaryotes, the mechanism is not very well understood, but it is believed to involve recognition of unsealed nicks in the new strand, as well as a short-term continuing association of some of the replication proteins with the new daughter strand after replication has completed.",True,mispaired,,,,
5339f118-21da-4b42-8161-6376cfda4de8,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Errors during DNA replication are not the only reason why mutations arise in DNA. Mutations, variations in the nucleotide sequence of a genome, can also occur because of damage to DNA. Such mutations may be of two types: induced or spontaneous. Induced mutations are those that result from an exposure to chemicals, UV rays, X-rays, or some other environmental agent. Spontaneous mutations occur without any exposure to any environmental agent; they are a result of natural reactions taking place within the body.",True,mispaired,,,,
ce861fdf-ed53-4c42-add2-c72056b860c5,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Nucleotide excision repair (NER),False,Nucleotide excision repair (NER),,,,
0c75deb5-1245-4821-82ce-2f39f050d22d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
0c75deb5-1245-4821-82ce-2f39f050d22d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
0c75deb5-1245-4821-82ce-2f39f050d22d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
0c75deb5-1245-4821-82ce-2f39f050d22d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4031e78b-f82d-4dcf-a53c-66468f554472,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"This repair mechanism is often employed when UV exposure causes the formation of pyrimidine dimers (thymine dimers). When exposed to UV light, thymines lying next to each other can form thymine dimers. In normal cells, they are excised and replaced. Xeroderma pigmentosa is a condition in which thymine dimerization from exposure to UV light is not repaired.",True,Nucleotide excision repair (NER),,,,
21d70f68-566a-4260-a1c9-1215028b4610,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Base excision repair (BER),False,Base excision repair (BER),,,,
b85eb1d7-f982-40a0-98f3-0210740d6961,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
b85eb1d7-f982-40a0-98f3-0210740d6961,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
b85eb1d7-f982-40a0-98f3-0210740d6961,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
b85eb1d7-f982-40a0-98f3-0210740d6961,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
7711f300-6202-4c54-b6f4-04df64cdedb2,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,BER,False,BER,,,,
e2b5e7cf-1728-4cfd-9b8e-40d8ea404995,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,NER,False,NER,,,,
dce49ab3-816b-4cc1-8e03-c006bde5f758,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Double-stranded break repair,False,Double-stranded break repair,,,,
06d07e79-5606-4301-a815-b6bafa5eb3fd,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Double-stranded breaks are caused by ionizing radiation, such as X-rays or radioactive particles. This can be repaired through two processes: nonhomologous end-joining and homologous recombination. The major difference between these two processes is in nonhomologous end-joining there is direct ligation of the two ends without the need for a DNA template. This can result in some DNA being lost in the process. In contrast, homologous recombination requires a DNA template to repair the break. This allows for restoration of the duplex without a loss of nucleotides.",True,Double-stranded break repair,,,,
b5d500ef-2ee6-45f3-b4a0-b97669949d59,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,10.2 References and resources,True,Double-stranded break repair,,,,
c865db5e-d49d-4997-9648-96bad1168d26,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
c865db5e-d49d-4997-9648-96bad1168d26,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
c865db5e-d49d-4997-9648-96bad1168d26,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
c865db5e-d49d-4997-9648-96bad1168d26,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
f528f99b-579e-4648-aacc-65bec71c474d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
f528f99b-579e-4648-aacc-65bec71c474d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
f528f99b-579e-4648-aacc-65bec71c474d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
f528f99b-579e-4648-aacc-65bec71c474d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
82e3729e-505f-484b-83c1-69b5b333cf5e,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,10.3 DNA Replication,True,Double-stranded break repair,,,,
e3e9df59-b76e-479f-b5ba-7c03dee9fc8a,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,The process of DNA replication can be summarized as follows:,False,The process of DNA replication can be summarized as follows:,,,,
b3886724-4429-4651-9dc6-f755eb701f79,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,DNA replication,False,DNA replication,,,,
3ab67972-e9e3-48ac-aa90-a6fe0d248da3,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The essential steps of replication are the same for both prokaryotes and eukaryotes. Before replication can start, the DNA has to be made available as a template. Eukaryotic DNA is bound to basic proteins known as histones to form structures called nucleosomes. Histones must be removed and then replaced during the replication process, which helps account for the lower replication rate in eukaryotes. The chromatin (the complex between DNA and proteins) may undergo some chemical modifications, so that the DNA may be able to slide off the proteins or be accessible to the enzymes of the DNA replication machinery.",True,DNA replication,,,,
7544909c-d981-4d0c-b027-e88427b0d66d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"One of the key players in DNA replication is the enzyme DNA polymerase, also known as DNA pol, which adds nucleotides one-by-one to the growing DNA chain that is complementary to the template strand.",True,DNA replication,,,,
94ad7f9d-6cee-48bd-af22-8984d36168e3,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"In prokaryotes, three main types of polymerases are known: DNA pol I, DNA pol II, and DNA pol III.",True,DNA replication,,,,
633d28de-9c73-4cd4-85da-f1064103ef54,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"In eukaryotes there are fourteen are known polymerases, of which five are known to have major roles during replication and have been well studied. They are known as pol α, pol β, pol γ, pol δ, and pol ε.",True,DNA replication,,,,
72af720d-5ec8-4b4d-927b-8bc48f82da5e,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,How does the replication machinery know where to begin?,False,How does the replication machinery know where to begin?,,,,
951b6fd1-d665-4750-b28d-e00a44d970ca,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"There are specific nucleotide sequences called origins of replication where replication begins. In prokaryotes, there is typically a single origin of replication on its one chromosome, and this is in contrast to eukaryotes that have many origins of replication across the chromosomes.",True,How does the replication machinery know where to begin?,,,,
6c2d29ee-f429-4a98-8a61-ffd4263d5bc2,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The origin of replication is recognized by certain proteins that bind to this site. An enzyme called helicase unwinds the DNA by breaking the hydrogen bonds between the nitrogenous base pairs. ATP hydrolysis is required for this process. As the DNA opens up, Y-shaped structures called replication forks are formed. Two replication forks are formed at the origin of replication, and these get extended bidirectionally as replication continues. Single-strand binding proteins coat the single strands of DNA near the replication fork to prevent the single-stranded DNA from winding back into a double helix.",True,How does the replication machinery know where to begin?,,,,
fa89020e-26a1-4d23-aa06-49366e2f482b,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"DNA polymerase has two important restrictions. First, it is able to add nucleotides only in the 5′ to 3′ direction (a new DNA strand can be only extended in this direction). Second, it also requires a free 3′-OH group to which it can add nucleotides by forming a phosphodiester bond between the 3′-OH end and the 5′ phosphate of the next nucleotide. This essentially means that it cannot add nucleotides if a free 3′-OH group is not available.",True,How does the replication machinery know where to begin?,,,,
02139b93-d5ce-43b1-ad8b-4baf6a2a6145,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Then how does it add the first nucleotide? The problem is solved with the help of a primer that provides the free 3′-OH end. RNA primase synthesizes an RNA segment that is about five to ten nucleotides long and complementary to the template DNA. Because this sequence primes the DNA synthesis, it is appropriately called the primer. DNA polymerase can now extend this RNA primer, adding nucleotides one-by-one that are complementary to the template strand.",True,How does the replication machinery know where to begin?,,,,
0c1da87b-399f-4a67-88bf-26d36d492420,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The DNA tends to become more highly coiled ahead of the replication fork. Topoisomerase breaks and reforms DNAʼs phosphate backbone ahead of the replication fork, thereby relieving the pressure that results from this “supercoiling.” Single-strand binding proteins bind to the single-stranded DNA to prevent the helix from re-forming.",True,How does the replication machinery know where to begin?,,,,
4022eccb-b782-4405-83a4-2fc25aca1d57,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Because DNA polymerase can only extend in the 5′ to 3′ direction, and because the DNA double helix is antiparallel, there is a problem at the replication fork. The two template DNA strands have opposing orientations: one strand is in the 5′ to 3′ direction, and the other is oriented in the 3′ to 5′ direction. Only one new DNA strand, the one that is complementary to the 3′ to 5′ parental DNA strand, can be synthesized continuously toward the replication fork. This continuously synthesized strand is known as the leading strand. The other strand, complementary to the 5′ to 3′ parental DNA, is extended away from the replication fork in small fragments known as Okazaki fragments, each requiring a primer to start the synthesis. New primer segments are laid down in the direction of the replication fork, but each pointing away from it.",True,How does the replication machinery know where to begin?,,,,
1b1dc433-2005-4e22-9b5a-ae17f82a04c6,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The overall direction of the lagging strand will be 3′ to 5′, and that of the leading strand 5′ to 3′. A protein called the sliding clamp holds the DNA polymerase in place as it continues to add nucleotides. The sliding clamp is a ring-shaped protein that binds to the DNA and holds the polymerase in place. As synthesis continues, the RNA primers are removed by the exonuclease activity of DNA pol I, which uses DNA behind the RNA as its own primer and fills in the gaps left by removal of the RNA nucleotides by the addition of DNA nucleotides. The nicks that remain between the newly synthesized DNA (that replaced the RNA primer) and the previously synthesized DNA are sealed by the enzyme DNA ligase, which catalyzes the formation of phosphodiester linkages between the 3′-OH end of one nucleotide and the 5′ phosphate end of the other fragment.",True,How does the replication machinery know where to begin?,,,,
7a5cb9f2-eb29-4a86-9d7d-b4ab4b4c6170,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Once the chromosome has been completely replicated, the two DNA copies move into two different cells during cell division.",True,How does the replication machinery know where to begin?,,,,
171d2b8f-9874-42d9-be2d-20bb1032b5ff,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Telomere replication,False,Telomere replication,,,,
0e9dbec9-b506-4e11-b859-69436f8f234c,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"In eukaryotes, leading strand synthesis continues until the end of the chromosome is reached. On the lagging strand, DNA is synthesized in short stretches, each of which is initiated by a separate primer. When the replication fork reaches the end of the linear chromosome, there is no way to replace the primer on the 5ʼ end of the lagging strand.",True,Telomere replication,,,,
ac3972a6-eada-456a-bf7d-c457d98d42c9,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"The DNA at the ends of the chromosome thus remains unpaired, and over time these ends, called telomeres, may get progressively shorter as cells continue to divide.",True,Telomere replication,,,,
2d4d5de5-2d4a-40ab-81f7-1d63d43cf053,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
2d4d5de5-2d4a-40ab-81f7-1d63d43cf053,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
2d4d5de5-2d4a-40ab-81f7-1d63d43cf053,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
2d4d5de5-2d4a-40ab-81f7-1d63d43cf053,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
b0a4cd91-b48c-4855-adc7-30cfbbcfbe95,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Table 10.1: Prokaryotic DNA replication: enzymes and their function.,True,Telomere replication,,,,
f686b4bb-6e38-467f-8b27-4815458fb40d,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Table 10.2: Difference between prokaryotic and eukaryotic replication.,True,Telomere replication,,,,
668d6a27-aa20-4b93-af7d-0fd71f6d25b5,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,10.3 References and resources,True,Telomere replication,,,,
4c0a01e0-28cd-402d-bc8d-89c231496522,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,Text,False,Text,,,,
467695d8-023b-40ba-b6ea-f09806c08655,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
467695d8-023b-40ba-b6ea-f09806c08655,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
467695d8-023b-40ba-b6ea-f09806c08655,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
467695d8-023b-40ba-b6ea-f09806c08655,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
5d565cd9-de91-4b29-905a-dcb7b32814df,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
5d565cd9-de91-4b29-905a-dcb7b32814df,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
5d565cd9-de91-4b29-905a-dcb7b32814df,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
5d565cd9-de91-4b29-905a-dcb7b32814df,https://pressbooks.lib.vt.edu/cellbio/,10.1 DNA Structure,https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/#chapter-85-section-1,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
3c46714f-7977-4880-ac32-91aef3be2f71,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Nucleotides and basic DNA structure,False,Nucleotides and basic DNA structure,,,,
467eb915-4667-4a4c-bc32-c940a1080e58,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The nucleotides combine with each other to produce phosphodiester bonds. The phosphate residue attached to the 5′ carbon of the sugar of one nucleotide forms a second ester linkage with the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, thereby forming a 5′-3′ phosphodiester bond. In a polynucleotide, one end of the chain has a free 5′ phosphate, and the other end has a free 3′-OH. These are called the 5′ and 3′ ends of the chain.",True,Nucleotides and basic DNA structure,,,,
233f6372-f65f-4b35-9eac-ef1872abb306,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Base-pairing takes place between a purine and pyrimidine on opposite strands, so that adenine and thymine are complementary base pairs, and cytosine and guanine are also complementary base pairs. The base pairs are stabilized by hydrogen bonds: adenine and thymine form two hydrogen bonds, and cytosine and guanine form three hydrogen bonds. The two strands are anti-parallel in nature; that is, the 3′ end of one strand faces the 5′ end of the other strand. The sugar and phosphate of the nucleotides form the backbone of the structure, whereas the nitrogenous bases are stacked inside, like the rungs of a ladder. The twisting of the two strands around each other results in the formation of uniformly spaced major and minor grooves.",True,Nucleotides and basic DNA structure,,,,
eb6f181a-ddb3-48e6-a5a5-a5dd123cdefd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
eb6f181a-ddb3-48e6-a5a5-a5dd123cdefd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
eb6f181a-ddb3-48e6-a5a5-a5dd123cdefd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
eb6f181a-ddb3-48e6-a5a5-a5dd123cdefd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,DNA has a double helix structure and phosphodiester bonds; the dotted lines between thymine and adenine and guanine and cytosine represent hydrogen bonds. The major and minor grooves are binding sites for DNA-binding proteins during processes such as transcription (the copying of RNA from DNA) and replication (figure 10.3).,True,Nucleotides and basic DNA structure,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
e5fb336f-a149-492b-ba9b-8e49b26d9989,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,DNA packaging and organization,False,DNA packaging and organization,,,,
4f0e434a-6e50-4221-9f67-567299ca8ff6,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Eukaryotic chromosomes consist of a linear DNA molecule complexed with protein (histones); this complex is called chromatin. Histones are evolutionarily conserved proteins that are rich in basic amino acids and form an octamer composed of two molecules of each of four different histones.,True,DNA packaging and organization,,,,
7708ec64-032e-4c6c-b657-db5a8256a460,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
7708ec64-032e-4c6c-b657-db5a8256a460,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
7708ec64-032e-4c6c-b657-db5a8256a460,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
7708ec64-032e-4c6c-b657-db5a8256a460,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The DNA (remember, it is negatively charged because of the phosphate groups) is wrapped tightly around the histone core. This interaction is facilitated through electrostatic interactions. The negatively charged phosphate groups on the DNA backbone are attracted to a positively charged lysine on the exposed surface of histones. This nucleosome is linked to the next one with the help of a linker DNA. This is also known as the “beads on a string” structure. With the help of a fifth histone, a string of nucleosomes is further compacted into a 30 nm fiber, which is the diameter of the structure. Metaphase chromosomes are even further condensed by association with scaffolding proteins. At the metaphase stage, the chromosomes are at their most compact, approximately 700 nm in width (figure 10.4).",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
e7591032-e111-4abf-85c5-dcb1b14cbd92,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"In interphase, eukaryotic chromosomes have two distinct regions that can be distinguished by staining. The tightly packaged region is known as heterochromatin, and the less dense region is known as euchromatin.",True,DNA packaging and organization,,,,
f644398a-bd7a-4dbf-80e9-7777d054f1f3,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Heterochromatin usually contains genes that are not expressed and is found in the regions of the centromere and telomeres.,True,DNA packaging and organization,,,,
d0629132-6724-4acd-b0ce-a93caf2046d4,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The euchromatin usually contains genes that are transcribed, with DNA packaged around nucleosomes but not further compacted.",True,DNA packaging and organization,,,,
5da81ded-3b5e-4a96-994d-160b1fc6151e,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Histone tails can be modified through both methylation and acetylation, which will alter the histone:DNA interaction. Histone methylation can have variable impacts on a given gene locus leading to a change in transcription. Histone acetylation relaxes the interactions of histones and DNA by removing the positive charge on lysine residues allowing the DNA to be transcriptionally accessible (euchromatin). DNA methylation, specifically to CpG islands, globally represses transcription. These modifications on histones and DNA can result in epigenetic influences that have an impact on many biological processes.",True,DNA packaging and organization,,,,
2be257d3-fdea-4b38-86b9-572d68b1bf3b,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Across the three billion base pair genome, genes are organized into clusters with only a fraction of the DNA coding for translated products. The remaining DNA was historically considered “junk,” however, more recently there is a new appreciation for the roles of noncoding DNA regions. Only half of the genome is unique DNA sequence, and only 1.5 percent codes for mRNA (~20,000 protein-coding genes). The remaining sequence can be categorized as:",True,DNA packaging and organization,,,,
a4f23c5c-37d6-41a8-9d46-5e11c40db3c1,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,10.1 References and resources,True,DNA packaging and organization,,,,
2fcf9b8f-5745-4804-af55-3e0fffc3db64,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Clark, M. A. Biology, 2nd ed. Houston, TX: OpenStax College, Rice University, 2018, Chapter 14: DNA Structure and Function.",True,DNA packaging and organization,,,,
379e8e86-e566-4856-acd9-282e3a0e0d35,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Karp, G., and J. G. Patton. Cell and Molecular Biology: Concepts and Experiments, 7th ed. Hoboken, NJ: John Wiley, 2013, Chapter 10: The Nature of the Gene and the Genome, Chapter 12: The Cell Nucleus and the Control of Gene Expression, Chapter 13: DNA Replication.",True,DNA packaging and organization,,,,
0f042a90-7d48-48a3-ac28-1257c539fc99,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 34, 38–40.",True,DNA packaging and organization,,,,
dbe56d0f-f533-41e5-8010-730499631628,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Nussbaum, R. L., R. R. McInnes, H. F. Willard, A. Hamosh, and M. W. Thompson. Thompson & Thompson Genetics  in Medicine, 8th ed. Philadelphia: Saunders/Elsevier, 2016, Chapter 2: The Introduction to the Human Genome.",True,DNA packaging and organization,,,,
c8146341-f133-4f0d-986d-48bdf7290c71,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
c8146341-f133-4f0d-986d-48bdf7290c71,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
c8146341-f133-4f0d-986d-48bdf7290c71,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
c8146341-f133-4f0d-986d-48bdf7290c71,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.1 Basic structure of nucleosides including the sugar (ribose or deoxyribose), base (pyrimidine or purine) and phosphate groups. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.1_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.1,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
ec0788c5-9184-4b51-ab3d-9522a6b1c570,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
ec0788c5-9184-4b51-ab3d-9522a6b1c570,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
ec0788c5-9184-4b51-ab3d-9522a6b1c570,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
ec0788c5-9184-4b51-ab3d-9522a6b1c570,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.2 Structure of pyrimidine and purine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.2_20210926. CC BY 4.0.",True,DNA packaging and organization,Figure 10.2,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
a5824aa4-dccb-4939-8e36-39940cee5d70,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
a5824aa4-dccb-4939-8e36-39940cee5d70,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
a5824aa4-dccb-4939-8e36-39940cee5d70,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
a5824aa4-dccb-4939-8e36-39940cee5d70,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.3 General structure and hydrogen bonding pattern of DNA. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/10.3_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons.",True,DNA packaging and organization,Figure 10.3,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
57a72aea-15d1-4abd-9d80-6bef425c49cd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
57a72aea-15d1-4abd-9d80-6bef425c49cd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
57a72aea-15d1-4abd-9d80-6bef425c49cd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
57a72aea-15d1-4abd-9d80-6bef425c49cd,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.4 Organizational structure of DNA illustrating condensation and supercoiling into chromosomes. 2021. https://archive.org/details/10.4_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY-SA 4.0. From Wikimedia Commons. And Figure 14.11. CC BY 4.0. From OpenStax.",True,DNA packaging and organization,Figure 10.4,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
741b4ffb-66a9-4e9d-a2b4-bd7277bb5bf5,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,10.2 DNA Repair,True,DNA packaging and organization,,,,
e5ed60fb-d608-4060-87bf-f37fa9bdfba0,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"DNA replication is a highly accurate process, but mistakes can occasionally occur, such as a DNA polymerase (DNA pol) inserting a wrong base. Uncorrected mistakes may sometimes lead to serious consequences, such as cancer. Repair mechanisms correct the mistakes. In rare cases, mistakes are not corrected, leading to mutations; in other cases, repair enzymes are themselves mutated or defective.",True,DNA packaging and organization,,,,
8c0336be-854f-41aa-b468-7bae22063620,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
8c0336be-854f-41aa-b468-7bae22063620,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
8c0336be-854f-41aa-b468-7bae22063620,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
8c0336be-854f-41aa-b468-7bae22063620,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Most of the mistakes during DNA replication are promptly corrected by the proofreading ability of DNA polymerase itself. In proofreading, the DNA pol reads the newly added base before adding the next one, so a correction can be made. The polymerase checks whether the newly added base has paired correctly with the base in the template strand. If it is the right base, the next nucleotide is added. If an incorrect base has been added, the enzyme makes a cut at the phosphodiester bond and releases the wrong nucleotide. This is performed by the 3′ exonuclease action of DNA pol. Once the incorrect nucleotide has been removed, it can be replaced by the correct one (figure 10.5(a)).",True,DNA packaging and organization,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
887cc740-132e-47d1-9c70-f4589560add0,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Mismatch repair,False,Mismatch repair,,,,
dea8336c-2ffa-4ac7-aca9-0d97018d3495,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
dea8336c-2ffa-4ac7-aca9-0d97018d3495,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
dea8336c-2ffa-4ac7-aca9-0d97018d3495,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
dea8336c-2ffa-4ac7-aca9-0d97018d3495,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Errors not addressed during replication are repaired through the process of mismatch repair (figure 10.5(b)). Specific repair enzymes recognize the mispaired nucleotide and excise part of the strand that contains it; the excised region is then resynthesized — typically during S phase of the cell cycle — and the enzymes involved are those used for DNA replication. If the mismatch remains uncorrected, it may lead to more permanent damage when the mismatched DNA is replicated. Deficiencies in this repair process can result in Lynch syndrome, which is characteristic of nonpolyposis colorectal cancer.",True,Mismatch repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
573ae727-90a9-4b00-95d0-b3181f1e3c1e,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,mispaired,False,mispaired,,,,
9b42400b-f2d6-487c-9945-0031867955a9,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"In prokaryotes, the parental strand is determined by the methyl groups on adenine bases, while the newly synthesized strand lacks them. Thus, DNA polymerase is able to remove the wrongly incorporated bases from the newly synthesized, non-methylated strand.",True,mispaired,,,,
cc59997c-75f9-4947-9eca-4eb985423d56,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"In eukaryotes, the mechanism is not very well understood, but it is believed to involve recognition of unsealed nicks in the new strand, as well as a short-term continuing association of some of the replication proteins with the new daughter strand after replication has completed.",True,mispaired,,,,
e11a0732-cc95-4cc6-b84f-ddaee384f6ee,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Errors during DNA replication are not the only reason why mutations arise in DNA. Mutations, variations in the nucleotide sequence of a genome, can also occur because of damage to DNA. Such mutations may be of two types: induced or spontaneous. Induced mutations are those that result from an exposure to chemicals, UV rays, X-rays, or some other environmental agent. Spontaneous mutations occur without any exposure to any environmental agent; they are a result of natural reactions taking place within the body.",True,mispaired,,,,
8e02c8a4-91e3-4f00-bffe-5bc8c1d20335,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Nucleotide excision repair (NER),False,Nucleotide excision repair (NER),,,,
70d81835-9557-4e35-a000-cfe74cd1e244,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
70d81835-9557-4e35-a000-cfe74cd1e244,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
70d81835-9557-4e35-a000-cfe74cd1e244,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
70d81835-9557-4e35-a000-cfe74cd1e244,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Another type of repair mechanism, nucleotide excision repair, is similar to mismatch repair, except that it is used to remove large, bulky damaged bases rather than mismatched ones. The repair enzymes replace abnormal, bulky, bases by making a cut on both the 3′ and 5′ ends of the damaged base. The segment of DNA is removed and replaced with the correctly paired nucleotides by the action of DNA pol. Once the bases are filled in, the remaining gap is sealed with a phosphodiester linkage catalyzed by DNA ligase (figure 10.5(c)).",True,Nucleotide excision repair (NER),Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4b1a8400-c831-4d11-a25b-9d48846a73db,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"This repair mechanism is often employed when UV exposure causes the formation of pyrimidine dimers (thymine dimers). When exposed to UV light, thymines lying next to each other can form thymine dimers. In normal cells, they are excised and replaced. Xeroderma pigmentosa is a condition in which thymine dimerization from exposure to UV light is not repaired.",True,Nucleotide excision repair (NER),,,,
e654ee6c-6e91-4d25-a9b1-f966c9a48ff0,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Base excision repair (BER),False,Base excision repair (BER),,,,
e8e6b3ca-86ef-4e89-8ffa-5244e6bc25d8,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
e8e6b3ca-86ef-4e89-8ffa-5244e6bc25d8,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
e8e6b3ca-86ef-4e89-8ffa-5244e6bc25d8,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
e8e6b3ca-86ef-4e89-8ffa-5244e6bc25d8,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The process of base excision repair (BER) is similar to NER but tends to repair small modifications to individual bases, such as deamination of cytosine to produce uracil. In this process, the aberrant base is detected by a glycosylase that will cleave the N-glycosidic bond joining the base to the deoxyribose sugar. This leaves an apurinic or apyrimidinic site (sugar phosphate backbone lacking a base), which is cleaved by an exonuclease and repaired through a similar process as mentioned above (figure 10.6).",True,Base excision repair (BER),Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
201e5107-a2db-4b09-b667-4b254dce1716,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,BER,False,BER,,,,
51c44d5b-cfaf-402f-a3b7-e8105c4ee419,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,NER,False,NER,,,,
f52eee2d-30f8-4467-a8c2-c7af401bb9e7,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Double-stranded break repair,False,Double-stranded break repair,,,,
20af7b65-abb3-4521-99f2-d68783193349,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Double-stranded breaks are caused by ionizing radiation, such as X-rays or radioactive particles. This can be repaired through two processes: nonhomologous end-joining and homologous recombination. The major difference between these two processes is in nonhomologous end-joining there is direct ligation of the two ends without the need for a DNA template. This can result in some DNA being lost in the process. In contrast, homologous recombination requires a DNA template to repair the break. This allows for restoration of the duplex without a loss of nucleotides.",True,Double-stranded break repair,,,,
9974b7d4-6fed-451c-b9aa-4a6bf06c2911,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,10.2 References and resources,True,Double-stranded break repair,,,,
a514dbaa-70dd-4f03-ae12-8caf431ded2d,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a514dbaa-70dd-4f03-ae12-8caf431ded2d,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a514dbaa-70dd-4f03-ae12-8caf431ded2d,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
a514dbaa-70dd-4f03-ae12-8caf431ded2d,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.5 Comparison on three types of repair. a) Proofreading b) Mismatch and c) Nucleotide excision repair. 2021. CC BY 4.0.",True,Double-stranded break repair,Figure 10.5,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
4282874f-9697-4de6-9f75-07ac534884ad,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
4282874f-9697-4de6-9f75-07ac534884ad,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
4282874f-9697-4de6-9f75-07ac534884ad,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
4282874f-9697-4de6-9f75-07ac534884ad,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.6 Summary of Base excision repair. This is a similar process to NER but requires a glycosylase. 2021. https://archive.org/details/10.6_20210926. CC BY-SA 4.0. Added DNA double helix grooves by Biochemlife. CC BY SA 4.0. From Wikimedia Commons.",True,Double-stranded break repair,Figure 10.6,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
d6f77343-69e7-4b6c-bb97-4ee660071026,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,10.3 DNA Replication,True,Double-stranded break repair,,,,
a5641e83-cfc3-4f56-bb94-b0d4d47d484d,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,The process of DNA replication can be summarized as follows:,False,The process of DNA replication can be summarized as follows:,,,,
36121ea7-7103-438b-99ae-d1ce803aa861,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,DNA replication,False,DNA replication,,,,
f49f07eb-30dd-44b8-9532-e09817624041,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The essential steps of replication are the same for both prokaryotes and eukaryotes. Before replication can start, the DNA has to be made available as a template. Eukaryotic DNA is bound to basic proteins known as histones to form structures called nucleosomes. Histones must be removed and then replaced during the replication process, which helps account for the lower replication rate in eukaryotes. The chromatin (the complex between DNA and proteins) may undergo some chemical modifications, so that the DNA may be able to slide off the proteins or be accessible to the enzymes of the DNA replication machinery.",True,DNA replication,,,,
3802c87f-8ca3-4bdc-887e-3177c3f86b44,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"One of the key players in DNA replication is the enzyme DNA polymerase, also known as DNA pol, which adds nucleotides one-by-one to the growing DNA chain that is complementary to the template strand.",True,DNA replication,,,,
abd4631c-4d4f-4f21-b693-2175f117f4dc,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"In prokaryotes, three main types of polymerases are known: DNA pol I, DNA pol II, and DNA pol III.",True,DNA replication,,,,
b488b168-d439-4ea6-82a7-0709d7022791,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"In eukaryotes there are fourteen are known polymerases, of which five are known to have major roles during replication and have been well studied. They are known as pol α, pol β, pol γ, pol δ, and pol ε.",True,DNA replication,,,,
2d782c41-471b-4a45-8573-16778f1e1d4b,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,How does the replication machinery know where to begin?,False,How does the replication machinery know where to begin?,,,,
2643da95-75e0-42d7-8298-016570ff076e,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"There are specific nucleotide sequences called origins of replication where replication begins. In prokaryotes, there is typically a single origin of replication on its one chromosome, and this is in contrast to eukaryotes that have many origins of replication across the chromosomes.",True,How does the replication machinery know where to begin?,,,,
572c9e5b-eb3d-48ef-839a-321a3a974282,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The origin of replication is recognized by certain proteins that bind to this site. An enzyme called helicase unwinds the DNA by breaking the hydrogen bonds between the nitrogenous base pairs. ATP hydrolysis is required for this process. As the DNA opens up, Y-shaped structures called replication forks are formed. Two replication forks are formed at the origin of replication, and these get extended bidirectionally as replication continues. Single-strand binding proteins coat the single strands of DNA near the replication fork to prevent the single-stranded DNA from winding back into a double helix.",True,How does the replication machinery know where to begin?,,,,
bfc782cd-629b-40de-9182-a596a3a047f4,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"DNA polymerase has two important restrictions. First, it is able to add nucleotides only in the 5′ to 3′ direction (a new DNA strand can be only extended in this direction). Second, it also requires a free 3′-OH group to which it can add nucleotides by forming a phosphodiester bond between the 3′-OH end and the 5′ phosphate of the next nucleotide. This essentially means that it cannot add nucleotides if a free 3′-OH group is not available.",True,How does the replication machinery know where to begin?,,,,
afa7bac6-b3f0-41f8-a742-87b185185cd6,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Then how does it add the first nucleotide? The problem is solved with the help of a primer that provides the free 3′-OH end. RNA primase synthesizes an RNA segment that is about five to ten nucleotides long and complementary to the template DNA. Because this sequence primes the DNA synthesis, it is appropriately called the primer. DNA polymerase can now extend this RNA primer, adding nucleotides one-by-one that are complementary to the template strand.",True,How does the replication machinery know where to begin?,,,,
2fafb4da-80ad-49d6-89d1-f581a1c3021c,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The DNA tends to become more highly coiled ahead of the replication fork. Topoisomerase breaks and reforms DNAʼs phosphate backbone ahead of the replication fork, thereby relieving the pressure that results from this “supercoiling.” Single-strand binding proteins bind to the single-stranded DNA to prevent the helix from re-forming.",True,How does the replication machinery know where to begin?,,,,
33b3e68c-7ef8-47df-99c2-1cb5a836e164,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Because DNA polymerase can only extend in the 5′ to 3′ direction, and because the DNA double helix is antiparallel, there is a problem at the replication fork. The two template DNA strands have opposing orientations: one strand is in the 5′ to 3′ direction, and the other is oriented in the 3′ to 5′ direction. Only one new DNA strand, the one that is complementary to the 3′ to 5′ parental DNA strand, can be synthesized continuously toward the replication fork. This continuously synthesized strand is known as the leading strand. The other strand, complementary to the 5′ to 3′ parental DNA, is extended away from the replication fork in small fragments known as Okazaki fragments, each requiring a primer to start the synthesis. New primer segments are laid down in the direction of the replication fork, but each pointing away from it.",True,How does the replication machinery know where to begin?,,,,
4c4633f7-9e71-42fd-a5a6-db699adbccf7,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The overall direction of the lagging strand will be 3′ to 5′, and that of the leading strand 5′ to 3′. A protein called the sliding clamp holds the DNA polymerase in place as it continues to add nucleotides. The sliding clamp is a ring-shaped protein that binds to the DNA and holds the polymerase in place. As synthesis continues, the RNA primers are removed by the exonuclease activity of DNA pol I, which uses DNA behind the RNA as its own primer and fills in the gaps left by removal of the RNA nucleotides by the addition of DNA nucleotides. The nicks that remain between the newly synthesized DNA (that replaced the RNA primer) and the previously synthesized DNA are sealed by the enzyme DNA ligase, which catalyzes the formation of phosphodiester linkages between the 3′-OH end of one nucleotide and the 5′ phosphate end of the other fragment.",True,How does the replication machinery know where to begin?,,,,
df0237a7-d453-439b-a9bb-05792f8e1622,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Once the chromosome has been completely replicated, the two DNA copies move into two different cells during cell division.",True,How does the replication machinery know where to begin?,,,,
c8a23660-f641-4922-adb4-a03a4c19edac,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Telomere replication,False,Telomere replication,,,,
fc2b49d4-b81a-450a-8444-ed56281d1bee,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"In eukaryotes, leading strand synthesis continues until the end of the chromosome is reached. On the lagging strand, DNA is synthesized in short stretches, each of which is initiated by a separate primer. When the replication fork reaches the end of the linear chromosome, there is no way to replace the primer on the 5ʼ end of the lagging strand.",True,Telomere replication,,,,
98596416-1572-44c6-a234-2a4793bd3705,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"The DNA at the ends of the chromosome thus remains unpaired, and over time these ends, called telomeres, may get progressively shorter as cells continue to divide.",True,Telomere replication,,,,
a9f8ba2a-a919-415e-86c0-893ac2341617,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
a9f8ba2a-a919-415e-86c0-893ac2341617,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
a9f8ba2a-a919-415e-86c0-893ac2341617,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
a9f8ba2a-a919-415e-86c0-893ac2341617,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Telomeres comprise repetitive sequences that code for no particular gene. In humans, a six-base-pair sequence, TTAGGG, is repeated 100 to 1,000 times in the telomere regions. In a way, these telomeres protect the genes from getting deleted as cells continue to divide. The telomeres are added to the ends of chromosomes by a separate enzyme, telomerase (figure 10.8), whose discovery helped in the understanding of how these repetitive chromosome ends are maintained. The telomerase enzyme contains a catalytic part and a built-in RNA template. It attaches to the end of the chromosome, and DNA nucleotides complementary to the RNA template are added on the 3′ end of the DNA strand. Once the 3′ end of the lagging strand template is sufficiently elongated, DNA polymerase can add the nucleotides complementary to the ends of the chromosomes. Thus, the ends of the chromosomes are replicated.",True,Telomere replication,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
0913a52d-37ee-4111-9b33-9b900c61d7d6,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Table 10.1: Prokaryotic DNA replication: enzymes and their function.,True,Telomere replication,,,,
140446cb-7ab9-4c5e-b63d-1a8e047c1a32,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Table 10.2: Difference between prokaryotic and eukaryotic replication.,True,Telomere replication,,,,
575b2ddd-3f36-4b43-826f-3a607d2f99fc,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,10.3 References and resources,True,Telomere replication,,,,
7a235b96-0de4-46da-b4e5-e603e265a985,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,Text,False,Text,,,,
46a6a08c-20e1-4a42-a1ef-52f50eb4af2a,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
46a6a08c-20e1-4a42-a1ef-52f50eb4af2a,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
46a6a08c-20e1-4a42-a1ef-52f50eb4af2a,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
46a6a08c-20e1-4a42-a1ef-52f50eb4af2a,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.7 Summary of DNA replication. 2021. https://archive.org/details/10.7_20210926. CC BY 4.0.",True,Text,Figure 10.7,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
810c4140-724d-4c7a-b96f-83b0dc532d42,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.3 DNA Replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
810c4140-724d-4c7a-b96f-83b0dc532d42,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.2 DNA Repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
810c4140-724d-4c7a-b96f-83b0dc532d42,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,10.1 DNA Structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
810c4140-724d-4c7a-b96f-83b0dc532d42,https://pressbooks.lib.vt.edu/cellbio/,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/cellbio/chapter/genes-genomes-and-dna/,"Grey, Kindred, Figure 10.8 Summary of Telomerase activity to fill the overhand on the lagging strand. 2021. CC BY 4.0.",True,Text,Figure 10.8,"10. Genes, Genomes, and DNA",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
ca47a127-5507-41e1-aada-aaf444b0b482,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Alcohol metabolism,False,Alcohol metabolism,,,,
61b2de04-5018-4d68-aba1-a5841a9e2072,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Fructose metabolism,False,Fructose metabolism,,,,
8e944053-e7f3-4558-8c9c-a72829e95c22,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,GLUT5,False,GLUT5,,,,
7507f8f6-be43-42bd-b30f-c62635f946ad,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Aldolase B is the rate-limiting enzyme of fructose metabolism, although it is not a rate-limiting enzyme of glycolysis. Aldolase B’s affinity for fructose 1-phosphate is lower than fructose 1,6-bisphosphate and is very slow at physiological levels of fructose 1-phosphate. Consequently, after high fructose consumption, fructose 1-phosphate will accumulate in the liver, and it is slowly converted to glycolytic intermediates over time (figures 9.1 and 9.2).",True,GLUT5,,,,
381e911f-f122-4f4c-b1a1-9e2ec7c68a22,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Deficiencies in fructose metabolism,False,Deficiencies in fructose metabolism,,,,
8f0bbf45-9144-4ea6-9975-5a6eaeaba9eb,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Essential fructosuria (fructokinase deficiency) and hereditary fructose intolerance (HFI) (a deficiency of the fructose 1-phosphate cleavage by aldolase B) are inherited disorders of fructose metabolism. A deficiency in fructokinase is a benign genetic disorder. In this case, an individual will have fructosuria; fructose is not phosphorylated and trapped in the cell. Consequently, any ingested fructose is shed in the urine. Hereditary fructose intolerance is caused by a deficiency in aldolase B and results in an accumulation of fructose 1-phosphate in the hepatocytes. Inability to metabolize fructose 1-phosphate can cause significant clinical symptoms, most notably hepatomegaly and fasting hypoglyemia. The accumulation of fructose 1-phosphate eventually inhibits both glycogenolysis and gluconeogenesis (due to a lack of free phosphate), leading to bouts of fasting hypoglycemia.",True,Deficiencies in fructose metabolism,,,,
38901013-9b74-494a-90ac-3c3e038e8c4c,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,HFI,False,HFI,,,,
5a3bb3a7-5c07-475b-899c-d0b21550c4e4,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,hypoglyemia,False,hypoglyemia,,,,
984044a2-7125-481b-8d22-9935950c44af,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Galactose metabolism,False,Galactose metabolism,,,,
d960cb95-529b-4963-b69f-4dcb9459192d,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
d960cb95-529b-4963-b69f-4dcb9459192d,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
d960cb95-529b-4963-b69f-4dcb9459192d,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
bc1173d7-ddeb-4a1e-83a0-6cd6eec21a12,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Deficiencies in galactose metabolism,False,Deficiencies in galactose metabolism,,,,
f7d31efc-20ae-405f-8c75-520317427e34,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Classical galactosemia, a deficiency of galactosyl uridylyltransferase (GALT), results in the accumulation of galactose 1-phosphate in the liver and the inhibition of hepatic glycogen metabolism and other pathways that require UDP-sugars. Cataracts can occur from the accumulation of galactose in the blood, which is converted to galactitol (the sugar alcohol of galactose) in the lens of the eye.",True,Deficiencies in galactose metabolism,,,,
38dbf470-9cba-4cb2-b3f6-de7102101fe4,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"The accumulating galactose 1-phosphate is especially toxic for the liver, kidneys, and central nervous system. If left untreated, the disease is fatal due to complications such as gram-negative sepsis or hepatic and renal failure. The absence of GALT activity can be detected any time after birth and screened for as part of newborn screening. It is essential to obtain results promptly, because children with classic galactosemia can have a life-threatening crisis within the first few days after birth. Infants with a positive result are placed on a lactose-free formula, and confirmatory testing is accomplished by measuring specific metabolite concentrations and enzyme activity in erythrocytes.",True,Deficiencies in galactose metabolism,,,,
e6688b43-614a-4a08-8847-8cff0bc57be7,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Nonclassical galactosemia causes fewer medical complications and presents with a different pattern of symptoms. Presentations can involve cataracts, delayed development, and kidney problems.",True,Deficiencies in galactose metabolism,,,,
da69a570-9c31-4fb8-8519-e78a67174c64,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,9.1 References and resources,True,Deficiencies in galactose metabolism,,,,
9ed65514-c630-4d8b-b557-1b39c172f69a,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 12: Metabolism of Monosaccharides and Disaccharides, Chapter 23: Effects of Insulin and Glucagon: Section IV.",True,Deficiencies in galactose metabolism,,,,
b70d1af8-929d-41e7-8deb-bc1ffa614d5d,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Le, T., and V.  Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72, 80–81.",True,Deficiencies in galactose metabolism,,,,
66f90ae8-b9e6-44ce-aa09-e2263b9d2f89,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 22: Generation of ATP from Glucose, Fructose and Galactose, Chapter 33: Ethanol Metabolism.",True,Deficiencies in galactose metabolism,,,,
357e95f9-3e09-4c98-be47-29a8847c28ef,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
357e95f9-3e09-4c98-be47-29a8847c28ef,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
357e95f9-3e09-4c98-be47-29a8847c28ef,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
ecd19c1d-21d9-47fd-bcdc-21ba5ecbd223,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
ecd19c1d-21d9-47fd-bcdc-21ba5ecbd223,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
ecd19c1d-21d9-47fd-bcdc-21ba5ecbd223,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
842dceeb-2da2-45db-b47e-1ca2470ad651,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
842dceeb-2da2-45db-b47e-1ca2470ad651,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
842dceeb-2da2-45db-b47e-1ca2470ad651,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
8713b42f-8bbf-46e8-9d20-3804596dcd7e,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
8713b42f-8bbf-46e8-9d20-3804596dcd7e,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
8713b42f-8bbf-46e8-9d20-3804596dcd7e,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
ad0a0b6f-cd4c-4887-adef-dc57c8f882b3,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,9.2 Alcohol Metabolism,True,Deficiencies in galactose metabolism,,,,
1275b4bf-961d-4bc3-89b9-35847742d9cf,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Metabolism of alcohol occurs primarily in the liver through two different oxidative pathways. The activity of each pathway depends on the ethanol concentration and the frequency of ethanol consumption.,True,Deficiencies in galactose metabolism,,,,
c3ee01a5-61c6-437a-a5b2-ddb94f82787d,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
c3ee01a5-61c6-437a-a5b2-ddb94f82787d,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
c3ee01a5-61c6-437a-a5b2-ddb94f82787d,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
3d2ddb67-7c67-40a5-b3cf-f1cf45523cc7,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,ALDH,False,ALDH,,,,
4597853d-1cf8-4ffe-b373-cf1581b9911a,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Consequences of ethanol metabolism in the liver,False,Consequences of ethanol metabolism in the liver,,,,
e270fb83-e8d2-4a00-ab1c-8dfcdda94640,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
e270fb83-e8d2-4a00-ab1c-8dfcdda94640,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
e270fb83-e8d2-4a00-ab1c-8dfcdda94640,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
d4120842-0a56-4bce-a133-32f926d9d479,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,Excessive alcohol consumption,False,Excessive alcohol consumption,,,,
92209e04-09ea-4e80-8a0b-5bd3bdbd1df4,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
92209e04-09ea-4e80-8a0b-5bd3bdbd1df4,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
92209e04-09ea-4e80-8a0b-5bd3bdbd1df4,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
595e0563-bc92-4878-a459-d19e686fad2e,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,MEOS,False,MEOS,,,,
6efecd15-12f6-470f-b61b-10cd79003dcb,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,P450,False,P450,,,,
eb469236-4d0a-482d-9468-5006df6d0d00,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Although the MEOS system does not impact the NADH/NAD+ ratio, that is not to suggest that induction of this system is without metabolic consequences. Induction of the P450 system can negatively impact the metabolism of other drugs causing serious side effects. One example of this is altered metabolism of acetaminophen (Tylenol). Acetaminophen can be glucuronylated or sulfated in the liver for safe excretion by the kidney. However, the cytochrome P450 system can metabolize acetaminophen to the toxic intermediate N-acetyl-p-benzoquinone imine (NAPQI), which requires conjugation with glutathione prior to excretion. The enzyme that produces NAPQI, CYP2E1, is induced by alcohol through the MEOS. Thus, individuals who chronically abuse alcohol have increased sensitivity to acetaminophen toxicity because a higher percentage of acetaminophen metabolism is directed toward NAPQI, compared with an individual with low levels of CYP2E1.",True,P450,,,,
de0bd9f2-bfa0-4c90-b99b-d70ad56769a9,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Ethanol is also an inhibitor of the phenobarbital-oxidizing P450 system. When large amounts of ethanol are consumed, the inactivation of phenobarbital is directly or indirectly inhibited. Therefore, when high doses of phenobarbital and ethanol are consumed at the same time, toxic levels of the barbiturate can accumulate in the blood.",True,P450,,,,
34c98be3-f26a-42b4-9cda-68e2255d244c,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,9.2 References and resources,True,P450,,,,
d5f65062-3d56-46c3-a9ef-91bacf624a74,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
d5f65062-3d56-46c3-a9ef-91bacf624a74,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
d5f65062-3d56-46c3-a9ef-91bacf624a74,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
666cdae3-ab2a-4fe1-820f-45d4c57b942f,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
666cdae3-ab2a-4fe1-820f-45d4c57b942f,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
666cdae3-ab2a-4fe1-820f-45d4c57b942f,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
a48032a6-dfbe-4e21-9004-eba417e95296,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
a48032a6-dfbe-4e21-9004-eba417e95296,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
a48032a6-dfbe-4e21-9004-eba417e95296,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
52db8b30-a982-4fe1-a506-2eafd8f3fcac,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
52db8b30-a982-4fe1-a506-2eafd8f3fcac,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
52db8b30-a982-4fe1-a506-2eafd8f3fcac,https://pressbooks.lib.vt.edu/cellbio/,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-2,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
c9360193-dbfb-4f5c-8222-e1dc71e5235f,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Alcohol metabolism,False,Alcohol metabolism,,,,
2208d1fb-8a1d-4c71-8cc1-f10ad7e5cb14,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Fructose metabolism,False,Fructose metabolism,,,,
92310e43-7a96-4a1b-a599-41ba5f33bc6d,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,GLUT5,False,GLUT5,,,,
65a8585e-2de4-42ff-aa14-ef6e78e3fa05,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Aldolase B is the rate-limiting enzyme of fructose metabolism, although it is not a rate-limiting enzyme of glycolysis. Aldolase B’s affinity for fructose 1-phosphate is lower than fructose 1,6-bisphosphate and is very slow at physiological levels of fructose 1-phosphate. Consequently, after high fructose consumption, fructose 1-phosphate will accumulate in the liver, and it is slowly converted to glycolytic intermediates over time (figures 9.1 and 9.2).",True,GLUT5,,,,
d885e375-dcdb-4e35-88bd-df4e98ec7250,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Deficiencies in fructose metabolism,False,Deficiencies in fructose metabolism,,,,
23ce05e8-86b4-47ff-875d-792adc3c24f2,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Essential fructosuria (fructokinase deficiency) and hereditary fructose intolerance (HFI) (a deficiency of the fructose 1-phosphate cleavage by aldolase B) are inherited disorders of fructose metabolism. A deficiency in fructokinase is a benign genetic disorder. In this case, an individual will have fructosuria; fructose is not phosphorylated and trapped in the cell. Consequently, any ingested fructose is shed in the urine. Hereditary fructose intolerance is caused by a deficiency in aldolase B and results in an accumulation of fructose 1-phosphate in the hepatocytes. Inability to metabolize fructose 1-phosphate can cause significant clinical symptoms, most notably hepatomegaly and fasting hypoglyemia. The accumulation of fructose 1-phosphate eventually inhibits both glycogenolysis and gluconeogenesis (due to a lack of free phosphate), leading to bouts of fasting hypoglycemia.",True,Deficiencies in fructose metabolism,,,,
64d9ab1c-15c8-4aa9-8691-f024dc538ed5,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,HFI,False,HFI,,,,
98c19d1f-416a-4358-a46a-2d0d43ef616a,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,hypoglyemia,False,hypoglyemia,,,,
c7605c37-3ebf-46e6-a946-0be43de2fad6,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Galactose metabolism,False,Galactose metabolism,,,,
ab435db7-c0ed-47e5-8715-d3184d1b6fd9,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
ab435db7-c0ed-47e5-8715-d3184d1b6fd9,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
ab435db7-c0ed-47e5-8715-d3184d1b6fd9,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
c20da853-5b32-45ac-b27d-66d715619be3,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Deficiencies in galactose metabolism,False,Deficiencies in galactose metabolism,,,,
3523f834-1e47-47db-af76-4d6c6d939c99,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Classical galactosemia, a deficiency of galactosyl uridylyltransferase (GALT), results in the accumulation of galactose 1-phosphate in the liver and the inhibition of hepatic glycogen metabolism and other pathways that require UDP-sugars. Cataracts can occur from the accumulation of galactose in the blood, which is converted to galactitol (the sugar alcohol of galactose) in the lens of the eye.",True,Deficiencies in galactose metabolism,,,,
a8b16023-65ca-4f4b-b836-90cce7aa95fd,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"The accumulating galactose 1-phosphate is especially toxic for the liver, kidneys, and central nervous system. If left untreated, the disease is fatal due to complications such as gram-negative sepsis or hepatic and renal failure. The absence of GALT activity can be detected any time after birth and screened for as part of newborn screening. It is essential to obtain results promptly, because children with classic galactosemia can have a life-threatening crisis within the first few days after birth. Infants with a positive result are placed on a lactose-free formula, and confirmatory testing is accomplished by measuring specific metabolite concentrations and enzyme activity in erythrocytes.",True,Deficiencies in galactose metabolism,,,,
3d9e8a57-c998-4c5d-a51c-9c7ec9032c6c,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Nonclassical galactosemia causes fewer medical complications and presents with a different pattern of symptoms. Presentations can involve cataracts, delayed development, and kidney problems.",True,Deficiencies in galactose metabolism,,,,
cf0c0991-8e83-49de-9115-2dfe5d73c890,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,9.1 References and resources,True,Deficiencies in galactose metabolism,,,,
47f296cb-f1b4-47e2-89f2-a7ac5ed0eb36,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 12: Metabolism of Monosaccharides and Disaccharides, Chapter 23: Effects of Insulin and Glucagon: Section IV.",True,Deficiencies in galactose metabolism,,,,
958ac3d3-71e0-4811-bff2-ea3afb932b1b,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Le, T., and V.  Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72, 80–81.",True,Deficiencies in galactose metabolism,,,,
b3998213-baef-4cc7-9ce2-9a000b8ca4a3,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 22: Generation of ATP from Glucose, Fructose and Galactose, Chapter 33: Ethanol Metabolism.",True,Deficiencies in galactose metabolism,,,,
5fbe9912-9d23-4982-a483-474cff5a3a87,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
5fbe9912-9d23-4982-a483-474cff5a3a87,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
5fbe9912-9d23-4982-a483-474cff5a3a87,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
8ee0a683-ce44-4c18-b9cf-9afa9d10bf97,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
8ee0a683-ce44-4c18-b9cf-9afa9d10bf97,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
8ee0a683-ce44-4c18-b9cf-9afa9d10bf97,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
86e8d50c-2e27-4edb-ba60-18f0959e79fe,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
86e8d50c-2e27-4edb-ba60-18f0959e79fe,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
86e8d50c-2e27-4edb-ba60-18f0959e79fe,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
31d225a6-5b7e-4a39-ac67-803c102de857,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
31d225a6-5b7e-4a39-ac67-803c102de857,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
31d225a6-5b7e-4a39-ac67-803c102de857,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
8aec299c-5ce4-45b8-8015-8935a401235d,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,9.2 Alcohol Metabolism,True,Deficiencies in galactose metabolism,,,,
8c79ef7e-11ad-42e5-8d48-f405ceb377ea,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Metabolism of alcohol occurs primarily in the liver through two different oxidative pathways. The activity of each pathway depends on the ethanol concentration and the frequency of ethanol consumption.,True,Deficiencies in galactose metabolism,,,,
f5c38ecc-a9b5-4227-81d4-5ec5ad8083d7,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
f5c38ecc-a9b5-4227-81d4-5ec5ad8083d7,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
f5c38ecc-a9b5-4227-81d4-5ec5ad8083d7,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
83d642cd-4b75-4038-b6ad-07fe31efe8bb,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,ALDH,False,ALDH,,,,
0804fe9d-8e97-4f0d-8e7f-90a669d19661,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Consequences of ethanol metabolism in the liver,False,Consequences of ethanol metabolism in the liver,,,,
2f68a128-fdf7-4a0f-8fd0-c528f2e2fdc1,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
2f68a128-fdf7-4a0f-8fd0-c528f2e2fdc1,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
2f68a128-fdf7-4a0f-8fd0-c528f2e2fdc1,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
1179442d-2f7c-4d15-a9d8-134d52c7f91f,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,Excessive alcohol consumption,False,Excessive alcohol consumption,,,,
b91cfa4a-742a-4965-8986-c47116eed3b6,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
b91cfa4a-742a-4965-8986-c47116eed3b6,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
b91cfa4a-742a-4965-8986-c47116eed3b6,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
19426423-611c-4460-9795-f615ad823cfe,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,MEOS,False,MEOS,,,,
09ddde3f-be9e-48c0-aaa7-51eeece298c5,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,P450,False,P450,,,,
c9b5cbb2-4a7a-4e6d-b0fa-317ae4fcb8b8,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Although the MEOS system does not impact the NADH/NAD+ ratio, that is not to suggest that induction of this system is without metabolic consequences. Induction of the P450 system can negatively impact the metabolism of other drugs causing serious side effects. One example of this is altered metabolism of acetaminophen (Tylenol). Acetaminophen can be glucuronylated or sulfated in the liver for safe excretion by the kidney. However, the cytochrome P450 system can metabolize acetaminophen to the toxic intermediate N-acetyl-p-benzoquinone imine (NAPQI), which requires conjugation with glutathione prior to excretion. The enzyme that produces NAPQI, CYP2E1, is induced by alcohol through the MEOS. Thus, individuals who chronically abuse alcohol have increased sensitivity to acetaminophen toxicity because a higher percentage of acetaminophen metabolism is directed toward NAPQI, compared with an individual with low levels of CYP2E1.",True,P450,,,,
6052aa19-5833-49eb-9f28-0d788c6c69c3,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Ethanol is also an inhibitor of the phenobarbital-oxidizing P450 system. When large amounts of ethanol are consumed, the inactivation of phenobarbital is directly or indirectly inhibited. Therefore, when high doses of phenobarbital and ethanol are consumed at the same time, toxic levels of the barbiturate can accumulate in the blood.",True,P450,,,,
4266391d-fde8-4292-8799-1dc92afb4ae5,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,9.2 References and resources,True,P450,,,,
0b9d44bf-1c79-4eeb-8db7-19e0edaad80c,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
0b9d44bf-1c79-4eeb-8db7-19e0edaad80c,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
0b9d44bf-1c79-4eeb-8db7-19e0edaad80c,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
19d5aed2-5b0d-4747-a1f0-77135e3f8cf5,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
19d5aed2-5b0d-4747-a1f0-77135e3f8cf5,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
19d5aed2-5b0d-4747-a1f0-77135e3f8cf5,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
9a8bf446-8d8e-4741-8521-28db5bbb6493,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
9a8bf446-8d8e-4741-8521-28db5bbb6493,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
9a8bf446-8d8e-4741-8521-28db5bbb6493,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
de86bc43-3865-4245-b7a6-b3a95bbec08d,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
de86bc43-3865-4245-b7a6-b3a95bbec08d,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
de86bc43-3865-4245-b7a6-b3a95bbec08d,https://pressbooks.lib.vt.edu/cellbio/,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/#chapter-81-section-1,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
fc956135-2639-4d26-893f-110698fa79fe,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Alcohol metabolism,False,Alcohol metabolism,,,,
a5a9c268-3ac0-4ff6-b9e9-2e8bdd5cce11,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Fructose metabolism,False,Fructose metabolism,,,,
68a6a254-e02a-473d-ac4a-bd6d6e3c29e3,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,GLUT5,False,GLUT5,,,,
3ce59596-f999-4aaf-ab95-99c2deff8e54,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Aldolase B is the rate-limiting enzyme of fructose metabolism, although it is not a rate-limiting enzyme of glycolysis. Aldolase B’s affinity for fructose 1-phosphate is lower than fructose 1,6-bisphosphate and is very slow at physiological levels of fructose 1-phosphate. Consequently, after high fructose consumption, fructose 1-phosphate will accumulate in the liver, and it is slowly converted to glycolytic intermediates over time (figures 9.1 and 9.2).",True,GLUT5,,,,
efe4833b-b368-4864-a052-60a38788b849,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Deficiencies in fructose metabolism,False,Deficiencies in fructose metabolism,,,,
36880ed2-b08e-49d4-ae53-e5864e30caa7,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Essential fructosuria (fructokinase deficiency) and hereditary fructose intolerance (HFI) (a deficiency of the fructose 1-phosphate cleavage by aldolase B) are inherited disorders of fructose metabolism. A deficiency in fructokinase is a benign genetic disorder. In this case, an individual will have fructosuria; fructose is not phosphorylated and trapped in the cell. Consequently, any ingested fructose is shed in the urine. Hereditary fructose intolerance is caused by a deficiency in aldolase B and results in an accumulation of fructose 1-phosphate in the hepatocytes. Inability to metabolize fructose 1-phosphate can cause significant clinical symptoms, most notably hepatomegaly and fasting hypoglyemia. The accumulation of fructose 1-phosphate eventually inhibits both glycogenolysis and gluconeogenesis (due to a lack of free phosphate), leading to bouts of fasting hypoglycemia.",True,Deficiencies in fructose metabolism,,,,
40062e2d-3606-4756-bc4c-19379ea78d4e,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,HFI,False,HFI,,,,
fdb032d6-de20-4887-b5cb-f309c06b4a1f,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,hypoglyemia,False,hypoglyemia,,,,
5f3dd68b-b2bd-433e-8adc-c4cf8b9dfc87,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Galactose metabolism,False,Galactose metabolism,,,,
fc6b0367-7d3f-41c4-b59a-9c0b5d6a9c38,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
fc6b0367-7d3f-41c4-b59a-9c0b5d6a9c38,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
fc6b0367-7d3f-41c4-b59a-9c0b5d6a9c38,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Galactose is consumed principally as lactose, which is cleaved to galactose and glucose in the intestine. Galactose is subsequently phosphorylated to galactose 1-phosphate by galactokinase (primarily in the liver). Following phosphorylation, galactose 1-phosphate is activated to a uridine diphosphate (UDP)-sugar by galactosyl uridylyltransferase (GALT). The metabolic pathway subsequently generates glucose 1-phosphate, which enters into the glycolytic pathway (figure 9.2)",True,Galactose metabolism,Figure 9.2,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
0f82a18f-8239-4ccc-8ecc-4a486b98a8be,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Deficiencies in galactose metabolism,False,Deficiencies in galactose metabolism,,,,
5225c184-2466-4b1c-a9dc-028594ab4281,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Classical galactosemia, a deficiency of galactosyl uridylyltransferase (GALT), results in the accumulation of galactose 1-phosphate in the liver and the inhibition of hepatic glycogen metabolism and other pathways that require UDP-sugars. Cataracts can occur from the accumulation of galactose in the blood, which is converted to galactitol (the sugar alcohol of galactose) in the lens of the eye.",True,Deficiencies in galactose metabolism,,,,
38ccc507-6a5d-4154-af5f-9aae8544d8df,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"The accumulating galactose 1-phosphate is especially toxic for the liver, kidneys, and central nervous system. If left untreated, the disease is fatal due to complications such as gram-negative sepsis or hepatic and renal failure. The absence of GALT activity can be detected any time after birth and screened for as part of newborn screening. It is essential to obtain results promptly, because children with classic galactosemia can have a life-threatening crisis within the first few days after birth. Infants with a positive result are placed on a lactose-free formula, and confirmatory testing is accomplished by measuring specific metabolite concentrations and enzyme activity in erythrocytes.",True,Deficiencies in galactose metabolism,,,,
d3f5c57c-60d6-4c06-967d-e9efc8fc5106,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Nonclassical galactosemia causes fewer medical complications and presents with a different pattern of symptoms. Presentations can involve cataracts, delayed development, and kidney problems.",True,Deficiencies in galactose metabolism,,,,
a25f5509-d0ad-4cbd-81a1-64f3306a2e51,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,9.1 References and resources,True,Deficiencies in galactose metabolism,,,,
f0e1d552-eaa1-4652-ae89-46a87a5d6b97,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 12: Metabolism of Monosaccharides and Disaccharides, Chapter 23: Effects of Insulin and Glucagon: Section IV.",True,Deficiencies in galactose metabolism,,,,
7a36dc4f-b462-453c-a610-f82986bc83bc,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Le, T., and V.  Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72, 80–81.",True,Deficiencies in galactose metabolism,,,,
c668ec0a-9b46-4282-a708-5b779f78b234,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 22: Generation of ATP from Glucose, Fructose and Galactose, Chapter 33: Ethanol Metabolism.",True,Deficiencies in galactose metabolism,,,,
32aa9970-ae5e-4d91-a1d8-978b80031ad1,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
32aa9970-ae5e-4d91-a1d8-978b80031ad1,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
32aa9970-ae5e-4d91-a1d8-978b80031ad1,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.1 Convergence of fructose and glucose metabolism. 2021. https://archive.org/details/9.1_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.1,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
b05432ce-8985-423c-9cae-c1149ef312b9,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
b05432ce-8985-423c-9cae-c1149ef312b9,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
b05432ce-8985-423c-9cae-c1149ef312b9,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.2 Fructose metabolism and reaction by Aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance while deficiencies in frutokinase can result in essential fructosuria. 2021. https://archive.org/details/9.2_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.2,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
06cee856-b926-4b69-8c0d-cf9d27b07850,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
06cee856-b926-4b69-8c0d-cf9d27b07850,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
06cee856-b926-4b69-8c0d-cf9d27b07850,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.3 Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate which enters the pathway. 2021. https://archive.org/details/9.3_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.3,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
5022b1bd-3d83-45ae-a000-933a6e1d6ab6,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
5022b1bd-3d83-45ae-a000-933a6e1d6ab6,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
5022b1bd-3d83-45ae-a000-933a6e1d6ab6,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.4 Comparison of Classical and Nonclassical galatosemia. 2021. https://archive.org/details/9.4_20210926. CC BY 4.0.",True,Deficiencies in galactose metabolism,Figure 9.4,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
7f5a80b7-2659-4e3a-914d-435eab83c3d3,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,9.2 Alcohol Metabolism,True,Deficiencies in galactose metabolism,,,,
82d38a00-e3da-4087-b65d-2336a001e638,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Metabolism of alcohol occurs primarily in the liver through two different oxidative pathways. The activity of each pathway depends on the ethanol concentration and the frequency of ethanol consumption.,True,Deficiencies in galactose metabolism,,,,
7578718e-5f2f-4891-88ee-ad21fc6e06d7,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
7578718e-5f2f-4891-88ee-ad21fc6e06d7,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
7578718e-5f2f-4891-88ee-ad21fc6e06d7,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At low concentrations, oxidation of ethanol is a two-step process that occurs in both the cytosol and the mitochondria (figure 9.5). The first step of the reaction by alcohol dehydrogenase (ADH) occurs in the cytosol and produces acetaldehyde. Acetaldehyde is converted into acetate in the mitochondria by acetaldehyde dehydrogenase (ALDH) and can be transported in the blood to be used as an energy source for peripheral tissues (figure 9.5). The acetate can be converted to acetyl-CoA by acetyl-CoA synthetase (figure 9.6), and this will be oxidized in the TCA cycle. Each step in the oxidation of ethanol produces NADH, which increases the ratio of NADH/NAD+. The increase in this ratio can alter metabolism of other substrates and cause metabolic dysfunction, which will be discussed below.",True,Deficiencies in galactose metabolism,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
8dd94abc-73b1-457c-a499-873264ab0aa4,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,ALDH,False,ALDH,,,,
7b0d255b-1ae7-44b3-9d1d-5df0294f9856,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Consequences of ethanol metabolism in the liver,False,Consequences of ethanol metabolism in the liver,,,,
159c7aa8-e91e-41ca-9e38-fd3c82c689f7,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
159c7aa8-e91e-41ca-9e38-fd3c82c689f7,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
159c7aa8-e91e-41ca-9e38-fd3c82c689f7,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At each step in ethanol oxidation, NADH is generated in both the mitochondrial and cytosolic compartments (figure 9.5). This can have major metabolic ramifications depending on the underlying metabolic environment (figure 9.7).",True,Consequences of ethanol metabolism in the liver,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
d1ba9bd5-bd16-4e63-bba0-7e181c3f0b68,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,Excessive alcohol consumption,False,Excessive alcohol consumption,,,,
4fbc3360-3a6f-43e3-b8a1-4f9414660206,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
4fbc3360-3a6f-43e3-b8a1-4f9414660206,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
4fbc3360-3a6f-43e3-b8a1-4f9414660206,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"At higher concentrations of ethanol, the microsomal ethanol oxidizing system (MEOS) becomes activated (figure 9.7; label 9). This pathway consists of a series of cytochrome P450 enzymes, which have a relatively high Km for ethanol and are located in the hepatic smooth endoplasmic reticulum (SER). This microsomal-ethanol oxidizing system also detoxifies drugs such as barbiturates (figure 9.8).",True,Excessive alcohol consumption,Figure 9.7,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
5ff8440f-cc0e-4cc8-8877-31dee55a4761,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,MEOS,False,MEOS,,,,
e935b8da-b833-4042-862f-d7dcde327274,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,P450,False,P450,,,,
c399e1cd-b047-401c-9f0d-1a825c2f8957,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Although the MEOS system does not impact the NADH/NAD+ ratio, that is not to suggest that induction of this system is without metabolic consequences. Induction of the P450 system can negatively impact the metabolism of other drugs causing serious side effects. One example of this is altered metabolism of acetaminophen (Tylenol). Acetaminophen can be glucuronylated or sulfated in the liver for safe excretion by the kidney. However, the cytochrome P450 system can metabolize acetaminophen to the toxic intermediate N-acetyl-p-benzoquinone imine (NAPQI), which requires conjugation with glutathione prior to excretion. The enzyme that produces NAPQI, CYP2E1, is induced by alcohol through the MEOS. Thus, individuals who chronically abuse alcohol have increased sensitivity to acetaminophen toxicity because a higher percentage of acetaminophen metabolism is directed toward NAPQI, compared with an individual with low levels of CYP2E1.",True,P450,,,,
b1407db3-b9f7-4fd9-a0dd-adc4e13f00fc,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Ethanol is also an inhibitor of the phenobarbital-oxidizing P450 system. When large amounts of ethanol are consumed, the inactivation of phenobarbital is directly or indirectly inhibited. Therefore, when high doses of phenobarbital and ethanol are consumed at the same time, toxic levels of the barbiturate can accumulate in the blood.",True,P450,,,,
0a8b8815-0be0-40dc-aaab-d1c763044757,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,9.2 References and resources,True,P450,,,,
c244af33-c99e-4245-8dec-ba41a1c8a659,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
c244af33-c99e-4245-8dec-ba41a1c8a659,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
c244af33-c99e-4245-8dec-ba41a1c8a659,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.5 Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria and NADH is produced in both steps of the pathway. 2021. https://archive.org/details/9.5_20210926. CC BY 4.0.",True,P450,Figure 9.5,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
6c28cc44-7841-4935-9b6b-9247172144ea,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
6c28cc44-7841-4935-9b6b-9247172144ea,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
6c28cc44-7841-4935-9b6b-9247172144ea,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Grey, Kindred, Figure 9.6 Overview of alcohol metabolism. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/9.6_20210926. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,P450,Figure 9.6,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
c8ed45bd-e235-4655-969a-7e3b59f46b91,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
c8ed45bd-e235-4655-969a-7e3b59f46b91,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
c8ed45bd-e235-4655-969a-7e3b59f46b91,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Lieberman M, Peet A. Figure 9.7 Clinical consequences of alcoholism. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 709. Figure 33.6 Acute effects of ethanol metabolism on lipid metabolism in the liver. 2017.",True,P450,Figure 9.7,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
bc40b018-637d-454d-8954-64e4594a9629,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9.2 Alcohol Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
bc40b018-637d-454d-8954-64e4594a9629,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9.1 Monosaccharide Metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
bc40b018-637d-454d-8954-64e4594a9629,https://pressbooks.lib.vt.edu/cellbio/,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/cellbio/chapter/disorders-of-monosaccharide-metabolism-and-other-metabolic-conditions/,"Lieberman M, Peet A. Figure 9.8 Ethanol detoxification by MEOS. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 704. Figure 33.3 The reaction catalyzed by the microsomal ethanol-oxidizing system (MEOS; which includes CYP2E1) in the endoplasmic reticulum (ER). 2017. Chemical structure by Henry Jakubowski.",True,P450,Figure 9.8,9. Disorders of Monosaccharide Metabolism and Other Metabolic Conditions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
35b738d4-8c78-4f33-9940-e90b1413ec3e,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Cofactors essential for amino acid metabolism,False,Cofactors essential for amino acid metabolism,,,,
544d24bb-ec26-455b-87cf-1f5801a693f4,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,BH4,False,BH4,,,,
cc97a5e7-dbe5-4aad-8763-186d8778e1c2,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,TH4,False,TH4,,,,
86dcaede-5e74-41e4-ab32-9c661cfd8775,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Pyridoxal phosphate (B6 or PLP),False,Pyridoxal phosphate (B6 or PLP),,,,
b6bb8549-c0c9-47c4-885c-bb9569190776,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,All transamination reactions require PLP as a cofactor. These reactions are essential for moving (or donating) a nitrogen from an amino acid to a keto-acid to generate a different amino acid.,True,Pyridoxal phosphate (B6 or PLP),,,,
b0caa426-62dd-488c-9474-82f6019bf1ca,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Tetrahydrobiopterin (BH4),False,Tetrahydrobiopterin (BH4),,,,
6dec849e-b869-4be8-968e-2135ae3f5239,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"This is a cofactor synthesized from GTP. It is oxidized during hydroxylation reactions, most notably the conversion of phenylalanine to tyrosine. Enzymatic deficiencies leading to decreased synthesis of BH4 can present similar to deficiencies in phenylalanine metabolism.",True,Tetrahydrobiopterin (BH4),,,,
a6ac08a9-2f35-47e8-b781-a9ef624fc665,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Tetrahydrofolate (FH4),False,Tetrahydrofolate (FH4),,,,
4a3d8910-4391-4a5c-96fd-7a12bc9cb0ec,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Folate can exist in many forms and is often referred to as tetrahydrofolate. FH4 is often found in various forms with a one-carbon group attached. These one-carbon groups, which make up the one-carbon pool, can be oxidized or reduced. One-carbon groups can be transferred to other compounds and play essential roles in the synthesis of glycine from serine, the synthesis of the base thymine (required for DNA synthesis), the purine bases required for both DNA and RNA synthesis, and the transfer of methyl groups to vitamin B12.",True,Tetrahydrofolate (FH4),,,,
6c89c888-7b67-450e-a6dc-de335703f3d3,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,FH4,False,FH4,,,,
0d046696-5ad5-4b1e-aee4-0d452f3e4084,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Synthesis of specialized products,False,Synthesis of specialized products,,,,
7f3cf870-f425-4323-aada-dc4aa9c9283b,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,The following highlights some of the key aspects of amino acid metabolism.,True,Synthesis of specialized products,,,,
d14c8181-0ca5-48d9-ac53-c2215a2dbc64,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Phenylalanine and tyrosine,False,Phenylalanine and tyrosine,,,,
16206c7e-e332-4515-81ca-14a70772cada,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Phenylalanine is an essential amino acid, and hydroxylation of Phe by phenylalanine hydroxylase (PAH) generates tyrosine (figure 8.1). This conversion requires BH4, and deficiencies in either the cofactor or the enzyme PAH can result in phenylketonuria. Additionally, the inability to synthesize tyrosine will make this a conditionally essential amino acid and potentially negatively impact the synthesis of downstream compounds illustrated in figure 8.1.",True,Phenylalanine and tyrosine,Figure 8.1,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
16206c7e-e332-4515-81ca-14a70772cada,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Phenylalanine is an essential amino acid, and hydroxylation of Phe by phenylalanine hydroxylase (PAH) generates tyrosine (figure 8.1). This conversion requires BH4, and deficiencies in either the cofactor or the enzyme PAH can result in phenylketonuria. Additionally, the inability to synthesize tyrosine will make this a conditionally essential amino acid and potentially negatively impact the synthesis of downstream compounds illustrated in figure 8.1.",True,Phenylalanine and tyrosine,Figure 8.1,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
43093863-1864-47d6-94d7-d1ff1fa7ad23,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism (tyrosinase), alkaptonuria (homogentisate oxidase), or tyrosinemia, which can manifest due to deficiencies in several enzymes along the pathway (figure 8.2).",True,Phenylalanine and tyrosine,Figure 8.2,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
43093863-1864-47d6-94d7-d1ff1fa7ad23,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism (tyrosinase), alkaptonuria (homogentisate oxidase), or tyrosinemia, which can manifest due to deficiencies in several enzymes along the pathway (figure 8.2).",True,Phenylalanine and tyrosine,Figure 8.2,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
26df42b3-31b9-4694-90e0-7382c05626d0,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Phenylketonuria,False,Phenylketonuria,,,,
4044afd2-a957-49e1-9580-ff0828ace245,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Phenylketonuria (PKU) is one of the more common amino acid metabolic disorders and is inherited in an autosomal recessive fashion. There are no symptoms of untreated phenylketonuria in the first months of life, therefore newborn screening is essential for diagnosis and initiation of treatment, which prevents the devastating effects of infantile hyperphenylalaninemia. The screening method detects elevated titers of the amino acid phenylalanine (Phe) in the blood. A positive test result (Phe greater than 150 μmol/L) prompts the physician to begin a phenylalaninerestricted formula and requires a confirmatory quantitative Phe level.",True,Phenylketonuria,,,,
992d916d-d44c-417c-930b-6915788280c8,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Glycine,False,Glycine,,,,
62fcbd91-103f-4ec6-bd00-d9dc700a6239,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Glycine is a key compound that functions as an essential substrate for various pathways including the folate cycle, nucleotide synthesis, and synthesis of porphyrins (heme), glutathione, and creatine. Glycine can be synthesized at the cellular level from 3-phosphoglycerate, an intermediate of glycolysis.",True,Glycine,,,,
e1efef65-f60b-4be5-aa6f-fb5441634949,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Arginine,False,Arginine,,,,
042cf5c3-c135-4981-b4cf-010373184884,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Arginine is a nonessential amino acid as it can be produced in the urea cycle. Deficiencies in the urea cycle can cause arginine to become conditionally essential. In these cases, management and supplementation are needed.",True,Arginine,,,,
4c4a932a-8555-44e2-a929-e3e3c90cc814,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Tryptophan,False,Tryptophan,,,,
1c7f1105-3b0b-4c96-903c-9ef6c3de37b7,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Tryptophan is an essential amino acid that is both ketogenic and glucogenic as it can be oxidized to produce alanine and acetyl-CoA. The ring structure can also be used to synthesize niacin, reducing the dietary requirement for this vitamin. Tryptophan metabolism to serotonin (and subsequently melatonin) requires BH4. Deficiencies here can lead to imbalances in these neurotransmitters (figure 8.3).",True,Tryptophan,Figure 8.3,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
1c7f1105-3b0b-4c96-903c-9ef6c3de37b7,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Tryptophan is an essential amino acid that is both ketogenic and glucogenic as it can be oxidized to produce alanine and acetyl-CoA. The ring structure can also be used to synthesize niacin, reducing the dietary requirement for this vitamin. Tryptophan metabolism to serotonin (and subsequently melatonin) requires BH4. Deficiencies here can lead to imbalances in these neurotransmitters (figure 8.3).",True,Tryptophan,Figure 8.3,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
fc673db9-622d-4ff5-9961-a69d377d43e1,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Glutamate,False,Glutamate,,,,
26ab8bb4-1aad-411d-b66d-b7bea7aa8540,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Glutamate plays many key roles in amino acid metabolism and provides substrates for GABA and glutathione synthesis (figure 8.4). Additionally, glutamate plays a key role in nitrogen movement within the body. Glutamate can be deaminated by glutamate dehydrogenase to yield α-ketoglutarate. This can enter directly into the TCA cycle or be transaminated (figure 8.4). Additionally, glutamate can be used to fix or free ammonium to generate glutamine — one of the essential, nontoxic carriers of ammonia.",True,Glutamate,Figure 8.4,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
26ab8bb4-1aad-411d-b66d-b7bea7aa8540,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Glutamate plays many key roles in amino acid metabolism and provides substrates for GABA and glutathione synthesis (figure 8.4). Additionally, glutamate plays a key role in nitrogen movement within the body. Glutamate can be deaminated by glutamate dehydrogenase to yield α-ketoglutarate. This can enter directly into the TCA cycle or be transaminated (figure 8.4). Additionally, glutamate can be used to fix or free ammonium to generate glutamine — one of the essential, nontoxic carriers of ammonia.",True,Glutamate,Figure 8.4,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
6179e956-4ab4-4a1c-8c3f-0df78582462e,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Isoleucine, leucine, and valine (branched-chain amino acids)",False,"Isoleucine, leucine, and valine (branched-chain amino acids)",,,,
46da66fe-da71-41bb-866e-5711d8e6cb0d,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Oxidation of these amino acids, collectively described as branched-chain amino acids, occurs in all tissues (except the liver) and is a key fuel source for skeletal muscle. As these amino acids are approximately 25 percent of the amino acid pool, they provide both energy and available substrate to replenish the TCA cycle. The initial step in their metabolism, like all amino acids, is the transamination to generate a keto-acid. These compounds then undergo oxidative decarboxylation by a multiunit enzyme similar to the pyruvate dehydrogenase complex with similar cofactor requirements (section 4.1), and the remaining carbons can enter the TCA cycle.",True,"Isoleucine, leucine, and valine (branched-chain amino acids)",,,,
0df839fa-ccbb-44fb-9bf0-84b5e0f0d78e,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Maple syrup urine disease,False,Maple syrup urine disease,,,,
41805e88-15e5-4281-b465-ea02fb392c67,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Deficiencies in metabolism of branched-chain amino acids can result in the diagnosis of maple syrup urine disease (MSUD). With an incidence of 1 in 100,000, MSUD is rare even among the inborn errors of metabolism. However, the distinct sweet odor, similar to that of maple syrup, distinguishes this condition as one of the more recognizable metabolic disorders. It is caused by deficient oxidative decarboxylation of α-keto-acid metabolites of leucine, isoleucine, and valine. Affected infants can become symptomatic during the first days of life, with poor feeding, lethargy, seizures, and occasionally coma. Milder forms of MSUD may present later in life, with developmental delays and intellectual disability. Maple syrup urine disease is primarily treated by diet but also by avoiding circumstances that increase catabolism such as high fever and dehydration. If a metabolic crisis occurs, emergency treatment in a hospital is necessary to stabilize the patient.",True,Maple syrup urine disease,,,,
91db2ddd-c571-4502-b73f-d3a95bea471c,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Methionine,False,Methionine,,,,
f3b6b42d-cf76-4c17-b9bb-8bfa473d604e,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Methionine is an essential amino acid with a complex metabolism of clinical importance. Its metabolism interfaces with the folate cycle, cobalamin remethylation, and the synthesis of S-adenosylmethionine (SAM). Enzymatic or cofactor deficiencies can result in elevated homocysteine levels (hyperhomocysteinemia), which can have negative impacts systemically. Methionine, required for the synthesis of SAM, can be obtained from the diet or produced from remethylation of homocysteine using vitamin B12.",True,Methionine,,,,
e75abb8e-395e-4c05-9fe3-b37bcb557218,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Initially, methionine will condense with ATP to form SAM. SAM has a charged methyl group, which can be transferred to many different acceptor molecules; this step is considered irreversible as the amount of energy released is substantial. SAM is used by many biological pathways to donate methyl groups, and it is in consistent demand. After SAM loses its methyl group, the resulting compound, S-adenosylhomocysteine (SAH), is hydrolyzed to homocysteine and adenosine.",True,Methionine,,,,
26763c6d-276a-41c0-b71a-fef1c15936c8,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Homocysteine, generated from this reaction, can either be remethylated in a reaction using both folate and cobalamin to resynthesize methionine or can be used for the synthesis or cysteine (figure 8.6).",True,Methionine,Figure 8.6,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
26763c6d-276a-41c0-b71a-fef1c15936c8,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Homocysteine, generated from this reaction, can either be remethylated in a reaction using both folate and cobalamin to resynthesize methionine or can be used for the synthesis or cysteine (figure 8.6).",True,Methionine,Figure 8.6,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
4796bbd7-1245-4aa0-ac60-342453e2fef6,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Remethylation of homocysteine,False,Remethylation of homocysteine,,,,
d288c3d0-bf2f-4d30-a972-1874804c9d0c,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Homocysteine can be converted back into methionine by using both methyl-FH4 and vitamin B12. (This is the only reaction in which methyl-FH4 can donate the methyl group.) In this reaction, the methyl group from FH4 is transferred to cobalamin associated with homocysteine methyltransferase. Homocysteine receives the methyl group from this charged cobalamin cofactor, and methionine is regenerated. If homocysteine methyltransferase is defective, or if vitamin B12 or FH4 levels are insufficient, homocysteine will accumulate. Elevated homocysteine levels have been linked to cardiovascular and neurological diseases. A consequence of vitamin B12 deficiency is the accumulation of methyl-FH4 and a decrease in other folate derivatives. This is known as the methyl-trap hypothesis; because of the B12 deficiency, most of the carbons in the FH4 pool are trapped in the methyl-FH4 form, which is the most stable. The carbons cannot be released from the folate because the one reaction in which they participate cannot occur because of the B12 deficiency. This leads to a functional folate deficiency, even though total levels of folate are normal.",True,Remethylation of homocysteine,,,,
a63b7772-34f4-4946-b4de-267cb0a8af92,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"A folate deficiency (whether functional or actual) leads to megaloblastic anemia caused by an inability of blood cell precursors to synthesize DNA and, therefore, to divide. This leads to large, partially replicated cells being released into the blood to attempt to replenish the cells that have died. Folate deficiencies also have been linked to an increased incidence of neural tube defects, such as spina bifida, in mothers who become pregnant while folate deficient.",True,Remethylation of homocysteine,,,,
3b816070-6cb9-4add-af04-ca7196a466f0,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Transsulfuration pathway,False,Transsulfuration pathway,,,,
05b21266-126e-48b3-97a5-fc4e536bac6d,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Further metabolism of homocysteine provides the sulfur atom for the synthesis of cysteine. In this two-step process, homocysteine first reacts with serine to form cystathionine. This is followed by cleavage of cystathionine, which yields cysteine and α-ketobutyrate. The first reaction in this sequence, catalyzed by cystathionine β-synthase, is inhibited by cysteine. Thus, methionine, via homocysteine, is not used for cysteine synthesis unless the levels of cysteine in the body are lower than required for its metabolic functions. An adequate dietary supply of cysteine, therefore, can “spare” (or reduce) the dietary requirement for methionine (figure 8.6).",True,Transsulfuration pathway,Figure 8.6,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
05b21266-126e-48b3-97a5-fc4e536bac6d,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Further metabolism of homocysteine provides the sulfur atom for the synthesis of cysteine. In this two-step process, homocysteine first reacts with serine to form cystathionine. This is followed by cleavage of cystathionine, which yields cysteine and α-ketobutyrate. The first reaction in this sequence, catalyzed by cystathionine β-synthase, is inhibited by cysteine. Thus, methionine, via homocysteine, is not used for cysteine synthesis unless the levels of cysteine in the body are lower than required for its metabolic functions. An adequate dietary supply of cysteine, therefore, can “spare” (or reduce) the dietary requirement for methionine (figure 8.6).",True,Transsulfuration pathway,Figure 8.6,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
d8f3fb15-3d31-4125-9ad5-a334bfb48178,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,Consequences of elevated homocysteine,False,Consequences of elevated homocysteine,,,,
13d69ff5-a9fb-4f18-8367-db1ea1640c20,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Homocysteine levels can accumulate in several ways, which are related to both folic acid and vitamin B12 metabolism. As SAM is constantly being used as a methyl donor, this results in a consistent production of SAH. Consequently, this leads to constant production of homocysteine. The homocysteine produced can be either remethylated to methionine or condensed with serine to form cystathionine. The major pathway of homocysteine metabolism is remethylation by N5-methyl-FH4, which requires vitamin B12. The liver also contains a second pathway in which betaine (a degradation product of choline) can donate a methyl group to homocysteine to form methionine, but this is a minor pathway. The conversion of homocysteine to cystathionine requires pyridoxal phosphate (PLP). Thus, if an individual is deficient in vitamin B12, the conversion of homocysteine to methionine by the major route is inhibited. This directs homocysteine to produce cystathionine, which eventually produces cysteine. Homocysteine also accumulates in the blood if a mutation is present in the enzyme that converts N5,N10-methylene-FH4 to N5-methyl-FH4. When this occurs, the levels of N5-methyl-FH4 are too low to allow homocysteine to be converted to methionine. The loss of this pathway, coupled with the feedback inhibition by cysteine on cystathionine formation, also leads to elevated homocysteine levels in the blood. A third way in which serum homocysteine levels can be elevated is by a mutated cystathionine β-synthase or a deficiency in vitamin B6, the required cofactor for that enzyme. These defects block the ability of homocysteine to be converted to cystathionine, and the homocysteine that does accumulate cannot all be accommodated by conversion to methionine. Thus, an accumulation of homocysteine results.",True,Consequences of elevated homocysteine,,,,
8ced2fa3-988f-45e1-87fc-4dc0c1d395aa,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,8.1 References and resources,True,Consequences of elevated homocysteine,,,,
9073a959-4469-4452-9fdc-ce3b70fb8e8e,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 20: Amino Acid Degradation and Synthesis, Chapter 21: Conversion of Amino Acids to Specialized Products.",True,Consequences of elevated homocysteine,,,,
c209815b-2793-44c0-9162-1a58319726ef,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 69, 83–85.",True,Consequences of elevated homocysteine,,,,
a1f1ddd4-cc27-483c-b67c-4f21685c54e1,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 37: Synthesis and Degradation of Amino Acids, Chapter 39: Tetrahydrofolate, Vitamin B12, and S-Adenosylmethionine.",True,Consequences of elevated homocysteine,,,,
cd742ede-9eb2-48a4-99fb-904aeb7d431d,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.1 Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria. 2021. https://archive.org/details/8.1-new. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.1,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
cd742ede-9eb2-48a4-99fb-904aeb7d431d,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.1 Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria. 2021. https://archive.org/details/8.1-new. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.1,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
8dcdd5f0-db7b-40fe-b2ae-45b11538848f,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.2 Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria or tyrosinemia. 2021. https://archive.org/details/8.2_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.2,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
8dcdd5f0-db7b-40fe-b2ae-45b11538848f,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.2 Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria or tyrosinemia. 2021. https://archive.org/details/8.2_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.2,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
e3d24482-c2a8-45ed-96ae-e2c967e18f7c,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.3 Metabolism of tryptophan to melatonin. 2021. https://archive.org/details/8.3_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.3,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
e3d24482-c2a8-45ed-96ae-e2c967e18f7c,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.3 Metabolism of tryptophan to melatonin. 2021. https://archive.org/details/8.3_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.3,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
3c1eedb2-7659-49c7-a967-0d710b807530,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.4 Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA. 2021. https://archive.org/details/8.4_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.4,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
3c1eedb2-7659-49c7-a967-0d710b807530,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.4 Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA. 2021. https://archive.org/details/8.4_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.4,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
7e976151-db13-4d35-9a8a-f30c3543f48e,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.5 Metabolism of branched chain amino acids. Deficiencies in BCKAD can result in the presentation of Maple Syrup Urine Disease. 2021. https://archive.org/details/8.5_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.5,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.5-scaled.jpg,Figure 8.5: Metabolism of branched-chain amino acids. Deficiencies in branched-chain keto acid dehydrogenase (BCKAD) can result in the presentation of maple syrup urine disease.
7e976151-db13-4d35-9a8a-f30c3543f48e,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.5 Metabolism of branched chain amino acids. Deficiencies in BCKAD can result in the presentation of Maple Syrup Urine Disease. 2021. https://archive.org/details/8.5_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.5,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.5-scaled.jpg,Figure 8.5: Metabolism of branched-chain amino acids. Deficiencies in branched-chain keto acid dehydrogenase (BCKAD) can result in the presentation of maple syrup urine disease.
dbf246f0-22e6-48a2-9180-376829c1ea55,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.6 Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine. 2021. https://archive.org/details/8.6_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.6,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
dbf246f0-22e6-48a2-9180-376829c1ea55,https://pressbooks.lib.vt.edu/cellbio/,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/#chapter-75-section-1,"Grey, Kindred, Figure 8.6 Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine. 2021. https://archive.org/details/8.6_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.6,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
38d002a6-dee6-4d94-82f9-774d97c4ac7c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Cofactors essential for amino acid metabolism,False,Cofactors essential for amino acid metabolism,,,,
61b30dd9-709e-4f9c-a9d1-c798761804a4,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,BH4,False,BH4,,,,
6bebbb1f-f2dc-4dfe-af89-c8ddcaf197bc,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,TH4,False,TH4,,,,
d8d567c9-3a89-4da5-99d8-984bc54d3d37,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Pyridoxal phosphate (B6 or PLP),False,Pyridoxal phosphate (B6 or PLP),,,,
fd5ac91b-1bdb-4284-a9c0-3e517dea3109,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,All transamination reactions require PLP as a cofactor. These reactions are essential for moving (or donating) a nitrogen from an amino acid to a keto-acid to generate a different amino acid.,True,Pyridoxal phosphate (B6 or PLP),,,,
271085ff-1067-4d84-9dbc-49aa71848be0,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Tetrahydrobiopterin (BH4),False,Tetrahydrobiopterin (BH4),,,,
90691613-7171-4782-b5bb-1093d0999520,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"This is a cofactor synthesized from GTP. It is oxidized during hydroxylation reactions, most notably the conversion of phenylalanine to tyrosine. Enzymatic deficiencies leading to decreased synthesis of BH4 can present similar to deficiencies in phenylalanine metabolism.",True,Tetrahydrobiopterin (BH4),,,,
9ed9f97e-d9db-403a-b5af-9641d0ee7673,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Tetrahydrofolate (FH4),False,Tetrahydrofolate (FH4),,,,
b8ea7863-012a-44ce-b9fb-5ec36b35eec2,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Folate can exist in many forms and is often referred to as tetrahydrofolate. FH4 is often found in various forms with a one-carbon group attached. These one-carbon groups, which make up the one-carbon pool, can be oxidized or reduced. One-carbon groups can be transferred to other compounds and play essential roles in the synthesis of glycine from serine, the synthesis of the base thymine (required for DNA synthesis), the purine bases required for both DNA and RNA synthesis, and the transfer of methyl groups to vitamin B12.",True,Tetrahydrofolate (FH4),,,,
3b9af234-ed67-4620-8128-7fd1769e289a,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,FH4,False,FH4,,,,
e7556edf-f8d7-492e-9754-98fdbcb353b9,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Synthesis of specialized products,False,Synthesis of specialized products,,,,
58f51430-0453-4717-af5e-6040df2a32c0,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,The following highlights some of the key aspects of amino acid metabolism.,True,Synthesis of specialized products,,,,
b8050a82-f988-4905-8b60-afd711a6990f,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Phenylalanine and tyrosine,False,Phenylalanine and tyrosine,,,,
52973ca6-0ae5-4b57-bc6b-e272496e3153,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Phenylalanine is an essential amino acid, and hydroxylation of Phe by phenylalanine hydroxylase (PAH) generates tyrosine (figure 8.1). This conversion requires BH4, and deficiencies in either the cofactor or the enzyme PAH can result in phenylketonuria. Additionally, the inability to synthesize tyrosine will make this a conditionally essential amino acid and potentially negatively impact the synthesis of downstream compounds illustrated in figure 8.1.",True,Phenylalanine and tyrosine,Figure 8.1,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
52973ca6-0ae5-4b57-bc6b-e272496e3153,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Phenylalanine is an essential amino acid, and hydroxylation of Phe by phenylalanine hydroxylase (PAH) generates tyrosine (figure 8.1). This conversion requires BH4, and deficiencies in either the cofactor or the enzyme PAH can result in phenylketonuria. Additionally, the inability to synthesize tyrosine will make this a conditionally essential amino acid and potentially negatively impact the synthesis of downstream compounds illustrated in figure 8.1.",True,Phenylalanine and tyrosine,Figure 8.1,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
00607d44-48d4-4b1b-b35d-de9d25e3ae98,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism (tyrosinase), alkaptonuria (homogentisate oxidase), or tyrosinemia, which can manifest due to deficiencies in several enzymes along the pathway (figure 8.2).",True,Phenylalanine and tyrosine,Figure 8.2,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
00607d44-48d4-4b1b-b35d-de9d25e3ae98,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism (tyrosinase), alkaptonuria (homogentisate oxidase), or tyrosinemia, which can manifest due to deficiencies in several enzymes along the pathway (figure 8.2).",True,Phenylalanine and tyrosine,Figure 8.2,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
ac143539-3bba-4958-8fcf-2e938936657a,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Phenylketonuria,False,Phenylketonuria,,,,
3cda493c-475d-4bfc-ad4d-46cf01075799,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Phenylketonuria (PKU) is one of the more common amino acid metabolic disorders and is inherited in an autosomal recessive fashion. There are no symptoms of untreated phenylketonuria in the first months of life, therefore newborn screening is essential for diagnosis and initiation of treatment, which prevents the devastating effects of infantile hyperphenylalaninemia. The screening method detects elevated titers of the amino acid phenylalanine (Phe) in the blood. A positive test result (Phe greater than 150 μmol/L) prompts the physician to begin a phenylalaninerestricted formula and requires a confirmatory quantitative Phe level.",True,Phenylketonuria,,,,
060ac2d5-1c56-4d83-bb12-ee333c4a1724,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Glycine,False,Glycine,,,,
5ee66f28-8a0d-467e-baff-5981e93d4431,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Glycine is a key compound that functions as an essential substrate for various pathways including the folate cycle, nucleotide synthesis, and synthesis of porphyrins (heme), glutathione, and creatine. Glycine can be synthesized at the cellular level from 3-phosphoglycerate, an intermediate of glycolysis.",True,Glycine,,,,
2ca1b4c6-6619-4ae0-b158-bee50687da43,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Arginine,False,Arginine,,,,
63219234-66fe-4bb4-8509-76f08bdc3560,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Arginine is a nonessential amino acid as it can be produced in the urea cycle. Deficiencies in the urea cycle can cause arginine to become conditionally essential. In these cases, management and supplementation are needed.",True,Arginine,,,,
efc5e77a-b955-4fea-937c-9940809d2da2,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Tryptophan,False,Tryptophan,,,,
184c9f58-af7d-4900-afb3-8193dac0a76f,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Tryptophan is an essential amino acid that is both ketogenic and glucogenic as it can be oxidized to produce alanine and acetyl-CoA. The ring structure can also be used to synthesize niacin, reducing the dietary requirement for this vitamin. Tryptophan metabolism to serotonin (and subsequently melatonin) requires BH4. Deficiencies here can lead to imbalances in these neurotransmitters (figure 8.3).",True,Tryptophan,Figure 8.3,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
184c9f58-af7d-4900-afb3-8193dac0a76f,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Tryptophan is an essential amino acid that is both ketogenic and glucogenic as it can be oxidized to produce alanine and acetyl-CoA. The ring structure can also be used to synthesize niacin, reducing the dietary requirement for this vitamin. Tryptophan metabolism to serotonin (and subsequently melatonin) requires BH4. Deficiencies here can lead to imbalances in these neurotransmitters (figure 8.3).",True,Tryptophan,Figure 8.3,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
4c523ed1-8669-42c2-8873-0cd6eb063c0c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Glutamate,False,Glutamate,,,,
ee233acf-8e99-4450-9592-a2c4e91e0815,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Glutamate plays many key roles in amino acid metabolism and provides substrates for GABA and glutathione synthesis (figure 8.4). Additionally, glutamate plays a key role in nitrogen movement within the body. Glutamate can be deaminated by glutamate dehydrogenase to yield α-ketoglutarate. This can enter directly into the TCA cycle or be transaminated (figure 8.4). Additionally, glutamate can be used to fix or free ammonium to generate glutamine — one of the essential, nontoxic carriers of ammonia.",True,Glutamate,Figure 8.4,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
ee233acf-8e99-4450-9592-a2c4e91e0815,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Glutamate plays many key roles in amino acid metabolism and provides substrates for GABA and glutathione synthesis (figure 8.4). Additionally, glutamate plays a key role in nitrogen movement within the body. Glutamate can be deaminated by glutamate dehydrogenase to yield α-ketoglutarate. This can enter directly into the TCA cycle or be transaminated (figure 8.4). Additionally, glutamate can be used to fix or free ammonium to generate glutamine — one of the essential, nontoxic carriers of ammonia.",True,Glutamate,Figure 8.4,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
6b03ed30-9c9a-4da5-a36f-de69d6bab7fb,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Isoleucine, leucine, and valine (branched-chain amino acids)",False,"Isoleucine, leucine, and valine (branched-chain amino acids)",,,,
67163f27-cf0b-4f6a-a589-bb8f4d3cff86,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Oxidation of these amino acids, collectively described as branched-chain amino acids, occurs in all tissues (except the liver) and is a key fuel source for skeletal muscle. As these amino acids are approximately 25 percent of the amino acid pool, they provide both energy and available substrate to replenish the TCA cycle. The initial step in their metabolism, like all amino acids, is the transamination to generate a keto-acid. These compounds then undergo oxidative decarboxylation by a multiunit enzyme similar to the pyruvate dehydrogenase complex with similar cofactor requirements (section 4.1), and the remaining carbons can enter the TCA cycle.",True,"Isoleucine, leucine, and valine (branched-chain amino acids)",,,,
5bd86424-4744-4c54-a36b-0aee97c3132a,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Maple syrup urine disease,False,Maple syrup urine disease,,,,
bd50671e-b31e-4050-ba26-9a49ad042931,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Deficiencies in metabolism of branched-chain amino acids can result in the diagnosis of maple syrup urine disease (MSUD). With an incidence of 1 in 100,000, MSUD is rare even among the inborn errors of metabolism. However, the distinct sweet odor, similar to that of maple syrup, distinguishes this condition as one of the more recognizable metabolic disorders. It is caused by deficient oxidative decarboxylation of α-keto-acid metabolites of leucine, isoleucine, and valine. Affected infants can become symptomatic during the first days of life, with poor feeding, lethargy, seizures, and occasionally coma. Milder forms of MSUD may present later in life, with developmental delays and intellectual disability. Maple syrup urine disease is primarily treated by diet but also by avoiding circumstances that increase catabolism such as high fever and dehydration. If a metabolic crisis occurs, emergency treatment in a hospital is necessary to stabilize the patient.",True,Maple syrup urine disease,,,,
2fd90910-3241-408f-845e-603dd795015a,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Methionine,False,Methionine,,,,
2aea5d1e-30bd-4de5-9c8d-644fefe8f24f,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Methionine is an essential amino acid with a complex metabolism of clinical importance. Its metabolism interfaces with the folate cycle, cobalamin remethylation, and the synthesis of S-adenosylmethionine (SAM). Enzymatic or cofactor deficiencies can result in elevated homocysteine levels (hyperhomocysteinemia), which can have negative impacts systemically. Methionine, required for the synthesis of SAM, can be obtained from the diet or produced from remethylation of homocysteine using vitamin B12.",True,Methionine,,,,
84dafa91-cf90-4bb5-ab4c-f486d2d2d52a,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Initially, methionine will condense with ATP to form SAM. SAM has a charged methyl group, which can be transferred to many different acceptor molecules; this step is considered irreversible as the amount of energy released is substantial. SAM is used by many biological pathways to donate methyl groups, and it is in consistent demand. After SAM loses its methyl group, the resulting compound, S-adenosylhomocysteine (SAH), is hydrolyzed to homocysteine and adenosine.",True,Methionine,,,,
b7693b11-853f-4e59-a26e-52388126ff81,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Homocysteine, generated from this reaction, can either be remethylated in a reaction using both folate and cobalamin to resynthesize methionine or can be used for the synthesis or cysteine (figure 8.6).",True,Methionine,Figure 8.6,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
b7693b11-853f-4e59-a26e-52388126ff81,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Homocysteine, generated from this reaction, can either be remethylated in a reaction using both folate and cobalamin to resynthesize methionine or can be used for the synthesis or cysteine (figure 8.6).",True,Methionine,Figure 8.6,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
4574bfd0-f955-4129-98fc-6a85076ed30f,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Remethylation of homocysteine,False,Remethylation of homocysteine,,,,
4c679612-66e2-4e41-be95-7f02d8bc5bbf,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Homocysteine can be converted back into methionine by using both methyl-FH4 and vitamin B12. (This is the only reaction in which methyl-FH4 can donate the methyl group.) In this reaction, the methyl group from FH4 is transferred to cobalamin associated with homocysteine methyltransferase. Homocysteine receives the methyl group from this charged cobalamin cofactor, and methionine is regenerated. If homocysteine methyltransferase is defective, or if vitamin B12 or FH4 levels are insufficient, homocysteine will accumulate. Elevated homocysteine levels have been linked to cardiovascular and neurological diseases. A consequence of vitamin B12 deficiency is the accumulation of methyl-FH4 and a decrease in other folate derivatives. This is known as the methyl-trap hypothesis; because of the B12 deficiency, most of the carbons in the FH4 pool are trapped in the methyl-FH4 form, which is the most stable. The carbons cannot be released from the folate because the one reaction in which they participate cannot occur because of the B12 deficiency. This leads to a functional folate deficiency, even though total levels of folate are normal.",True,Remethylation of homocysteine,,,,
78fd4c28-d4b6-416f-9a21-6f216ca94a4b,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"A folate deficiency (whether functional or actual) leads to megaloblastic anemia caused by an inability of blood cell precursors to synthesize DNA and, therefore, to divide. This leads to large, partially replicated cells being released into the blood to attempt to replenish the cells that have died. Folate deficiencies also have been linked to an increased incidence of neural tube defects, such as spina bifida, in mothers who become pregnant while folate deficient.",True,Remethylation of homocysteine,,,,
819ac457-6fd2-4a88-969d-bc5cd1322e08,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Transsulfuration pathway,False,Transsulfuration pathway,,,,
735cc535-6eaa-48c6-a924-3d529dfb186c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Further metabolism of homocysteine provides the sulfur atom for the synthesis of cysteine. In this two-step process, homocysteine first reacts with serine to form cystathionine. This is followed by cleavage of cystathionine, which yields cysteine and α-ketobutyrate. The first reaction in this sequence, catalyzed by cystathionine β-synthase, is inhibited by cysteine. Thus, methionine, via homocysteine, is not used for cysteine synthesis unless the levels of cysteine in the body are lower than required for its metabolic functions. An adequate dietary supply of cysteine, therefore, can “spare” (or reduce) the dietary requirement for methionine (figure 8.6).",True,Transsulfuration pathway,Figure 8.6,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
735cc535-6eaa-48c6-a924-3d529dfb186c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Further metabolism of homocysteine provides the sulfur atom for the synthesis of cysteine. In this two-step process, homocysteine first reacts with serine to form cystathionine. This is followed by cleavage of cystathionine, which yields cysteine and α-ketobutyrate. The first reaction in this sequence, catalyzed by cystathionine β-synthase, is inhibited by cysteine. Thus, methionine, via homocysteine, is not used for cysteine synthesis unless the levels of cysteine in the body are lower than required for its metabolic functions. An adequate dietary supply of cysteine, therefore, can “spare” (or reduce) the dietary requirement for methionine (figure 8.6).",True,Transsulfuration pathway,Figure 8.6,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
a5db95d0-9f66-451e-922d-9fd38b7ae21d,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,Consequences of elevated homocysteine,False,Consequences of elevated homocysteine,,,,
5003e133-d1cb-4e2c-9660-fcb3c6cfad76,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Homocysteine levels can accumulate in several ways, which are related to both folic acid and vitamin B12 metabolism. As SAM is constantly being used as a methyl donor, this results in a consistent production of SAH. Consequently, this leads to constant production of homocysteine. The homocysteine produced can be either remethylated to methionine or condensed with serine to form cystathionine. The major pathway of homocysteine metabolism is remethylation by N5-methyl-FH4, which requires vitamin B12. The liver also contains a second pathway in which betaine (a degradation product of choline) can donate a methyl group to homocysteine to form methionine, but this is a minor pathway. The conversion of homocysteine to cystathionine requires pyridoxal phosphate (PLP). Thus, if an individual is deficient in vitamin B12, the conversion of homocysteine to methionine by the major route is inhibited. This directs homocysteine to produce cystathionine, which eventually produces cysteine. Homocysteine also accumulates in the blood if a mutation is present in the enzyme that converts N5,N10-methylene-FH4 to N5-methyl-FH4. When this occurs, the levels of N5-methyl-FH4 are too low to allow homocysteine to be converted to methionine. The loss of this pathway, coupled with the feedback inhibition by cysteine on cystathionine formation, also leads to elevated homocysteine levels in the blood. A third way in which serum homocysteine levels can be elevated is by a mutated cystathionine β-synthase or a deficiency in vitamin B6, the required cofactor for that enzyme. These defects block the ability of homocysteine to be converted to cystathionine, and the homocysteine that does accumulate cannot all be accommodated by conversion to methionine. Thus, an accumulation of homocysteine results.",True,Consequences of elevated homocysteine,,,,
62c22890-e155-41ea-8498-15dc25ffe987,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,8.1 References and resources,True,Consequences of elevated homocysteine,,,,
fb96ecd8-d9c2-4b59-bff8-870ace318914,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 20: Amino Acid Degradation and Synthesis, Chapter 21: Conversion of Amino Acids to Specialized Products.",True,Consequences of elevated homocysteine,,,,
c8101727-ff51-479b-861a-54b6b1dda56b,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 69, 83–85.",True,Consequences of elevated homocysteine,,,,
965ec5ed-7866-4658-ad42-a33aac9f6534,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 37: Synthesis and Degradation of Amino Acids, Chapter 39: Tetrahydrofolate, Vitamin B12, and S-Adenosylmethionine.",True,Consequences of elevated homocysteine,,,,
e062e86e-f609-45ba-8e59-b49ed1d9353c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.1 Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria. 2021. https://archive.org/details/8.1-new. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.1,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
e062e86e-f609-45ba-8e59-b49ed1d9353c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.1 Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria. 2021. https://archive.org/details/8.1-new. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.1,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
9a1a8053-4389-41be-b5dd-145944e06f1d,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.2 Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria or tyrosinemia. 2021. https://archive.org/details/8.2_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.2,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
9a1a8053-4389-41be-b5dd-145944e06f1d,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.2 Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria or tyrosinemia. 2021. https://archive.org/details/8.2_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.2,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
c5e9ab4e-d8af-4b86-bbd1-cf6460b1d47b,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.3 Metabolism of tryptophan to melatonin. 2021. https://archive.org/details/8.3_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.3,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
c5e9ab4e-d8af-4b86-bbd1-cf6460b1d47b,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.3 Metabolism of tryptophan to melatonin. 2021. https://archive.org/details/8.3_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.3,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
baf48adc-1d1f-498b-a479-b1d3bbaaa5dd,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.4 Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA. 2021. https://archive.org/details/8.4_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.4,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
baf48adc-1d1f-498b-a479-b1d3bbaaa5dd,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.4 Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA. 2021. https://archive.org/details/8.4_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.4,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
4d310e95-ff81-4817-bde5-e7743b615220,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.5 Metabolism of branched chain amino acids. Deficiencies in BCKAD can result in the presentation of Maple Syrup Urine Disease. 2021. https://archive.org/details/8.5_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.5,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.5-scaled.jpg,Figure 8.5: Metabolism of branched-chain amino acids. Deficiencies in branched-chain keto acid dehydrogenase (BCKAD) can result in the presentation of maple syrup urine disease.
4d310e95-ff81-4817-bde5-e7743b615220,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.5 Metabolism of branched chain amino acids. Deficiencies in BCKAD can result in the presentation of Maple Syrup Urine Disease. 2021. https://archive.org/details/8.5_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.5,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.5-scaled.jpg,Figure 8.5: Metabolism of branched-chain amino acids. Deficiencies in branched-chain keto acid dehydrogenase (BCKAD) can result in the presentation of maple syrup urine disease.
c48972d2-5a7c-4659-a8eb-e7288054de8c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.6 Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine. 2021. https://archive.org/details/8.6_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.6,8.1 Amino Acid Metabolism and Specialized Products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
c48972d2-5a7c-4659-a8eb-e7288054de8c,https://pressbooks.lib.vt.edu/cellbio/,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/cellbio/chapter/amino-acid-metabolism-and-heritable-disorders-of-degradation/,"Grey, Kindred, Figure 8.6 Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine. 2021. https://archive.org/details/8.6_20210926. CC BY 4.0.",True,Consequences of elevated homocysteine,Figure 8.6,8. Amino Acid Metabolism and Heritable Disorders of Degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
397a86ba-6bc9-4d73-b9dc-6885d7985219,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,monosphosphate,False,monosphosphate,,,,
14bfcd49-41a8-4da1-a08c-13562c5d81db,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Oxidative and nonoxidative functions,False,Oxidative and nonoxidative functions,,,,
b0e54d27-17fc-4590-956c-ad9c1593e234,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"There are two parts of the pathway that are distinct and can be regulated independently. The first phase, or oxidative phase, consists of two irreversible oxidations that produce NADPH. As noted above, NADPH is required for reductive detoxification and fatty acid synthesis. (NADPH is not oxidized in the ETC.) In the red blood cell, this is extremely important as the PPP pathway provides the only source of NADPH. NADPH is essential to maintain sufficient levels of reduced glutathione in the red blood cell. Glutathione is a tripeptide commonly used in tissues to detoxify free radicals and reduce cellular oxidation.",True,Oxidative and nonoxidative functions,,,,
892e0996-4fc2-4d34-8935-7b4af306730f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
892e0996-4fc2-4d34-8935-7b4af306730f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
892e0996-4fc2-4d34-8935-7b4af306730f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
3039684a-e284-46bb-bab9-1a7a4549c5b4,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,nonoxidative,False,nonoxidative,,,,
2644fd85-575f-4d90-89dc-377757a76399,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Any compounds unused by the nonoxidative pathway will eventually be converted to fructose 6-phosphate or glyceraldehyde 3-phosphate, both of which will re-enter the glycolytic pathway (figures 7.1 and 7.2).",True,nonoxidative,,,,
6128e8aa-0bf7-4131-9221-e348311bd56f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Regulation of the pentose phosphate pathway,False,Regulation of the pentose phosphate pathway,,,,
f9ca581e-2fc4-4113-bd70-bbd80939deeb,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The key regulatory enzyme for the pentose phosphate pathway is within the oxidative portion. Glucose 6-phosphate dehydrogenase oxidizes glucose 6-phosphate to 6-phosphogluconolactone, and is regulated by negative feedback. In this two-step reaction NADPH is also produced, and high levels of NADPH will inhibit the activity of glucose 6-phosphate dehydrogenase. This ensures NADPH is only generated as needed by the cell; this is the primary regulatory mechanism within the pathway.",True,Regulation of the pentose phosphate pathway,,,,
00b1d987-90dc-41f9-aa60-3fe9fc7b90cc,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
00b1d987-90dc-41f9-aa60-3fe9fc7b90cc,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
00b1d987-90dc-41f9-aa60-3fe9fc7b90cc,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
db5ed125-3b58-4b0b-bd90-b47b3abff61b,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Requirement of the pentose phosphate pathway in RBCs,False,Requirement of the pentose phosphate pathway in RBCs,,,,
d4a8e0d7-14de-4ec0-9e57-490a8cfb7b45,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
d4a8e0d7-14de-4ec0-9e57-490a8cfb7b45,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
d4a8e0d7-14de-4ec0-9e57-490a8cfb7b45,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
6a5a3f6a-390c-4c2e-84d9-2cb2800cb1b7,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,RBCs,False,RBCs,,,,
88776739-a963-4fcf-8f3a-95d57868500d,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
88776739-a963-4fcf-8f3a-95d57868500d,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
88776739-a963-4fcf-8f3a-95d57868500d,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
d78ec241-fd3c-4ace-a3f3-f4784471b4e1,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Summary of pathway regulation,False,Summary of pathway regulation,,,,
fb88e68b-0221-4412-9b06-56553062ebb5,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Table 7.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
aec2819a-a20f-441e-8bb9-ac1a9c244b9c,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,7.1 References and resources,True,Summary of pathway regulation,,,,
6b3b2e3a-d57d-416e-9a30-e88c5f4a7b8a,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 13: Pentose Phosphate Pathway and NAPDH, Chapter 22: Nucleotide Metabolism.",True,Summary of pathway regulation,,,,
9d5c48f7-a337-45b3-9591-0b2ecb659d51,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 35–37, 79.",True,Summary of pathway regulation,,,,
2037d387-961d-463e-9059-7136f0139c90,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 27: Pentose Phosphate Pathway, Chapter 39: Purine and Pyrimidine Synthesis.",True,Summary of pathway regulation,,,,
27e8ece4-e5df-4f85-9255-e613a836d416,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
27e8ece4-e5df-4f85-9255-e613a836d416,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
27e8ece4-e5df-4f85-9255-e613a836d416,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
66cea327-3e3b-44c7-9cc6-e1a3d1e25c21,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
66cea327-3e3b-44c7-9cc6-e1a3d1e25c21,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
66cea327-3e3b-44c7-9cc6-e1a3d1e25c21,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
519c386e-ebb1-48ee-bd20-6515b2fa93d1,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
519c386e-ebb1-48ee-bd20-6515b2fa93d1,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
519c386e-ebb1-48ee-bd20-6515b2fa93d1,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
1346248e-2709-4a17-9ba1-a6bccf35cca0,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,7.2 Nucleotide Synthesis,True,Summary of pathway regulation,,,,
396185b1-1dbc-427b-acb3-35b6417eebff,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
396185b1-1dbc-427b-acb3-35b6417eebff,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
396185b1-1dbc-427b-acb3-35b6417eebff,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
3946bf72-a982-47ba-b4e5-bc6324d8c5f3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
3946bf72-a982-47ba-b4e5-bc6324d8c5f3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
3946bf72-a982-47ba-b4e5-bc6324d8c5f3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
fc7741dd-78b4-488f-943b-2d86b7c23ddc,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Nucleotide synthesis will be described below, but one of the fundamental requirements of the synthesis of either purines or pyrimidines is the need for a five-carbon sugar (ribose). This sugar is generated through glucose oxidation via the pentose phosphate pathway.",True,Summary of pathway regulation,,,,
c4d80872-6249-48af-837c-c13415097e87,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"For purines synthesis, the base is synthesized and attached to the sugar, while for pyrimidine synthesis, the sugar group is added after the base is produced. In either case, ribose is the added sugar, and this must be converted to the deoxyribose form before the bases can be used for DNA synthesis.",True,Summary of pathway regulation,,,,
af504975-77d8-44f6-9c73-29321b230197,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Conversion of ribose to deoxyribose nucleotides,False,Conversion of ribose to deoxyribose nucleotides,,,,
9834eeb0-f220-4e02-ad9e-f55d3cd00939,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"All bases are synthesized in the ribose form and used directly for transcription. They can be converted to the deoxy form, which is needed for DNA replication. The enzyme, ribonucleotide reductase, converts the diphosphate form of a ribose base to the deoxybase form. The enzyme has two sites for regulation: an enzyme activity site and a substrate specificity site. The enzyme activity site must have ATP/ADP bound for the enzyme to be active, while the substrate specificity site will bind different nucleotides influencing the enzyme substrate preference, therefore altering which base is being acted upon depending on cellular needs.",True,Conversion of ribose to deoxyribose nucleotides,,,,
010d816e-3634-4dfd-8e84-be8665391c1d,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,deoxybase,False,deoxybase,,,,
703fab2a-61ab-4f56-8f2d-9bbe9b02f8b1,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Generation of 5-phosphoribosyl-1-phosphate (PRPP),False,Generation of 5-phosphoribosyl-1-phosphate (PRPP),,,,
b6aca37f-cfe6-4c57-a4dc-a48830ec8132,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
b6aca37f-cfe6-4c57-a4dc-a48830ec8132,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
b6aca37f-cfe6-4c57-a4dc-a48830ec8132,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
057818a5-f187-4257-9f4e-34d68af059f7,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Regulation of PRPP synthase,False,Regulation of PRPP synthase,,,,
08424222-b298-46c3-a405-2c7f5891aa08,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The enzyme, PRPP synthetase, is activated by Pi (inorganic phosphate) and inhibited by the purine bases adenine and guanine.",True,Regulation of PRPP synthase,,,,
db897b3d-e2c1-4087-86f4-dc763bbfc14d,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Synthesis of purines,False,Synthesis of purines,,,,
6f5295f5-80c1-47c5-aa93-d8867fe62de9,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
6f5295f5-80c1-47c5-aa93-d8867fe62de9,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
6f5295f5-80c1-47c5-aa93-d8867fe62de9,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
c32d7346-8cdc-47c7-b269-32e337cb9efb,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,TH4,False,TH4,,,,
ebe969c3-463a-43dd-93b0-a09f441e78c1,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,5ʼphosphoribosylamine,False,5ʼphosphoribosylamine,,,,
82f35f50-1af8-4bb4-9384-521819eb1723,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,phosphoribosylpyrophate,False,phosphoribosylpyrophate,,,,
2f286e15-cfbe-4efb-bcd6-9c46b9913b36,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,amidotransferase,False,amidotransferase,,,,
f06db364-ac35-4e6b-bd1f-d8d7a97e0db3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,GPAT,False,GPAT,,,,
8447f87d-1470-45cb-bc9b-cd008fae35ba,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Regulation of purine synthesis,False,Regulation of purine synthesis,,,,
483d7939-babe-4e1e-9292-5462b44a8f2f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The regulatory enzyme GPAT is allosterically activated by PRPP and inhibited by IMP, AMP, and GMP. All three must be present to inhibit activity of this enzyme.",True,Regulation of purine synthesis,,,,
079983b5-c0b9-453d-b622-551c1b672f8d,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Degradation of purines,False,Degradation of purines,,,,
2db2e660-1c37-4f4e-8ce1-fa92f6b103c6,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Like amino acids, nucleotides contain nitrogen and must be degraded in a manner that allows for proper nitrogen disposal either through the urea cycle or by the synthesis of a nontoxic compound.",True,Degradation of purines,,,,
a81e5c48-c7b2-4ee4-9473-92a693b3e62c,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
a81e5c48-c7b2-4ee4-9473-92a693b3e62c,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
a81e5c48-c7b2-4ee4-9473-92a693b3e62c,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
2d94c725-7aa2-4f84-a09a-e818f8530169,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
2d94c725-7aa2-4f84-a09a-e818f8530169,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
2d94c725-7aa2-4f84-a09a-e818f8530169,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
bf7465e5-d5b9-45f5-a31a-e427277b07ad,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,underexcretion,False,underexcretion,,,,
45674bd5-99a6-43ba-840d-c077560408df,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Secondary hyperuricemia is also seen in individuals with myeloproliferative disorders undergoing therapy where there is excess cellular turnover (cell lysis leads to an accumulation of nucleotides) or in cases of Von Gierke disease or fructose intolerance, which increases substrate for PRPP synthesis. Xanthine oxidase inhibitors, such as allopurinol, are used as part of the management of gout.",True,underexcretion,,,,
a094cd5b-6121-4006-8a1e-8dfb84974f6c,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Salvage of purines,False,Salvage of purines,,,,
39664de6-7ecf-4a24-96f5-a92f6809b6e3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
39664de6-7ecf-4a24-96f5-a92f6809b6e3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
39664de6-7ecf-4a24-96f5-a92f6809b6e3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
40fcdaea-3d9f-4beb-8a3a-42097f8b2f4e,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,APRT,False,APRT,,,,
e5e5d97e-6fc1-4fd9-844e-89f6bf85f52d,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,rephosphorylated,False,rephosphorylated,,,,
a1ddebdc-7316-4bef-887a-9da7af9a20c0,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Synthesis of pyrimidines,False,Synthesis of pyrimidines,,,,
681d9f3c-b496-4486-970e-dbfc9cafc734,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
681d9f3c-b496-4486-970e-dbfc9cafc734,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
681d9f3c-b496-4486-970e-dbfc9cafc734,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
b1bf9d85-f06d-41e5-b0c9-20e7bfa39dfc,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
b1bf9d85-f06d-41e5-b0c9-20e7bfa39dfc,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
b1bf9d85-f06d-41e5-b0c9-20e7bfa39dfc,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
6699d8e0-db95-4b6c-b7d3-72ca390dc812,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Defects in pyrimidine synthesis most commonly present as an increase in orotic acid in the urine. Deficiencies in the attachment of PRPP to orotate (or the decarboxylation of orotate monosphosphate) can result in the accumulation of orotic acid; similarly deficiencies of the urea cycle, which lead to an accumulation of carbamoyl phosphate, can increase flux through pyrimidine synthesis and cause an increase in orotic acid. Accumulation of orotic acid is used as a clinical indicator of pyrimidine deficiencies or deficiencies in the urea cycle.",True,Synthesis of pyrimidines,,,,
1d9edae7-fbbc-4855-8b94-e0fb5da75216,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Regulation of pyrimidine synthesis,False,Regulation of pyrimidine synthesis,,,,
cdf9a5ec-e390-446f-a023-ab520f37f3d1,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,The reaction catalyzed by CSPII is the regulatory step in the pathway and is activated by PRPP and ATP and inhibited by UTP.,True,Regulation of pyrimidine synthesis,,,,
5928dd45-c995-4707-a7f2-17c4deb0cb44,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Clinical importance of folate cycle inhibitors and synthesis of dTMP,False,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
15599fc7-273f-4c10-92db-e3d5ee5909e3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
15599fc7-273f-4c10-92db-e3d5ee5909e3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
15599fc7-273f-4c10-92db-e3d5ee5909e3,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
d8321c1a-07c2-41d0-8b9c-01bfccd9083b,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,Table 7.2: Summary of pathway regulation.,True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
47657f91-15ef-4b6f-a069-5aec71d3c498,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,7.2 References and resources,True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
9a32f8f5-95a2-4ed3-92ee-a53a49319730,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
9a32f8f5-95a2-4ed3-92ee-a53a49319730,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
9a32f8f5-95a2-4ed3-92ee-a53a49319730,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
c0837ec7-f830-4ae7-b000-215b3b31f951,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
c0837ec7-f830-4ae7-b000-215b3b31f951,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
c0837ec7-f830-4ae7-b000-215b3b31f951,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
a6924b41-c8f7-4a27-adea-ca57e00891ef,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
a6924b41-c8f7-4a27-adea-ca57e00891ef,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
a6924b41-c8f7-4a27-adea-ca57e00891ef,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
c835e108-61cc-4430-a35b-fd575d7b0497,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
c835e108-61cc-4430-a35b-fd575d7b0497,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
c835e108-61cc-4430-a35b-fd575d7b0497,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
6abc310d-e5fd-4d65-a3ad-0b24c5062e58,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
6abc310d-e5fd-4d65-a3ad-0b24c5062e58,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
6abc310d-e5fd-4d65-a3ad-0b24c5062e58,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
d7ac3650-56b9-4714-997e-3bcb1f07736f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
d7ac3650-56b9-4714-997e-3bcb1f07736f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
d7ac3650-56b9-4714-997e-3bcb1f07736f,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
273cadd0-50bb-4fd7-9a44-94dda8b743c4,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
273cadd0-50bb-4fd7-9a44-94dda8b743c4,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
273cadd0-50bb-4fd7-9a44-94dda8b743c4,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
7b5e44d8-e86c-4763-8946-93ce2f3fe5df,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
7b5e44d8-e86c-4763-8946-93ce2f3fe5df,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
7b5e44d8-e86c-4763-8946-93ce2f3fe5df,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
df611471-e98d-464d-b982-a0030a8eea30,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
df611471-e98d-464d-b982-a0030a8eea30,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
df611471-e98d-464d-b982-a0030a8eea30,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
0869898c-2cbd-4d9f-8f7f-f149e30c7855,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
0869898c-2cbd-4d9f-8f7f-f149e30c7855,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
0869898c-2cbd-4d9f-8f7f-f149e30c7855,https://pressbooks.lib.vt.edu/cellbio/,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-2,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
f31b82ac-67ac-4cea-8cc8-e9e7a8d05dbf,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,monosphosphate,False,monosphosphate,,,,
9b2ddd5b-1bb0-4ae6-ade1-e9c7873a5def,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Oxidative and nonoxidative functions,False,Oxidative and nonoxidative functions,,,,
9078d5a1-33a3-46d4-a934-64b87ca18721,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"There are two parts of the pathway that are distinct and can be regulated independently. The first phase, or oxidative phase, consists of two irreversible oxidations that produce NADPH. As noted above, NADPH is required for reductive detoxification and fatty acid synthesis. (NADPH is not oxidized in the ETC.) In the red blood cell, this is extremely important as the PPP pathway provides the only source of NADPH. NADPH is essential to maintain sufficient levels of reduced glutathione in the red blood cell. Glutathione is a tripeptide commonly used in tissues to detoxify free radicals and reduce cellular oxidation.",True,Oxidative and nonoxidative functions,,,,
8d71a774-d5c3-42a2-baa9-793e4b3090e1,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
8d71a774-d5c3-42a2-baa9-793e4b3090e1,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
8d71a774-d5c3-42a2-baa9-793e4b3090e1,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
8fd00be4-12ba-4215-8036-bce51dae11d1,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,nonoxidative,False,nonoxidative,,,,
5968c090-e151-44ba-8967-1a3b03dd658e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Any compounds unused by the nonoxidative pathway will eventually be converted to fructose 6-phosphate or glyceraldehyde 3-phosphate, both of which will re-enter the glycolytic pathway (figures 7.1 and 7.2).",True,nonoxidative,,,,
279f03f8-9f56-4824-9c80-0ee207168d9d,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Regulation of the pentose phosphate pathway,False,Regulation of the pentose phosphate pathway,,,,
19cf7ced-edbd-490e-a3bb-b238fbfea001,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The key regulatory enzyme for the pentose phosphate pathway is within the oxidative portion. Glucose 6-phosphate dehydrogenase oxidizes glucose 6-phosphate to 6-phosphogluconolactone, and is regulated by negative feedback. In this two-step reaction NADPH is also produced, and high levels of NADPH will inhibit the activity of glucose 6-phosphate dehydrogenase. This ensures NADPH is only generated as needed by the cell; this is the primary regulatory mechanism within the pathway.",True,Regulation of the pentose phosphate pathway,,,,
c997aa50-9950-4e03-8a5b-254eb776f65d,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
c997aa50-9950-4e03-8a5b-254eb776f65d,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
c997aa50-9950-4e03-8a5b-254eb776f65d,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
01a7c5f1-ce8a-4938-9d3f-a2e3f3c5e3e7,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Requirement of the pentose phosphate pathway in RBCs,False,Requirement of the pentose phosphate pathway in RBCs,,,,
df1ee629-8b62-40a7-97ab-9604d07b46c2,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
df1ee629-8b62-40a7-97ab-9604d07b46c2,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
df1ee629-8b62-40a7-97ab-9604d07b46c2,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
386e2973-9f5a-458f-a4f6-6ae5d61dd956,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,RBCs,False,RBCs,,,,
137e3606-854d-4f88-9158-dc00457b200e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
137e3606-854d-4f88-9158-dc00457b200e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
137e3606-854d-4f88-9158-dc00457b200e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
f7fade60-824b-4b5a-b71b-4d866db4e801,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Summary of pathway regulation,False,Summary of pathway regulation,,,,
1cab6907-f610-4e0c-ae78-07a566acff3c,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Table 7.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
3d97f2c2-dee4-471d-bc5b-762dc582db9b,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,7.1 References and resources,True,Summary of pathway regulation,,,,
c47115cd-51c8-4b9e-91e1-5e86c91d91f9,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 13: Pentose Phosphate Pathway and NAPDH, Chapter 22: Nucleotide Metabolism.",True,Summary of pathway regulation,,,,
1c7ce7e6-3ecf-4a50-a963-5b4ba083efbc,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 35–37, 79.",True,Summary of pathway regulation,,,,
5287dcb9-933d-4898-960e-d8f7e447891b,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 27: Pentose Phosphate Pathway, Chapter 39: Purine and Pyrimidine Synthesis.",True,Summary of pathway regulation,,,,
b81f36eb-e0d6-426b-b71e-f63e9524162f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
b81f36eb-e0d6-426b-b71e-f63e9524162f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
b81f36eb-e0d6-426b-b71e-f63e9524162f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
04e78c0c-ccd1-4f96-9a12-d430243d315f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
04e78c0c-ccd1-4f96-9a12-d430243d315f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
04e78c0c-ccd1-4f96-9a12-d430243d315f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
8989dfe7-356f-43dc-a78b-2da8c15dcb4a,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
8989dfe7-356f-43dc-a78b-2da8c15dcb4a,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
8989dfe7-356f-43dc-a78b-2da8c15dcb4a,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
a311022d-fb3d-496c-bb44-0789a6b61b98,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,7.2 Nucleotide Synthesis,True,Summary of pathway regulation,,,,
e639d400-0d6c-494c-b5ad-c4a8961477ef,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
e639d400-0d6c-494c-b5ad-c4a8961477ef,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
e639d400-0d6c-494c-b5ad-c4a8961477ef,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
f923b072-7d04-4878-b574-7391621532c8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
f923b072-7d04-4878-b574-7391621532c8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
f923b072-7d04-4878-b574-7391621532c8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
8fd22348-d855-4b5d-8c22-6f1128375a73,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Nucleotide synthesis will be described below, but one of the fundamental requirements of the synthesis of either purines or pyrimidines is the need for a five-carbon sugar (ribose). This sugar is generated through glucose oxidation via the pentose phosphate pathway.",True,Summary of pathway regulation,,,,
04cd2ee3-9c99-4cf0-a368-0352c48664e4,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"For purines synthesis, the base is synthesized and attached to the sugar, while for pyrimidine synthesis, the sugar group is added after the base is produced. In either case, ribose is the added sugar, and this must be converted to the deoxyribose form before the bases can be used for DNA synthesis.",True,Summary of pathway regulation,,,,
12a850ef-9684-40e3-a814-2a2202b1c1ad,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Conversion of ribose to deoxyribose nucleotides,False,Conversion of ribose to deoxyribose nucleotides,,,,
288fe93f-5ee9-4677-ab5b-f005cfcfdb26,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"All bases are synthesized in the ribose form and used directly for transcription. They can be converted to the deoxy form, which is needed for DNA replication. The enzyme, ribonucleotide reductase, converts the diphosphate form of a ribose base to the deoxybase form. The enzyme has two sites for regulation: an enzyme activity site and a substrate specificity site. The enzyme activity site must have ATP/ADP bound for the enzyme to be active, while the substrate specificity site will bind different nucleotides influencing the enzyme substrate preference, therefore altering which base is being acted upon depending on cellular needs.",True,Conversion of ribose to deoxyribose nucleotides,,,,
8e36c210-7b70-4a4a-9b97-bd75655b7876,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,deoxybase,False,deoxybase,,,,
e4d32ffd-b8a9-4513-8379-d1e51227a285,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Generation of 5-phosphoribosyl-1-phosphate (PRPP),False,Generation of 5-phosphoribosyl-1-phosphate (PRPP),,,,
8303a8d3-4d77-4056-8c88-be16aac981a8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
8303a8d3-4d77-4056-8c88-be16aac981a8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
8303a8d3-4d77-4056-8c88-be16aac981a8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
bc4c3ab0-eeaf-4e62-8644-d3d09d99276c,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Regulation of PRPP synthase,False,Regulation of PRPP synthase,,,,
60c7c52d-2b73-4453-ae7a-d697fccab00a,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The enzyme, PRPP synthetase, is activated by Pi (inorganic phosphate) and inhibited by the purine bases adenine and guanine.",True,Regulation of PRPP synthase,,,,
fbe2d033-f17e-4a8c-b4af-d31cabe727a5,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Synthesis of purines,False,Synthesis of purines,,,,
d4c4a0ee-21d9-4201-81c8-f3e512f58675,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
d4c4a0ee-21d9-4201-81c8-f3e512f58675,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
d4c4a0ee-21d9-4201-81c8-f3e512f58675,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
baa829ca-160b-4542-a2d2-7b35ea8e8945,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,TH4,False,TH4,,,,
e190706d-dd72-4283-b497-1bf6e542f0ce,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,5ʼphosphoribosylamine,False,5ʼphosphoribosylamine,,,,
9c64db4b-15e5-423b-9e20-41eda56c5385,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,phosphoribosylpyrophate,False,phosphoribosylpyrophate,,,,
e31fde60-562f-483a-960b-e99838ce1167,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,amidotransferase,False,amidotransferase,,,,
e66a6715-6d93-4d23-92ca-cd2cc462f82d,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,GPAT,False,GPAT,,,,
3a26400b-afa2-461e-ada6-4ccb32d4b6ce,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Regulation of purine synthesis,False,Regulation of purine synthesis,,,,
62f6b7fd-2254-4bc1-8795-c843b1178e7e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The regulatory enzyme GPAT is allosterically activated by PRPP and inhibited by IMP, AMP, and GMP. All three must be present to inhibit activity of this enzyme.",True,Regulation of purine synthesis,,,,
790c3dbf-d3dd-4113-934b-936e22f24f34,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Degradation of purines,False,Degradation of purines,,,,
b5b55792-6691-431c-a3cd-39d288736bc6,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Like amino acids, nucleotides contain nitrogen and must be degraded in a manner that allows for proper nitrogen disposal either through the urea cycle or by the synthesis of a nontoxic compound.",True,Degradation of purines,,,,
91c3622e-d319-4d85-a77d-2d42ffcda7bc,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
91c3622e-d319-4d85-a77d-2d42ffcda7bc,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
91c3622e-d319-4d85-a77d-2d42ffcda7bc,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
322eb914-e534-480c-b4ab-c77f7415bfb7,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
322eb914-e534-480c-b4ab-c77f7415bfb7,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
322eb914-e534-480c-b4ab-c77f7415bfb7,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
846826d4-72e1-44f1-b88e-7d8449954cc0,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,underexcretion,False,underexcretion,,,,
c8e68b65-34fa-4e45-847a-b0ff0e184d4b,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Secondary hyperuricemia is also seen in individuals with myeloproliferative disorders undergoing therapy where there is excess cellular turnover (cell lysis leads to an accumulation of nucleotides) or in cases of Von Gierke disease or fructose intolerance, which increases substrate for PRPP synthesis. Xanthine oxidase inhibitors, such as allopurinol, are used as part of the management of gout.",True,underexcretion,,,,
6aa14b8d-c657-4227-8b44-51b10ce25b11,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Salvage of purines,False,Salvage of purines,,,,
0c5a441c-b213-43a3-829a-efe04505f658,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
0c5a441c-b213-43a3-829a-efe04505f658,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
0c5a441c-b213-43a3-829a-efe04505f658,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
d15b331b-6ff4-40ed-9e89-c64f1e6bdc92,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,APRT,False,APRT,,,,
26ff9fa2-3020-490a-b5a4-f4d69ecc3aa7,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,rephosphorylated,False,rephosphorylated,,,,
b65a152f-b1d5-4ca3-b08b-96afe7bda6b7,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Synthesis of pyrimidines,False,Synthesis of pyrimidines,,,,
fb3cab62-8800-49fb-864c-e57c2eff118f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
fb3cab62-8800-49fb-864c-e57c2eff118f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
fb3cab62-8800-49fb-864c-e57c2eff118f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
db0b5864-38a6-43f7-99bb-cbb241980073,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
db0b5864-38a6-43f7-99bb-cbb241980073,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
db0b5864-38a6-43f7-99bb-cbb241980073,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
d1b0ec4e-8b22-4129-a335-87da6e38c95b,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Defects in pyrimidine synthesis most commonly present as an increase in orotic acid in the urine. Deficiencies in the attachment of PRPP to orotate (or the decarboxylation of orotate monosphosphate) can result in the accumulation of orotic acid; similarly deficiencies of the urea cycle, which lead to an accumulation of carbamoyl phosphate, can increase flux through pyrimidine synthesis and cause an increase in orotic acid. Accumulation of orotic acid is used as a clinical indicator of pyrimidine deficiencies or deficiencies in the urea cycle.",True,Synthesis of pyrimidines,,,,
efd734be-c4af-4bc3-b14a-50e53400b633,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Regulation of pyrimidine synthesis,False,Regulation of pyrimidine synthesis,,,,
17cda780-5ef9-4870-92d4-6faff7fd35ee,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,The reaction catalyzed by CSPII is the regulatory step in the pathway and is activated by PRPP and ATP and inhibited by UTP.,True,Regulation of pyrimidine synthesis,,,,
7b261aa2-3c89-41cd-acc8-f11cb4fa3a82,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Clinical importance of folate cycle inhibitors and synthesis of dTMP,False,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
04de751d-72b7-4c69-9292-80038371b37e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
04de751d-72b7-4c69-9292-80038371b37e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
04de751d-72b7-4c69-9292-80038371b37e,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
5bd1f216-215e-44f9-95be-7d7642c43424,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,Table 7.2: Summary of pathway regulation.,True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
272b529e-6fb7-493d-a61e-a1a3f353f0b0,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,7.2 References and resources,True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
630f4e00-fd04-4b93-8048-9a4412218394,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
630f4e00-fd04-4b93-8048-9a4412218394,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
630f4e00-fd04-4b93-8048-9a4412218394,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
c84c8474-c745-49e8-aa75-9fd6954230a1,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
c84c8474-c745-49e8-aa75-9fd6954230a1,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
c84c8474-c745-49e8-aa75-9fd6954230a1,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
b67056d8-49df-4ce7-91c2-e520bbf80232,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
b67056d8-49df-4ce7-91c2-e520bbf80232,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
b67056d8-49df-4ce7-91c2-e520bbf80232,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
fd2e35eb-0bb2-4e08-8dce-52f23ed4f50f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
fd2e35eb-0bb2-4e08-8dce-52f23ed4f50f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
fd2e35eb-0bb2-4e08-8dce-52f23ed4f50f,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
acd18275-6f7c-481d-b877-74b215dcfe0a,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
acd18275-6f7c-481d-b877-74b215dcfe0a,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
acd18275-6f7c-481d-b877-74b215dcfe0a,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
a3148c9f-b6f9-418c-abb5-3007210869f8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
a3148c9f-b6f9-418c-abb5-3007210869f8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
a3148c9f-b6f9-418c-abb5-3007210869f8,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
431d8600-71f7-48ac-bcce-93d27d31b9ff,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
431d8600-71f7-48ac-bcce-93d27d31b9ff,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
431d8600-71f7-48ac-bcce-93d27d31b9ff,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
32e9d433-0efc-41ec-8c05-82bed9daa93b,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
32e9d433-0efc-41ec-8c05-82bed9daa93b,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
32e9d433-0efc-41ec-8c05-82bed9daa93b,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
3526b211-19ed-4b5d-8319-9157abdb0bee,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
3526b211-19ed-4b5d-8319-9157abdb0bee,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
3526b211-19ed-4b5d-8319-9157abdb0bee,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
77c6b528-ccd7-46c2-8f59-d03c3bdce241,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
77c6b528-ccd7-46c2-8f59-d03c3bdce241,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
77c6b528-ccd7-46c2-8f59-d03c3bdce241,https://pressbooks.lib.vt.edu/cellbio/,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/#chapter-72-section-1,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
9565343a-7108-48b2-8f0a-07398103bfbf,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,monosphosphate,False,monosphosphate,,,,
29adef45-350e-4eae-a90d-bd1adc815b08,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Oxidative and nonoxidative functions,False,Oxidative and nonoxidative functions,,,,
a759a3cc-58f0-4993-ab91-72bba30a8032,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"There are two parts of the pathway that are distinct and can be regulated independently. The first phase, or oxidative phase, consists of two irreversible oxidations that produce NADPH. As noted above, NADPH is required for reductive detoxification and fatty acid synthesis. (NADPH is not oxidized in the ETC.) In the red blood cell, this is extremely important as the PPP pathway provides the only source of NADPH. NADPH is essential to maintain sufficient levels of reduced glutathione in the red blood cell. Glutathione is a tripeptide commonly used in tissues to detoxify free radicals and reduce cellular oxidation.",True,Oxidative and nonoxidative functions,,,,
d17280c6-b210-4560-a0e8-ffb56e4daf8b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
d17280c6-b210-4560-a0e8-ffb56e4daf8b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
d17280c6-b210-4560-a0e8-ffb56e4daf8b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The nonoxidative phase of the pathway allows for the conversion of ribulose 5-phosphate into ribose 5-phosphate, which is needed for nucleotide synthesis (figure 7.1). All of these interconversions in the nonoxidative pathway are reversible and use the enzymes transketolase or transaldolase to move two-carbon or three-carbon units on to other sugar moieties to generate a variety of sugar intermediates. Transketolase requires thiamine pyrophosphate (TPP) as a cofactor. This is of clinical relevance as TPP levels can be measured by addressing the activity of transketolase in a blood sample. A reduction in transketolase activity is an indicator of a thiamine deficiency.",True,Oxidative and nonoxidative functions,Figure 7.1,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
1c3b9628-cf15-4f39-9571-127f548cc41e,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,nonoxidative,False,nonoxidative,,,,
ffda0ad5-ae95-4736-bfd3-0f8db46e870e,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Any compounds unused by the nonoxidative pathway will eventually be converted to fructose 6-phosphate or glyceraldehyde 3-phosphate, both of which will re-enter the glycolytic pathway (figures 7.1 and 7.2).",True,nonoxidative,,,,
2e1229d8-1c80-40c5-a360-7b37debbe235,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Regulation of the pentose phosphate pathway,False,Regulation of the pentose phosphate pathway,,,,
47b73a8d-4dce-4f50-8aa4-d55637d128a9,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The key regulatory enzyme for the pentose phosphate pathway is within the oxidative portion. Glucose 6-phosphate dehydrogenase oxidizes glucose 6-phosphate to 6-phosphogluconolactone, and is regulated by negative feedback. In this two-step reaction NADPH is also produced, and high levels of NADPH will inhibit the activity of glucose 6-phosphate dehydrogenase. This ensures NADPH is only generated as needed by the cell; this is the primary regulatory mechanism within the pathway.",True,Regulation of the pentose phosphate pathway,,,,
29388fa2-b060-411d-ae3c-353639bcb5f1,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
29388fa2-b060-411d-ae3c-353639bcb5f1,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
29388fa2-b060-411d-ae3c-353639bcb5f1,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The nonoxidative phase is not regulated; however, in conditions where there is a high demand for nucleotide production (such as in the case for highly proliferative cells), the nonoxidative part of the pathway can function independently of the oxidative phase to produce ribose 5-phosphate from the glycolytic intermediates fructose 6-phosphate and glyceraldehyde 3-phosphate (figure 7.2).",True,Regulation of the pentose phosphate pathway,Figure 7.2,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
bbbc3034-4aa1-442b-ab06-7bc7e9d51c16,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Requirement of the pentose phosphate pathway in RBCs,False,Requirement of the pentose phosphate pathway in RBCs,,,,
cbb403cb-f1ec-448c-94fc-0a1be6f65581,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
cbb403cb-f1ec-448c-94fc-0a1be6f65581,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
cbb403cb-f1ec-448c-94fc-0a1be6f65581,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The two essential products of this pathway are NADPH and ribose 5-phosphate. NADPH is a high-energy compound often used for reductive biosynthesis as it cannot be oxidized in the ETC. It is also used by many tissues to scavenge (and detoxify) reactive oxygen species (ROS) before causing cellular damage. This is especially important in red blood cells; RBCs lack malic enzyme, making this the only pathway that can generate NADPH. A lack of NADPH in RBCs (such as due to a glucose 6-phosphate dehydrogenase deficiency) can cause excessive hemolysis, leading to the clinical presentation of jaundice (figure 7.3).",True,Requirement of the pentose phosphate pathway in RBCs,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
14d7e5fd-4929-4269-a3ba-dc7268146d52,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,RBCs,False,RBCs,,,,
ca285c77-09b0-44d7-90d7-f3880a3f263b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
ca285c77-09b0-44d7-90d7-f3880a3f263b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
ca285c77-09b0-44d7-90d7-f3880a3f263b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Glutathione (GSH) is a tripeptide compound consisting of glutamate, cysteine, and glycine. It plays a key role in scavenging reactive oxygen species (ROS), which cause both DNA and cellular/protein damage. Reduction of GSH in the red blood cell is done exclusively through a series of oxidation reduction reactions using NADPH. The loss of NADPH in RBCs therefore increases ROS and can lead to hemolysis (figure 7.3).",True,RBCs,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
51fb6582-a94c-4a55-a73b-b4c28c22ed81,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Summary of pathway regulation,False,Summary of pathway regulation,,,,
6c9135f8-1ed6-4540-a183-b2d740deb73b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Table 7.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
962a6b82-d389-4d25-aa06-e1c45edbac09,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,7.1 References and resources,True,Summary of pathway regulation,,,,
40638bb9-1b5b-45d2-a79b-d452ec9d6e52,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 13: Pentose Phosphate Pathway and NAPDH, Chapter 22: Nucleotide Metabolism.",True,Summary of pathway regulation,,,,
a1ddad4d-8020-4a59-8903-4ad7bc573756,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 35–37, 79.",True,Summary of pathway regulation,,,,
05bcc713-2b73-4e4f-b27d-0e5a1599f7b5,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 27: Pentose Phosphate Pathway, Chapter 39: Purine and Pyrimidine Synthesis.",True,Summary of pathway regulation,,,,
20b65f92-2f03-462f-aed6-988cbdd7baf4,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
20b65f92-2f03-462f-aed6-988cbdd7baf4,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
20b65f92-2f03-462f-aed6-988cbdd7baf4,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.2 Pentose pathway and its connection to glycolysis and glutathione synthesis. 2021. https://archive.org/details/7.2_20210926. CC BY 4.0.",True,Summary of pathway regulation,Figure 7.2,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
d408f0e4-cc73-4e94-a229-7f290269e8b9,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
d408f0e4-cc73-4e94-a229-7f290269e8b9,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
d408f0e4-cc73-4e94-a229-7f290269e8b9,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.1 Overview of the pentose phosphate pathway and its interface with glycolysis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 543. Figure 27.1 Overview of the pentose phosphate pathway. 2017.",True,Summary of pathway regulation,Figure 7.1,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
be564236-5990-44a2-ac05-09766e8650b7,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
be564236-5990-44a2-ac05-09766e8650b7,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
be564236-5990-44a2-ac05-09766e8650b7,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.3 NADPH in the red blood cell as a means of reducing glutathione. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 549. Figure 27.7 Hemolysis caused by reactive oxygen species (ROS). 2017.",True,Summary of pathway regulation,Figure 7.3,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
3340dc2f-d89e-430e-a782-9c5821178965,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,7.2 Nucleotide Synthesis,True,Summary of pathway regulation,,,,
12d8227f-4aba-4e16-af4d-4a2260b85514,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
12d8227f-4aba-4e16-af4d-4a2260b85514,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
12d8227f-4aba-4e16-af4d-4a2260b85514,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Nucleotides are the fundamental building blocks essential for the synthesis of DNA and RNA. Each nucleotide contains three functional groups: a sugar, a base, and phosphate (figure 7.4).",True,Summary of pathway regulation,Figure 7.4,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
7bcc0947-60aa-4885-98aa-cdd4531ee0a8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
7bcc0947-60aa-4885-98aa-cdd4531ee0a8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
7bcc0947-60aa-4885-98aa-cdd4531ee0a8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Nucleotides can be divided into two groups: pyrimidines and purines. The family of pyrimidines includes thymine (T), cytosine (C), and uracil (U), which is only incorporated into RNA. These compounds contain a single-ringed nitrogenous base that pairs with a purine nucleotide counterpart. Thymine pairs with adenine forming two hydrogen bonds, in contrast to cytosine, which pairs with guanine to form three hydrogen bonds. Purines, both guanine (G) and adenine (A), are double-ringed structures and more difficult to break down in the body. As such, the salvage pathway for purine metabolism is of importance (figure 7.5).",True,Summary of pathway regulation,Figure 7.5,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
32a8afd5-69ab-491b-8cbc-a4386bd4f43a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Nucleotide synthesis will be described below, but one of the fundamental requirements of the synthesis of either purines or pyrimidines is the need for a five-carbon sugar (ribose). This sugar is generated through glucose oxidation via the pentose phosphate pathway.",True,Summary of pathway regulation,,,,
951880dd-a94b-44eb-81ec-47b451c863fc,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"For purines synthesis, the base is synthesized and attached to the sugar, while for pyrimidine synthesis, the sugar group is added after the base is produced. In either case, ribose is the added sugar, and this must be converted to the deoxyribose form before the bases can be used for DNA synthesis.",True,Summary of pathway regulation,,,,
d41058d9-2449-4d14-9b36-4e44b25554d6,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Conversion of ribose to deoxyribose nucleotides,False,Conversion of ribose to deoxyribose nucleotides,,,,
75b9c615-9c8a-40ea-95f0-badad01d81ce,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"All bases are synthesized in the ribose form and used directly for transcription. They can be converted to the deoxy form, which is needed for DNA replication. The enzyme, ribonucleotide reductase, converts the diphosphate form of a ribose base to the deoxybase form. The enzyme has two sites for regulation: an enzyme activity site and a substrate specificity site. The enzyme activity site must have ATP/ADP bound for the enzyme to be active, while the substrate specificity site will bind different nucleotides influencing the enzyme substrate preference, therefore altering which base is being acted upon depending on cellular needs.",True,Conversion of ribose to deoxyribose nucleotides,,,,
78ec49a3-d05c-4170-82ce-d379942d94b6,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,deoxybase,False,deoxybase,,,,
b9e7f6fa-4374-4b2d-9c91-0c46dd294150,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Generation of 5-phosphoribosyl-1-phosphate (PRPP),False,Generation of 5-phosphoribosyl-1-phosphate (PRPP),,,,
6230e844-84e2-4e54-ae6e-d1e2fcd82f3a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
6230e844-84e2-4e54-ae6e-d1e2fcd82f3a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
6230e844-84e2-4e54-ae6e-d1e2fcd82f3a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Ribose 5-phosphate is not used directly for either purine or pyrimidine synthesis, rather it is used to synthesize the “active pentose” — 5-phosphoribosyl-1-pyrophosphate (PRPP). The conversion is catalyzed by the enzyme phosphoribosyl-1-pyrophosphate (PRPP) synthase. PRPP is the activated five-carbon sugar used for nucleotide synthesis and provides both the sugar and phosphate group to nucleotides (figure 7.6).",True,Generation of 5-phosphoribosyl-1-phosphate (PRPP),Figure 7.6,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
7ff42e6f-2b65-411c-b9cc-2097a9bd7aed,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Regulation of PRPP synthase,False,Regulation of PRPP synthase,,,,
7e68f1c7-9df9-404d-b354-06c90d3038d2,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The enzyme, PRPP synthetase, is activated by Pi (inorganic phosphate) and inhibited by the purine bases adenine and guanine.",True,Regulation of PRPP synthase,,,,
bcde8107-9b8c-4219-aabb-1805ff488b17,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Synthesis of purines,False,Synthesis of purines,,,,
9aa878dd-6083-4c83-8ea7-257f4e54d661,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
9aa878dd-6083-4c83-8ea7-257f4e54d661,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
9aa878dd-6083-4c83-8ea7-257f4e54d661,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Purines are composed of a bicyclic structure that is synthesized from carbon and nitrogen donated from various compounds such as carbon dioxide, glycine, glutamine, aspartate, and tetrahydrofolate (TH4). The synthesis of purines starts with the synthesis of 5ʼphosphoribosylamine from PRPP and glutamine. The enzyme glutamine phosphoribosylpyrophate amidotransferase (GPAT) catalyzes this reaction and is the committed step in purine synthesis (figure 7.7). Synthesis continues for nine additional steps culminating in the synthesis of inosine monophosphate (IMP), which contains the base hypoxanthine. IMP is used to generate both AMP and GMP. The synthesis of both AMP and GMP requires energy in the form of the alternative base (i.e., the synthesis of GMP requires ATP while AMP synthesis requires energy in the form of GTP). The synthesis of AMP and GMP is regulated by feedback inhibition (figures 7.7 and 7.8). This allows for the maintenance of nucleotides in a relative ratio that is required for cellular processes. The generated nucleotide monophosphates can be converted to the di and triphosphate forms by nucleotide specific kinases, which will transfer phosphate groups to maintain a balance of the mono, di, and triphosphate forms.",True,Synthesis of purines,Figure 7.7,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
e6dcd293-58d8-4e2d-ab21-2aa7381e7daa,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,TH4,False,TH4,,,,
6ae765f4-5dc7-468e-821d-2cfd8d171b21,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,5ʼphosphoribosylamine,False,5ʼphosphoribosylamine,,,,
8dbba0d0-d849-416c-8b8f-e8c5f3895e5c,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,phosphoribosylpyrophate,False,phosphoribosylpyrophate,,,,
15421c09-4d70-4581-917a-b2c7282fb644,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,amidotransferase,False,amidotransferase,,,,
1faa5a7f-80af-4eb5-b8c7-980befc94717,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,GPAT,False,GPAT,,,,
5f6d9ae2-4666-49a6-81f4-c6b1a947ec7b,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Regulation of purine synthesis,False,Regulation of purine synthesis,,,,
a4e27c6e-9817-47ad-8f67-9f9648e7957c,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The regulatory enzyme GPAT is allosterically activated by PRPP and inhibited by IMP, AMP, and GMP. All three must be present to inhibit activity of this enzyme.",True,Regulation of purine synthesis,,,,
e2dc7acc-8823-4a2a-aa37-6cb09c655d50,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Degradation of purines,False,Degradation of purines,,,,
0b92ce1c-3346-454f-9f40-c05c69e757d8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Like amino acids, nucleotides contain nitrogen and must be degraded in a manner that allows for proper nitrogen disposal either through the urea cycle or by the synthesis of a nontoxic compound.",True,Degradation of purines,,,,
468d080d-7b62-49d8-b9d0-998c293089ce,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
468d080d-7b62-49d8-b9d0-998c293089ce,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
468d080d-7b62-49d8-b9d0-998c293089ce,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Degradation of dietary nucleotides occurs in the gut, while nucleotides from de novo synthesis are degraded in the liver. The fundamental process involves the dismantling of the sugar, phosphate, and base structure into their own respective units (figure 7.9). In the case of purine degradation, the base is excreted in the form of uric acid. Purine nucleoside phosphorylase converts inosine and guanosine to their respective bases (hypoxanthine and guanine). Finally, xanthine oxidase will oxidize hypoxanthine to xanthine (guanine can be deaminated to xanthine), and xanthine can be further oxidized to uric acid by the same enzyme. Uric acid is excreted in the urine.",True,Degradation of purines,Figure 7.9,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
e1d36d8a-a1d8-450d-a428-15dbe01d8f60,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
e1d36d8a-a1d8-450d-a428-15dbe01d8f60,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
e1d36d8a-a1d8-450d-a428-15dbe01d8f60,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Excess uric acid, hyperuricemia, can cause the precipitation of uric acid crystals in the joints eliciting an inflammatory reaction causing acute pain or gout. The majority of individuals diagnosed with gout present due to underexcretion of uric acid. And this can be caused by the presence of other pathologies, such as lactic acidosis or the use of diuretics. Less common presentations of gout are associated with overproduction of uric acid, which can be caused by increased activity of PRPP synthetase or deficiency in purine recycling enzyme HGPRT caused by Lesch-Nyhan syndrome (figure 7.10).",True,Degradation of purines,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
1f7f24d9-39aa-4519-b24c-64cb1867c5c8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,underexcretion,False,underexcretion,,,,
06500e17-c4a0-47f2-b12a-f0525b8d4908,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Secondary hyperuricemia is also seen in individuals with myeloproliferative disorders undergoing therapy where there is excess cellular turnover (cell lysis leads to an accumulation of nucleotides) or in cases of Von Gierke disease or fructose intolerance, which increases substrate for PRPP synthesis. Xanthine oxidase inhibitors, such as allopurinol, are used as part of the management of gout.",True,underexcretion,,,,
de467244-de29-4bd1-b06e-16373bda887e,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Salvage of purines,False,Salvage of purines,,,,
170fd073-8c3a-4e8f-8ca0-13c4b9429a8d,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
170fd073-8c3a-4e8f-8ca0-13c4b9429a8d,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
170fd073-8c3a-4e8f-8ca0-13c4b9429a8d,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"The ability to recycle nucleotides is specifically important in the case of purines as de novo synthesis uses much more ATP than salvage. The degradation product of purine bases is uric acid, which is an insoluble compound, and accumulation can result in several clinical disorders as previously discussed. As such, purine bases can also undergo salvage reaction where bases are recycled and used in a new process. To reduce the amount of uric acid production, purines can be salvaged and reconverted back to their triphosphate form to be reused. There are two primary enzymes involved in the salvage pathway: adenine phosphoribosyltransferase (APRT) and xanthine-guanine phosphoribosyltransferase (HGPRT) (figure 7.10). These enzymes will recombine the base (either adenine, guanine, or hypoxanthine) with PRPP to generate AMP, GMP, or IMP respectively. Adenosine is the only nucleoside that can be rephosphorylated to its monosphosphate form using adenosine kinase (figure 7.11). All other nucleosides must be degraded to their free base before they can be salvaged.",True,Salvage of purines,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
2c196628-d646-4b65-a993-267383ec4ed1,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,APRT,False,APRT,,,,
304a6d2c-3952-4b74-9feb-0560825860f6,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,rephosphorylated,False,rephosphorylated,,,,
e6319baf-986e-4236-b0ee-3747db5972d5,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Synthesis of pyrimidines,False,Synthesis of pyrimidines,,,,
9097a7a0-5543-434d-a656-86a0b76c19c8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
9097a7a0-5543-434d-a656-86a0b76c19c8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
9097a7a0-5543-434d-a656-86a0b76c19c8,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"In contrast to purine synthesis, the pyrimidine bases are synthesized before the ribose sugar and phosphate groups are added in the form of PRPP (figure 7.12). The initial step of the pathways involves the synthesis of carbamoyl phosphate from glutamine, carbon dioxide, and 2 ATP. Carbamoyl phosphate synthetase II (CSPII) catalyzes this reaction. (Note there is an analogous enzyme in the mitochondria for the urea cycle termed carbamoyl phosphate synthetase I, which also generates carbamoyl phosphate.) Of clinical importance is the intermediate orotate. Elevations of orotate (orotic acid) are consistent with enzymatic deficiencies in this pathway or urea cycle deficiencies such as a defect in ornithine transcarbamoylase. In the case of a urea cycle deficiency, an excess carbamoyl phosphate can enter pyrimidine synthesis leading to a build up of orotate. Following the synthesis of carbamoyl phosphate, a series of subsequent reactions yield uracil monosphosphate, which is the intermediate of pyrimidine synthesis.",True,Synthesis of pyrimidines,Figure 7.12,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
1a7f7d28-4f35-43da-9beb-d92eaf10a513,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
1a7f7d28-4f35-43da-9beb-d92eaf10a513,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
1a7f7d28-4f35-43da-9beb-d92eaf10a513,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"UMP, much like IMP, serves as the intermediate to pyrimidine synthesis and can undergo sequential phosphorylation to form UTP, which can be converted to cytidine (CTP). Alternatively, UMP can be converted to a deoxy form (dUDP) to be used as substrate for the synthesis of thymidine. The conversion of dUDP to dTMP is catalyzed by thymidylate synthase, which requires folate (N5,N10 methylene tetrahydrofolate) as a methyl and hydrogen donor to complete this conversion (figure 7.13).",True,Synthesis of pyrimidines,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
7e1f354c-3b71-495a-8749-45f29f0746b3,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Defects in pyrimidine synthesis most commonly present as an increase in orotic acid in the urine. Deficiencies in the attachment of PRPP to orotate (or the decarboxylation of orotate monosphosphate) can result in the accumulation of orotic acid; similarly deficiencies of the urea cycle, which lead to an accumulation of carbamoyl phosphate, can increase flux through pyrimidine synthesis and cause an increase in orotic acid. Accumulation of orotic acid is used as a clinical indicator of pyrimidine deficiencies or deficiencies in the urea cycle.",True,Synthesis of pyrimidines,,,,
8d04472b-0b1b-4299-818e-e860507eeab0,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Regulation of pyrimidine synthesis,False,Regulation of pyrimidine synthesis,,,,
46c3e6be-336e-43af-8997-00b3e17cf810,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,The reaction catalyzed by CSPII is the regulatory step in the pathway and is activated by PRPP and ATP and inhibited by UTP.,True,Regulation of pyrimidine synthesis,,,,
56f79fd8-9e1f-4bdd-b294-133c5a5ff464,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Clinical importance of folate cycle inhibitors and synthesis of dTMP,False,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
54432d8d-3b56-4e9e-aee0-fe3b59866a84,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
54432d8d-3b56-4e9e-aee0-fe3b59866a84,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
54432d8d-3b56-4e9e-aee0-fe3b59866a84,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Synthesis of dTMP for DNA synthesis is the rate-limiting step for the replication process, and therefore disruption of this conversion is very effective at reducing cellular proliferation. Inhibition of thymidylate synthase by 5-fluorouracil (5-FU) is a common anticancer treatment. 5-FU functions as a thymine analog and will irreversibly bind the enzyme. Similarly, methotrexate is an inhibitor of dihyrofolate reductase (DHFR), which is part of the folate cycle needed to reduce dihydrofolate to tetrahydrofolate. Inhibition of this process reduces substrate needed for the thymidylate synthase reaction and has a similar effect as inhibition of by 5-FU (figure 7.13).",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
41911dc2-23a8-42b2-a00f-0e346ba1f52a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,Table 7.2: Summary of pathway regulation.,True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
36ec4f83-f505-4817-bea8-84378f5b416c,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,7.2 References and resources,True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,,,,
f6db0f1b-e742-4091-95aa-f30d35cba647,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
f6db0f1b-e742-4091-95aa-f30d35cba647,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
f6db0f1b-e742-4091-95aa-f30d35cba647,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.5 Overview of purine and pyrimidine bases. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/7.5_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.5,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
1c3908a4-c39e-4d17-a915-137e3cdb9d34,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
1c3908a4-c39e-4d17-a915-137e3cdb9d34,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
1c3908a4-c39e-4d17-a915-137e3cdb9d34,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.6 Synthesis of PRPP and regulation of PRPP synthetase. 2021. https://archive.org/details/7.6_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.6,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
204094d3-cc65-4968-a6c5-0df0322663b1,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
204094d3-cc65-4968-a6c5-0df0322663b1,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
204094d3-cc65-4968-a6c5-0df0322663b1,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.7 Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.7_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.7,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
0ace97aa-5a01-45ba-bc2a-a2153c867cbc,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
0ace97aa-5a01-45ba-bc2a-a2153c867cbc,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
0ace97aa-5a01-45ba-bc2a-a2153c867cbc,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.8 Purine synthesis and regulation of glutamine:phosphoribosylpyrophosphate amidotransferase. 2021. https://archive.org/details/7.8_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.8,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
648ba50b-7254-440b-b2d6-3d4c31856d6a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
648ba50b-7254-440b-b2d6-3d4c31856d6a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
648ba50b-7254-440b-b2d6-3d4c31856d6a,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.9 Breakdown of nucleotides. 2021. https://archive.org/details/7.9_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.9,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
96b734e0-e018-48d9-bb05-b8d02bcf3353,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
96b734e0-e018-48d9-bb05-b8d02bcf3353,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
96b734e0-e018-48d9-bb05-b8d02bcf3353,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.10 Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid. 2021. https://archive.org/details/7.10_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.10,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
27f4bb79-129d-4326-b451-8415e7cce049,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
27f4bb79-129d-4326-b451-8415e7cce049,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
27f4bb79-129d-4326-b451-8415e7cce049,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.11 Nucleotide specific pathways for base salvage. 2021. https://archive.org/details/7.11_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.11,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
bd531971-6c05-4215-b844-9a646a700e92,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
bd531971-6c05-4215-b844-9a646a700e92,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
bd531971-6c05-4215-b844-9a646a700e92,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.12 Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway. 2021. https://archive.org/details/7.12_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.12,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
debc7b54-b939-4741-bfcc-90e7bb81654c,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
debc7b54-b939-4741-bfcc-90e7bb81654c,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
debc7b54-b939-4741-bfcc-90e7bb81654c,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Grey, Kindred, Figure 7.13 Interaction of thymidylate synthesis with the folate cycle. SHMT: Serine hydroxymethyltransferase; DHFR: Dihydrofolate reductase. 2021. https://archive.org/details/7.13_20210926. CC BY 4.0.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.13,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
d6f05a2a-db07-4f19-9025-c999fc4d6400,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,7.2 Nucleotide Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
d6f05a2a-db07-4f19-9025-c999fc4d6400,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,7.1 Pentose Phosphate Pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
d6f05a2a-db07-4f19-9025-c999fc4d6400,https://pressbooks.lib.vt.edu/cellbio/,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/cellbio/chapter/pentose-phosphate-pathway-ppp-purine-and-pyrimidine-metabolism/,"Lieberman M, Peet A. Figure 7.4 Basic structure of nucleotides. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 216. Figure 12.3 Nucleoside and nucleotide structures displayed with ribose as the sugar. 2017. Chemical structure by Henry Jakubowski.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 7.4,"7. Pentose Phosphate Pathway (PPP), Purine and Pyrimidine Metabolism",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
2687100e-d1c9-4625-9b84-ea3b77ba33bd,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 6.2,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
2687100e-d1c9-4625-9b84-ea3b77ba33bd,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 6.2,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
2687100e-d1c9-4625-9b84-ea3b77ba33bd,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Clinical importance of folate cycle inhibitors and synthesis of dTMP,Figure 6.2,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
8d7fe116-f60a-4a61-88cd-0961f127ab33,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Synthesis of mevalonate from acetyl-CoA,False,Synthesis of mevalonate from acetyl-CoA,,,,
3c0c346b-71a3-475e-a7c0-179b405e4362,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
3c0c346b-71a3-475e-a7c0-179b405e4362,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
3c0c346b-71a3-475e-a7c0-179b405e4362,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
98a86980-39f3-4f2f-819a-955e68ab9df8,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The subsequent steps of the pathway proceed largely unregulated, and mevalonate is used to synthesize isoprenoid units (five-carbon units). These five-carbon chains are joined in a head-to-tail fashion generating squalene, thirty-carbons, which undergoes a cyclization reaction after epoxidation. The cyclized product, lanosterol, undergoes several reactions to generate the final product, cholesterol.",True,Synthesis of mevalonate from acetyl-CoA,,,,
50e01029-22ab-4818-9722-bfb5e0dbb14f,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,epoxidation,False,epoxidation,,,,
af9bab10-b2c5-4f97-b692-b575bc4b05fb,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,cyclized,False,cyclized,,,,
33ea1670-798e-4a54-9b74-aa4db49692d3,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Regulation of cholesterol synthesis,False,Regulation of cholesterol synthesis,,,,
80e88c2d-7741-433c-8d0d-839e47a7d52e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
80e88c2d-7741-433c-8d0d-839e47a7d52e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
80e88c2d-7741-433c-8d0d-839e47a7d52e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
207ca93b-3194-49d1-b6ac-a9fa83394f5b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Transcriptional control,False,Transcriptional control,,,,
214551e2-61ed-4790-a279-6c92c53209f3,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
214551e2-61ed-4790-a279-6c92c53209f3,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
214551e2-61ed-4790-a279-6c92c53209f3,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
3aeff1ac-560b-4a72-ab00-0429f0e15659,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Proteolytic degradation of HMG-CoA reductase,False,Proteolytic degradation of HMG-CoA reductase,,,,
ec4c4ef0-b3c7-48ca-96ca-35c8178a5341,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The amount of HMG-CoA reductase can also be influenced by proteolytic degradation. The membrane domains of HMG-CoA reductase contain sterol-sensing regions, which are similar to those in SCAP. As levels of cholesterol (or its derivatives) increase in the cell, this causes a change in the oligomerization state of the membrane domain of HMG-CoA reductase, rendering the enzyme more susceptible to proteolysis. This, in turn, decreases the activity of the enzyme.",True,Proteolytic degradation of HMG-CoA reductase,,,,
aaadc42d-9c6f-478e-b71e-d46a25f4869e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Regulation by covalent modification,False,Regulation by covalent modification,,,,
b0c9c72c-d605-4ef9-831f-d57cbfc1a13b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Much like other anabolic enzymes, the activity of HMG-CoA reductase can be influenced by phosphorylation. Elevated glucagon levels increase phosphorylation of the enzyme, thereby inactivating it, whereas hyperinsulinemia increases the activity of the reductase by activating phosphatases, which dephosphorylate the reductase. Increased levels of intracellular sterols may also increase phosphorylation of HMG-CoA reductase, thereby reducing its activity as well (feedback suppression).",True,Regulation by covalent modification,,,,
4532c44e-cdba-4819-8735-198438bdebea,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Adenosine monophosphate (AMP)-activated protein kinase can also phosphorylate and inactivate HMG-CoA reductase. Thus, cholesterol synthesis decreases when ATP levels are low and increases when ATP levels are high, similar to what occurs with fatty acid synthesis (recall that acetyl-CoA carboxylase is also phosphorylated and inhibited by the AMP-activated protein kinase; section 4.4.)",True,Regulation by covalent modification,,,,
bf60b2c1-5295-4f52-b064-c74baffa2db5,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Several fates of cholesterol,False,Several fates of cholesterol,,,,
12c923cd-eae8-44c8-b352-818c9a0a1d70,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Almost all mammalian cells are capable of producing cholesterol. Most of the biosynthesis of cholesterol occurs within liver cells, although the gut, the adrenal cortex, and the gonads (as well as the placenta in pregnant women) also produce significant quantities of the sterol. A small portion of hepatic cholesterol is used for the synthesis of hepatic membranes, but the bulk of synthesized cholesterol is secreted from the hepatocyte as one of three compounds: cholesterol esters, biliary cholesterol (cholesterol found in the bile), or bile acids.",True,Several fates of cholesterol,,,,
dd874644-e16a-4614-b007-cee1c90c3718,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Cholesterol esterification and transport,False,Cholesterol esterification and transport,,,,
9ede71cf-1469-48e1-be43-fd8d7171b0fb,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
9ede71cf-1469-48e1-be43-fd8d7171b0fb,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
9ede71cf-1469-48e1-be43-fd8d7171b0fb,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
fad78e77-a394-4126-ba42-1b1a18bb8225,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Synthesis of specialized products,False,Synthesis of specialized products,,,,
f236022a-c9d1-472f-8edc-3b69bba5ce8d,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The hepatic cholesterol pool serves as a source of cholesterol for the synthesis of the relatively hydrophilic bile acids and their salts. These derivatives of cholesterol are effective detergents because they contain both polar and nonpolar regions. They are introduced into the biliary ducts of the liver. They are stored and concentrated in the gallbladder and later discharged into the gut in response to the ingestion of food. Finally, cholesterol is the precursor of all five classes of steroid hormones: glucocorticoids, mineralocorticoids, androgens, estrogens, and progestins. Cholesterol and steroid hormones are transported through the blood from their sites of synthesis to their target organs. Because of their hydrophobicity, they must be complexed with a serum protein. Serum albumin can act as a nonspecific carrier for the steroid hormones, but there are specific carriers as well (section 2.1).",True,Synthesis of specialized products,,,,
454c78e1-f270-4eac-afa0-a664cafea36c,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,6.1 References and resources,True,Synthesis of specialized products,,,,
f40832f7-1c5c-4c67-96db-cd371f00fb37,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 15: Metabolism of Dietary Lipids, Chapter 18: Cholesterol and Steroid Metabolism.",True,Synthesis of specialized products,,,,
81442bf1-bc27-4826-be31-285f6c5d112c,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 92–94.",True,Synthesis of specialized products,,,,
4ae65743-884b-453d-a227-1102ad059aaa,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 29: Digestion and Transport of Dietary Lipids, Chapter 32: Cholesterol Absorption: Synthesis, Metabolism and Fate Section.",True,Synthesis of specialized products,,,,
f51ac553-16fd-4d88-8973-03f5c227d35d,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
f51ac553-16fd-4d88-8973-03f5c227d35d,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
f51ac553-16fd-4d88-8973-03f5c227d35d,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
0ce7b188-33dc-4c0f-a80e-a3432650e62b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
0ce7b188-33dc-4c0f-a80e-a3432650e62b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
0ce7b188-33dc-4c0f-a80e-a3432650e62b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
c0396940-c7f0-4e1f-a060-a37566658578,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
c0396940-c7f0-4e1f-a060-a37566658578,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
c0396940-c7f0-4e1f-a060-a37566658578,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
eb03d963-af07-4c7c-b48c-01a3562951ee,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
eb03d963-af07-4c7c-b48c-01a3562951ee,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
eb03d963-af07-4c7c-b48c-01a3562951ee,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
3e1b3cbc-717d-4a3f-9998-2a56de7cd452,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
3e1b3cbc-717d-4a3f-9998-2a56de7cd452,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
3e1b3cbc-717d-4a3f-9998-2a56de7cd452,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
ca403ebf-f143-4273-b51b-9cad6f2683dc,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,6.2 Lipid Transport,True,Synthesis of specialized products,,,,
e9ad3c68-d453-4393-a928-2c51370d5008,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Most of the lipids found in the body fall into the categories of fatty acids and triacylglycerols (TAGs); glycerophospholipids and sphingolipids; eicosanoids; cholesterol, bile salts, and steroid hormones; and fat-soluble vitamins. These lipids have very diverse chemical structures and functions. However, they are related by a common property, their relative insolubility in water.",True,Synthesis of specialized products,,,,
491ae0dd-d107-41d3-9409-8a5b02b4f31e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,TAGs,False,TAGs,,,,
1e1074ac-ef70-43ce-b84d-7d0f9ba0e939,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
1e1074ac-ef70-43ce-b84d-7d0f9ba0e939,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
1e1074ac-ef70-43ce-b84d-7d0f9ba0e939,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
6e690769-0660-48bf-a4ff-78208ea290a8,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"In addition to the lipid components of lipoproteins, they contain protein components termed apoproteins. The complement of apoproteins on each lipoprotein is unique and is a distinguishing characteristic of each family of lipoproteins. The apoproteins (“apo” describes the protein within the shell of the particle in its lipid-free form) not only add to the hydrophilicity and structural stability of the particle, but they have other functions as well: (1) They activate certain enzymes required for normal lipoprotein metabolism, and (2) they act as ligands on the surface of the lipoprotein that target specific receptors on peripheral tissues that require lipoprotein delivery for their innate cellular functions.",True,TAGs,,,,
b3c198a1-6ba8-4e8f-8889-8509dd94b254,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,hydrophilicity,False,hydrophilicity,,,,
528cac11-ccc5-4ba3-86ea-925a4abeacef,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Chylomicrons: Transport of dietary lipids,False,Chylomicrons: Transport of dietary lipids,,,,
19e4374e-a9e9-4532-8402-33b92129522a,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
19e4374e-a9e9-4532-8402-33b92129522a,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
19e4374e-a9e9-4532-8402-33b92129522a,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
61f7c54a-6611-483c-81ff-6f65a3d6b334,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Chylomicrons are the largest lipoproteins and contain cholesterol and fat-soluble vitamins, in addition to their major component, dietary TAGs. The major apoprotein associated with chylomicrons as they leave the intestinal cells is ApoB-48. (The B-48 apoprotein is structurally and genetically related to the B-100 apoprotein synthesized in the liver that serves as a major protein of VLDL.) Microsomal transfer protein (MTP) aids in the loading of apoB-48 protein onto the chylomicron before the nascent chylomicron is secreted. Nascent chylomicrons are secreted by the intestinal epithelial cells into the chyle of the lymphatic system and enter the blood through the thoracic duct. Nascent chylomicrons begin to enter the blood within one to two hours after the start of a meal; as the meal is digested and absorbed, they continue to enter the blood for many hours. Chylomicron maturation occurs in circulation as they accept additional apoproteins from high-density lipoprotein (HDL) (figures 6.7 and 6.10).",True,Chylomicrons: Transport of dietary lipids,,,,
1fb9aa77-009e-4ae1-97dc-ae12f1e692b5,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"HDL predominantly transfers apoproteins E and CII to the nascent chylomicrons. ApoE is recognized by membrane receptors, and this interaction allows apoE-bearing lipoproteins to enter these cells by endocytosis; once inside the cell the particle is broken down through a lysosomal-mediated process. ApoCII acts as an activator of lipoprotein lipase (LPL), the enzyme on capillary endothelial cells, which digests the TAGs of the chylomicrons and VLDLs in the blood.",True,Chylomicrons: Transport of dietary lipids,,,,
be8c55b8-c867-466a-8eec-afc199bce682,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Fate of chylomicrons,False,Fate of chylomicrons,,,,
3fd33b2f-7760-4f1c-97b6-c8ffcc954661,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The TAGs transported by chylomicrons are hydrolyzed by lipoprotein lipase (LPL), an enzyme present on endothelial cells that line the capillary walls. ApoCII on the chylomicron will interact with LPL and activate the enzyme. Insulin stimulates the synthesis and secretion of LPL so that after a meal, when triglyceride levels increase in circulation, LPL is upregulated (through insulin release) to facilitate the hydrolysis of fatty acids from the triglyceride.",True,Fate of chylomicrons,,,,
f05ea9ff-6f1a-4be2-a775-8b3105ba3226,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Therefore, adipose LPL is more active after a meal, when chylomicron levels are elevated in the blood. The fatty acids released from TAGs by LPL are eventually repackaged in the adipose tissue and stored as TAGs within the tissue.",True,Fate of chylomicrons,,,,
58bc7319-583a-49d6-a833-8fb9049cb4f8,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The portion of a chylomicron that remains in the blood after LPL action is known as a chylomicron remnant. The remnant has returned (or lost) many of the apoC molecules bound to the mature chylomicron, exposing apoE. The remaining remnant binds to apoE receptors on hepatocytes, and is taken up by the process of endocytosis. Lysosomes fuse with the endocytic vesicles, and the chylomicron remnants are degraded by lysosomal enzymes. The products released through this degradation process (e.g., amino acids, fatty acids, cholesterol, etc.) can be recycled within the cell.",True,Fate of chylomicrons,,,,
f7f60d0d-a339-46bb-b35e-c9555a5d0754,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,VLDL: Transport of TAGs and cholesterol synthesized in the liver,False,VLDL: Transport of TAGs and cholesterol synthesized in the liver,,,,
84b462ad-96d0-472f-8da4-c09a5ab9a59a,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
84b462ad-96d0-472f-8da4-c09a5ab9a59a,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
84b462ad-96d0-472f-8da4-c09a5ab9a59a,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
a7832ccd-7df7-4aa2-8c23-274080dc5d9e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
a7832ccd-7df7-4aa2-8c23-274080dc5d9e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
a7832ccd-7df7-4aa2-8c23-274080dc5d9e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
a522eb7b-53b4-4afb-aa65-92f3e083f3ee,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Fate of VLDL,False,Fate of VLDL,,,,
a2a785be-d3f0-4ec2-bd4f-1ba416acea3b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
a2a785be-d3f0-4ec2-bd4f-1ba416acea3b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
a2a785be-d3f0-4ec2-bd4f-1ba416acea3b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
9ba4b49d-857f-4038-9059-9bd7c62eed83,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,HDL: Reverse cholesterol transport,False,HDL: Reverse cholesterol transport,,,,
dc9e84b3-c161-4992-8d11-23080026ca9f,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The primary function of high-density lipoprotein (HDL) is to transport excess cholesterol obtained from peripheral tissues to the liver. HDL also has other roles integral to lipid transport such as exchanging proteins and lipids with chylomicrons and VLDL. HDL particles can be created by several mechanisms, however, nascent HDLs are primarily secreted from the liver and intestine as a relatively small particles whose shell, like that of other lipoproteins, contains phospholipids, free cholesterol, and a variety of apoproteins, specifically apoAI, apoAII, apoCI, and apoCII. Very low levels of triacylglycerols or cholesterol esters are found in the hollow core of this early, or nascent, version of HDL.",True,HDL: Reverse cholesterol transport,,,,
dad1f10e-9b0f-4a5e-8937-a872f4bc7524,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
dad1f10e-9b0f-4a5e-8937-a872f4bc7524,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
dad1f10e-9b0f-4a5e-8937-a872f4bc7524,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
4da54279-98e2-4d23-8cd3-8a118bd8b8a9,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Fate of HDL,False,Fate of HDL,,,,
6b8c0c52-ebfd-41fb-abfc-2009813205ed,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"In the process of maturation, the nascent HDL particles accumulate phospholipids and cholesterol from cells lining the blood vessels. As the central hollow core of nascent HDL progressively fills with cholesterol esters, HDL takes on a more globular shape to eventually form the mature HDL particle. A major benefit of HDL particles derives from their ability to remove cholesterol from cholesterol-laden cells and to return the cholesterol to the liver, a process known as reverse cholesterol transport. This is particularly beneficial in vascular tissue; by reducing cellular cholesterol levels in the subintimal space, the likelihood that foam cells (lipid-laden macrophages that engulf oxidized LDL cholesterol) will form within the blood vessel wall is reduced.",True,Fate of HDL,,,,
72a76514-97d2-4758-b87f-7f78d35977d4,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
72a76514-97d2-4758-b87f-7f78d35977d4,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
72a76514-97d2-4758-b87f-7f78d35977d4,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
e9abdebf-773e-4179-bf7b-20f6fe7cedfd,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Mature HDL particles can bind to specific receptors on hepatocytes (such as the apoE receptor), but the primary means of clearance of HDL from the blood is through its uptake by the scavenger receptor SR-B1. This receptor is present on many cell types, and once the HDL particle is bound to the receptor, its cholesterol and cholesterol esters are transferred into the cells. When depleted of cholesterol and its esters, the HDL particle dissociates from the SR-B1 receptor and reenters the circulation.",True,Fate of HDL,,,,
906e072b-e29e-4e80-a877-091d0e636dbb,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,HDL interactions with other particles,False,HDL interactions with other particles,,,,
56d46975-79b7-4571-9deb-23b06436b732,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"As previously mentioned, HDL plays a key role in the maturation of both chylomicrons and VLDL. First, HDL transfers apoE and apoCII to chylomicrons and to VLDL. The apoCII stimulates the degradation of the TAGs of chylomicrons and VLDL by activating LPL. After digestion of the chylomicrons and the VLDL TAGs, apoE and apoCII are transferred back to HDL.",True,HDL interactions with other particles,,,,
b19d98b4-f02a-45e2-bb8e-082c4b819299,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
b19d98b4-f02a-45e2-bb8e-082c4b819299,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
b19d98b4-f02a-45e2-bb8e-082c4b819299,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
a9f6cccc-2113-49d4-8a50-8e51d4af679e,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Lipoprotein receptor-mediated endocytosis,False,Lipoprotein receptor-mediated endocytosis,,,,
48095600-24b8-4c72-88aa-3556a7c6dae7,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"As VLDLs mature to LDLs, these lipoproteins can be taken up through an interaction of the ApoB100 with the LDL receptors on the cell surface. The receptors for LDL are found in clathrin-coated pits within the cell membrane of the target cells. Upon receptor ligand interaction, the plasma membrane in the vicinity of the receptor‒LDL complex invaginates and fuses to form an endocytic vesicle. These vesicles then fuse with lysosomes, and the cholesterol esters of LDL are hydrolyzed to form free cholesterol, which is rapidly re-esterified through the action of ACAT. This rapid re-esterification is necessary to avoid the damaging effect of high levels of free cholesterol on cellular membranes.",True,Lipoprotein receptor-mediated endocytosis,,,,
25f6199d-ded6-4bcd-9265-7857911ad5f1,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
25f6199d-ded6-4bcd-9265-7857911ad5f1,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
25f6199d-ded6-4bcd-9265-7857911ad5f1,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
fed3baf8-45be-46ab-a2d5-77e9bf2047d8,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,6.2 References and resources,True,Lipoprotein receptor-mediated endocytosis,,,,
c5adc32d-bfb0-4914-814b-f61b9e904759,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
c5adc32d-bfb0-4914-814b-f61b9e904759,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
c5adc32d-bfb0-4914-814b-f61b9e904759,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
f80ed7ae-fc53-44b7-b6ed-655d6158696c,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
f80ed7ae-fc53-44b7-b6ed-655d6158696c,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
f80ed7ae-fc53-44b7-b6ed-655d6158696c,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
10da76d4-1616-4c77-a52d-4434a0b73c1d,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
10da76d4-1616-4c77-a52d-4434a0b73c1d,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
10da76d4-1616-4c77-a52d-4434a0b73c1d,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
cceb5fdc-50d2-47d7-9f23-20f78d5bd0d1,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
cceb5fdc-50d2-47d7-9f23-20f78d5bd0d1,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
cceb5fdc-50d2-47d7-9f23-20f78d5bd0d1,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
e7131b43-1fa8-4fb3-ad35-9a3b8ec0af3b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
e7131b43-1fa8-4fb3-ad35-9a3b8ec0af3b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
e7131b43-1fa8-4fb3-ad35-9a3b8ec0af3b,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
0585668d-eb07-4c87-b748-39d6ce97ba63,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
0585668d-eb07-4c87-b748-39d6ce97ba63,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
0585668d-eb07-4c87-b748-39d6ce97ba63,https://pressbooks.lib.vt.edu/cellbio/,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-2,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
8a3ab5ba-d5bc-4d3d-8783-148efaadecd1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.2,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
8a3ab5ba-d5bc-4d3d-8783-148efaadecd1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.2,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
8a3ab5ba-d5bc-4d3d-8783-148efaadecd1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.2,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
40e7cc79-4eb5-4fae-8b5e-83e7be76aec1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Synthesis of mevalonate from acetyl-CoA,False,Synthesis of mevalonate from acetyl-CoA,,,,
238a0e96-80df-40ce-92ad-83071e03a2c6,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
238a0e96-80df-40ce-92ad-83071e03a2c6,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
238a0e96-80df-40ce-92ad-83071e03a2c6,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
35db4813-26f9-4202-a4e8-4c92b9180821,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The subsequent steps of the pathway proceed largely unregulated, and mevalonate is used to synthesize isoprenoid units (five-carbon units). These five-carbon chains are joined in a head-to-tail fashion generating squalene, thirty-carbons, which undergoes a cyclization reaction after epoxidation. The cyclized product, lanosterol, undergoes several reactions to generate the final product, cholesterol.",True,Synthesis of mevalonate from acetyl-CoA,,,,
ad49fa53-265d-4a1a-86c3-d47c05032b8d,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,epoxidation,False,epoxidation,,,,
1234eabf-5ecf-44f6-9e65-6c9c97489cff,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,cyclized,False,cyclized,,,,
916a1d44-1069-4053-a2cf-bffba99764af,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Regulation of cholesterol synthesis,False,Regulation of cholesterol synthesis,,,,
73f27a38-f06f-4888-a31c-aa4d11777bf0,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
73f27a38-f06f-4888-a31c-aa4d11777bf0,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
73f27a38-f06f-4888-a31c-aa4d11777bf0,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
1821e6c8-9909-4ac1-819e-6f938729124a,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Transcriptional control,False,Transcriptional control,,,,
487ba9e6-3a39-4797-8c8a-383004baaed5,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
487ba9e6-3a39-4797-8c8a-383004baaed5,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
487ba9e6-3a39-4797-8c8a-383004baaed5,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
4c525015-7794-4126-9029-55661283cbd9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Proteolytic degradation of HMG-CoA reductase,False,Proteolytic degradation of HMG-CoA reductase,,,,
6f21ea53-d6f6-46a5-a023-f5095dd5ff3c,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The amount of HMG-CoA reductase can also be influenced by proteolytic degradation. The membrane domains of HMG-CoA reductase contain sterol-sensing regions, which are similar to those in SCAP. As levels of cholesterol (or its derivatives) increase in the cell, this causes a change in the oligomerization state of the membrane domain of HMG-CoA reductase, rendering the enzyme more susceptible to proteolysis. This, in turn, decreases the activity of the enzyme.",True,Proteolytic degradation of HMG-CoA reductase,,,,
a2151802-0229-4b82-bf8c-0e8d50b87884,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Regulation by covalent modification,False,Regulation by covalent modification,,,,
1df4309b-b825-4691-924e-1af062b1fe82,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Much like other anabolic enzymes, the activity of HMG-CoA reductase can be influenced by phosphorylation. Elevated glucagon levels increase phosphorylation of the enzyme, thereby inactivating it, whereas hyperinsulinemia increases the activity of the reductase by activating phosphatases, which dephosphorylate the reductase. Increased levels of intracellular sterols may also increase phosphorylation of HMG-CoA reductase, thereby reducing its activity as well (feedback suppression).",True,Regulation by covalent modification,,,,
a601d2ab-569f-4dd1-97fd-7b7c31e44085,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Adenosine monophosphate (AMP)-activated protein kinase can also phosphorylate and inactivate HMG-CoA reductase. Thus, cholesterol synthesis decreases when ATP levels are low and increases when ATP levels are high, similar to what occurs with fatty acid synthesis (recall that acetyl-CoA carboxylase is also phosphorylated and inhibited by the AMP-activated protein kinase; section 4.4.)",True,Regulation by covalent modification,,,,
e843da7c-60b6-4c91-aca2-a42b9b021e2c,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Several fates of cholesterol,False,Several fates of cholesterol,,,,
5e3dcd45-b6a6-4928-8913-7e723517cc7e,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Almost all mammalian cells are capable of producing cholesterol. Most of the biosynthesis of cholesterol occurs within liver cells, although the gut, the adrenal cortex, and the gonads (as well as the placenta in pregnant women) also produce significant quantities of the sterol. A small portion of hepatic cholesterol is used for the synthesis of hepatic membranes, but the bulk of synthesized cholesterol is secreted from the hepatocyte as one of three compounds: cholesterol esters, biliary cholesterol (cholesterol found in the bile), or bile acids.",True,Several fates of cholesterol,,,,
a2af7afd-3213-4147-8d96-d4fce23289a6,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Cholesterol esterification and transport,False,Cholesterol esterification and transport,,,,
68852c2f-79b7-41a4-8727-80808cae8dfc,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
68852c2f-79b7-41a4-8727-80808cae8dfc,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
68852c2f-79b7-41a4-8727-80808cae8dfc,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
4e7acc65-9692-476e-b485-51fdf7ece42c,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Synthesis of specialized products,False,Synthesis of specialized products,,,,
f7ebe2be-389c-4ee6-ac38-ddf7858efd3b,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The hepatic cholesterol pool serves as a source of cholesterol for the synthesis of the relatively hydrophilic bile acids and their salts. These derivatives of cholesterol are effective detergents because they contain both polar and nonpolar regions. They are introduced into the biliary ducts of the liver. They are stored and concentrated in the gallbladder and later discharged into the gut in response to the ingestion of food. Finally, cholesterol is the precursor of all five classes of steroid hormones: glucocorticoids, mineralocorticoids, androgens, estrogens, and progestins. Cholesterol and steroid hormones are transported through the blood from their sites of synthesis to their target organs. Because of their hydrophobicity, they must be complexed with a serum protein. Serum albumin can act as a nonspecific carrier for the steroid hormones, but there are specific carriers as well (section 2.1).",True,Synthesis of specialized products,,,,
489fbb68-305d-4939-a0c5-376fa0da1452,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,6.1 References and resources,True,Synthesis of specialized products,,,,
fa7d582c-a61b-4d37-acaf-f561ac248136,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 15: Metabolism of Dietary Lipids, Chapter 18: Cholesterol and Steroid Metabolism.",True,Synthesis of specialized products,,,,
cd810ac4-213b-4a1f-b940-5ecdb91fe7bb,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 92–94.",True,Synthesis of specialized products,,,,
281fb0dd-4103-481e-ac80-947a7324ae22,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 29: Digestion and Transport of Dietary Lipids, Chapter 32: Cholesterol Absorption: Synthesis, Metabolism and Fate Section.",True,Synthesis of specialized products,,,,
7effc2f0-8f09-407f-8bd1-d0a881cc6ca8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
7effc2f0-8f09-407f-8bd1-d0a881cc6ca8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
7effc2f0-8f09-407f-8bd1-d0a881cc6ca8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
5416925a-0ce1-447d-8669-dbbcc1007607,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
5416925a-0ce1-447d-8669-dbbcc1007607,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
5416925a-0ce1-447d-8669-dbbcc1007607,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
726f42f2-0a64-41b3-831f-a03059e2f403,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
726f42f2-0a64-41b3-831f-a03059e2f403,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
726f42f2-0a64-41b3-831f-a03059e2f403,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
7aa44d76-c5b5-456f-be54-577eebd8b1b3,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
7aa44d76-c5b5-456f-be54-577eebd8b1b3,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
7aa44d76-c5b5-456f-be54-577eebd8b1b3,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
44dca2b6-d1b4-4f03-be58-1c15255c6643,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
44dca2b6-d1b4-4f03-be58-1c15255c6643,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
44dca2b6-d1b4-4f03-be58-1c15255c6643,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
86e0de0e-8af7-4fb7-b4e4-32a03b6145a9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,6.2 Lipid Transport,True,Synthesis of specialized products,,,,
494df976-147c-4aa8-9ddc-2fceb0eeb9a6,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Most of the lipids found in the body fall into the categories of fatty acids and triacylglycerols (TAGs); glycerophospholipids and sphingolipids; eicosanoids; cholesterol, bile salts, and steroid hormones; and fat-soluble vitamins. These lipids have very diverse chemical structures and functions. However, they are related by a common property, their relative insolubility in water.",True,Synthesis of specialized products,,,,
0a10394f-3c94-48aa-88c8-34101b0f4d55,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,TAGs,False,TAGs,,,,
dbec047f-0d49-4aac-a880-a0f394c40c30,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
dbec047f-0d49-4aac-a880-a0f394c40c30,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
dbec047f-0d49-4aac-a880-a0f394c40c30,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
8a130e2f-6dbf-4eba-876a-a44529c8cc9f,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"In addition to the lipid components of lipoproteins, they contain protein components termed apoproteins. The complement of apoproteins on each lipoprotein is unique and is a distinguishing characteristic of each family of lipoproteins. The apoproteins (“apo” describes the protein within the shell of the particle in its lipid-free form) not only add to the hydrophilicity and structural stability of the particle, but they have other functions as well: (1) They activate certain enzymes required for normal lipoprotein metabolism, and (2) they act as ligands on the surface of the lipoprotein that target specific receptors on peripheral tissues that require lipoprotein delivery for their innate cellular functions.",True,TAGs,,,,
10ff04f5-fedb-4b40-9849-e83238097ceb,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,hydrophilicity,False,hydrophilicity,,,,
c0f4996b-abbb-4615-b3dd-a8340a4fea12,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Chylomicrons: Transport of dietary lipids,False,Chylomicrons: Transport of dietary lipids,,,,
e78976a8-b7e1-4ae7-88fd-841e9103f761,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
e78976a8-b7e1-4ae7-88fd-841e9103f761,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
e78976a8-b7e1-4ae7-88fd-841e9103f761,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
add39c7b-b79a-4cc6-885b-352575343acd,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Chylomicrons are the largest lipoproteins and contain cholesterol and fat-soluble vitamins, in addition to their major component, dietary TAGs. The major apoprotein associated with chylomicrons as they leave the intestinal cells is ApoB-48. (The B-48 apoprotein is structurally and genetically related to the B-100 apoprotein synthesized in the liver that serves as a major protein of VLDL.) Microsomal transfer protein (MTP) aids in the loading of apoB-48 protein onto the chylomicron before the nascent chylomicron is secreted. Nascent chylomicrons are secreted by the intestinal epithelial cells into the chyle of the lymphatic system and enter the blood through the thoracic duct. Nascent chylomicrons begin to enter the blood within one to two hours after the start of a meal; as the meal is digested and absorbed, they continue to enter the blood for many hours. Chylomicron maturation occurs in circulation as they accept additional apoproteins from high-density lipoprotein (HDL) (figures 6.7 and 6.10).",True,Chylomicrons: Transport of dietary lipids,,,,
a2dcb7f9-f154-4df6-9784-bf3e042ffdcb,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"HDL predominantly transfers apoproteins E and CII to the nascent chylomicrons. ApoE is recognized by membrane receptors, and this interaction allows apoE-bearing lipoproteins to enter these cells by endocytosis; once inside the cell the particle is broken down through a lysosomal-mediated process. ApoCII acts as an activator of lipoprotein lipase (LPL), the enzyme on capillary endothelial cells, which digests the TAGs of the chylomicrons and VLDLs in the blood.",True,Chylomicrons: Transport of dietary lipids,,,,
487d274d-d276-49c9-9b76-ca01e1db44db,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Fate of chylomicrons,False,Fate of chylomicrons,,,,
0454ae4a-525e-42e2-96aa-daacadd75331,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The TAGs transported by chylomicrons are hydrolyzed by lipoprotein lipase (LPL), an enzyme present on endothelial cells that line the capillary walls. ApoCII on the chylomicron will interact with LPL and activate the enzyme. Insulin stimulates the synthesis and secretion of LPL so that after a meal, when triglyceride levels increase in circulation, LPL is upregulated (through insulin release) to facilitate the hydrolysis of fatty acids from the triglyceride.",True,Fate of chylomicrons,,,,
12db0343-bf0d-48a2-983c-f414ada5ac0a,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Therefore, adipose LPL is more active after a meal, when chylomicron levels are elevated in the blood. The fatty acids released from TAGs by LPL are eventually repackaged in the adipose tissue and stored as TAGs within the tissue.",True,Fate of chylomicrons,,,,
6abfddb9-eb13-4de0-9e86-c14743028077,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The portion of a chylomicron that remains in the blood after LPL action is known as a chylomicron remnant. The remnant has returned (or lost) many of the apoC molecules bound to the mature chylomicron, exposing apoE. The remaining remnant binds to apoE receptors on hepatocytes, and is taken up by the process of endocytosis. Lysosomes fuse with the endocytic vesicles, and the chylomicron remnants are degraded by lysosomal enzymes. The products released through this degradation process (e.g., amino acids, fatty acids, cholesterol, etc.) can be recycled within the cell.",True,Fate of chylomicrons,,,,
ca6de76f-5b8c-4be1-8b67-ecc9fa8746f8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,VLDL: Transport of TAGs and cholesterol synthesized in the liver,False,VLDL: Transport of TAGs and cholesterol synthesized in the liver,,,,
72dcb04b-8903-42f5-b8dd-204abdd8586b,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
72dcb04b-8903-42f5-b8dd-204abdd8586b,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
72dcb04b-8903-42f5-b8dd-204abdd8586b,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
98d51281-db48-415c-8d9e-2022a1ea37ed,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
98d51281-db48-415c-8d9e-2022a1ea37ed,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
98d51281-db48-415c-8d9e-2022a1ea37ed,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
df4c9034-5250-4e55-9648-0674fddb3846,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Fate of VLDL,False,Fate of VLDL,,,,
194b9659-ff0e-409f-be8d-33fbb407906a,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
194b9659-ff0e-409f-be8d-33fbb407906a,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
194b9659-ff0e-409f-be8d-33fbb407906a,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
704534f5-82e7-4512-a018-01e7fc2aed5c,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,HDL: Reverse cholesterol transport,False,HDL: Reverse cholesterol transport,,,,
2ea80ed4-54d0-4449-be2a-fb3b98961aa1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The primary function of high-density lipoprotein (HDL) is to transport excess cholesterol obtained from peripheral tissues to the liver. HDL also has other roles integral to lipid transport such as exchanging proteins and lipids with chylomicrons and VLDL. HDL particles can be created by several mechanisms, however, nascent HDLs are primarily secreted from the liver and intestine as a relatively small particles whose shell, like that of other lipoproteins, contains phospholipids, free cholesterol, and a variety of apoproteins, specifically apoAI, apoAII, apoCI, and apoCII. Very low levels of triacylglycerols or cholesterol esters are found in the hollow core of this early, or nascent, version of HDL.",True,HDL: Reverse cholesterol transport,,,,
1c7a7889-d49d-4ef4-8a12-2f5b4fdd5541,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
1c7a7889-d49d-4ef4-8a12-2f5b4fdd5541,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
1c7a7889-d49d-4ef4-8a12-2f5b4fdd5541,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
ce8de735-a8b6-4876-b861-92b3cce2828a,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Fate of HDL,False,Fate of HDL,,,,
dfc82545-6749-4756-b8d5-d610213a295f,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"In the process of maturation, the nascent HDL particles accumulate phospholipids and cholesterol from cells lining the blood vessels. As the central hollow core of nascent HDL progressively fills with cholesterol esters, HDL takes on a more globular shape to eventually form the mature HDL particle. A major benefit of HDL particles derives from their ability to remove cholesterol from cholesterol-laden cells and to return the cholesterol to the liver, a process known as reverse cholesterol transport. This is particularly beneficial in vascular tissue; by reducing cellular cholesterol levels in the subintimal space, the likelihood that foam cells (lipid-laden macrophages that engulf oxidized LDL cholesterol) will form within the blood vessel wall is reduced.",True,Fate of HDL,,,,
0d8dfdeb-8ffc-49a8-be02-e3057ad57075,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
0d8dfdeb-8ffc-49a8-be02-e3057ad57075,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
0d8dfdeb-8ffc-49a8-be02-e3057ad57075,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
7abc88bc-330f-40db-9f83-ece8261029a8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Mature HDL particles can bind to specific receptors on hepatocytes (such as the apoE receptor), but the primary means of clearance of HDL from the blood is through its uptake by the scavenger receptor SR-B1. This receptor is present on many cell types, and once the HDL particle is bound to the receptor, its cholesterol and cholesterol esters are transferred into the cells. When depleted of cholesterol and its esters, the HDL particle dissociates from the SR-B1 receptor and reenters the circulation.",True,Fate of HDL,,,,
a55552b3-9b6f-4aa7-82c5-c2cf5f961477,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,HDL interactions with other particles,False,HDL interactions with other particles,,,,
b9e7cb34-32d1-48d8-8b68-a33551955f2c,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"As previously mentioned, HDL plays a key role in the maturation of both chylomicrons and VLDL. First, HDL transfers apoE and apoCII to chylomicrons and to VLDL. The apoCII stimulates the degradation of the TAGs of chylomicrons and VLDL by activating LPL. After digestion of the chylomicrons and the VLDL TAGs, apoE and apoCII are transferred back to HDL.",True,HDL interactions with other particles,,,,
af9eee19-48cd-4a51-8511-152073c78122,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
af9eee19-48cd-4a51-8511-152073c78122,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
af9eee19-48cd-4a51-8511-152073c78122,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
1a94c71c-3582-4070-a13a-77fd9eafe2d5,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Lipoprotein receptor-mediated endocytosis,False,Lipoprotein receptor-mediated endocytosis,,,,
9eb1006a-712e-443a-99ab-1bd93ab68409,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"As VLDLs mature to LDLs, these lipoproteins can be taken up through an interaction of the ApoB100 with the LDL receptors on the cell surface. The receptors for LDL are found in clathrin-coated pits within the cell membrane of the target cells. Upon receptor ligand interaction, the plasma membrane in the vicinity of the receptor‒LDL complex invaginates and fuses to form an endocytic vesicle. These vesicles then fuse with lysosomes, and the cholesterol esters of LDL are hydrolyzed to form free cholesterol, which is rapidly re-esterified through the action of ACAT. This rapid re-esterification is necessary to avoid the damaging effect of high levels of free cholesterol on cellular membranes.",True,Lipoprotein receptor-mediated endocytosis,,,,
94e5871e-4add-4606-92dd-127f1319efb7,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
94e5871e-4add-4606-92dd-127f1319efb7,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
94e5871e-4add-4606-92dd-127f1319efb7,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
78be3b78-8446-4571-b95f-054b67c63b8d,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,6.2 References and resources,True,Lipoprotein receptor-mediated endocytosis,,,,
a55798ca-76f3-4c2e-83a5-6f73e92d2f9e,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
a55798ca-76f3-4c2e-83a5-6f73e92d2f9e,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
a55798ca-76f3-4c2e-83a5-6f73e92d2f9e,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
dfb150a8-fe8f-48a5-9dfa-997ec408c9e9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
dfb150a8-fe8f-48a5-9dfa-997ec408c9e9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
dfb150a8-fe8f-48a5-9dfa-997ec408c9e9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
1ea88f25-9902-45e1-b88b-33278b9c83e1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
1ea88f25-9902-45e1-b88b-33278b9c83e1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
1ea88f25-9902-45e1-b88b-33278b9c83e1,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
3612ca5a-ac91-4aa1-83f7-25e5b69260a9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
3612ca5a-ac91-4aa1-83f7-25e5b69260a9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
3612ca5a-ac91-4aa1-83f7-25e5b69260a9,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
f29168cd-8ab4-4ea7-838c-bf1ed8481cbc,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
f29168cd-8ab4-4ea7-838c-bf1ed8481cbc,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
f29168cd-8ab4-4ea7-838c-bf1ed8481cbc,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
2e7627e9-e1ec-4ec7-9a64-53a777921ea8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
2e7627e9-e1ec-4ec7-9a64-53a777921ea8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
2e7627e9-e1ec-4ec7-9a64-53a777921ea8,https://pressbooks.lib.vt.edu/cellbio/,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/#chapter-69-section-1,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
cc5cd845-008a-4939-8899-b33a54300b19,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.2,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
cc5cd845-008a-4939-8899-b33a54300b19,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.2,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
cc5cd845-008a-4939-8899-b33a54300b19,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Cholesterol synthesis takes place in the cytosol, and the acetyl-CoA needed can be obtained from several sources such as β-oxidation of fatty acids, the oxidation of ketogenic amino acids, such as leucine and lysine, and the pyruvate dehydrogenase reaction (acetyl-CoA shuttled out of the mitochondria is in the form of citrate, which is cleaved into acetyl-CoA and pyruvate by citrate lyase). The process of cholesterol synthesis involves four stages (figure 6.2); however, only the first stage is regulated and will be focused on here.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.2,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
55572073-f6c5-436d-b551-6aa836069650,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Synthesis of mevalonate from acetyl-CoA,False,Synthesis of mevalonate from acetyl-CoA,,,,
0e4c2df0-167a-4c63-9b78-e82ab3bbb343,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
0e4c2df0-167a-4c63-9b78-e82ab3bbb343,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
0e4c2df0-167a-4c63-9b78-e82ab3bbb343,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The first stage of cholesterol synthesis leads to the production of the intermediate mevalonate. The synthesis of mevalonate is the committed, rate-limiting step in cholesterol formation. In this reaction, two molecules of acetyl-CoA condense, forming acetoacetyl-CoA, which then condenses with a third molecule of acetyl-CoA to yield the six-carbon compound β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) (figure 6.3) (the cytosolic HMG-CoA synthase in this reaction is distinct from the mitochondrial HMG-CoA synthase that catalyzes a similar reaction involved in production of ketone bodies). The committed step and major point of regulation of cholesterol synthesis involves reduction of HMG-CoA to mevalonate, in a reaction that is catalyzed by HMG-CoA reductase.",True,Synthesis of mevalonate from acetyl-CoA,Figure 6.3,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
fa050124-54fa-4acb-a2db-fdb59db6b6fc,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The subsequent steps of the pathway proceed largely unregulated, and mevalonate is used to synthesize isoprenoid units (five-carbon units). These five-carbon chains are joined in a head-to-tail fashion generating squalene, thirty-carbons, which undergoes a cyclization reaction after epoxidation. The cyclized product, lanosterol, undergoes several reactions to generate the final product, cholesterol.",True,Synthesis of mevalonate from acetyl-CoA,,,,
02e32198-e253-43a4-b9c8-d9a7c8f8e392,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,epoxidation,False,epoxidation,,,,
a77f2250-ff44-43ca-a3a8-06733d02664b,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,cyclized,False,cyclized,,,,
f3b7aa10-fe7b-42cb-80c1-97e627815f40,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Regulation of cholesterol synthesis,False,Regulation of cholesterol synthesis,,,,
7084f3ba-c9ad-4da3-96f9-24d91c8f174f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
7084f3ba-c9ad-4da3-96f9-24d91c8f174f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
7084f3ba-c9ad-4da3-96f9-24d91c8f174f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,The major regulatory enzyme for cholesterol synthesis is HMG-CoA reductase. This enzyme is tightly controlled by many different types of regulation and can be influenced by hormonal changes as well as cellular needs (figure 6.4). This is also one of the primary pharmacological targets for the management of hypercholesterolemia. The statins are direct inhibitors of this enzyme.,True,Regulation of cholesterol synthesis,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
21bdedb4-14d1-4b50-8b57-301865d3875a,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Transcriptional control,False,Transcriptional control,,,,
48fa28f4-939f-4888-8ffc-d003aea6b338,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
48fa28f4-939f-4888-8ffc-d003aea6b338,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
48fa28f4-939f-4888-8ffc-d003aea6b338,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The rate of synthesis of HMG-CoA reductase messenger RNA (mRNA) is controlled by one of the family of sterol-regulatory element-binding proteins (SREBPs). SREBPs are integral proteins of the endoplasmic reticulum (ER). When cholesterol levels in the cell are high, the SREBP is bound to SCAP (SREBP cleavage activating protein) in the ER membrane. When cholesterol levels drop, the sterol leaves its SCAP-binding site, and the SREBP:SCAP complex is transported to the Golgi apparatus. Within the Golgi, two proteolytic cleavages occur, which release the N-terminal transcription factor domain from the Golgi membrane. Once released, the active amino terminal component travels to the nucleus to bind to sterol-regulatory elements (SREs). Binding to this upstream element enhances transcription of the HMG-CoA reductase gene. The soluble SREBPs are rapidly turned over and need to be continuously produced to stimulate reductase mRNA transcription effectively. As cholesterol levels in the cell increase, due to de novo synthesis, cholesterol will bind to SCAP and prevent translocation of the complex to the Golgi, leading to a decrease in transcription of the reductase gene and thus less reductase protein being produced (figure 6.4).",True,Transcriptional control,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
3cd3f724-0170-4e15-bf2d-e60a567efacf,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Proteolytic degradation of HMG-CoA reductase,False,Proteolytic degradation of HMG-CoA reductase,,,,
818c2df4-2d3a-4807-a4ea-41c230029bbc,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The amount of HMG-CoA reductase can also be influenced by proteolytic degradation. The membrane domains of HMG-CoA reductase contain sterol-sensing regions, which are similar to those in SCAP. As levels of cholesterol (or its derivatives) increase in the cell, this causes a change in the oligomerization state of the membrane domain of HMG-CoA reductase, rendering the enzyme more susceptible to proteolysis. This, in turn, decreases the activity of the enzyme.",True,Proteolytic degradation of HMG-CoA reductase,,,,
4eac9e32-3bb2-426e-87e2-1b11ec4cfbc3,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Regulation by covalent modification,False,Regulation by covalent modification,,,,
3f2ef5b5-43f7-44b2-a8d8-915b3bb3837d,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Much like other anabolic enzymes, the activity of HMG-CoA reductase can be influenced by phosphorylation. Elevated glucagon levels increase phosphorylation of the enzyme, thereby inactivating it, whereas hyperinsulinemia increases the activity of the reductase by activating phosphatases, which dephosphorylate the reductase. Increased levels of intracellular sterols may also increase phosphorylation of HMG-CoA reductase, thereby reducing its activity as well (feedback suppression).",True,Regulation by covalent modification,,,,
9fe1de7d-384d-45c3-b1b9-0b6cf5fba1e4,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Adenosine monophosphate (AMP)-activated protein kinase can also phosphorylate and inactivate HMG-CoA reductase. Thus, cholesterol synthesis decreases when ATP levels are low and increases when ATP levels are high, similar to what occurs with fatty acid synthesis (recall that acetyl-CoA carboxylase is also phosphorylated and inhibited by the AMP-activated protein kinase; section 4.4.)",True,Regulation by covalent modification,,,,
51c1e10f-e154-4ee9-bc8a-592d787d61a4,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Several fates of cholesterol,False,Several fates of cholesterol,,,,
f8a45397-dc64-4500-aad8-0a9a6bee702f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Almost all mammalian cells are capable of producing cholesterol. Most of the biosynthesis of cholesterol occurs within liver cells, although the gut, the adrenal cortex, and the gonads (as well as the placenta in pregnant women) also produce significant quantities of the sterol. A small portion of hepatic cholesterol is used for the synthesis of hepatic membranes, but the bulk of synthesized cholesterol is secreted from the hepatocyte as one of three compounds: cholesterol esters, biliary cholesterol (cholesterol found in the bile), or bile acids.",True,Several fates of cholesterol,,,,
59f92066-351f-4862-a89d-ea70253a5cdc,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Cholesterol esterification and transport,False,Cholesterol esterification and transport,,,,
b61f20ee-466c-40bd-8cf6-bc8893279efe,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
b61f20ee-466c-40bd-8cf6-bc8893279efe,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
b61f20ee-466c-40bd-8cf6-bc8893279efe,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Cholesterol is an amphipathic molecule (containing both polar and nonpolar regions), and in its native state it can freely diffuse through membranes. In order to be stored in cells, cholesterol must be modified by increasing its hydrophobicity. Cholesterol ester production in the liver is catalyzed by acyl-CoA‒cholesterol acyl transferase (ACAT). ACAT catalyzes the transfer of a fatty acid from coenzyme A to the hydroxyl group on carbon 3 of cholesterol. (This is similar to the reaction catalyzed by lecithin:cholesterol acyltransferase within the plasma associated with HDLs; figure 6.5.) Regardless of whether the additional group is an acyl chain or phosphatidylcholine, the resulting cholesterol esters are more hydrophobic than free cholesterol. The liver packages some of the esterified cholesterol into the hollow core of lipoproteins, primarily VLDL. VLDL is secreted from the hepatocyte into the blood and transports the cholesterol esters (triacylglycerols, phospholipids, apoproteins, etc.) to the tissues that require greater amounts of cholesterol than they can synthesize de novo. These tissues then use the cholesterol for the synthesis of membranes, the formation of steroid hormones, and the biosynthesis of vitamin D.",True,Cholesterol esterification and transport,Figure 6.5,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
48330070-06c5-48d7-9282-69bfb2bac1f5,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Synthesis of specialized products,False,Synthesis of specialized products,,,,
be45f37a-f8f4-44b7-823c-2538653c85e6,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The hepatic cholesterol pool serves as a source of cholesterol for the synthesis of the relatively hydrophilic bile acids and their salts. These derivatives of cholesterol are effective detergents because they contain both polar and nonpolar regions. They are introduced into the biliary ducts of the liver. They are stored and concentrated in the gallbladder and later discharged into the gut in response to the ingestion of food. Finally, cholesterol is the precursor of all five classes of steroid hormones: glucocorticoids, mineralocorticoids, androgens, estrogens, and progestins. Cholesterol and steroid hormones are transported through the blood from their sites of synthesis to their target organs. Because of their hydrophobicity, they must be complexed with a serum protein. Serum albumin can act as a nonspecific carrier for the steroid hormones, but there are specific carriers as well (section 2.1).",True,Synthesis of specialized products,,,,
3ab1f9bd-754a-4bf9-89fe-273c795ca2e2,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,6.1 References and resources,True,Synthesis of specialized products,,,,
fb35db10-091e-4dd4-8415-76a50933af54,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 15: Metabolism of Dietary Lipids, Chapter 18: Cholesterol and Steroid Metabolism.",True,Synthesis of specialized products,,,,
2a2750dc-2e7a-4574-8475-e5daceabc1d6,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 92–94.",True,Synthesis of specialized products,,,,
b9f4d930-225f-4015-b182-f713aa02fc37,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 29: Digestion and Transport of Dietary Lipids, Chapter 32: Cholesterol Absorption: Synthesis, Metabolism and Fate Section.",True,Synthesis of specialized products,,,,
0ac30076-ca7e-4bad-98ed-a4956e5b0d43,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
0ac30076-ca7e-4bad-98ed-a4956e5b0d43,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
0ac30076-ca7e-4bad-98ed-a4956e5b0d43,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.1 Structure of cholesterol. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.1_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.1,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
c925c301-3ca5-48fa-a184-97b0c3cd7fef,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
c925c301-3ca5-48fa-a184-97b0c3cd7fef,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
c925c301-3ca5-48fa-a184-97b0c3cd7fef,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.2 Cholesterol synthetic pathway. 2021. https://archive.org/details/6.2_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.2,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
b40c0456-48db-45fd-bc0e-e5824a637c5e,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
b40c0456-48db-45fd-bc0e-e5824a637c5e,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
b40c0456-48db-45fd-bc0e-e5824a637c5e,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.3 Regulatory step catalyzed by HMG-CoA reductase. 2021. https://archive.org/details/6.3_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.3,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
67ec9e3d-0c38-465e-acee-bc8933825f0f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
67ec9e3d-0c38-465e-acee-bc8933825f0f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
67ec9e3d-0c38-465e-acee-bc8933825f0f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Grey, Kindred, Figure 6.5 Esterification of cholesterol by LCAT. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/6.5_20210924. CC BY 4.0.",True,Synthesis of specialized products,Figure 6.5,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
6e5fcdb9-31ba-4eb9-9f3d-2573b7068582,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
6e5fcdb9-31ba-4eb9-9f3d-2573b7068582,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
6e5fcdb9-31ba-4eb9-9f3d-2573b7068582,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.4 Regulation of cholesterol synthesis. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 647. Figure 32.6 Regulation of 3-hydroxymethylglutryl coenzyme A (HMG-CoA reductase activity. 2017. Added squiggle by Made by Made from the Noun Project and ion channel by Léa Lortal from the Noun Project.",True,Synthesis of specialized products,Figure 6.4,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
2bbdac05-8eb7-4b5f-b7a0-4aedd5701da6,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,6.2 Lipid Transport,True,Synthesis of specialized products,,,,
fc919343-4167-4554-96ec-628d2dc14cab,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Most of the lipids found in the body fall into the categories of fatty acids and triacylglycerols (TAGs); glycerophospholipids and sphingolipids; eicosanoids; cholesterol, bile salts, and steroid hormones; and fat-soluble vitamins. These lipids have very diverse chemical structures and functions. However, they are related by a common property, their relative insolubility in water.",True,Synthesis of specialized products,,,,
48b42256-1d2c-4444-9b84-b9087f20d3e9,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,TAGs,False,TAGs,,,,
6cec53c7-aca1-4aa1-82a5-e6b927db7c77,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
6cec53c7-aca1-4aa1-82a5-e6b927db7c77,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
6cec53c7-aca1-4aa1-82a5-e6b927db7c77,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"As such, a transport system for distribution of major lipids is in place to aid in the movement of these compounds. This system involves the family of lipoproteins, which have distinct roles in carrying dietary lipids, lipids synthesized through de novo mechanism in the liver, and for reverse cholesterol transport (figure 6.6).",True,TAGs,Figure 6.6,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
061bc1db-c702-4f55-a7fd-1de2ca1f17d0,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"In addition to the lipid components of lipoproteins, they contain protein components termed apoproteins. The complement of apoproteins on each lipoprotein is unique and is a distinguishing characteristic of each family of lipoproteins. The apoproteins (“apo” describes the protein within the shell of the particle in its lipid-free form) not only add to the hydrophilicity and structural stability of the particle, but they have other functions as well: (1) They activate certain enzymes required for normal lipoprotein metabolism, and (2) they act as ligands on the surface of the lipoprotein that target specific receptors on peripheral tissues that require lipoprotein delivery for their innate cellular functions.",True,TAGs,,,,
f8cc5c91-3a41-4121-986d-d0e096a52035,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,hydrophilicity,False,hydrophilicity,,,,
cf7e9012-8516-4ae6-b10d-e18bd6dc602d,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Chylomicrons: Transport of dietary lipids,False,Chylomicrons: Transport of dietary lipids,,,,
7bc98471-71cd-4b55-9abd-ced8190cd6e4,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
7bc98471-71cd-4b55-9abd-ced8190cd6e4,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
7bc98471-71cd-4b55-9abd-ced8190cd6e4,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Fatty acids, which are stored as TAGs, serve as fuels, providing the body with its major source of energy. TAGs are the major dietary lipids and are digested in the lumen of the intestine. The initial digestive products, free fatty acids and 2-monoacylglycerol, are reconverted to TAGs in intestinal epithelial cells, packaged in lipoproteins known as chylomicrons, and secreted into the lymph (figure 6.7).",True,Chylomicrons: Transport of dietary lipids,Figure 6.7,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
df9795d6-416c-4799-b941-36abf1d17042,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Chylomicrons are the largest lipoproteins and contain cholesterol and fat-soluble vitamins, in addition to their major component, dietary TAGs. The major apoprotein associated with chylomicrons as they leave the intestinal cells is ApoB-48. (The B-48 apoprotein is structurally and genetically related to the B-100 apoprotein synthesized in the liver that serves as a major protein of VLDL.) Microsomal transfer protein (MTP) aids in the loading of apoB-48 protein onto the chylomicron before the nascent chylomicron is secreted. Nascent chylomicrons are secreted by the intestinal epithelial cells into the chyle of the lymphatic system and enter the blood through the thoracic duct. Nascent chylomicrons begin to enter the blood within one to two hours after the start of a meal; as the meal is digested and absorbed, they continue to enter the blood for many hours. Chylomicron maturation occurs in circulation as they accept additional apoproteins from high-density lipoprotein (HDL) (figures 6.7 and 6.10).",True,Chylomicrons: Transport of dietary lipids,,,,
15ac38ad-1688-420d-b220-0e00d902e293,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"HDL predominantly transfers apoproteins E and CII to the nascent chylomicrons. ApoE is recognized by membrane receptors, and this interaction allows apoE-bearing lipoproteins to enter these cells by endocytosis; once inside the cell the particle is broken down through a lysosomal-mediated process. ApoCII acts as an activator of lipoprotein lipase (LPL), the enzyme on capillary endothelial cells, which digests the TAGs of the chylomicrons and VLDLs in the blood.",True,Chylomicrons: Transport of dietary lipids,,,,
e9bd1fd3-e9dc-494c-951a-681fd19cf3a9,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Fate of chylomicrons,False,Fate of chylomicrons,,,,
4d02603a-d038-46c0-9825-f6fb3e1c3c38,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The TAGs transported by chylomicrons are hydrolyzed by lipoprotein lipase (LPL), an enzyme present on endothelial cells that line the capillary walls. ApoCII on the chylomicron will interact with LPL and activate the enzyme. Insulin stimulates the synthesis and secretion of LPL so that after a meal, when triglyceride levels increase in circulation, LPL is upregulated (through insulin release) to facilitate the hydrolysis of fatty acids from the triglyceride.",True,Fate of chylomicrons,,,,
cb54981d-7205-4547-a5cc-3deed516e846,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Therefore, adipose LPL is more active after a meal, when chylomicron levels are elevated in the blood. The fatty acids released from TAGs by LPL are eventually repackaged in the adipose tissue and stored as TAGs within the tissue.",True,Fate of chylomicrons,,,,
0208caab-0255-4afe-82eb-2749a0f12f75,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The portion of a chylomicron that remains in the blood after LPL action is known as a chylomicron remnant. The remnant has returned (or lost) many of the apoC molecules bound to the mature chylomicron, exposing apoE. The remaining remnant binds to apoE receptors on hepatocytes, and is taken up by the process of endocytosis. Lysosomes fuse with the endocytic vesicles, and the chylomicron remnants are degraded by lysosomal enzymes. The products released through this degradation process (e.g., amino acids, fatty acids, cholesterol, etc.) can be recycled within the cell.",True,Fate of chylomicrons,,,,
d4832fe3-133c-43f1-8fad-7b31deb05aa7,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,VLDL: Transport of TAGs and cholesterol synthesized in the liver,False,VLDL: Transport of TAGs and cholesterol synthesized in the liver,,,,
dfed1689-356d-4a89-8e57-0dbe0fd3a29c,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
dfed1689-356d-4a89-8e57-0dbe0fd3a29c,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
dfed1689-356d-4a89-8e57-0dbe0fd3a29c,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Very low-density lipoprotein (VLDL) is produced in the liver, mainly from lipogenesis. Lipogenesis is an insulin-stimulated process through which excess glucose is converted to fatty acids (section 4.4), which are subsequently esterified to glycerol to form TAGs. TAGs produced in the smooth endoplasmic reticulum of the liver are packaged with cholesterol, phospholipids, and proteins (synthesized in the rough endoplasmic reticulum) to form VLDLs. Apart from their initial origin, VLDLs and chylomicrons are very similar with respect to maturation and activity. The VLDL particles acquire apoB-100 through an MTP-mediated reaction before being released into circulation. Within circulation, VLDLs also interact with HDL and acquire ApoCII and ApoE (figure 6.8). Like chylomicrons, VLDLs are also hydrolyzed by lipoprotein lipase (LPL), and the released fatty acids can be taken up by muscle and other tissues to be oxidized. After a meal, these fatty acids are also taken up by adipose tissue and stored as TAGs. In summary, the process of dietary versus de novo lipid transport has many parallels, which are compared in figure 6.9.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.8,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
7d8eef9c-623f-4cf3-847e-955c8ee1087a,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
7d8eef9c-623f-4cf3-847e-955c8ee1087a,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
7d8eef9c-623f-4cf3-847e-955c8ee1087a,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Although VLDLs and chylomicrons have similar roles in the cell, it is important to keep them distinct. The comparison between the transport of exogenous lipids and endogenous lipids is illustrated in figure 6.9. Because the fatty acids stored in adipose tissue come both from chylomicrons and VLDL, we produce our major fat stores both from dietary fat (which is transported by chylomicrons) and dietary sugar (which can be synthesized into TAGs and packaged into VLDL). An excess of dietary protein also can be used to produce the fatty acids for VLDL synthesis. Clinically, measured triacylglycerols (under fasting conditions) will largely reflect the VLDL contribution.",True,VLDL: Transport of TAGs and cholesterol synthesized in the liver,Figure 6.9,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
f4be5864-9ca4-412d-b4a6-e4fdb2c3ea19,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Fate of VLDL,False,Fate of VLDL,,,,
9a1f5bc0-1ad5-4254-8c3a-7de9f3dfcb71,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
9a1f5bc0-1ad5-4254-8c3a-7de9f3dfcb71,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
9a1f5bc0-1ad5-4254-8c3a-7de9f3dfcb71,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Much like the conversion of chylomicrons to chylomicron remnants, LPL converts VLDL to an intermediate-density lipoprotein (IDL). IDLs, having relatively low TAG content, are taken up by the liver through endocytosis, and degraded lysosomes as discussed above. IDL may also be converted to low-density lipoprotein (LDL) by further digestion of TAGs. Endocytosis of LDL occurs in peripheral tissues (and the liver) and is the major means of cholesterol transport and delivery to peripheral tissues. LDLs taken up by peripheral tissues will help increase the amount of intracellular cholesterol and therefore influence the regulation of HMG-CoA reductase (figure 6.11).",True,Fate of VLDL,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
0ae84b7b-f18c-4301-88b1-6008b51d3c0e,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,HDL: Reverse cholesterol transport,False,HDL: Reverse cholesterol transport,,,,
4f68b2a5-1b45-4a8d-ab01-6cd940bc53fe,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The primary function of high-density lipoprotein (HDL) is to transport excess cholesterol obtained from peripheral tissues to the liver. HDL also has other roles integral to lipid transport such as exchanging proteins and lipids with chylomicrons and VLDL. HDL particles can be created by several mechanisms, however, nascent HDLs are primarily secreted from the liver and intestine as a relatively small particles whose shell, like that of other lipoproteins, contains phospholipids, free cholesterol, and a variety of apoproteins, specifically apoAI, apoAII, apoCI, and apoCII. Very low levels of triacylglycerols or cholesterol esters are found in the hollow core of this early, or nascent, version of HDL.",True,HDL: Reverse cholesterol transport,,,,
468c2fc9-8a22-4130-9581-e22f47e71da3,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
468c2fc9-8a22-4130-9581-e22f47e71da3,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
468c2fc9-8a22-4130-9581-e22f47e71da3,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"HDLs can also be generated through budding of apoA from chylomicrons and VLDL particles or from free apoAI, which may be shed from other circulating lipoproteins. In this case, the apoAI acquires cholesterol and phospholipids from other lipoproteins and cell membranes, forming a nascent-like HDL particle within the circulation (figure 6.10).",True,HDL: Reverse cholesterol transport,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
8f3b6def-0a65-4742-9d58-28af631e5ea9,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Fate of HDL,False,Fate of HDL,,,,
53e2e808-d8bb-4d58-86bc-9e322efbaf19,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"In the process of maturation, the nascent HDL particles accumulate phospholipids and cholesterol from cells lining the blood vessels. As the central hollow core of nascent HDL progressively fills with cholesterol esters, HDL takes on a more globular shape to eventually form the mature HDL particle. A major benefit of HDL particles derives from their ability to remove cholesterol from cholesterol-laden cells and to return the cholesterol to the liver, a process known as reverse cholesterol transport. This is particularly beneficial in vascular tissue; by reducing cellular cholesterol levels in the subintimal space, the likelihood that foam cells (lipid-laden macrophages that engulf oxidized LDL cholesterol) will form within the blood vessel wall is reduced.",True,Fate of HDL,,,,
aa0568ab-0a2b-410c-8c7d-cf18f102431b,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
aa0568ab-0a2b-410c-8c7d-cf18f102431b,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
aa0568ab-0a2b-410c-8c7d-cf18f102431b,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Reverse cholesterol transport requires a movement of cholesterol from cellular stores to the lipoprotein particle. Cells contain the protein ABCA1 (ATP-binding cassette protein 1) that uses ATP hydrolysis to move cholesterol from the inner leaflet of the membrane to the outer leaflet. Once the cholesterol has reached the outer membrane leaflet, the HDL particle can accept it. To trap the cholesterol within the HDL core, the HDL particle acquires the enzyme lecithin-cholesterol acyltransferase (LCAT) from the circulation (figure 6.10). LCAT catalyzes the transfer of a fatty acid from the 2-position of lecithin (phosphatidylcholine) in the phospholipid shell of the particle to the 3-hydroxyl group of cholesterol, forming a cholesterol ester. The cholesterol esters form the core of the HDL particle and are no longer free to return to the cell.",True,Fate of HDL,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
9a873a15-36d5-4f83-91ab-50cb94cd6cf9,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Mature HDL particles can bind to specific receptors on hepatocytes (such as the apoE receptor), but the primary means of clearance of HDL from the blood is through its uptake by the scavenger receptor SR-B1. This receptor is present on many cell types, and once the HDL particle is bound to the receptor, its cholesterol and cholesterol esters are transferred into the cells. When depleted of cholesterol and its esters, the HDL particle dissociates from the SR-B1 receptor and reenters the circulation.",True,Fate of HDL,,,,
281de5b4-b85e-403a-bdce-d31eabd4aa4d,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,HDL interactions with other particles,False,HDL interactions with other particles,,,,
46ae9fde-feb4-4a86-bc15-9f70e441d847,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"As previously mentioned, HDL plays a key role in the maturation of both chylomicrons and VLDL. First, HDL transfers apoE and apoCII to chylomicrons and to VLDL. The apoCII stimulates the degradation of the TAGs of chylomicrons and VLDL by activating LPL. After digestion of the chylomicrons and the VLDL TAGs, apoE and apoCII are transferred back to HDL.",True,HDL interactions with other particles,,,,
ab73057b-32cd-423a-8967-7e5862fd1b5f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
ab73057b-32cd-423a-8967-7e5862fd1b5f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
ab73057b-32cd-423a-8967-7e5862fd1b5f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Another key interaction HDL has with VLDL allows for the redistribution of cholesterol between the two lipoproteins. When HDL obtains free cholesterol from cell membranes, HDL either transports the free cholesterol and cholesterol esters directly to the liver or it can exchange its cholesterol for TAGs in an interaction with VLDL. The cholesterol esterase transfer protein (CETP) resides in circulation and exchanges TAGs from VLDLs with cholesterol-esters from HDL. The greater the concentration of triacylglycerol-rich lipoproteins in the blood, the greater the rate of these exchanges. The CETP exchange pathway may partially explain the observation that whenever triacylglycerol-rich lipoproteins are present in the blood in high concentrations, the amount of cholesterol reaching the liver via cholesterol-enriched VLDL and VLDL remnants increases (figure 6.10), and is consistent with a proportional reduction in the total amount of cholesterol and cholesterol esters that are transferred directly to the liver via HDL.",True,HDL interactions with other particles,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
df6a48c4-aeac-415a-be19-6a4a02233b93,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Lipoprotein receptor-mediated endocytosis,False,Lipoprotein receptor-mediated endocytosis,,,,
6d80f7bb-ac99-4197-aaf5-05266e705529,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"As VLDLs mature to LDLs, these lipoproteins can be taken up through an interaction of the ApoB100 with the LDL receptors on the cell surface. The receptors for LDL are found in clathrin-coated pits within the cell membrane of the target cells. Upon receptor ligand interaction, the plasma membrane in the vicinity of the receptor‒LDL complex invaginates and fuses to form an endocytic vesicle. These vesicles then fuse with lysosomes, and the cholesterol esters of LDL are hydrolyzed to form free cholesterol, which is rapidly re-esterified through the action of ACAT. This rapid re-esterification is necessary to avoid the damaging effect of high levels of free cholesterol on cellular membranes.",True,Lipoprotein receptor-mediated endocytosis,,,,
308c80c9-a7ad-4b65-896b-8a92b6d49253,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
308c80c9-a7ad-4b65-896b-8a92b6d49253,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
308c80c9-a7ad-4b65-896b-8a92b6d49253,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"The synthesis of the LDL receptor itself is regulated by feedback inhibition as intracellular levels of cholesterol increase. One probable mechanism for this feedback regulation involves one or more of the SREBPs described earlier. These proteins or the cofactors that are required for the full expression of genes that code for the LDL receptor are also capable of sensing the concentration of cholesterol (and its derivatives) within the cell. When sterol levels are high, the process that leads to the binding of the SREBP to the SRE of these genes is suppressed. The rate of synthesis from mRNA for the LDL receptor is reduced under these circumstances. This, in turn, appropriately reduces the amount of cholesterol that can enter these cholesterol-rich cells by receptor-mediated endocytosis (down-regulation of receptor synthesis). When the intracellular levels of cholesterol decrease, these processes are reversed, and cells act to increase their cholesterol levels. Both synthesis of cholesterol from acetyl-CoA and synthesis of LDL receptors are stimulated. An increased number of receptors (up-regulation of receptor synthesis) results in an increased uptake of LDL cholesterol from the blood, with a subsequent reduction of LDL cholesterol levels. At the same time, the cellular cholesterol pool is replenished (figure 6.11).",True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
4d38009c-c7c2-4c3f-b805-813e9e6a4852,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,6.2 References and resources,True,Lipoprotein receptor-mediated endocytosis,,,,
c624714d-2e3d-4c48-976b-c5dcf2ccf611,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
c624714d-2e3d-4c48-976b-c5dcf2ccf611,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
c624714d-2e3d-4c48-976b-c5dcf2ccf611,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Ferrier D. Figure 6.6 Overview of lipoprotein size and structure. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 227. Figure 18.13 Plasma lipoprotein particles exhibit a range of sizes and densities, and typical values are shown. 2017.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.6,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
6e01058e-55cb-4efa-948f-6678435e08b3,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
6e01058e-55cb-4efa-948f-6678435e08b3,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
6e01058e-55cb-4efa-948f-6678435e08b3,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,Ferrier D. Figure 6.11 Uptake of LDL and regulation of cholesterol synthesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 233. Figure 18.20 Cellular uptake and degradation of low-density lipoprotein (LDL) particles. 2017. Added squiggle by Made by Made from the Noun Project.,True,Lipoprotein receptor-mediated endocytosis,Figure 6.11,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
a5229f30-36ba-454c-b34f-34f74e4821ec,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
a5229f30-36ba-454c-b34f-34f74e4821ec,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
a5229f30-36ba-454c-b34f-34f74e4821ec,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.7 Transport of dietary lipids via chylomicrons. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 601. Figure 29.11 Fate of chylomicrons. 2017. Added Liver by Liam Mitchell from the Noun Project, Muscle by Laymik from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.7,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
d672345a-3a91-4885-83dd-980b6f771e69,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
d672345a-3a91-4885-83dd-980b6f771e69,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
d672345a-3a91-4885-83dd-980b6f771e69,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.8 Transport of TAGs from de novo synthesis using VLDL. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 680. Figure 32.12 Fate of very-low-desnity lipoprteins (VLDL). 2017. Added macrophage by Léa Lortal from the Noun Project, Liver by Liam Mitchell from the Noun Project, and red blood cells by Lucas Helle from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.8,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
68ebff60-9867-486d-83e5-6eaded45127f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
68ebff60-9867-486d-83e5-6eaded45127f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
68ebff60-9867-486d-83e5-6eaded45127f,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Lieberman M, Peet A. Figure 6.10 Interaction of chylomicrons and VLDL with HDL in circulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 683. Figure 32.15 Functions and fate of high-density lipoprotein (HDL). 2017. Added Liver by Liam Mitchell from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.10,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
374b993b-2c08-4e45-b71b-dce6876e0513,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6.2 Lipid Transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
374b993b-2c08-4e45-b71b-dce6876e0513,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6.1 Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
374b993b-2c08-4e45-b71b-dce6876e0513,https://pressbooks.lib.vt.edu/cellbio/,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/lipoprotein-metabolism-and-cholesterol-synthesis/,"Loscalzo J. Figure 6.9 Comparison of the role of chylomicrons and VLDLs in lipid transport. Adapted under Fair Use from Harrison’s Cardiovascular Medicine 2 ed. online. Figure 31.2 The exogenous and endogenous lipoprotein metabolic pathways. 2013. Added Small Intestine by PJ Witt from the Noun Project, Liver by Liam Mitchell from the Noun Project, and Muscle by Laymik from the Noun Project.",True,Lipoprotein receptor-mediated endocytosis,Figure 6.9,6. Lipoprotein Metabolism and Cholesterol Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
7b1c39a6-f646-4be5-abd9-a048ac421ab0,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lipolysis, β-oxidation, and ketogenesis",False,"Lipolysis, β-oxidation, and ketogenesis",,,,
e3ff7342-0e4b-4798-a2d1-2a22eb37ce15,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Urea cycle and nitrogen metabolism,False,Urea cycle and nitrogen metabolism,,,,
c47897ec-9681-4c6c-95b1-08fe4cfe0234,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Glycogenolysis (see section 4.5),True,Urea cycle and nitrogen metabolism,,,,
be5d552c-0325-4f4a-bb11-c49abb636892,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
be5d552c-0325-4f4a-bb11-c49abb636892,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
be5d552c-0325-4f4a-bb11-c49abb636892,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
be5d552c-0325-4f4a-bb11-c49abb636892,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
e3b226cb-1f77-4afc-815b-e7daab1dbe0d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
e3b226cb-1f77-4afc-815b-e7daab1dbe0d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
e3b226cb-1f77-4afc-815b-e7daab1dbe0d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
e3b226cb-1f77-4afc-815b-e7daab1dbe0d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
6a899269-e34c-4a7c-8091-516cd47f8475,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,GNG,False,GNG,,,,
bfe2dea3-9907-4e6e-8e5d-13c9417525e1,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Substrates for GNG,False,Substrates for GNG,,,,
025be493-9651-4d8e-b190-88b05087b090,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Amino acids,False,Amino acids,,,,
791a7b80-2845-490c-b751-394d6b7310e7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
791a7b80-2845-490c-b751-394d6b7310e7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
791a7b80-2845-490c-b751-394d6b7310e7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
791a7b80-2845-490c-b751-394d6b7310e7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
1e3c26be-c0fe-46a6-bc40-51c26716a790,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,phosphoenol,False,phosphoenol,,,,
4669f3ad-9c9b-468a-b683-5d2adffde3f8,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,OAA,False,OAA,,,,
6a02efc7-1ed6-4bc4-8ff9-661aed0218e4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Lactate,False,Lactate,,,,
c827d3f2-88d2-4b93-9996-ea3bb4eb386e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
c827d3f2-88d2-4b93-9996-ea3bb4eb386e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
c827d3f2-88d2-4b93-9996-ea3bb4eb386e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
c827d3f2-88d2-4b93-9996-ea3bb4eb386e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
1bec3daf-3791-49b9-b886-65acd7a911e4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Glycerol,False,Glycerol,,,,
cc7d6716-b10f-4fb4-b3a9-06aa2d5b05dd,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
cc7d6716-b10f-4fb4-b3a9-06aa2d5b05dd,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
cc7d6716-b10f-4fb4-b3a9-06aa2d5b05dd,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
cc7d6716-b10f-4fb4-b3a9-06aa2d5b05dd,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
e8361666-7b2c-4bde-9d13-73924fed2e7b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Interconnection of GNG and other metabolic pathways,False,Interconnection of GNG and other metabolic pathways,,,,
688be0dc-83fd-415f-8951-c710e297c9da,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis is heavily reliant on support from other pathways. It requires amino acids for carbon substrates from cortisol-mediated protein catabolism. The ability of those amino acids to be deaminated relies on the ability of the urea cycle to remove ammonia in the form of nontoxic urea, and perhaps most importantly, gluconeogenesis relies on the process of β-oxidation.",True,Interconnection of GNG and other metabolic pathways,,,,
065694cf-1966-4b06-ae61-911679bb5195,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,β-oxidation,False,β-oxidation,,,,
7e2cee11-9914-4584-835a-e7e9b36678d9,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,The process of β-oxidation supports gluconeogenesis in two major ways:,False,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
d207e8ae-ee2f-4d28-844e-c5e1dd26b8eb,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Acetyl-CoA produced from β-oxidation itself is not a substrate for gluconeogenesis, rather it is required for allosteric activation of pyruvate carboxylase, which is the first step in GNG. Again, acetyl-CoA is not a substrate for this process; it is fully oxidized in the TCA cycle and provides no additional carbons to be exported from the TCA cycle as malate. Therefore the cell has to rely on amino acid carbon skeletons, glycerol, and lactate as substrates for glucose production (section 5.2).",True,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
245f82dd-6bf7-4bca-b2eb-7a4f003fff41,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Regulation of gluconeogenesis,False,Regulation of gluconeogenesis,,,,
31084380-5736-4457-b5b5-d7b89a684a20,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),False,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
977b4b53-5358-41f0-8d9f-4ff563e872f7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
977b4b53-5358-41f0-8d9f-4ff563e872f7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
977b4b53-5358-41f0-8d9f-4ff563e872f7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
977b4b53-5358-41f0-8d9f-4ff563e872f7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
468dd3a5-1956-4116-8626-1ce68cda9a38,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Once phosphoenol pyruvate (PEP) is synthesized, it will continue through the reverse process using the glycolytic enzymes until it reaches its next irreversible conversion.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
1176e1c5-1396-4cfc-a289-460b785672de,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Fructose 1,6-bisphosphatase (FBP1)",False,"Fructose 1,6-bisphosphatase (FBP1)",,,,
12c5c357-49fb-4f02-8d67-cf4e9a649d4b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
12c5c357-49fb-4f02-8d67-cf4e9a649d4b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
12c5c357-49fb-4f02-8d67-cf4e9a649d4b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
12c5c357-49fb-4f02-8d67-cf4e9a649d4b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
a9b7cea1-4ae3-4760-b736-cbe9e0e7eaa4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
a9b7cea1-4ae3-4760-b736-cbe9e0e7eaa4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
a9b7cea1-4ae3-4760-b736-cbe9e0e7eaa4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
a9b7cea1-4ae3-4760-b736-cbe9e0e7eaa4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
a9b7cea1-4ae3-4760-b736-cbe9e0e7eaa4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
a9b7cea1-4ae3-4760-b736-cbe9e0e7eaa4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
17fe2ac4-ba2c-4d8a-b262-33428e0f1236,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Glucose 6-phosphatase,False,Glucose 6-phosphatase,,,,
59fba310-3cf6-4493-8ac4-8e0b4fdaa8fe,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Finally, glucose 6-phosphatase is required to dephosphorylate glucose 6-phosphate so it can be released from the liver. This is a key step for both glycogenolysis and gluconeogenesis, and deficiencies in this enzyme can lead to severe bouts of fasting hypoglycemia.",True,Glucose 6-phosphatase,,,,
ae547752-a237-4170-9895-90a3dad25b2e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Glycogenolysis,False,Glycogenolysis,,,,
7ad90183-5361-4821-9895-0ea40f1b77f1,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In contrast to glycogen synthesis, glycogenolysis is the release of glucose 6-phosphate from glycogen stores. It can occur in both the liver and the skeletal muscle but under two different conditions (figures 5.6 and 5.7). As noted above, this is a pathway active in the fasted state.",True,Glycogenolysis,,,,
0270cd4d-a42f-478b-8bb0-4b5abde2d47a,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Regulation of glycogenolysis,False,Regulation of glycogenolysis,,,,
26f235cc-b67c-4beb-8032-0438fa807114,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Hepatic glycogenolysis,False,Hepatic glycogenolysis,,,,
fa5d48ba-43a0-4051-aa22-ab6715431fd8,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
fa5d48ba-43a0-4051-aa22-ab6715431fd8,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
fa5d48ba-43a0-4051-aa22-ab6715431fd8,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
fa5d48ba-43a0-4051-aa22-ab6715431fd8,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
0136b268-ce9f-421f-a8e0-ac901b689c59,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Epinephrine can also enhance hepatic glycogenolysis by binding an α-agonist receptor. This initiates the cleavage of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol 1,4,5-triphosphate (IP3) and diacylglyerol (DAG) by phospholipase C. IP3 stimulates Ca2+ release from endoplasmic reticulum and results in both:",True,Hepatic glycogenolysis,,,,
580d830e-0119-4afc-9404-ff5e83fc86f0,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In all cases, the glucose 6-phosphate released from glycogen stores is dephosphorylated by glucose 6-phosphatase and released from the liver.",True,Hepatic glycogenolysis,,,,
4ee53eca-0ece-4f27-a58b-e4234fc5c994,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Skeletal muscle glycogenolysis,False,Skeletal muscle glycogenolysis,,,,
3c6aa6e4-a20f-4622-968a-8135e39ad619,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
3c6aa6e4-a20f-4622-968a-8135e39ad619,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
3c6aa6e4-a20f-4622-968a-8135e39ad619,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
3c6aa6e4-a20f-4622-968a-8135e39ad619,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
b916f06d-1ac9-41cd-b35c-e8b5c62ebc1c,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Summary of pathway regulation,False,Summary of pathway regulation,,,,
6aa6a40f-ccef-4e08-90f9-792fcc96a0b2,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Table 5.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
09cc9c78-560d-4da8-b03b-4f4d4dc1efe7,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,5.1 References and resources,True,Summary of pathway regulation,,,,
a0533ceb-fbf0-43f2-956c-40dca7e555e8,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 10: Gluconeogenesis: Section II, III, IV, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section III, IV, V, Chapter 19: Removal of Nitrogen from Amino Acids: Section V, VI, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
b4146c8c-38a4-42e0-a148-5f101ceaf66f,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 78, 82, 86, 89–90.",True,Summary of pathway regulation,,,,
49133e69-5fc3-46ce-a3fe-66c9fd162e74,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 3: The Fasted State, Chapter 19: Basic Concepts in Regulation, Chapter 24: Oxidative Phosphorylation and the ETC, Chapter 26: Formation of Glycogen, Chapter 28: Gluconeogenesis, Chapter 30: Oxidation of Fatty Acids, Chapter 34: Integration of Carbohydrate and Lipid Metabolism, Chapter 36: Fate of Amino Acids Nitrogen: Urea Cycle.",True,Summary of pathway regulation,,,,
20d405f0-cd3d-4473-b170-f2e2ae4a0a30,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
20d405f0-cd3d-4473-b170-f2e2ae4a0a30,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
20d405f0-cd3d-4473-b170-f2e2ae4a0a30,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
20d405f0-cd3d-4473-b170-f2e2ae4a0a30,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
637bfd44-e906-4889-8fb7-7168d8ca045b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
637bfd44-e906-4889-8fb7-7168d8ca045b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
637bfd44-e906-4889-8fb7-7168d8ca045b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
637bfd44-e906-4889-8fb7-7168d8ca045b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
3a9a80da-139c-4a46-9c26-dbe221f1f137,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
3a9a80da-139c-4a46-9c26-dbe221f1f137,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
3a9a80da-139c-4a46-9c26-dbe221f1f137,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
3a9a80da-139c-4a46-9c26-dbe221f1f137,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
6ca281ca-6636-41c7-b32b-52d5a4bcdffb,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
6ca281ca-6636-41c7-b32b-52d5a4bcdffb,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
6ca281ca-6636-41c7-b32b-52d5a4bcdffb,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
6ca281ca-6636-41c7-b32b-52d5a4bcdffb,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
45892f06-a8d1-4ed8-81b0-95bd80579035,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
45892f06-a8d1-4ed8-81b0-95bd80579035,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
45892f06-a8d1-4ed8-81b0-95bd80579035,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
45892f06-a8d1-4ed8-81b0-95bd80579035,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
ead8efc0-2306-43e9-8ca4-80d8d6e54c9d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
ead8efc0-2306-43e9-8ca4-80d8d6e54c9d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
ead8efc0-2306-43e9-8ca4-80d8d6e54c9d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
ead8efc0-2306-43e9-8ca4-80d8d6e54c9d,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
e9cea747-d390-4b49-91d9-1135adf763aa,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
e9cea747-d390-4b49-91d9-1135adf763aa,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
e9cea747-d390-4b49-91d9-1135adf763aa,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
e9cea747-d390-4b49-91d9-1135adf763aa,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
4338022d-aaa7-4b00-aea9-503a6ebe50be,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",True,Summary of pathway regulation,,,,
b5b6da0b-d292-48ae-adb5-f481024dd9d6,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The processes of lipolysis, β-oxidation, and ketogenesis work in concert within the cell but should be considered distinct pathways.",True,Summary of pathway regulation,,,,
91066c4b-092d-4a87-9a24-6d084fab3a08,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Lipolysis,False,Lipolysis,,,,
c84fb514-70b7-4c18-8cbe-8a0feba2d288,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
c84fb514-70b7-4c18-8cbe-8a0feba2d288,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
c84fb514-70b7-4c18-8cbe-8a0feba2d288,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
c84fb514-70b7-4c18-8cbe-8a0feba2d288,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
5c87a414-2e54-48c9-98ff-f9fbfa14168b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,TAGs,False,TAGs,,,,
c6e2365c-b9c9-4d83-b4a9-c48afe9ae8fe,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,LCFAs,False,LCFAs,,,,
1f85bff7-60d9-47c5-83b8-cf8e9e457a35,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,β-oxidation (oxidation of free fatty acids),False,β-oxidation (oxidation of free fatty acids),,,,
7090d0cb-1e2e-4de6-8726-0e196ce4b830,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7090d0cb-1e2e-4de6-8726-0e196ce4b830,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7090d0cb-1e2e-4de6-8726-0e196ce4b830,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7090d0cb-1e2e-4de6-8726-0e196ce4b830,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
c406f662-2904-4039-8c73-323a6642e996,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
c406f662-2904-4039-8c73-323a6642e996,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
c406f662-2904-4039-8c73-323a6642e996,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
c406f662-2904-4039-8c73-323a6642e996,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4d7d6248-5b8e-4594-89dd-8596d6e31a76,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4d7d6248-5b8e-4594-89dd-8596d6e31a76,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4d7d6248-5b8e-4594-89dd-8596d6e31a76,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4d7d6248-5b8e-4594-89dd-8596d6e31a76,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
6705722a-174e-4725-9a90-74d99af118b2,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Regulation of β-oxidation,False,Regulation of β-oxidation,,,,
d2e1ace2-a3cc-4495-b382-beb7d66696ab,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
d2e1ace2-a3cc-4495-b382-beb7d66696ab,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
d2e1ace2-a3cc-4495-b382-beb7d66696ab,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
d2e1ace2-a3cc-4495-b382-beb7d66696ab,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
c1a17b77-054f-4dd1-b787-d0e20b287813,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Ketogenesis,False,Ketogenesis,,,,
7592682d-cc74-44e6-8c22-01de8a817bb1,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
7592682d-cc74-44e6-8c22-01de8a817bb1,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
7592682d-cc74-44e6-8c22-01de8a817bb1,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
7592682d-cc74-44e6-8c22-01de8a817bb1,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
e8b2c041-78e0-45e7-ba6c-31161566065c,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
e8b2c041-78e0-45e7-ba6c-31161566065c,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
e8b2c041-78e0-45e7-ba6c-31161566065c,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
e8b2c041-78e0-45e7-ba6c-31161566065c,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
eec41915-2c09-4a80-94e9-742520e4e4d8,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Table 5.2: Summary of pathway regulation.,True,Ketogenesis,,,,
76872677-0281-4e4f-b803-3400ad732ead,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,5.2 References and resources,True,Ketogenesis,,,,
613a1709-7cca-44c6-bde7-611783049734,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Text,False,Text,,,,
9dae9c6a-6b01-489c-a0a0-8f4e18d54722,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
9dae9c6a-6b01-489c-a0a0-8f4e18d54722,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
9dae9c6a-6b01-489c-a0a0-8f4e18d54722,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
9dae9c6a-6b01-489c-a0a0-8f4e18d54722,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
7f7607ab-6f28-4180-98dd-635e703a4736,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7f7607ab-6f28-4180-98dd-635e703a4736,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7f7607ab-6f28-4180-98dd-635e703a4736,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7f7607ab-6f28-4180-98dd-635e703a4736,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
812224f7-67aa-4c25-bb64-ebf3c90bb24b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
812224f7-67aa-4c25-bb64-ebf3c90bb24b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
812224f7-67aa-4c25-bb64-ebf3c90bb24b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
812224f7-67aa-4c25-bb64-ebf3c90bb24b,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
104e50ce-c6c8-402f-8933-1b18df5c4620,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
104e50ce-c6c8-402f-8933-1b18df5c4620,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
104e50ce-c6c8-402f-8933-1b18df5c4620,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
104e50ce-c6c8-402f-8933-1b18df5c4620,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
0aa9b910-1639-4a13-bf0d-ba377672fa43,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,5.3 Nitrogen Metabolism and the Urea Cycle,True,Text,,,,
398e30a1-9d07-425c-92b9-be0f1b0c477e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Amino acids play key roles as precursors to nitrogen-containing compounds (such as nucleotides and neurotransmitters), as substrates for protein synthesis, and as an oxidizable substrate for energy production (or storage). Unlike carbohydrate and lipid metabolism, we must be concerned with the fates of both the carbon- and nitrogen-containing moieties when discussing the metabolism of amino acids. In the case of amino acids, nitrogen is released as ammonia (NH3), and at physiological pH the majority of ammonia is present as an ammonium ion (NH4+). (It is important to note that only ammonia can cross cellular membranes.) The majority of ammonia is incorporated into urea (in the liver) and excreted by the kidney, while the remaining carbon-containing skeleton is oxidized or utilized in other anabolic pathways (i.e., gluconeogenesis).",True,Text,,,,
400db309-7e07-4eaf-8c3c-64c126598d52,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Transport of nitrogen via amino acids,False,Transport of nitrogen via amino acids,,,,
a44c3075-cf55-4e40-a49a-d4ee94549854,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The amino acid pool is continually in flux and can be influenced by both dietary protein consumption as well as normal protein turnover within the tissues. Given that the major site of nitrogen disposal is the liver, a mechanism for transport of excess amino acid nitrogen from the peripheral tissues to the liver is in place. Both alanine and glutamine play an essential role as nontoxic carriers of ammonia from peripheral tissues to the liver (figures 5.12 and 5.13). To generate alanine and glutamine for transport, amino acids can undergo transamination reactions.",True,Transport of nitrogen via amino acids,,,,
164007f2-2285-4801-ba73-55d03e1f5929,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Transamination: The movement of nitrogen,False,Transamination: The movement of nitrogen,,,,
1b9b2a04-c146-45cf-9bea-c2465731cb20,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Amino transferases are a family of enzymes (which require pyridoxal phosphate; PLP) as a cofactor to help transfer nitrogen from amino acids on to keto-acid backbones. These enzymes do not free ammonia, but will transfer nitrogen from an amino group to a keto-group in an exchange or transferase reaction. Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) are common and clinically relevant transferases. AST will preferentially accept aspartate and transaminate it in a reaction with α-ketoglutarate (the keto-acid of glutamate) to generate oxaloacetate (OAA) (the keto-acid of aspartate) and glutamate (figures 5.12 and 5.13).",True,Transamination: The movement of nitrogen,,,,
80fd8a89-87be-46a7-9c4e-f77538c4cda5,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",False,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",,,,
719c0809-1e48-4c89-aba5-84881dc6f07e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
719c0809-1e48-4c89-aba5-84881dc6f07e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
719c0809-1e48-4c89-aba5-84881dc6f07e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
719c0809-1e48-4c89-aba5-84881dc6f07e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
ac7d7a67-1be1-45f1-9ead-01dc39a38090,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,GDH,False,GDH,,,,
7c1ca1ac-8a56-4c9f-a40f-459b1c72a858,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7c1ca1ac-8a56-4c9f-a40f-459b1c72a858,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7c1ca1ac-8a56-4c9f-a40f-459b1c72a858,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7c1ca1ac-8a56-4c9f-a40f-459b1c72a858,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
4e735630-8767-4095-a6e4-f4e8ba10fa4f,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In skeletal muscle, the alanine-glucose cycle is commonly used for the transport of nitrogen from the skeletal muscle to the liver. In this process, ammonia from amino acid degradation is transaminated to form glutamate. Alanine aminotransferase (AST) will transaminate glutamate with pyruvate to generate alanine (and α-ketoglutarate). The alanine is released and transported to the liver where it will undergo another transamination to generate pyruvate, which is used as a substrate for glucose production (gluconeogenesis). The glucose is released from the liver and oxidized by the skeletal muscle.",True,GDH,,,,
31da73ee-240e-49ce-9d81-6f2223ca0127,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
31da73ee-240e-49ce-9d81-6f2223ca0127,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
31da73ee-240e-49ce-9d81-6f2223ca0127,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
31da73ee-240e-49ce-9d81-6f2223ca0127,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
d5f0b896-e88c-465c-8b8d-766fa5321e30,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Urea cycle,False,Urea cycle,,,,
18bac7bc-5c0d-42e3-a70f-f16ec01d5f6a,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Ammonia freed in the liver by glutaminase (or glutamate dehydrogenase) will readily enter the urea cycle to be incorporated into urea. A functioning urea cycle is essential for the disposal of nitrogen from catabolic processes, and if dysfunction occurs the accumulation of ammonia can be life threatening.",True,Urea cycle,,,,
59140a94-84bc-45a2-9fd9-2fe3a8ab28a2,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,The urea cycle occurs in the liver and spans both the mitochondria and the cytosolic compartments. The initial free ammonia diffuses through the mitochondrial membrane and is fixed with carbon dioxide (in the form of bicarbonate) during the initial step in this process (figures 5.15 and 5.16). It is important to remember that the synthesis of urea is an anabolic process that requires ATP. Therefore deficiencies in ATP production can inhibit nitrogen disposal as well.,True,Urea cycle,,,,
d303e33b-9eb9-4623-8991-0cd9b2793531,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"The product of this pathway, urea, is made of two nitrogenous groups with the first coming from the free ammonia released by glutaminase. The second nitrogen is added later in the cycle by aspartate (figures 5.16 and 5.17).",True,Urea cycle,,,,
e6434e01-5eb5-46db-97ea-e8fe9f4191cb,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Regulation of the urea cycle,False,Regulation of the urea cycle,,,,
e6e4c0fb-98e1-4c65-9504-bf6a798c0c1f,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
e6e4c0fb-98e1-4c65-9504-bf6a798c0c1f,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
e6e4c0fb-98e1-4c65-9504-bf6a798c0c1f,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
e6e4c0fb-98e1-4c65-9504-bf6a798c0c1f,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
9a2e40ed-8b34-45e2-ab61-0a9bc350f30e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
9a2e40ed-8b34-45e2-ab61-0a9bc350f30e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
9a2e40ed-8b34-45e2-ab61-0a9bc350f30e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
9a2e40ed-8b34-45e2-ab61-0a9bc350f30e,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
4b51e50f-78a0-40f4-b2cf-bc492b0a6480,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"In summary, the process of nitrogen movement from the peripheral tissues to the liver is essential. It involves transamination reactions to produce alanine, and the synthesis of glutamine (by glutamine synthetase) to generate two nontoxic carriers of ammonia. Once transported to the liver, again, transamination coupled with the reactions of glutaminase and glutamate dehydrogenase will allow for ammonia to be freed and enter into the urea cycle.",True,Regulation of the urea cycle,,,,
f45b82f5-1883-4805-9438-447c72ff08c2,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,Table 5.3: Summary of pathway regulation.,True,Regulation of the urea cycle,,,,
77c037e3-9cea-4d8c-a377-442839103abc,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,5.3 References and resources,True,Regulation of the urea cycle,,,,
43879706-fc4d-483a-a54e-4fc7ebb32013,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
43879706-fc4d-483a-a54e-4fc7ebb32013,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
43879706-fc4d-483a-a54e-4fc7ebb32013,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
43879706-fc4d-483a-a54e-4fc7ebb32013,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
81dd6117-2309-4ee1-b282-91240a0cdd35,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
81dd6117-2309-4ee1-b282-91240a0cdd35,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
81dd6117-2309-4ee1-b282-91240a0cdd35,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
81dd6117-2309-4ee1-b282-91240a0cdd35,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
b3e4c6e1-66f3-4773-b47c-df948f2bd5dc,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
b3e4c6e1-66f3-4773-b47c-df948f2bd5dc,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
b3e4c6e1-66f3-4773-b47c-df948f2bd5dc,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
b3e4c6e1-66f3-4773-b47c-df948f2bd5dc,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
13b8f0b2-872e-4035-bd86-4ba0cda7d9e4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
13b8f0b2-872e-4035-bd86-4ba0cda7d9e4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
13b8f0b2-872e-4035-bd86-4ba0cda7d9e4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
13b8f0b2-872e-4035-bd86-4ba0cda7d9e4,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
b4966179-5ceb-4d55-8a4f-3c9b61607114,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
b4966179-5ceb-4d55-8a4f-3c9b61607114,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
b4966179-5ceb-4d55-8a4f-3c9b61607114,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
b4966179-5ceb-4d55-8a4f-3c9b61607114,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
9edfde3a-6a31-4086-af9a-7ae4a94536ed,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
9edfde3a-6a31-4086-af9a-7ae4a94536ed,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
9edfde3a-6a31-4086-af9a-7ae4a94536ed,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
9edfde3a-6a31-4086-af9a-7ae4a94536ed,https://pressbooks.lib.vt.edu/cellbio/,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-3,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
aa64cc5c-ca60-4b4d-9ba2-f8639443fa1f,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lipolysis, β-oxidation, and ketogenesis",False,"Lipolysis, β-oxidation, and ketogenesis",,,,
5e5fd18e-0612-47d5-837d-f53a17696a48,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Urea cycle and nitrogen metabolism,False,Urea cycle and nitrogen metabolism,,,,
26b84431-7245-4655-9300-bea6b0c5c1fb,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Glycogenolysis (see section 4.5),True,Urea cycle and nitrogen metabolism,,,,
09e7a01e-1aed-48ca-9c45-074f288ebe9d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
09e7a01e-1aed-48ca-9c45-074f288ebe9d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
09e7a01e-1aed-48ca-9c45-074f288ebe9d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
09e7a01e-1aed-48ca-9c45-074f288ebe9d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
5e09a932-8412-4051-8653-88ddd1f4dfa5,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
5e09a932-8412-4051-8653-88ddd1f4dfa5,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
5e09a932-8412-4051-8653-88ddd1f4dfa5,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
5e09a932-8412-4051-8653-88ddd1f4dfa5,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
5d0763c1-6d08-472e-bdfe-dda08a2fdfe4,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,GNG,False,GNG,,,,
a099d757-7736-4e29-861c-bafa3043b528,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Substrates for GNG,False,Substrates for GNG,,,,
81e354ee-7431-477f-b14f-412a99e615a7,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Amino acids,False,Amino acids,,,,
a050cd91-018d-4b4d-9987-bf2087261157,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
a050cd91-018d-4b4d-9987-bf2087261157,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
a050cd91-018d-4b4d-9987-bf2087261157,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
a050cd91-018d-4b4d-9987-bf2087261157,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
9e4a0767-b562-43c6-a53e-7497cd0d7dee,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,phosphoenol,False,phosphoenol,,,,
861d1987-3ab9-42c2-aca1-5219e3a3bf23,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,OAA,False,OAA,,,,
9e47b65f-de9f-4b31-b695-902ccc9dc9ae,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Lactate,False,Lactate,,,,
b3d07c23-f3f4-4007-81a7-ab2d018a2904,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
b3d07c23-f3f4-4007-81a7-ab2d018a2904,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
b3d07c23-f3f4-4007-81a7-ab2d018a2904,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
b3d07c23-f3f4-4007-81a7-ab2d018a2904,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
50ada65b-14d6-44e4-b821-11f37be964d7,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Glycerol,False,Glycerol,,,,
10fbae8c-6f7d-4836-8020-c09093874ae0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
10fbae8c-6f7d-4836-8020-c09093874ae0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
10fbae8c-6f7d-4836-8020-c09093874ae0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
10fbae8c-6f7d-4836-8020-c09093874ae0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
3555933e-1a2e-45f6-91fd-7606e9e91f93,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Interconnection of GNG and other metabolic pathways,False,Interconnection of GNG and other metabolic pathways,,,,
1e2fae35-b62c-4aa4-aac1-ffb421d861da,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis is heavily reliant on support from other pathways. It requires amino acids for carbon substrates from cortisol-mediated protein catabolism. The ability of those amino acids to be deaminated relies on the ability of the urea cycle to remove ammonia in the form of nontoxic urea, and perhaps most importantly, gluconeogenesis relies on the process of β-oxidation.",True,Interconnection of GNG and other metabolic pathways,,,,
7cfc3b43-ce49-498a-89bc-9412fa64cbfd,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,β-oxidation,False,β-oxidation,,,,
c321eec3-7277-49e6-aece-39a2be128e4d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,The process of β-oxidation supports gluconeogenesis in two major ways:,False,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
e80fa49e-e613-4ce6-9ffe-db976bdfce5e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Acetyl-CoA produced from β-oxidation itself is not a substrate for gluconeogenesis, rather it is required for allosteric activation of pyruvate carboxylase, which is the first step in GNG. Again, acetyl-CoA is not a substrate for this process; it is fully oxidized in the TCA cycle and provides no additional carbons to be exported from the TCA cycle as malate. Therefore the cell has to rely on amino acid carbon skeletons, glycerol, and lactate as substrates for glucose production (section 5.2).",True,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
4366fcca-3bc9-4e26-addc-8c46b1a409cd,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Regulation of gluconeogenesis,False,Regulation of gluconeogenesis,,,,
ffcf7d16-52fc-47a3-bc50-17d0a333fe87,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),False,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
28e6eb9a-3934-4282-a5f1-78979941720a,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
28e6eb9a-3934-4282-a5f1-78979941720a,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
28e6eb9a-3934-4282-a5f1-78979941720a,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
28e6eb9a-3934-4282-a5f1-78979941720a,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
ce7fa267-0029-4230-8d16-7ed8e23e515e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Once phosphoenol pyruvate (PEP) is synthesized, it will continue through the reverse process using the glycolytic enzymes until it reaches its next irreversible conversion.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
0e0b5251-d078-4dfd-8a74-56551c4a30e0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Fructose 1,6-bisphosphatase (FBP1)",False,"Fructose 1,6-bisphosphatase (FBP1)",,,,
4cd0d8bc-e9a6-4f35-8957-4183b10b465d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
4cd0d8bc-e9a6-4f35-8957-4183b10b465d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
4cd0d8bc-e9a6-4f35-8957-4183b10b465d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
4cd0d8bc-e9a6-4f35-8957-4183b10b465d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
288677fc-f54d-448c-b22c-f6fffb42402e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
288677fc-f54d-448c-b22c-f6fffb42402e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
288677fc-f54d-448c-b22c-f6fffb42402e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
288677fc-f54d-448c-b22c-f6fffb42402e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
288677fc-f54d-448c-b22c-f6fffb42402e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
288677fc-f54d-448c-b22c-f6fffb42402e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
f62b880d-f656-42d4-b9f3-7b576fc10237,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Glucose 6-phosphatase,False,Glucose 6-phosphatase,,,,
d9006518-8dfb-4d89-be08-5e1ac8ed1ab0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Finally, glucose 6-phosphatase is required to dephosphorylate glucose 6-phosphate so it can be released from the liver. This is a key step for both glycogenolysis and gluconeogenesis, and deficiencies in this enzyme can lead to severe bouts of fasting hypoglycemia.",True,Glucose 6-phosphatase,,,,
847250f5-8eaa-4812-9b28-496911c27abb,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Glycogenolysis,False,Glycogenolysis,,,,
e70f1b68-0694-43f2-9a37-bf5a71cba28a,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In contrast to glycogen synthesis, glycogenolysis is the release of glucose 6-phosphate from glycogen stores. It can occur in both the liver and the skeletal muscle but under two different conditions (figures 5.6 and 5.7). As noted above, this is a pathway active in the fasted state.",True,Glycogenolysis,,,,
f32f105a-0d9f-4239-a1dc-48651cfdccca,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Regulation of glycogenolysis,False,Regulation of glycogenolysis,,,,
763ac891-e53a-4afc-a6fe-0d2915c5a220,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Hepatic glycogenolysis,False,Hepatic glycogenolysis,,,,
9e1d006b-975e-4f9f-803a-f3dcb18861f1,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
9e1d006b-975e-4f9f-803a-f3dcb18861f1,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
9e1d006b-975e-4f9f-803a-f3dcb18861f1,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
9e1d006b-975e-4f9f-803a-f3dcb18861f1,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
73d96878-aa92-497f-8f71-95e392adaaa2,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Epinephrine can also enhance hepatic glycogenolysis by binding an α-agonist receptor. This initiates the cleavage of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol 1,4,5-triphosphate (IP3) and diacylglyerol (DAG) by phospholipase C. IP3 stimulates Ca2+ release from endoplasmic reticulum and results in both:",True,Hepatic glycogenolysis,,,,
fb4832c2-9ba7-4a31-917f-a2c57a2e0546,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In all cases, the glucose 6-phosphate released from glycogen stores is dephosphorylated by glucose 6-phosphatase and released from the liver.",True,Hepatic glycogenolysis,,,,
dd9addd2-5a11-42de-a39d-e4ed6c33a8ef,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Skeletal muscle glycogenolysis,False,Skeletal muscle glycogenolysis,,,,
b453a5b3-fefe-4f9c-8048-c38dc7fa8d07,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
b453a5b3-fefe-4f9c-8048-c38dc7fa8d07,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
b453a5b3-fefe-4f9c-8048-c38dc7fa8d07,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
b453a5b3-fefe-4f9c-8048-c38dc7fa8d07,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
f9f28285-28b7-477a-82b6-13d5a49a3e8d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Summary of pathway regulation,False,Summary of pathway regulation,,,,
6c12417e-1c6d-4c06-b10d-5a2c386396b0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Table 5.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
df722104-1e29-456d-8536-8ce07cddf2f4,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,5.1 References and resources,True,Summary of pathway regulation,,,,
253b6ccc-70a9-4cda-a4a8-636d80f9e100,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 10: Gluconeogenesis: Section II, III, IV, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section III, IV, V, Chapter 19: Removal of Nitrogen from Amino Acids: Section V, VI, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
97b570d6-2555-4597-8b78-bc99ea037b83,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 78, 82, 86, 89–90.",True,Summary of pathway regulation,,,,
e3d6d11d-3289-49c4-b7e8-b4c85bd4aae8,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 3: The Fasted State, Chapter 19: Basic Concepts in Regulation, Chapter 24: Oxidative Phosphorylation and the ETC, Chapter 26: Formation of Glycogen, Chapter 28: Gluconeogenesis, Chapter 30: Oxidation of Fatty Acids, Chapter 34: Integration of Carbohydrate and Lipid Metabolism, Chapter 36: Fate of Amino Acids Nitrogen: Urea Cycle.",True,Summary of pathway regulation,,,,
c4aea27d-6584-41b1-bf35-de1656861b74,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
c4aea27d-6584-41b1-bf35-de1656861b74,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
c4aea27d-6584-41b1-bf35-de1656861b74,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
c4aea27d-6584-41b1-bf35-de1656861b74,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
84bc3028-3e1f-4082-9822-635feb9e255d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
84bc3028-3e1f-4082-9822-635feb9e255d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
84bc3028-3e1f-4082-9822-635feb9e255d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
84bc3028-3e1f-4082-9822-635feb9e255d,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
6d268028-44ec-4601-98cc-b6d1245c0c2e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
6d268028-44ec-4601-98cc-b6d1245c0c2e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
6d268028-44ec-4601-98cc-b6d1245c0c2e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
6d268028-44ec-4601-98cc-b6d1245c0c2e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
201c68d9-f83f-427c-9e75-df7c49bd3e50,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
201c68d9-f83f-427c-9e75-df7c49bd3e50,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
201c68d9-f83f-427c-9e75-df7c49bd3e50,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
201c68d9-f83f-427c-9e75-df7c49bd3e50,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
f9a1063e-a2e2-44c6-a5a5-017c63d5a3fb,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
f9a1063e-a2e2-44c6-a5a5-017c63d5a3fb,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
f9a1063e-a2e2-44c6-a5a5-017c63d5a3fb,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
f9a1063e-a2e2-44c6-a5a5-017c63d5a3fb,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
75a373b8-aee7-44ed-9c27-d5eda0155ae6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
75a373b8-aee7-44ed-9c27-d5eda0155ae6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
75a373b8-aee7-44ed-9c27-d5eda0155ae6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
75a373b8-aee7-44ed-9c27-d5eda0155ae6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
6a36b128-d85b-4b6c-b450-4ba51e37cec6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
6a36b128-d85b-4b6c-b450-4ba51e37cec6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
6a36b128-d85b-4b6c-b450-4ba51e37cec6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
6a36b128-d85b-4b6c-b450-4ba51e37cec6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
e6e2544b-cadd-4c86-b64f-b5fdf3e01a64,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",True,Summary of pathway regulation,,,,
341a0b13-b7c4-4b39-a144-56890f53a0db,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The processes of lipolysis, β-oxidation, and ketogenesis work in concert within the cell but should be considered distinct pathways.",True,Summary of pathway regulation,,,,
20d3b62e-3463-4c24-8af8-bd99e2cc4fe6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Lipolysis,False,Lipolysis,,,,
fad524b7-e3f4-4af2-b988-773d48226377,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
fad524b7-e3f4-4af2-b988-773d48226377,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
fad524b7-e3f4-4af2-b988-773d48226377,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
fad524b7-e3f4-4af2-b988-773d48226377,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
fb17055a-e71c-4f09-9a21-f50eb6115134,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,TAGs,False,TAGs,,,,
1acba2f7-6a91-4e36-97da-745cb65bb995,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,LCFAs,False,LCFAs,,,,
cfefad51-efb1-40a6-be0f-e68d8ed39cd2,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,β-oxidation (oxidation of free fatty acids),False,β-oxidation (oxidation of free fatty acids),,,,
5d95e0f8-4fc8-4813-9232-c87b4c2704e2,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
5d95e0f8-4fc8-4813-9232-c87b4c2704e2,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
5d95e0f8-4fc8-4813-9232-c87b4c2704e2,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
5d95e0f8-4fc8-4813-9232-c87b4c2704e2,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
27710d29-aad7-4d83-a347-3e042e8bf363,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
27710d29-aad7-4d83-a347-3e042e8bf363,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
27710d29-aad7-4d83-a347-3e042e8bf363,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
27710d29-aad7-4d83-a347-3e042e8bf363,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
adceee31-757e-4e13-9dda-8c014d7793be,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
adceee31-757e-4e13-9dda-8c014d7793be,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
adceee31-757e-4e13-9dda-8c014d7793be,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
adceee31-757e-4e13-9dda-8c014d7793be,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
e78d3af2-9535-45c1-9f60-191fd7490aab,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Regulation of β-oxidation,False,Regulation of β-oxidation,,,,
ec3005a5-d3dd-4269-b783-37f442dbb449,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
ec3005a5-d3dd-4269-b783-37f442dbb449,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
ec3005a5-d3dd-4269-b783-37f442dbb449,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
ec3005a5-d3dd-4269-b783-37f442dbb449,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
e008669c-2afa-4187-b0d3-b047b7e85ee3,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Ketogenesis,False,Ketogenesis,,,,
df960079-c426-4d2d-9250-c83153fcbd95,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
df960079-c426-4d2d-9250-c83153fcbd95,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
df960079-c426-4d2d-9250-c83153fcbd95,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
df960079-c426-4d2d-9250-c83153fcbd95,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
6ee994cb-08f9-469b-8ed8-0f82fb88bdf4,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
6ee994cb-08f9-469b-8ed8-0f82fb88bdf4,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
6ee994cb-08f9-469b-8ed8-0f82fb88bdf4,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
6ee994cb-08f9-469b-8ed8-0f82fb88bdf4,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
35e8f1f1-1d1f-4504-bd2d-3f96b33e5e7f,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Table 5.2: Summary of pathway regulation.,True,Ketogenesis,,,,
39c4b5d5-4b1f-492a-bf4a-c538a289d7d0,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,5.2 References and resources,True,Ketogenesis,,,,
c5982055-58bf-4eb3-a615-04df6e3f3173,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Text,False,Text,,,,
334f1f5c-878d-40db-ab4c-d794a0a0b334,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
334f1f5c-878d-40db-ab4c-d794a0a0b334,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
334f1f5c-878d-40db-ab4c-d794a0a0b334,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
334f1f5c-878d-40db-ab4c-d794a0a0b334,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
77a0acdb-fd1e-4fd4-befb-20b2a398e4db,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
77a0acdb-fd1e-4fd4-befb-20b2a398e4db,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
77a0acdb-fd1e-4fd4-befb-20b2a398e4db,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
77a0acdb-fd1e-4fd4-befb-20b2a398e4db,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
e98008fe-d777-428b-9ce6-561ac494c5c3,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
e98008fe-d777-428b-9ce6-561ac494c5c3,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
e98008fe-d777-428b-9ce6-561ac494c5c3,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
e98008fe-d777-428b-9ce6-561ac494c5c3,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
c0ce73b9-4033-4b1b-a86f-55599409790b,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
c0ce73b9-4033-4b1b-a86f-55599409790b,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
c0ce73b9-4033-4b1b-a86f-55599409790b,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
c0ce73b9-4033-4b1b-a86f-55599409790b,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
3df71578-aab4-4a09-98b2-5a5ab60ee318,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,5.3 Nitrogen Metabolism and the Urea Cycle,True,Text,,,,
435382e3-ed10-49f1-a5cd-70cd0834af61,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Amino acids play key roles as precursors to nitrogen-containing compounds (such as nucleotides and neurotransmitters), as substrates for protein synthesis, and as an oxidizable substrate for energy production (or storage). Unlike carbohydrate and lipid metabolism, we must be concerned with the fates of both the carbon- and nitrogen-containing moieties when discussing the metabolism of amino acids. In the case of amino acids, nitrogen is released as ammonia (NH3), and at physiological pH the majority of ammonia is present as an ammonium ion (NH4+). (It is important to note that only ammonia can cross cellular membranes.) The majority of ammonia is incorporated into urea (in the liver) and excreted by the kidney, while the remaining carbon-containing skeleton is oxidized or utilized in other anabolic pathways (i.e., gluconeogenesis).",True,Text,,,,
58b1058e-3cf7-4f62-9df6-5f7f62d6d32e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Transport of nitrogen via amino acids,False,Transport of nitrogen via amino acids,,,,
34f2c8e0-0128-4835-8c86-5e4141c195b6,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The amino acid pool is continually in flux and can be influenced by both dietary protein consumption as well as normal protein turnover within the tissues. Given that the major site of nitrogen disposal is the liver, a mechanism for transport of excess amino acid nitrogen from the peripheral tissues to the liver is in place. Both alanine and glutamine play an essential role as nontoxic carriers of ammonia from peripheral tissues to the liver (figures 5.12 and 5.13). To generate alanine and glutamine for transport, amino acids can undergo transamination reactions.",True,Transport of nitrogen via amino acids,,,,
bbd7c011-d932-4830-b309-c0ef87ca2181,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Transamination: The movement of nitrogen,False,Transamination: The movement of nitrogen,,,,
880d6256-75ea-4256-8e44-15c3c9365167,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Amino transferases are a family of enzymes (which require pyridoxal phosphate; PLP) as a cofactor to help transfer nitrogen from amino acids on to keto-acid backbones. These enzymes do not free ammonia, but will transfer nitrogen from an amino group to a keto-group in an exchange or transferase reaction. Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) are common and clinically relevant transferases. AST will preferentially accept aspartate and transaminate it in a reaction with α-ketoglutarate (the keto-acid of glutamate) to generate oxaloacetate (OAA) (the keto-acid of aspartate) and glutamate (figures 5.12 and 5.13).",True,Transamination: The movement of nitrogen,,,,
7592a974-8729-4676-8c16-5a8dd20d6636,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",False,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",,,,
a88a052d-691b-410c-a93c-70e5570e9c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
a88a052d-691b-410c-a93c-70e5570e9c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
a88a052d-691b-410c-a93c-70e5570e9c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
a88a052d-691b-410c-a93c-70e5570e9c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
f5533190-d88e-4e7b-b46e-bf8ab744dafa,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,GDH,False,GDH,,,,
73f4ddb7-a1da-40f1-9d11-8b08e0c09e21,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
73f4ddb7-a1da-40f1-9d11-8b08e0c09e21,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
73f4ddb7-a1da-40f1-9d11-8b08e0c09e21,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
73f4ddb7-a1da-40f1-9d11-8b08e0c09e21,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
e4b82c9f-8799-4edd-b9c8-0af73d056f3a,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In skeletal muscle, the alanine-glucose cycle is commonly used for the transport of nitrogen from the skeletal muscle to the liver. In this process, ammonia from amino acid degradation is transaminated to form glutamate. Alanine aminotransferase (AST) will transaminate glutamate with pyruvate to generate alanine (and α-ketoglutarate). The alanine is released and transported to the liver where it will undergo another transamination to generate pyruvate, which is used as a substrate for glucose production (gluconeogenesis). The glucose is released from the liver and oxidized by the skeletal muscle.",True,GDH,,,,
c7027549-f343-45a3-8c63-ab0845eddd0e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
c7027549-f343-45a3-8c63-ab0845eddd0e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
c7027549-f343-45a3-8c63-ab0845eddd0e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
c7027549-f343-45a3-8c63-ab0845eddd0e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
f765e90b-2f7f-4fd0-8944-cdc2dc690ebd,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Urea cycle,False,Urea cycle,,,,
d5f3daab-0799-457d-90e8-75c556244f12,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Ammonia freed in the liver by glutaminase (or glutamate dehydrogenase) will readily enter the urea cycle to be incorporated into urea. A functioning urea cycle is essential for the disposal of nitrogen from catabolic processes, and if dysfunction occurs the accumulation of ammonia can be life threatening.",True,Urea cycle,,,,
4f15703e-245c-436a-bef1-9ccf4b24db4a,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,The urea cycle occurs in the liver and spans both the mitochondria and the cytosolic compartments. The initial free ammonia diffuses through the mitochondrial membrane and is fixed with carbon dioxide (in the form of bicarbonate) during the initial step in this process (figures 5.15 and 5.16). It is important to remember that the synthesis of urea is an anabolic process that requires ATP. Therefore deficiencies in ATP production can inhibit nitrogen disposal as well.,True,Urea cycle,,,,
0cacde12-30df-418c-8393-e21afbde0c48,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"The product of this pathway, urea, is made of two nitrogenous groups with the first coming from the free ammonia released by glutaminase. The second nitrogen is added later in the cycle by aspartate (figures 5.16 and 5.17).",True,Urea cycle,,,,
9b39d51e-6272-4cc4-bcab-30e2ff8c8f16,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Regulation of the urea cycle,False,Regulation of the urea cycle,,,,
2f0c045a-e802-4865-9db3-1ad199e5945e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
2f0c045a-e802-4865-9db3-1ad199e5945e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
2f0c045a-e802-4865-9db3-1ad199e5945e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
2f0c045a-e802-4865-9db3-1ad199e5945e,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
29ddbef2-2c1c-49d9-b790-760cb90a5b8c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
29ddbef2-2c1c-49d9-b790-760cb90a5b8c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
29ddbef2-2c1c-49d9-b790-760cb90a5b8c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
29ddbef2-2c1c-49d9-b790-760cb90a5b8c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
ed6095f4-1428-4693-ab99-24d6409f7315,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"In summary, the process of nitrogen movement from the peripheral tissues to the liver is essential. It involves transamination reactions to produce alanine, and the synthesis of glutamine (by glutamine synthetase) to generate two nontoxic carriers of ammonia. Once transported to the liver, again, transamination coupled with the reactions of glutaminase and glutamate dehydrogenase will allow for ammonia to be freed and enter into the urea cycle.",True,Regulation of the urea cycle,,,,
78b53d22-8f80-4eda-9f41-771bacc8e4d4,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,Table 5.3: Summary of pathway regulation.,True,Regulation of the urea cycle,,,,
b1754307-e44b-4778-953f-cd4493456d4b,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,5.3 References and resources,True,Regulation of the urea cycle,,,,
8f56f6ba-c866-4428-b26d-19277b064ccc,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
8f56f6ba-c866-4428-b26d-19277b064ccc,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
8f56f6ba-c866-4428-b26d-19277b064ccc,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
8f56f6ba-c866-4428-b26d-19277b064ccc,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
990a40bb-1112-4f75-96f0-c48c40292a70,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
990a40bb-1112-4f75-96f0-c48c40292a70,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
990a40bb-1112-4f75-96f0-c48c40292a70,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
990a40bb-1112-4f75-96f0-c48c40292a70,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
842ed0a5-1e63-43ce-ac22-2efefd755148,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
842ed0a5-1e63-43ce-ac22-2efefd755148,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
842ed0a5-1e63-43ce-ac22-2efefd755148,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
842ed0a5-1e63-43ce-ac22-2efefd755148,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
84591423-39d4-4e0c-a79d-facb4aa92429,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
84591423-39d4-4e0c-a79d-facb4aa92429,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
84591423-39d4-4e0c-a79d-facb4aa92429,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
84591423-39d4-4e0c-a79d-facb4aa92429,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
ab4b1e65-2998-4d54-b2f1-1c37deffbead,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
ab4b1e65-2998-4d54-b2f1-1c37deffbead,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
ab4b1e65-2998-4d54-b2f1-1c37deffbead,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
ab4b1e65-2998-4d54-b2f1-1c37deffbead,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
f3cb76df-dc45-4815-8896-3f59d0894c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
f3cb76df-dc45-4815-8896-3f59d0894c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
f3cb76df-dc45-4815-8896-3f59d0894c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
f3cb76df-dc45-4815-8896-3f59d0894c1c,https://pressbooks.lib.vt.edu/cellbio/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-2,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
1f4c4e13-312f-4ac2-a228-a84bc0c2d11c,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lipolysis, β-oxidation, and ketogenesis",False,"Lipolysis, β-oxidation, and ketogenesis",,,,
af2af29b-a0ba-4b97-852a-9166dd6acc77,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Urea cycle and nitrogen metabolism,False,Urea cycle and nitrogen metabolism,,,,
49d56ef0-da37-41a5-b3a5-e918eccdd3c5,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Glycogenolysis (see section 4.5),True,Urea cycle and nitrogen metabolism,,,,
0fd1f73a-51ec-47e5-b5e0-81b621167cd4,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
0fd1f73a-51ec-47e5-b5e0-81b621167cd4,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
0fd1f73a-51ec-47e5-b5e0-81b621167cd4,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
0fd1f73a-51ec-47e5-b5e0-81b621167cd4,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
fb5a44d0-e16d-4b86-a848-5cbf07b3eb98,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
fb5a44d0-e16d-4b86-a848-5cbf07b3eb98,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
fb5a44d0-e16d-4b86-a848-5cbf07b3eb98,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
fb5a44d0-e16d-4b86-a848-5cbf07b3eb98,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
c7a808a2-c48d-4183-81d4-fdc4fd01dbc4,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,GNG,False,GNG,,,,
276f987c-cd4a-4e22-be30-9566230c9978,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Substrates for GNG,False,Substrates for GNG,,,,
cacf8b3c-d7ea-489a-b769-1232b7253c2e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Amino acids,False,Amino acids,,,,
10168178-b1aa-4567-b083-d2191d0d53d1,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
10168178-b1aa-4567-b083-d2191d0d53d1,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
10168178-b1aa-4567-b083-d2191d0d53d1,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
10168178-b1aa-4567-b083-d2191d0d53d1,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
40753d19-4582-4dd8-859b-96087c527b90,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,phosphoenol,False,phosphoenol,,,,
342c2e03-88de-4d39-81ab-bcd4aad6f081,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,OAA,False,OAA,,,,
71f1b4a8-33a9-455d-abe5-b701ec48d45f,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Lactate,False,Lactate,,,,
a3b5b2a7-94b5-4160-a919-ab7f93c59f5a,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
a3b5b2a7-94b5-4160-a919-ab7f93c59f5a,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
a3b5b2a7-94b5-4160-a919-ab7f93c59f5a,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
a3b5b2a7-94b5-4160-a919-ab7f93c59f5a,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
c7edd38a-e79a-4c0b-81db-8df34c34ad32,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Glycerol,False,Glycerol,,,,
e3009fcb-c509-428a-b89b-860578462224,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
e3009fcb-c509-428a-b89b-860578462224,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
e3009fcb-c509-428a-b89b-860578462224,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
e3009fcb-c509-428a-b89b-860578462224,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
e06c1d7c-170f-42f8-9a8c-fb0635c380f8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Interconnection of GNG and other metabolic pathways,False,Interconnection of GNG and other metabolic pathways,,,,
e2d0f68b-8c0a-4f03-8240-252728c72c50,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis is heavily reliant on support from other pathways. It requires amino acids for carbon substrates from cortisol-mediated protein catabolism. The ability of those amino acids to be deaminated relies on the ability of the urea cycle to remove ammonia in the form of nontoxic urea, and perhaps most importantly, gluconeogenesis relies on the process of β-oxidation.",True,Interconnection of GNG and other metabolic pathways,,,,
4979948b-e614-4bff-a76e-d83e405e0c84,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,β-oxidation,False,β-oxidation,,,,
8d24ef2a-94c9-43f7-b294-598d163971c9,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,The process of β-oxidation supports gluconeogenesis in two major ways:,False,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
6dda752f-ac1b-4065-94c4-0d09b93901c6,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Acetyl-CoA produced from β-oxidation itself is not a substrate for gluconeogenesis, rather it is required for allosteric activation of pyruvate carboxylase, which is the first step in GNG. Again, acetyl-CoA is not a substrate for this process; it is fully oxidized in the TCA cycle and provides no additional carbons to be exported from the TCA cycle as malate. Therefore the cell has to rely on amino acid carbon skeletons, glycerol, and lactate as substrates for glucose production (section 5.2).",True,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
3c10fb8c-905a-4eaf-b64f-7ae245de80ba,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Regulation of gluconeogenesis,False,Regulation of gluconeogenesis,,,,
72816091-91c0-466c-a343-899266df1d81,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),False,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
958e26cf-6d94-4345-b7e5-73387fc319cf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
958e26cf-6d94-4345-b7e5-73387fc319cf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
958e26cf-6d94-4345-b7e5-73387fc319cf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
958e26cf-6d94-4345-b7e5-73387fc319cf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
07147988-e685-481f-89c4-55a91e057387,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Once phosphoenol pyruvate (PEP) is synthesized, it will continue through the reverse process using the glycolytic enzymes until it reaches its next irreversible conversion.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
8227dc6f-7149-4a2f-bd5e-b9de34a5290b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Fructose 1,6-bisphosphatase (FBP1)",False,"Fructose 1,6-bisphosphatase (FBP1)",,,,
793af2d4-757c-4740-adfa-89b426627fbc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
793af2d4-757c-4740-adfa-89b426627fbc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
793af2d4-757c-4740-adfa-89b426627fbc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
793af2d4-757c-4740-adfa-89b426627fbc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
9fcfdf74-090a-47d8-a52e-01b6c951cd8e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
9fcfdf74-090a-47d8-a52e-01b6c951cd8e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
9fcfdf74-090a-47d8-a52e-01b6c951cd8e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
9fcfdf74-090a-47d8-a52e-01b6c951cd8e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
9fcfdf74-090a-47d8-a52e-01b6c951cd8e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
9fcfdf74-090a-47d8-a52e-01b6c951cd8e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
a585542d-48f9-4564-ba2f-1ef0573d4b73,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Glucose 6-phosphatase,False,Glucose 6-phosphatase,,,,
9d2148c8-c37f-486c-bcc4-ee01429473b4,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Finally, glucose 6-phosphatase is required to dephosphorylate glucose 6-phosphate so it can be released from the liver. This is a key step for both glycogenolysis and gluconeogenesis, and deficiencies in this enzyme can lead to severe bouts of fasting hypoglycemia.",True,Glucose 6-phosphatase,,,,
f7787abc-c226-4478-80a7-f325c1982f90,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Glycogenolysis,False,Glycogenolysis,,,,
9f6d1da0-60f3-4d6e-b8d2-d610562dcebb,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In contrast to glycogen synthesis, glycogenolysis is the release of glucose 6-phosphate from glycogen stores. It can occur in both the liver and the skeletal muscle but under two different conditions (figures 5.6 and 5.7). As noted above, this is a pathway active in the fasted state.",True,Glycogenolysis,,,,
68949888-76d5-4ea0-9351-0725f1741a85,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Regulation of glycogenolysis,False,Regulation of glycogenolysis,,,,
a0b9ce34-8782-4339-a0a8-19b6aba9de17,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Hepatic glycogenolysis,False,Hepatic glycogenolysis,,,,
d471b05f-f208-4783-83c4-bfb1b09029a7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
d471b05f-f208-4783-83c4-bfb1b09029a7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
d471b05f-f208-4783-83c4-bfb1b09029a7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
d471b05f-f208-4783-83c4-bfb1b09029a7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
5f74fd0b-d8f9-4b25-8b39-0b642c541628,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Epinephrine can also enhance hepatic glycogenolysis by binding an α-agonist receptor. This initiates the cleavage of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol 1,4,5-triphosphate (IP3) and diacylglyerol (DAG) by phospholipase C. IP3 stimulates Ca2+ release from endoplasmic reticulum and results in both:",True,Hepatic glycogenolysis,,,,
ce87d9e0-25e5-40f2-acef-f2d5731772f3,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In all cases, the glucose 6-phosphate released from glycogen stores is dephosphorylated by glucose 6-phosphatase and released from the liver.",True,Hepatic glycogenolysis,,,,
3c6b9208-e914-4dc4-a491-e5c0ab96e666,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Skeletal muscle glycogenolysis,False,Skeletal muscle glycogenolysis,,,,
d6024881-ff90-4d7f-8a6c-2c92eb8c284d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
d6024881-ff90-4d7f-8a6c-2c92eb8c284d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
d6024881-ff90-4d7f-8a6c-2c92eb8c284d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
d6024881-ff90-4d7f-8a6c-2c92eb8c284d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
7d421666-b048-4f70-9081-f4b4e3968351,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Summary of pathway regulation,False,Summary of pathway regulation,,,,
45f19cce-072d-43bf-94f1-7ffc3ebae0fc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Table 5.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
4a0183ce-f1e8-4f7c-83c4-3354c265382e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,5.1 References and resources,True,Summary of pathway regulation,,,,
71a6c960-97ac-4828-89d8-1ef9111890af,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 10: Gluconeogenesis: Section II, III, IV, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section III, IV, V, Chapter 19: Removal of Nitrogen from Amino Acids: Section V, VI, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
f8ccb7c4-bbfe-459a-bd23-b85dc2714b17,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 78, 82, 86, 89–90.",True,Summary of pathway regulation,,,,
944d2bda-313e-4e1d-af5d-3762778cdca2,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 3: The Fasted State, Chapter 19: Basic Concepts in Regulation, Chapter 24: Oxidative Phosphorylation and the ETC, Chapter 26: Formation of Glycogen, Chapter 28: Gluconeogenesis, Chapter 30: Oxidation of Fatty Acids, Chapter 34: Integration of Carbohydrate and Lipid Metabolism, Chapter 36: Fate of Amino Acids Nitrogen: Urea Cycle.",True,Summary of pathway regulation,,,,
a634c084-29ae-4910-93e9-5709d9484d10,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
a634c084-29ae-4910-93e9-5709d9484d10,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
a634c084-29ae-4910-93e9-5709d9484d10,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
a634c084-29ae-4910-93e9-5709d9484d10,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
acecb6ca-8a78-42b8-b8aa-f6f17dcef36d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
acecb6ca-8a78-42b8-b8aa-f6f17dcef36d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
acecb6ca-8a78-42b8-b8aa-f6f17dcef36d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
acecb6ca-8a78-42b8-b8aa-f6f17dcef36d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
e91cee62-1fc5-4e02-8ffe-1f7144ce9c18,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
e91cee62-1fc5-4e02-8ffe-1f7144ce9c18,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
e91cee62-1fc5-4e02-8ffe-1f7144ce9c18,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
e91cee62-1fc5-4e02-8ffe-1f7144ce9c18,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
372732f3-be8d-4180-b028-83ea39b788bf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
372732f3-be8d-4180-b028-83ea39b788bf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
372732f3-be8d-4180-b028-83ea39b788bf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
372732f3-be8d-4180-b028-83ea39b788bf,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
70f5c7c0-7ce1-497a-bf99-5860eb49a4a8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
70f5c7c0-7ce1-497a-bf99-5860eb49a4a8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
70f5c7c0-7ce1-497a-bf99-5860eb49a4a8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
70f5c7c0-7ce1-497a-bf99-5860eb49a4a8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
8b8cca64-9aac-4f95-a102-4ef1b1f9ea9e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
8b8cca64-9aac-4f95-a102-4ef1b1f9ea9e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
8b8cca64-9aac-4f95-a102-4ef1b1f9ea9e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
8b8cca64-9aac-4f95-a102-4ef1b1f9ea9e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
2a83fd25-bc24-410d-be00-ab2cca78d3de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
2a83fd25-bc24-410d-be00-ab2cca78d3de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
2a83fd25-bc24-410d-be00-ab2cca78d3de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
2a83fd25-bc24-410d-be00-ab2cca78d3de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
b5a8bfae-65d9-4e2b-ae0a-f39d93679670,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",True,Summary of pathway regulation,,,,
a37b6501-3c7f-4f6e-92eb-26b25226b257,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The processes of lipolysis, β-oxidation, and ketogenesis work in concert within the cell but should be considered distinct pathways.",True,Summary of pathway regulation,,,,
f6453f8f-4316-4998-bad8-e2112ea05fd9,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Lipolysis,False,Lipolysis,,,,
1f82c94e-9ea4-4136-b9ed-b8da9790e3b6,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
1f82c94e-9ea4-4136-b9ed-b8da9790e3b6,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
1f82c94e-9ea4-4136-b9ed-b8da9790e3b6,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
1f82c94e-9ea4-4136-b9ed-b8da9790e3b6,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
6bfbe85f-ac9e-4e69-89f4-c3ae569a9463,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,TAGs,False,TAGs,,,,
b92671f2-2c81-4587-a1d1-76af494c9f42,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,LCFAs,False,LCFAs,,,,
905d4298-bba5-46ab-869b-88663d587b91,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,β-oxidation (oxidation of free fatty acids),False,β-oxidation (oxidation of free fatty acids),,,,
f91e4ede-013b-489f-96cd-71f95e86b6f8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
f91e4ede-013b-489f-96cd-71f95e86b6f8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
f91e4ede-013b-489f-96cd-71f95e86b6f8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
f91e4ede-013b-489f-96cd-71f95e86b6f8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7758461c-f0ca-4fcb-a87f-47d13d2e0ef5,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7758461c-f0ca-4fcb-a87f-47d13d2e0ef5,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7758461c-f0ca-4fcb-a87f-47d13d2e0ef5,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
7758461c-f0ca-4fcb-a87f-47d13d2e0ef5,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4fe0776a-3bda-4765-afc3-86cb5ad1c382,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4fe0776a-3bda-4765-afc3-86cb5ad1c382,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4fe0776a-3bda-4765-afc3-86cb5ad1c382,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
4fe0776a-3bda-4765-afc3-86cb5ad1c382,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
6a879542-6f96-4b50-8e3b-0066e0a6b34a,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Regulation of β-oxidation,False,Regulation of β-oxidation,,,,
ad53a7ee-09c7-47ce-8d4f-c765fc38bd93,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
ad53a7ee-09c7-47ce-8d4f-c765fc38bd93,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
ad53a7ee-09c7-47ce-8d4f-c765fc38bd93,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
ad53a7ee-09c7-47ce-8d4f-c765fc38bd93,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
b2ce4594-07d8-4238-8735-b33f0fa14c45,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Ketogenesis,False,Ketogenesis,,,,
37ab6d28-35ed-4d28-a189-e74daa8058cc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
37ab6d28-35ed-4d28-a189-e74daa8058cc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
37ab6d28-35ed-4d28-a189-e74daa8058cc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
37ab6d28-35ed-4d28-a189-e74daa8058cc,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
130fbf45-1667-44ca-8e14-552a27024971,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
130fbf45-1667-44ca-8e14-552a27024971,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
130fbf45-1667-44ca-8e14-552a27024971,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
130fbf45-1667-44ca-8e14-552a27024971,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
ac22a803-7129-4de8-bd97-6eee6cc8122d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Table 5.2: Summary of pathway regulation.,True,Ketogenesis,,,,
72f6d736-19f0-4e64-be13-b1216d2ebab7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,5.2 References and resources,True,Ketogenesis,,,,
f7d4d6b4-d2b2-48ed-962c-4afbd00cadf0,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Text,False,Text,,,,
db2890e6-b628-4260-a65f-d04c63f018b2,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
db2890e6-b628-4260-a65f-d04c63f018b2,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
db2890e6-b628-4260-a65f-d04c63f018b2,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
db2890e6-b628-4260-a65f-d04c63f018b2,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
3ffa605e-a5bd-4854-90a0-b16cbb5cf2f7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
3ffa605e-a5bd-4854-90a0-b16cbb5cf2f7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
3ffa605e-a5bd-4854-90a0-b16cbb5cf2f7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
3ffa605e-a5bd-4854-90a0-b16cbb5cf2f7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
91324bb3-59cf-483d-ae7e-463217c25840,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
91324bb3-59cf-483d-ae7e-463217c25840,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
91324bb3-59cf-483d-ae7e-463217c25840,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
91324bb3-59cf-483d-ae7e-463217c25840,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
7970a766-2436-4247-a147-5ace55a0a48b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
7970a766-2436-4247-a147-5ace55a0a48b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
7970a766-2436-4247-a147-5ace55a0a48b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
7970a766-2436-4247-a147-5ace55a0a48b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
5029db33-7e45-4b05-aee8-6b85f6e0bb00,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,5.3 Nitrogen Metabolism and the Urea Cycle,True,Text,,,,
cfc547d8-3b62-4e9f-9b6b-287f366e4089,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Amino acids play key roles as precursors to nitrogen-containing compounds (such as nucleotides and neurotransmitters), as substrates for protein synthesis, and as an oxidizable substrate for energy production (or storage). Unlike carbohydrate and lipid metabolism, we must be concerned with the fates of both the carbon- and nitrogen-containing moieties when discussing the metabolism of amino acids. In the case of amino acids, nitrogen is released as ammonia (NH3), and at physiological pH the majority of ammonia is present as an ammonium ion (NH4+). (It is important to note that only ammonia can cross cellular membranes.) The majority of ammonia is incorporated into urea (in the liver) and excreted by the kidney, while the remaining carbon-containing skeleton is oxidized or utilized in other anabolic pathways (i.e., gluconeogenesis).",True,Text,,,,
59eceecd-5219-4b42-80af-9c0fe1f6c0c4,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Transport of nitrogen via amino acids,False,Transport of nitrogen via amino acids,,,,
f8d92a94-97fa-467f-8eeb-bc2be68dd8be,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The amino acid pool is continually in flux and can be influenced by both dietary protein consumption as well as normal protein turnover within the tissues. Given that the major site of nitrogen disposal is the liver, a mechanism for transport of excess amino acid nitrogen from the peripheral tissues to the liver is in place. Both alanine and glutamine play an essential role as nontoxic carriers of ammonia from peripheral tissues to the liver (figures 5.12 and 5.13). To generate alanine and glutamine for transport, amino acids can undergo transamination reactions.",True,Transport of nitrogen via amino acids,,,,
062e2b66-e72a-45d1-9759-3194a3281aca,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Transamination: The movement of nitrogen,False,Transamination: The movement of nitrogen,,,,
0b7200d4-734e-4de3-a7ef-5d2e90ca28ab,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Amino transferases are a family of enzymes (which require pyridoxal phosphate; PLP) as a cofactor to help transfer nitrogen from amino acids on to keto-acid backbones. These enzymes do not free ammonia, but will transfer nitrogen from an amino group to a keto-group in an exchange or transferase reaction. Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) are common and clinically relevant transferases. AST will preferentially accept aspartate and transaminate it in a reaction with α-ketoglutarate (the keto-acid of glutamate) to generate oxaloacetate (OAA) (the keto-acid of aspartate) and glutamate (figures 5.12 and 5.13).",True,Transamination: The movement of nitrogen,,,,
1add3b85-b02d-4811-bb23-e1b173415835,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",False,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",,,,
7be298ad-cda3-4579-8bfd-1f222add47de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7be298ad-cda3-4579-8bfd-1f222add47de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7be298ad-cda3-4579-8bfd-1f222add47de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7be298ad-cda3-4579-8bfd-1f222add47de,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
f8dd1f54-6074-4228-82ff-b19a64b7d32a,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,GDH,False,GDH,,,,
11702fef-ec5e-400e-a2e0-27e3d65fb191,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
11702fef-ec5e-400e-a2e0-27e3d65fb191,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
11702fef-ec5e-400e-a2e0-27e3d65fb191,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
11702fef-ec5e-400e-a2e0-27e3d65fb191,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
3793db03-52a3-44a0-ab49-81447a16f47d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In skeletal muscle, the alanine-glucose cycle is commonly used for the transport of nitrogen from the skeletal muscle to the liver. In this process, ammonia from amino acid degradation is transaminated to form glutamate. Alanine aminotransferase (AST) will transaminate glutamate with pyruvate to generate alanine (and α-ketoglutarate). The alanine is released and transported to the liver where it will undergo another transamination to generate pyruvate, which is used as a substrate for glucose production (gluconeogenesis). The glucose is released from the liver and oxidized by the skeletal muscle.",True,GDH,,,,
7464fa01-f514-440a-8686-19c80d23a249,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7464fa01-f514-440a-8686-19c80d23a249,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7464fa01-f514-440a-8686-19c80d23a249,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
7464fa01-f514-440a-8686-19c80d23a249,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
6fcfd516-b9d4-4849-bc07-a54aa43705be,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Urea cycle,False,Urea cycle,,,,
1240c03c-cf0a-4c22-9753-4ff2c429135e,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Ammonia freed in the liver by glutaminase (or glutamate dehydrogenase) will readily enter the urea cycle to be incorporated into urea. A functioning urea cycle is essential for the disposal of nitrogen from catabolic processes, and if dysfunction occurs the accumulation of ammonia can be life threatening.",True,Urea cycle,,,,
39c72e38-52ba-4357-b65f-5fc78af2a758,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,The urea cycle occurs in the liver and spans both the mitochondria and the cytosolic compartments. The initial free ammonia diffuses through the mitochondrial membrane and is fixed with carbon dioxide (in the form of bicarbonate) during the initial step in this process (figures 5.15 and 5.16). It is important to remember that the synthesis of urea is an anabolic process that requires ATP. Therefore deficiencies in ATP production can inhibit nitrogen disposal as well.,True,Urea cycle,,,,
7dee1254-227d-4ec7-8ffd-0f5e082d2070,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"The product of this pathway, urea, is made of two nitrogenous groups with the first coming from the free ammonia released by glutaminase. The second nitrogen is added later in the cycle by aspartate (figures 5.16 and 5.17).",True,Urea cycle,,,,
e3a1df5a-6277-4c50-8979-d66b4163bb99,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Regulation of the urea cycle,False,Regulation of the urea cycle,,,,
da2c9f17-c4dc-4dc2-99be-677133be6e56,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
da2c9f17-c4dc-4dc2-99be-677133be6e56,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
da2c9f17-c4dc-4dc2-99be-677133be6e56,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
da2c9f17-c4dc-4dc2-99be-677133be6e56,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
baf0791b-ce6a-4287-b12b-8b4cfdf1130b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
baf0791b-ce6a-4287-b12b-8b4cfdf1130b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
baf0791b-ce6a-4287-b12b-8b4cfdf1130b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
baf0791b-ce6a-4287-b12b-8b4cfdf1130b,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
e4e02b02-c54d-4403-a11b-8a9e29b518ab,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"In summary, the process of nitrogen movement from the peripheral tissues to the liver is essential. It involves transamination reactions to produce alanine, and the synthesis of glutamine (by glutamine synthetase) to generate two nontoxic carriers of ammonia. Once transported to the liver, again, transamination coupled with the reactions of glutaminase and glutamate dehydrogenase will allow for ammonia to be freed and enter into the urea cycle.",True,Regulation of the urea cycle,,,,
8566e019-05f7-4b9c-b5d9-60dba33d403c,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,Table 5.3: Summary of pathway regulation.,True,Regulation of the urea cycle,,,,
58e97ddd-a7c0-4b9d-ba36-15d81b1e40e7,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,5.3 References and resources,True,Regulation of the urea cycle,,,,
b6954a73-d3d7-4fa5-b3c9-7af583a859fd,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
b6954a73-d3d7-4fa5-b3c9-7af583a859fd,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
b6954a73-d3d7-4fa5-b3c9-7af583a859fd,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
b6954a73-d3d7-4fa5-b3c9-7af583a859fd,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
dfc88fd2-4dc6-4cb0-a651-1a4b7065ed69,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
dfc88fd2-4dc6-4cb0-a651-1a4b7065ed69,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
dfc88fd2-4dc6-4cb0-a651-1a4b7065ed69,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
dfc88fd2-4dc6-4cb0-a651-1a4b7065ed69,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
b068830f-2dd0-4c0c-acaa-262154eb76e8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
b068830f-2dd0-4c0c-acaa-262154eb76e8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
b068830f-2dd0-4c0c-acaa-262154eb76e8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
b068830f-2dd0-4c0c-acaa-262154eb76e8,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
e8aa13de-759d-401c-8a8c-ec019789de1c,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
e8aa13de-759d-401c-8a8c-ec019789de1c,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
e8aa13de-759d-401c-8a8c-ec019789de1c,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
e8aa13de-759d-401c-8a8c-ec019789de1c,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
64d021cb-0481-4089-9dee-9fe45ee7f281,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
64d021cb-0481-4089-9dee-9fe45ee7f281,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
64d021cb-0481-4089-9dee-9fe45ee7f281,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
64d021cb-0481-4089-9dee-9fe45ee7f281,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
5887e3b9-af01-4a99-8dad-5fa1ddc6467d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
5887e3b9-af01-4a99-8dad-5fa1ddc6467d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
5887e3b9-af01-4a99-8dad-5fa1ddc6467d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
5887e3b9-af01-4a99-8dad-5fa1ddc6467d,https://pressbooks.lib.vt.edu/cellbio/,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/#chapter-67-section-1,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
ed9b71ef-386c-4769-a100-2d41769c2ea4,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lipolysis, β-oxidation, and ketogenesis",False,"Lipolysis, β-oxidation, and ketogenesis",,,,
6026d589-0ae3-4ee6-86de-899c6770832a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Urea cycle and nitrogen metabolism,False,Urea cycle and nitrogen metabolism,,,,
91ef2ecc-a3b6-4588-8de7-93a82d819d2c,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Glycogenolysis (see section 4.5),True,Urea cycle and nitrogen metabolism,,,,
44e48c71-daf8-45bc-8310-da74554a6439,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
44e48c71-daf8-45bc-8310-da74554a6439,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
44e48c71-daf8-45bc-8310-da74554a6439,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
44e48c71-daf8-45bc-8310-da74554a6439,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis and glycogenolysis are the two pathways essential for glucose homeostasis. Figure 5.1 illustrates the time frame and overlap of glycogenolysis and gluconeogenesis. These pathways are activated nearly simultaneously when the insulin to glucagon ratio becomes sufficiently reduced. Over time, the reliance on the pathways changes.",True,Urea cycle and nitrogen metabolism,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
5477e321-a48e-454d-94a3-547d07f05bb2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
5477e321-a48e-454d-94a3-547d07f05bb2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
5477e321-a48e-454d-94a3-547d07f05bb2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
5477e321-a48e-454d-94a3-547d07f05bb2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis (GNG) is an anabolic pathway that produces glucose from lactate, glycerol, or glucogenic amino acids. This pathway is activated primarily in the liver during fasting and is coordinated with the catabolic pathways of β-oxidation and protein catabolism. The pathway follows the reverse of glycolysis with the exception of four unique enzymes, which overcome the irreversible steps of glycolysis (figure 5.2).",True,Urea cycle and nitrogen metabolism,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
242e97ce-e994-409e-8745-dbc4ba57d5e7,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,GNG,False,GNG,,,,
51b071ef-c435-4e39-9683-d3f4aa59d679,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Substrates for GNG,False,Substrates for GNG,,,,
db05b768-0113-49a1-8b67-181a562f150d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Amino acids,False,Amino acids,,,,
44b1e229-0007-42ad-8b91-1577aa45f491,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
44b1e229-0007-42ad-8b91-1577aa45f491,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
44b1e229-0007-42ad-8b91-1577aa45f491,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
44b1e229-0007-42ad-8b91-1577aa45f491,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The primary substrates for GNG are derived from glucogenic amino acids released through cortisol-mediated protein catabolism. In the fasted state, cortisol is elevated, and it supports fasted state pathways through the activation of protein catabolism — in the skeletal muscle — and by increasing the transcription of enzymes needed for gluconeogenesis (specifically phosphoenol carboxykinase (PEPCK)). As amino acids are released from the skeletal muscle, primarily as glutamine and alanine, they are taken up by the liver. In order to be used for glucose synthesis, they undergo transamination to generate a useful intermediate of the TCA cycle, predominantly α-ketoglutarate and pyruvate (see figures 5.3 and 5.10) . In the case of alanine, this can be transaminated to generate pyruvate. Glutamine will first be deaminated by glutaminase, and the remaining glutamate will be transaminated to form α-ketoglutarate (see figure 5.11). Both pyruvate and α-ketoglutarate will increase substrates in the TCA cycle, ultimately increasing the pool of available malate to be shuttled out of the mitochondria. It is through this process of protein catabolism and transamination that glucogenic amino acids contribute to the synthesis of oxaloacetate (OAA) needed for gluconeogenesis.",True,Amino acids,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
d83f5223-e9d0-43ba-80ea-2cf2647ce2db,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,phosphoenol,False,phosphoenol,,,,
7117c8ce-67b3-4dfc-a416-5b5ec189ba05,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,OAA,False,OAA,,,,
c0b5a018-fb4b-4a83-9b88-b9bcf19f0024,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Lactate,False,Lactate,,,,
20b257e7-8fc8-4f9b-adfd-8b3e3f4b45c3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
20b257e7-8fc8-4f9b-adfd-8b3e3f4b45c3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
20b257e7-8fc8-4f9b-adfd-8b3e3f4b45c3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
20b257e7-8fc8-4f9b-adfd-8b3e3f4b45c3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lactate is primarily produced through the Cori cycle or from anaerobic glucose oxidation. (Note: The Cori cycle, or lactic acid cycle, refers to the metabolic pathway in which lactate produced by anaerobic glycolysis in the muscle or RBC travels to the liver and is converted to glucose. The glucose returns to the peripheral tissues and is metabolized back to lactate.) Once in the liver, lactate can be oxidized back to pyruvate through the reverse reaction catalyzed by lactate dehydrogenase (figure 5.3).",True,Lactate,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
ef81284c-a8f8-48c1-b637-1c02397834f0,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Glycerol,False,Glycerol,,,,
a1dbc5a4-a069-4e0b-9401-024b383bdda1,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
a1dbc5a4-a069-4e0b-9401-024b383bdda1,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
a1dbc5a4-a069-4e0b-9401-024b383bdda1,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
a1dbc5a4-a069-4e0b-9401-024b383bdda1,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"When lipolysis is stimulated by epinephrine or glucagon, activation of hormone-sensitive lipase in the adipose allows for the hydrolysis of triacylglycerol into three free fatty acid chains and glycerol. The glycerol released into circulation will be taken up by the liver. Once in the liver it can be converted into dihydroxyacetone phosphate (DHAP), a glycolytic intermediate. This is an additional way in which carbons can be obtained for glucose synthesis (figure 5.4).",True,Glycerol,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
431ef73c-09f6-4427-9761-b6b4af9a948e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Interconnection of GNG and other metabolic pathways,False,Interconnection of GNG and other metabolic pathways,,,,
b11917e7-d2f2-4efb-8cba-5e0d56544363,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis is heavily reliant on support from other pathways. It requires amino acids for carbon substrates from cortisol-mediated protein catabolism. The ability of those amino acids to be deaminated relies on the ability of the urea cycle to remove ammonia in the form of nontoxic urea, and perhaps most importantly, gluconeogenesis relies on the process of β-oxidation.",True,Interconnection of GNG and other metabolic pathways,,,,
01fabd0a-ad14-429b-b3ed-52744ba1812d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,β-oxidation,False,β-oxidation,,,,
b4093b80-e757-4f08-b96f-557b55d0b076,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,The process of β-oxidation supports gluconeogenesis in two major ways:,False,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
17208549-d68a-4806-8d60-befca7fd249f,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Acetyl-CoA produced from β-oxidation itself is not a substrate for gluconeogenesis, rather it is required for allosteric activation of pyruvate carboxylase, which is the first step in GNG. Again, acetyl-CoA is not a substrate for this process; it is fully oxidized in the TCA cycle and provides no additional carbons to be exported from the TCA cycle as malate. Therefore the cell has to rely on amino acid carbon skeletons, glycerol, and lactate as substrates for glucose production (section 5.2).",True,The process of β-oxidation supports gluconeogenesis in two major ways:,,,,
c88ae11f-efcc-43e8-b5e0-93c0d27b8713,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Regulation of gluconeogenesis,False,Regulation of gluconeogenesis,,,,
2ebdb7cb-3836-4eb1-8b37-f7b6303b6980,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),False,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
11a21e9c-cdc4-4ee7-95b5-a3cdff99c200,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
11a21e9c-cdc4-4ee7-95b5-a3cdff99c200,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
11a21e9c-cdc4-4ee7-95b5-a3cdff99c200,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
11a21e9c-cdc4-4ee7-95b5-a3cdff99c200,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Gluconeogenesis is essentially the reverse of glycolysis with four key regulatory steps that allow the bypass of the three irreversible steps of glycolysis (figure 5.2). This initial step of GNG starts in the mitochondria using pyruvate carboxylase (figure 5.5). This enzyme converts pyruvate in the mitochondria to oxaloacetate and requires biotin as a cofactor. This enzyme is allosterically activated by acetyl-CoA. The OAA produced is reduced to malate, which is shuttled out of the mitochondria using the malate-aspartate shuttle. Once in the cytosol, the malate is oxidized back to OAA and decarboxylated by the enzyme phosphoenol carboxykinase (PEPCK) to generate phosphoenol pyruvate (figure 5.3). The combination of these two enzymes, pyruvate carboxylase and PEPCK, allows the cell to bypass the irreversible step catalyzed by pyruvate kinase.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
70c71869-8832-49b5-a768-2b4daa4c2ef2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Once phosphoenol pyruvate (PEP) is synthesized, it will continue through the reverse process using the glycolytic enzymes until it reaches its next irreversible conversion.",True,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),,,,
e4e88807-9d96-496f-893e-4ddeebcdf44b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Fructose 1,6-bisphosphatase (FBP1)",False,"Fructose 1,6-bisphosphatase (FBP1)",,,,
a892ffe7-9563-48be-be44-2c70954e9d82,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
a892ffe7-9563-48be-be44-2c70954e9d82,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
a892ffe7-9563-48be-be44-2c70954e9d82,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
a892ffe7-9563-48be-be44-2c70954e9d82,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As PEP continues through the reverse of glycolysis, fructose 1,6-bisphosphate is generated. To bypass the irreversible step catalyzed by phosphofructokinase 1 (PFK1) in glycolysis, the enzyme fructose 1,6-bisphosphatase (FBP1) is present and dephosphorylates fructose 1,6-bisphosphate to produce fructose 6-phosphate. This enzyme, FBP1, is inhibited by AMP and fructose 2,6-bisphosphate (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
0a488760-898b-4f36-b705-37af3f4c6080,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
0a488760-898b-4f36-b705-37af3f4c6080,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
0a488760-898b-4f36-b705-37af3f4c6080,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
0a488760-898b-4f36-b705-37af3f4c6080,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
0a488760-898b-4f36-b705-37af3f4c6080,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
0a488760-898b-4f36-b705-37af3f4c6080,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Like glycolysis, there is an additional regulation here by the bifunctional enzyme phosphofructokinase 2 (PFK2)/fructose 2,6-bisphosphatase (figure 4.1). This bifunctional enzyme functions as a kinase in the fed state (PFK2) and generates fructose 2,6-bisphosphate that allosterically activates PFK1. In the fasted state the enzyme is phosphorylated by glucagon-activated protein kinase A, and this actives the phosphatase activity of the enzyme. The enzyme dephosphorylates fructose 2,6-bisphosphate and therefore reduces the allosteric activation of PFK1 facilitating the reverse reaction by fructose 1,6-bisphosphatase (figure 5.2).",True,"Fructose 1,6-bisphosphatase (FBP1)",Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
adceaf74-ddca-4d58-a4f8-adb9ab6a8f31,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Glucose 6-phosphatase,False,Glucose 6-phosphatase,,,,
a3fc0aa0-efc3-4e4c-a14c-1cf88cb4bd03,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Finally, glucose 6-phosphatase is required to dephosphorylate glucose 6-phosphate so it can be released from the liver. This is a key step for both glycogenolysis and gluconeogenesis, and deficiencies in this enzyme can lead to severe bouts of fasting hypoglycemia.",True,Glucose 6-phosphatase,,,,
f82ca8ee-e084-49ff-bce1-3ceda8031e0a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Glycogenolysis,False,Glycogenolysis,,,,
6decc7a6-7f5c-4a9b-a44b-aad2ac64c48c,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In contrast to glycogen synthesis, glycogenolysis is the release of glucose 6-phosphate from glycogen stores. It can occur in both the liver and the skeletal muscle but under two different conditions (figures 5.6 and 5.7). As noted above, this is a pathway active in the fasted state.",True,Glycogenolysis,,,,
7e56c1e6-4b3f-4219-baae-fbc3aa893a6e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Regulation of glycogenolysis,False,Regulation of glycogenolysis,,,,
9dde74dc-e0e6-4db4-99ea-90d4f4754b8b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Hepatic glycogenolysis,False,Hepatic glycogenolysis,,,,
e6199231-9730-4e92-928c-bb46221427c5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
e6199231-9730-4e92-928c-bb46221427c5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
e6199231-9730-4e92-928c-bb46221427c5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
e6199231-9730-4e92-928c-bb46221427c5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In the liver, glucagon will initiate glycogenolysis through a GPCR-mediated signaling cascade. This leads to the activation of adenylyl cyclase and an increase in cAMP. cAMP activates protein kinase A, which phosphorylates and activates glycogen phosphorylase. Glycogen phosphorylase will initiate glycogen degradation. Also under these conditions, using the same mechanism, glycogen synthase will be phosphorylated and inactivated, ensuring glycogen synthesis is not occurring at the same time (figure 5.6).",True,Hepatic glycogenolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
416c66f3-db14-423d-bd55-a9eaf01e76a8,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Epinephrine can also enhance hepatic glycogenolysis by binding an α-agonist receptor. This initiates the cleavage of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol 1,4,5-triphosphate (IP3) and diacylglyerol (DAG) by phospholipase C. IP3 stimulates Ca2+ release from endoplasmic reticulum and results in both:",True,Hepatic glycogenolysis,,,,
a002337d-b8ad-4f43-af60-cf6bd55785d2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In all cases, the glucose 6-phosphate released from glycogen stores is dephosphorylated by glucose 6-phosphatase and released from the liver.",True,Hepatic glycogenolysis,,,,
b41c388b-3262-471a-b42b-0ddc5e43948e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Skeletal muscle glycogenolysis,False,Skeletal muscle glycogenolysis,,,,
7c560a48-1817-4060-82f5-6f7311eaca4b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
7c560a48-1817-4060-82f5-6f7311eaca4b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
7c560a48-1817-4060-82f5-6f7311eaca4b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
7c560a48-1817-4060-82f5-6f7311eaca4b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Skeletal muscle glycogen is not impacted by glucagon but responds to AMP, Ca2+, and epinephrine (figure 5.7).",True,Skeletal muscle glycogenolysis,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
1364783e-7813-420b-a84f-f15128485e76,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Summary of pathway regulation,False,Summary of pathway regulation,,,,
264ed27f-26ff-4d15-aa85-ac449b7aac64,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Table 5.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
ef33031a-4789-47cd-8da0-f30f2f0e565b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,5.1 References and resources,True,Summary of pathway regulation,,,,
56a810fa-5516-4631-abc8-ae58fff282d9,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 10: Gluconeogenesis: Section II, III, IV, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section III, IV, V, Chapter 19: Removal of Nitrogen from Amino Acids: Section V, VI, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
fd0270d5-72a1-44a8-ba01-7aaf541cdd0b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 78, 82, 86, 89–90.",True,Summary of pathway regulation,,,,
797a5aee-a4a8-419b-9695-b80330221523,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 3: The Fasted State, Chapter 19: Basic Concepts in Regulation, Chapter 24: Oxidative Phosphorylation and the ETC, Chapter 26: Formation of Glycogen, Chapter 28: Gluconeogenesis, Chapter 30: Oxidation of Fatty Acids, Chapter 34: Integration of Carbohydrate and Lipid Metabolism, Chapter 36: Fate of Amino Acids Nitrogen: Urea Cycle.",True,Summary of pathway regulation,,,,
985dd0ed-ffbd-45ed-a61e-163a72cbc70d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
985dd0ed-ffbd-45ed-a61e-163a72cbc70d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
985dd0ed-ffbd-45ed-a61e-163a72cbc70d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
985dd0ed-ffbd-45ed-a61e-163a72cbc70d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Ferrier D. Figure 5.1 Glucose production by glycogenolysis and gluconeogenesis. Adapted under Fair Use from Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp 329. Figure 24.11 Sources of blood glucose after ingestion of 100 g of glucose. 2017.,True,Summary of pathway regulation,Figure 5.1,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
6237d865-09e0-4e80-a358-4075e9d3e951,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
6237d865-09e0-4e80-a358-4075e9d3e951,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
6237d865-09e0-4e80-a358-4075e9d3e951,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
6237d865-09e0-4e80-a358-4075e9d3e951,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.2 Comparison of glycolysis and gluconeogenesis. 2021. https://archive.org/details/5.2-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.2,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
14e0ab96-09cb-4a0c-b122-84505e555957,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
14e0ab96-09cb-4a0c-b122-84505e555957,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
14e0ab96-09cb-4a0c-b122-84505e555957,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
14e0ab96-09cb-4a0c-b122-84505e555957,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.3 Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway. 2021. https://archive.org/details/5.3_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
be4d350c-14de-4a6f-aae9-dec735197e08,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
be4d350c-14de-4a6f-aae9-dec735197e08,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
be4d350c-14de-4a6f-aae9-dec735197e08,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
be4d350c-14de-4a6f-aae9-dec735197e08,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.4 Glycerol as a substrate for gluconeogenesis, after phosphorylation to glycerol 3 -phosphate it can be converted to DHAP which can enter directly into glycolysis. 2021. https://archive.org/details/5.4_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.4,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
c105b3f8-fcfc-4bad-8a47-fd0fb4fe8913,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
c105b3f8-fcfc-4bad-8a47-fd0fb4fe8913,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
c105b3f8-fcfc-4bad-8a47-fd0fb4fe8913,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
c105b3f8-fcfc-4bad-8a47-fd0fb4fe8913,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.5 Reaction catalyzed by pyruvate carboxylase, this allows the by pass of the irreversible step catalyzed by pyruvate kinase. 2021. https://archive.org/details/5.5_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 5.5,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
bd29b925-1f2c-4074-be67-486e8e1f7ac2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
bd29b925-1f2c-4074-be67-486e8e1f7ac2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
bd29b925-1f2c-4074-be67-486e8e1f7ac2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
bd29b925-1f2c-4074-be67-486e8e1f7ac2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.7 Skeletal muscle glycogenolysis. 2021. https://archive.org/details/5.7_20210924. CC BY 4.0. Added Muscle by Pascal Heß from the Noun Project.",True,Summary of pathway regulation,Figure 5.7,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
182dac61-7a03-4ee6-8d36-5c984c3113a0,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
182dac61-7a03-4ee6-8d36-5c984c3113a0,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
182dac61-7a03-4ee6-8d36-5c984c3113a0,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
182dac61-7a03-4ee6-8d36-5c984c3113a0,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lieberman M, Peet A. Figure 5.6 Hepatic glycogenolysis by epinephrine. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 534. Figure 26.7 Regulation of glycogen synthesis and degradation in the liver. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
bb86c247-3f8b-4417-883b-2897f201db43,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"5.2 Lipolysis, β-oxidation, and Ketogenesis",True,Summary of pathway regulation,,,,
a7871b75-ca8b-4f8d-ba91-bec8d22df70e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The processes of lipolysis, β-oxidation, and ketogenesis work in concert within the cell but should be considered distinct pathways.",True,Summary of pathway regulation,,,,
e9cf9501-c0ca-499b-8445-e397e4534a18,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Lipolysis,False,Lipolysis,,,,
bbc29847-f8e5-4f27-a557-d96e587d8c2a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
bbc29847-f8e5-4f27-a557-d96e587d8c2a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
bbc29847-f8e5-4f27-a557-d96e587d8c2a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
bbc29847-f8e5-4f27-a557-d96e587d8c2a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Lipolysis is the release of fatty acids from adipose tissue where they are stored as triacylglycerols (TAGs). This process is mediated by increasing levels of glucagon and epinephrine, which bind G-protein coupled receptors on the adipose tissue and activate lipolysis This cell-signaling cascade phosphorylates and activates hormone-sensitive lipase, the regulatory enzyme for lipolysis. Once phosphorylated (through hormone-mediated increase in cAMP) this enzyme will hydrolyze TAGs to three long-chain fatty acids (LCFAs) and glycerol. The LCFAs are released into the bloodstream and will circulate bound to albumin (fatty acids are hydrophobic and require a protein carrier). LCFAs will be taken up and oxidized by peripheral tissues and the liver under fasted conditions. The glycerol will also be released and used as a substrate for hepatic gluconeogenesis (section 5.1) (figure 5.6).",True,Lipolysis,Figure 5.6,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
1ab27d18-324f-4f39-9629-160ef816dacc,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,TAGs,False,TAGs,,,,
48cedbfe-4161-4481-8872-d7ba748328a3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,LCFAs,False,LCFAs,,,,
323a1c75-e154-4c26-907d-5aa65b10ace2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,β-oxidation (oxidation of free fatty acids),False,β-oxidation (oxidation of free fatty acids),,,,
eb07e593-2429-4d06-b84b-fce81a01d0e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
eb07e593-2429-4d06-b84b-fce81a01d0e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
eb07e593-2429-4d06-b84b-fce81a01d0e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
eb07e593-2429-4d06-b84b-fce81a01d0e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Fatty acid oxidation is a high energy yielding process. It can support the cellular energy needs during fasting and under conditions when excess energy is needed (exercise). After uptake from circulation, the LCFAs must be transferred into the mitochondria where β-oxidation occurs. Initially, the LCFAs are activated to acyl-CoA derivatives in the cytosol by acyl-CoA synthetase. The fatty acyl-CoA can then be transferred across the mitochondrial membranes using a series of transport proteins: carnitine palmitoyltransferase 1 and 2 (CPT1 and CPT2) (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
72364186-17a0-4a72-b3f1-c44b84ba233a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
72364186-17a0-4a72-b3f1-c44b84ba233a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
72364186-17a0-4a72-b3f1-c44b84ba233a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
72364186-17a0-4a72-b3f1-c44b84ba233a,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"CPT1 sits on the outer mitochondrial membrane and transfers the fatty acyl-CoA to carnitine. Fatty acyl carnitine is transferred into the mitochondrial matrix through CPT2, and the carnitine is released and recycled. Only long-chain fatty acyl-CoAs require carnitine as a carrier; short- and medium-chain fatty acids can move into the mitochondria without the assistance of these transporters. Once in the matrix, the fatty acyl-CoA is now ready to undergo β-oxidation (figure 5.9).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
050437fe-5651-4ecb-8798-ce790177a858,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
050437fe-5651-4ecb-8798-ce790177a858,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
050437fe-5651-4ecb-8798-ce790177a858,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
050437fe-5651-4ecb-8798-ce790177a858,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is an iterative process that involves a series of enzymes that preferentially oxidize different length fatty acids (long, medium, and short). The full β-oxidation spiral consists of four steps that result in the generation of acetyl-CoA, NADH, and FADH2 for each cycle (figure 5.9). The NADH and FADH2 generated will be oxidized in the ETC to produce ATP. The acetyl-CoA can be oxidized in the TCA cycle, but more likely it will be used in ketogenesis. Oxidation of odd chain fatty acids will result in the generation of propionyl-CoA as the final carbon unit, which can also be oxidized in the TCA cycle. The acetyl-CoA from β-oxidation also plays a key role in the allosteric activation of pyruvate carboxylase, which is necessary for gluconeogenesis to occur (section 5.1).",True,β-oxidation (oxidation of free fatty acids),Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
264b40da-56d4-4bf6-a84e-4ff8a1ffe131,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Regulation of β-oxidation,False,Regulation of β-oxidation,,,,
dded9d2e-dd07-41f4-8f6f-3cc02599f366,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
dded9d2e-dd07-41f4-8f6f-3cc02599f366,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
dded9d2e-dd07-41f4-8f6f-3cc02599f366,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
dded9d2e-dd07-41f4-8f6f-3cc02599f366,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"β-oxidation is regulated primarily at the level of transport of LCFAs across the mitochondrial membrane. Malonyl-CoA will inhibit CPT1 therefore ensuring that β-oxidation is not occurring at the same time as fatty acid synthesis (figure 5.10; section 4.4). Additionally, the rate of ATP production (ATP/ADP ratio) will also regulate the rate of NADH and FADH2 produced through β-oxidation (figure 5.10).",True,Regulation of β-oxidation,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
0c9c84c6-9676-49de-9a93-303109bab501,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Ketogenesis,False,Ketogenesis,,,,
894234f6-29aa-43dc-a6b9-f01c54a60dc5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
894234f6-29aa-43dc-a6b9-f01c54a60dc5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
894234f6-29aa-43dc-a6b9-f01c54a60dc5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
894234f6-29aa-43dc-a6b9-f01c54a60dc5,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"As mentioned above, the acetyl-CoA produced by β-oxidation is primarily used for ketogenesis — the synthesis of ketone bodies. Substrates for ketogenesis can also come from the oxidation of ketogenic amino acids. In the fasted state, the process of β-oxidation generates a significant amount of acetyl-CoA, and although some of this substrate can be oxidized in the TCA cycle, we need to consider the other metabolic processes occurring. First, the significant amount of NADH generated through β-oxidation reduces flux through the TCA cycle by decreasing the activity of both α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. Second, the process of gluconeogenesis is occurring, and intermediates of the TCA cycle, specifically malate, are actively being moved out of the mitochondria. The combination of these two processes reduces the TCA cycle activity allowing for an accumulation of acetyl-CoA. As acetyl-CoA levels elevate in the mitochondria, this will drive the thiolase reaction to generate acetoacetyl-CoA from two acetyl-CoA molecules (figure 5.11).",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
54a0879a-cb0f-4308-b401-7481244cc674,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
54a0879a-cb0f-4308-b401-7481244cc674,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
54a0879a-cb0f-4308-b401-7481244cc674,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
54a0879a-cb0f-4308-b401-7481244cc674,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This compound is the substrate for HMG-CoA synthase, which generates 3-hydroxy-3-methyl glutaryl-CoA (HMG-CoA). HMG-CoA is then accepted by HMG-CoA lyase where an acetyl-CoA group is removed to generate acetoacetate. Acetoacetate can either undergo spontaneous decarboxylation to acetone, which can be exhaled, or it can be reduced to β-hydroxybutyrate using NADH. Acetoacetate and β-hydroxybutyrate are the two primary ketone bodies in circulation, and the ratio of the two is dependent on levels of NADH (figure 5.11). These two ketone bodies can be used as fuel in most tissues with the exception of the liver, which lacks thiophorase, the enzyme needed to metabolize these substrates. Ketone oxidation is not a primary fuel source, as fatty acid oxidation is preferred, but it can supply energy to some peripheral tissues. The brain can also oxidize ketones but only under extreme situations, such as starvation states.",True,Ketogenesis,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
55d74afc-a192-4cec-9fde-ae027c5bc8bf,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Table 5.2: Summary of pathway regulation.,True,Ketogenesis,,,,
6da4f954-53c0-4ce9-9536-3adb16abb259,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,5.2 References and resources,True,Ketogenesis,,,,
4d51f3e2-4329-41bd-8a50-799ec6c8f4cc,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Text,False,Text,,,,
9b986f4d-65be-485e-af49-af2eeb4c2199,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
9b986f4d-65be-485e-af49-af2eeb4c2199,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
9b986f4d-65be-485e-af49-af2eeb4c2199,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
9b986f4d-65be-485e-af49-af2eeb4c2199,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.8 Process of lipolysis. 2021. https://archive.org/details/5.6_20210924. CC BY 4.0. Added red blood cells by Lucas Helle from the Noun Project.",True,Text,Figure 5.8,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
28774d9f-a31e-4599-b291-44f506131410,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
28774d9f-a31e-4599-b291-44f506131410,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
28774d9f-a31e-4599-b291-44f506131410,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
28774d9f-a31e-4599-b291-44f506131410,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.9 Overview of LCFA transport into the mitochondria and β-oxidation. 2021. https://archive.org/details/5.7_20210924_202109. CC BY 4.0.",True,Text,Figure 5.9,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
00f0ccf7-d7b4-49b7-9278-3b56e089f933,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
00f0ccf7-d7b4-49b7-9278-3b56e089f933,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
00f0ccf7-d7b4-49b7-9278-3b56e089f933,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
00f0ccf7-d7b4-49b7-9278-3b56e089f933,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.10 Regulation of β-oxidation. 2021. https://archive.org/details/5.8_20210924. CC BY 4.0.",True,Text,Figure 5.10,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
93b6917d-16f8-4412-a139-74d4080c5735,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
93b6917d-16f8-4412-a139-74d4080c5735,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
93b6917d-16f8-4412-a139-74d4080c5735,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
93b6917d-16f8-4412-a139-74d4080c5735,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.11 Overview of ketone body formation. 2021. https://archive.org/details/5.9-deleted. CC BY 4.0.",True,Text,Figure 5.11,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
33f9c35a-76a7-4f88-8f5f-262515d52848,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,5.3 Nitrogen Metabolism and the Urea Cycle,True,Text,,,,
188df890-b25d-4ff5-8a73-f2a5e0aabc20,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Amino acids play key roles as precursors to nitrogen-containing compounds (such as nucleotides and neurotransmitters), as substrates for protein synthesis, and as an oxidizable substrate for energy production (or storage). Unlike carbohydrate and lipid metabolism, we must be concerned with the fates of both the carbon- and nitrogen-containing moieties when discussing the metabolism of amino acids. In the case of amino acids, nitrogen is released as ammonia (NH3), and at physiological pH the majority of ammonia is present as an ammonium ion (NH4+). (It is important to note that only ammonia can cross cellular membranes.) The majority of ammonia is incorporated into urea (in the liver) and excreted by the kidney, while the remaining carbon-containing skeleton is oxidized or utilized in other anabolic pathways (i.e., gluconeogenesis).",True,Text,,,,
e1ba2eda-1bea-4c33-a895-890116386f32,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Transport of nitrogen via amino acids,False,Transport of nitrogen via amino acids,,,,
c53e61a7-07cd-4727-b917-08b38f01567b,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The amino acid pool is continually in flux and can be influenced by both dietary protein consumption as well as normal protein turnover within the tissues. Given that the major site of nitrogen disposal is the liver, a mechanism for transport of excess amino acid nitrogen from the peripheral tissues to the liver is in place. Both alanine and glutamine play an essential role as nontoxic carriers of ammonia from peripheral tissues to the liver (figures 5.12 and 5.13). To generate alanine and glutamine for transport, amino acids can undergo transamination reactions.",True,Transport of nitrogen via amino acids,,,,
6adbbe75-14e1-43c9-9cc2-5f7848b6e72d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Transamination: The movement of nitrogen,False,Transamination: The movement of nitrogen,,,,
43f9afb3-0628-40f1-a365-7c164abada74,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Amino transferases are a family of enzymes (which require pyridoxal phosphate; PLP) as a cofactor to help transfer nitrogen from amino acids on to keto-acid backbones. These enzymes do not free ammonia, but will transfer nitrogen from an amino group to a keto-group in an exchange or transferase reaction. Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) are common and clinically relevant transferases. AST will preferentially accept aspartate and transaminate it in a reaction with α-ketoglutarate (the keto-acid of glutamate) to generate oxaloacetate (OAA) (the keto-acid of aspartate) and glutamate (figures 5.12 and 5.13).",True,Transamination: The movement of nitrogen,,,,
5bc65dc3-f831-4888-b739-9125ed42e55d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",False,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",,,,
be29927e-7bf6-4404-ad97-c91ff0ac6b3e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
be29927e-7bf6-4404-ad97-c91ff0ac6b3e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
be29927e-7bf6-4404-ad97-c91ff0ac6b3e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
be29927e-7bf6-4404-ad97-c91ff0ac6b3e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In addition to transaminases, there are three other enzymes that play essential roles in nitrogen transport. Glutamate dehydrogenase (GDH) is present in most tissues and is one of the few enzymes able to fix or free ammonia. In figure 5.14, in the skeletal muscle, glutamate dehydrogenase is illustrated fixing ammonia to α-ketoglutarate to generate glutamate, while in the liver it is shown freeing ammonia in the reverse reaction. The direction of the reaction will be influenced by several factors including cellular needs, the levels of NAD+ or NADP+, and levels of ammonia (figure 5.14).",True,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
625201fb-9a0a-4435-aaaf-036ed949c8a3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,GDH,False,GDH,,,,
d4539315-dbb1-4d75-af37-7c831293c4a2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
d4539315-dbb1-4d75-af37-7c831293c4a2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
d4539315-dbb1-4d75-af37-7c831293c4a2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
d4539315-dbb1-4d75-af37-7c831293c4a2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In peripheral tissues, glutamate generated from transamination or from the GDH reaction can be used to fix an additional ammonia to generate glutamine. This reaction, catalyzed by glutamine synthetase, facilitates the synthesis and subsequent movement of excess nitrogen from peripheral tissues to the liver (figure 5.14).",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
eb44a945-87c0-4c00-bb22-22cb102f657d,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In skeletal muscle, the alanine-glucose cycle is commonly used for the transport of nitrogen from the skeletal muscle to the liver. In this process, ammonia from amino acid degradation is transaminated to form glutamate. Alanine aminotransferase (AST) will transaminate glutamate with pyruvate to generate alanine (and α-ketoglutarate). The alanine is released and transported to the liver where it will undergo another transamination to generate pyruvate, which is used as a substrate for glucose production (gluconeogenesis). The glucose is released from the liver and oxidized by the skeletal muscle.",True,GDH,,,,
332b4b24-6d5b-415c-b6dc-6f67294c84ee,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
332b4b24-6d5b-415c-b6dc-6f67294c84ee,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
332b4b24-6d5b-415c-b6dc-6f67294c84ee,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
332b4b24-6d5b-415c-b6dc-6f67294c84ee,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The other key enzyme in nitrogen metabolism is glutaminase. Glutaminase, is active in the liver and responsible for deaminating glutamine as it is shuttled into the liver. The free ammonia can enter into the urea cycle, and the remaining glutamate can be transaminated to generate α-ketoglutarate. This is in contrast to glutamine synthetase, which is primarily used by peripheral tissues as a means of generating glutamine to remove ammonia from the tissues to the liver (figure 5.14). Nitrogen metabolism, unlike glucose metabolism, is fairly consistent in the fed and fasted states. Excess dietary amino acids, which are not stored, will also require deamination, and the carbons can be stored as either glycogen or fat.",True,GDH,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
a49fb102-4dc0-4a1d-a7a3-0035354cf8e7,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Urea cycle,False,Urea cycle,,,,
550c22b6-42d3-49a5-b568-b2dddcbcfc5e,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Ammonia freed in the liver by glutaminase (or glutamate dehydrogenase) will readily enter the urea cycle to be incorporated into urea. A functioning urea cycle is essential for the disposal of nitrogen from catabolic processes, and if dysfunction occurs the accumulation of ammonia can be life threatening.",True,Urea cycle,,,,
672a4853-fab9-449b-854b-b62b576f23e9,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,The urea cycle occurs in the liver and spans both the mitochondria and the cytosolic compartments. The initial free ammonia diffuses through the mitochondrial membrane and is fixed with carbon dioxide (in the form of bicarbonate) during the initial step in this process (figures 5.15 and 5.16). It is important to remember that the synthesis of urea is an anabolic process that requires ATP. Therefore deficiencies in ATP production can inhibit nitrogen disposal as well.,True,Urea cycle,,,,
5f9f9bb8-7e19-46e3-a828-a4c1eed3bec8,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"The product of this pathway, urea, is made of two nitrogenous groups with the first coming from the free ammonia released by glutaminase. The second nitrogen is added later in the cycle by aspartate (figures 5.16 and 5.17).",True,Urea cycle,,,,
ec1ca17b-799b-4272-b242-9e06cd9018a9,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Regulation of the urea cycle,False,Regulation of the urea cycle,,,,
a897b567-9974-4953-905c-d3fc0d731ee3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
a897b567-9974-4953-905c-d3fc0d731ee3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
a897b567-9974-4953-905c-d3fc0d731ee3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
a897b567-9974-4953-905c-d3fc0d731ee3,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"This pathway is predominantly regulated at one key enzyme, carbamoyl phosphate synthetase 1 (figure 5.16). This enzyme requires N-acetylglutamate (NAGS) as an allosteric activator. The synthesis of NAGS is enhanced by arginine, which is an intermediate of the urea cycle. Therefore the cycle provides positive feedback on itself. As flux through the urea cycle increases, and synthesis of arginine increases, this will enhance NAGS production and increase synthesis of carbamoyl phosphate.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
d1480c7c-6dc9-48e3-b0b3-4d92a3bc4687,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
d1480c7c-6dc9-48e3-b0b3-4d92a3bc4687,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
d1480c7c-6dc9-48e3-b0b3-4d92a3bc4687,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
d1480c7c-6dc9-48e3-b0b3-4d92a3bc4687,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Unlike the other pathways discussed, the urea cycle functions independent of hormonal control as it functions to dispose of nitrogen either from excess dietary sources or from protein catabolism/turnover. In the fasted state this is especially important as the carbon skeletons produced are required as substrates for gluconeogenesis (see figure 5.3). In the fed state, amino acids can be deaminated and contribute to the carbon pool (see figures 4.12 and 4.13).",True,Regulation of the urea cycle,Figure 5.3,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
3ce8b4cd-e2ce-4136-996f-cfa01c7d4ecd,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"In summary, the process of nitrogen movement from the peripheral tissues to the liver is essential. It involves transamination reactions to produce alanine, and the synthesis of glutamine (by glutamine synthetase) to generate two nontoxic carriers of ammonia. Once transported to the liver, again, transamination coupled with the reactions of glutaminase and glutamate dehydrogenase will allow for ammonia to be freed and enter into the urea cycle.",True,Regulation of the urea cycle,,,,
c361c402-53e3-4138-92fd-3b6f70d1e799,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,Table 5.3: Summary of pathway regulation.,True,Regulation of the urea cycle,,,,
498f1f6a-d178-4909-96e2-fce860780ff6,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,5.3 References and resources,True,Regulation of the urea cycle,,,,
e1f5d7c6-bfa0-4013-b1ee-e5272aa52e76,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
e1f5d7c6-bfa0-4013-b1ee-e5272aa52e76,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
e1f5d7c6-bfa0-4013-b1ee-e5272aa52e76,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
e1f5d7c6-bfa0-4013-b1ee-e5272aa52e76,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.12. Figure 5.12: Transamination reaction. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project and Muscle by Laymik from the Noun Project.",True,Regulation of the urea cycle,Figure 5.12,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
ec1559a3-0cd1-4e11-8a7c-36b9f56be9e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
ec1559a3-0cd1-4e11-8a7c-36b9f56be9e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
ec1559a3-0cd1-4e11-8a7c-36b9f56be9e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
ec1559a3-0cd1-4e11-8a7c-36b9f56be9e2,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.13 Reactions catalyzed by glutamate dehydrogenase, glutaminase and glutamine synthetase. 2021. https://archive.org/details/5.11_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.13,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
cc6594c9-5560-45f9-9f1c-897485c77716,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
cc6594c9-5560-45f9-9f1c-897485c77716,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
cc6594c9-5560-45f9-9f1c-897485c77716,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
cc6594c9-5560-45f9-9f1c-897485c77716,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.14 Movement of ammonia from peripheral tissues to the liver. 2021. https://archive.org/details/5.12_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.14,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
f4400811-e8a7-4f44-a5ae-3a6f27d72676,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
f4400811-e8a7-4f44-a5ae-3a6f27d72676,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
f4400811-e8a7-4f44-a5ae-3a6f27d72676,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
f4400811-e8a7-4f44-a5ae-3a6f27d72676,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.15 Overview of the urea cycle, the pathway spans both the mitochondria and cytosol. 2021. https://archive.org/details/5.13_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.15,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
d474ba9b-61ce-48de-be52-c103d6b73606,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
d474ba9b-61ce-48de-be52-c103d6b73606,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
d474ba9b-61ce-48de-be52-c103d6b73606,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
d474ba9b-61ce-48de-be52-c103d6b73606,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.16 Key regulatory step in the urea cycle. CPS1 is activated by N-acetyl glutamate. 2021. https://archive.org/details/5.14_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.16,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
4c912f94-cdb2-460d-baaf-31ccfb1430fc,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.3 Nitrogen Metabolism and the Urea Cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
4c912f94-cdb2-460d-baaf-31ccfb1430fc,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,"5.2 Lipolysis, β-oxidation, and Ketogenesis",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
4c912f94-cdb2-460d-baaf-31ccfb1430fc,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5.1 Gluconeogenesis and Glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
4c912f94-cdb2-460d-baaf-31ccfb1430fc,https://pressbooks.lib.vt.edu/cellbio/,5. Fuel for Later,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-later/,"Grey, Kindred, Figure 5.17 Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea. 2021. https://archive.org/details/5.15_20210924. CC BY 4.0.",True,Regulation of the urea cycle,Figure 5.17,5. Fuel for Later,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
e4417fd7-1cde-4029-b4b8-466b9ac497b6,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),False,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),,,,
d151714e-e211-4edd-9467-f2f7c1ce1d8f,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Fatty acid synthesis,False,Fatty acid synthesis,,,,
19902bcc-2518-42e6-b492-33a6d4a7887c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycogen synthesis,False,Glycogen synthesis,,,,
89331358-5434-445b-9c81-2ae393c91396,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,reoxidize,False,reoxidize,,,,
bb720179-7194-4274-889f-25cef4b79f72,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of glycolysis,False,Regulation of glycolysis,,,,
afd375b8-13ae-4f33-9191-ec36c46ba669,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
afd375b8-13ae-4f33-9191-ec36c46ba669,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
afd375b8-13ae-4f33-9191-ec36c46ba669,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
afd375b8-13ae-4f33-9191-ec36c46ba669,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
afd375b8-13ae-4f33-9191-ec36c46ba669,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
afd375b8-13ae-4f33-9191-ec36c46ba669,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
b73b8a09-aa6e-46a2-9f8d-ca9393d14e26,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glucokinase: Glucose to glucose 6-phosphate,False,Glucokinase: Glucose to glucose 6-phosphate,,,,
4c99a8ba-f5ca-4834-83cf-d7ffb0fee66e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
4c99a8ba-f5ca-4834-83cf-d7ffb0fee66e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
4c99a8ba-f5ca-4834-83cf-d7ffb0fee66e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
4c99a8ba-f5ca-4834-83cf-d7ffb0fee66e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
4c99a8ba-f5ca-4834-83cf-d7ffb0fee66e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
4c99a8ba-f5ca-4834-83cf-d7ffb0fee66e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
95186c0a-6bbe-4121-93e2-35f301d4e233,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,GLUT2,False,GLUT2,,,,
52cd4589-a316-49e0-9233-fe727bcaedf3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In skeletal muscle, and most other peripheral tissues, glucose is phosphorylated by hexokinase.",True,GLUT2,,,,
a74a413e-d043-440b-ad55-229a7622957c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
a74a413e-d043-440b-ad55-229a7622957c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
a74a413e-d043-440b-ad55-229a7622957c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
a74a413e-d043-440b-ad55-229a7622957c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
a74a413e-d043-440b-ad55-229a7622957c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
a74a413e-d043-440b-ad55-229a7622957c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
c7afe26b-3e14-4021-8fa0-2637e524fe6c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of glucokinase and hexokinase,False,Regulation of glucokinase and hexokinase,,,,
ba90fa8f-51ce-44e5-b2eb-208e7863f8fe,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba90fa8f-51ce-44e5-b2eb-208e7863f8fe,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba90fa8f-51ce-44e5-b2eb-208e7863f8fe,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba90fa8f-51ce-44e5-b2eb-208e7863f8fe,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba90fa8f-51ce-44e5-b2eb-208e7863f8fe,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba90fa8f-51ce-44e5-b2eb-208e7863f8fe,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
d2b6004f-9971-4b27-97fa-450533eb13e2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,GKRP,False,GKRP,,,,
47822f91-b671-4ec7-b6a2-507b2f5703c5,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",False,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
8f6dcb97-16b0-4142-9ef3-7b5efde32885,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Following glucose phosphorylation to glucose 6-phosphate, the glucose 6-phosphate can be used for glycogen synthesis or the pentose phosphate pathway. Substrate that continues through glycolysis is isomerized to fructose 6-phosphate, which is the substrate for the reaction catalyzed by phosphofructokinase 1 (PFK1).",True,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
a68759cc-fc7a-41b3-9fb7-a063e7886b0c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,PFK1,False,PFK1,,,,
a0eaa7cf-d1d0-465e-98d5-fb5a00854513,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of phosphofructokinase 1 (PFK1),False,Regulation of phosphofructokinase 1 (PFK1),,,,
fdacf8fe-f3db-456f-8667-54e2a70e5232,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Regulation of phosphofructokinase 1 is primarily through allosteric activation by AMP and fructose 2,6-bisphosphate. High AMP levels would indicate a lack of energy within the cell, and this would increase flux through glycolysis by enhancing the activity of PFK1. PFK1 is also inhibited by citrate and ATP; levels of these compounds are indicative of a high energy state, suggesting there are sufficient oxidation productions and glucose is diverted to storage pathways.",True,Regulation of phosphofructokinase 1 (PFK1),,,,
71cbabba-acd0-4808-a451-a5ac34d45271,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
71cbabba-acd0-4808-a451-a5ac34d45271,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
71cbabba-acd0-4808-a451-a5ac34d45271,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
71cbabba-acd0-4808-a451-a5ac34d45271,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
71cbabba-acd0-4808-a451-a5ac34d45271,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
71cbabba-acd0-4808-a451-a5ac34d45271,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
96face07-81cf-462f-8815-78ee1b74530a,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,PFK2,False,PFK2,,,,
9e90d8c7-c96e-41d4-9bf5-9f68d113a511,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,FBP2,False,FBP2,,,,
6d353cdc-bc4d-4227-a5b1-ce39cc90c954,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,False,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
59b70598-463a-4196-b8eb-966f430036d7,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Following the synthesis of fructose 1,6-phosphate, aldolase will cleave this substrate into dihydroxyacetone and glyceraldehyde 3-phosphate. These three carbon compounds will be used to synthesize pyruvate in the final regulatory step of the pathway catalyzed by pyruvate kinase (PK).",True,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
0fd34eae-724b-4047-ba90-e263fee17ba3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of pyruvate kinase (PK),False,Regulation of pyruvate kinase (PK),,,,
ac905808-95b6-434a-9a70-8656cdb678a3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
ac905808-95b6-434a-9a70-8656cdb678a3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
ac905808-95b6-434a-9a70-8656cdb678a3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
ac905808-95b6-434a-9a70-8656cdb678a3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
ac905808-95b6-434a-9a70-8656cdb678a3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
ac905808-95b6-434a-9a70-8656cdb678a3,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
96a0aba5-7305-4891-922b-2ea68ad223a5,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,phosphoenol,False,phosphoenol,,,,
2ff95533-7c38-4bad-85d8-964301b04d09,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Movement of NADH from the cytosol to the mitochondria,False,Movement of NADH from the cytosol to the mitochondria,,,,
ee9325a2-2700-4bad-830a-ee586b259e8a,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The NADH generated in the cytosol by glycolysis must be oxidized back to NAD+ in order to maintain a pool of NAD+ needed for glucose oxidation. As NADH oxidation takes place in the mitochondria, and the membrane is not permeable to NADH, two shuttles are used to move cytosolic NADH into the mitochondria. These processes are a way to get energy out of cytoplasmic NADH into the mitochondria.",True,Movement of NADH from the cytosol to the mitochondria,,,,
68b1e2c2-1982-48ae-933c-fcf179930945,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Glycerol 3-phosphate shuttle,False,Glycerol 3-phosphate shuttle,,,,
17aa2606-72d4-4e61-9e35-9819dbee0be4,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
17aa2606-72d4-4e61-9e35-9819dbee0be4,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
17aa2606-72d4-4e61-9e35-9819dbee0be4,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
17aa2606-72d4-4e61-9e35-9819dbee0be4,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
17aa2606-72d4-4e61-9e35-9819dbee0be4,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
17aa2606-72d4-4e61-9e35-9819dbee0be4,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
fbc537cf-9fc9-4af6-9ae1-b046568cf3e9,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,dihydroxyacetonephosphate,False,dihydroxyacetonephosphate,,,,
201d3927-2b2f-49a3-b2f4-3509a2d68e79,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Malate-aspartate shuttle,False,Malate-aspartate shuttle,,,,
7b9ae9f5-ccb1-4f7b-bbb3-7d299dd10b23,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
7b9ae9f5-ccb1-4f7b-bbb3-7d299dd10b23,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
7b9ae9f5-ccb1-4f7b-bbb3-7d299dd10b23,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
7b9ae9f5-ccb1-4f7b-bbb3-7d299dd10b23,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
7b9ae9f5-ccb1-4f7b-bbb3-7d299dd10b23,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
7b9ae9f5-ccb1-4f7b-bbb3-7d299dd10b23,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
8cf12648-5043-4387-a69b-5194137e276b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,OAA,False,OAA,,,,
a4d37c2c-adc9-4ce3-b972-5c9b0c78c707,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,canʼt,False,canʼt,,,,
73553fc7-0e1e-4638-8e63-59ea5f682246,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Pyruvate dehydrogenase complex,False,Pyruvate dehydrogenase complex,,,,
74d1430c-769e-45ff-9b76-ae5777285d6f,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Under aerobic conditions, the pyruvate produced by glycolysis will be oxidized to acetyl-CoA using the pyruvate dehydrogenase complex (PDC). This enzyme is a key transition point between cytosolic and mitochondrial metabolism. This complex is composed of three subunits, which require the cofactors thiamine pyrophosphate, lipoic acid, and FADH2; NADH is also required for the reaction to move forward. The enzyme is highly regulated by both covalent and allosteric regulation. Deficiencies of the PDC can be recessive or X-linked (depending on the subunit deficient) and present with symptoms of lactic acidosis after consuming a meal high in carbohydrates. This metabolic deficiency can be managed by delivering a ketogenic diet and bypassing glycolysis all together.",True,Pyruvate dehydrogenase complex,,,,
a29736f7-c06b-424e-8533-ad12f4bcfae2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,FADH,False,FADH,,,,
6ea8ef4f-2900-455d-9ca9-d2fded06cf40,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of the pyruvate dehydrogenase complex (PDC),False,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
833f75de-e02a-4897-8a04-a84f27f22f99,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The PDC is regulated by allosteric and covalent regulations. The complex itself can be allosterically activated by pyruvate and NAD+. Elevation of substrate (pyruvate) will enhance flux through this enzyme as will the indication of low energy states as triggered by high NAD+ levels. The PDC is also inhibited by acetyl-CoA and NADH directly. Product inhibition is a very common regulatory mechanism, and high NADH would signal sufficient energy levels, therefore decreasing activity of the PDC.",True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
7467b7b5-2f7c-42c8-b0f4-f7e7867d3606,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,The PDC is also regulated through covalent modification. Phosphorylation of the complex will decrease activity of the enzyme.,True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
e0994ed2-87b2-42fd-886b-4fdc72e9ba7e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e0994ed2-87b2-42fd-886b-4fdc72e9ba7e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e0994ed2-87b2-42fd-886b-4fdc72e9ba7e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e0994ed2-87b2-42fd-886b-4fdc72e9ba7e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e0994ed2-87b2-42fd-886b-4fdc72e9ba7e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e0994ed2-87b2-42fd-886b-4fdc72e9ba7e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
5e79685c-44a0-44e3-87c5-ac44bbdf9a20,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Summary of pathway regulation,False,Summary of pathway regulation,,,,
7a500298-e875-471b-8309-393871378e6d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Table 4.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
dd2c9d30-3292-4bdb-8daf-c318feeb6309,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.1 References and resources,True,Summary of pathway regulation,,,,
3e593a1a-7907-43ee-b913-bb6429005204,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 6: Bioenergetics and Oxidative Phosphorylation: Section V, VI, Chapter 8: Introduction to Metabolism and Glycolysis, Chapter 9: TCA Cycle and Pyruvate Dehydrogenase Complex: Section IIA, IIB, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section II, IV, V, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
67748f32-55ad-4385-9ecc-749abb04b3e9,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72–78, 85–89.",True,Summary of pathway regulation,,,,
7ff36049-e9fc-4281-9709-d04b9e27ccec,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 19: Basic Concepts of Regulation: Section IV.A.1.2, Chapter 20: Cellular Bioenergetics, Chapter 22: Generation of ATP from Glucose: Section I.A.B.C, III, Chapter 24: Oxidative Phosphorylation and the ETC: Section I.E, II, III, Chapter 31: Synthesis of Fatty Acids: Section I.A.B, IV, V.",True,Summary of pathway regulation,,,,
fdbdc43c-05bb-44ce-bcd2-25fdaacd8c13,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
fdbdc43c-05bb-44ce-bcd2-25fdaacd8c13,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
fdbdc43c-05bb-44ce-bcd2-25fdaacd8c13,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
fdbdc43c-05bb-44ce-bcd2-25fdaacd8c13,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
fdbdc43c-05bb-44ce-bcd2-25fdaacd8c13,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
fdbdc43c-05bb-44ce-bcd2-25fdaacd8c13,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
757b3fe9-1a08-48ca-b1c7-04b24e3993bf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
757b3fe9-1a08-48ca-b1c7-04b24e3993bf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
757b3fe9-1a08-48ca-b1c7-04b24e3993bf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
757b3fe9-1a08-48ca-b1c7-04b24e3993bf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
757b3fe9-1a08-48ca-b1c7-04b24e3993bf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
757b3fe9-1a08-48ca-b1c7-04b24e3993bf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
09b30862-fd9e-4711-b247-160213284a3d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
09b30862-fd9e-4711-b247-160213284a3d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
09b30862-fd9e-4711-b247-160213284a3d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
09b30862-fd9e-4711-b247-160213284a3d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
09b30862-fd9e-4711-b247-160213284a3d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
09b30862-fd9e-4711-b247-160213284a3d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
4ee985f8-1ab4-4120-887e-ed41d05bee52,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
4ee985f8-1ab4-4120-887e-ed41d05bee52,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
4ee985f8-1ab4-4120-887e-ed41d05bee52,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
4ee985f8-1ab4-4120-887e-ed41d05bee52,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
4ee985f8-1ab4-4120-887e-ed41d05bee52,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
4ee985f8-1ab4-4120-887e-ed41d05bee52,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ffc804e7-554f-4db3-9f29-9b105a2d77f6,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ffc804e7-554f-4db3-9f29-9b105a2d77f6,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ffc804e7-554f-4db3-9f29-9b105a2d77f6,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ffc804e7-554f-4db3-9f29-9b105a2d77f6,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ffc804e7-554f-4db3-9f29-9b105a2d77f6,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ffc804e7-554f-4db3-9f29-9b105a2d77f6,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
9ef14bee-eeea-4811-b9cc-b126c83604af,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9ef14bee-eeea-4811-b9cc-b126c83604af,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9ef14bee-eeea-4811-b9cc-b126c83604af,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9ef14bee-eeea-4811-b9cc-b126c83604af,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9ef14bee-eeea-4811-b9cc-b126c83604af,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9ef14bee-eeea-4811-b9cc-b126c83604af,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
a1175804-87ee-455a-b1e5-9c46ef4afbba,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
a1175804-87ee-455a-b1e5-9c46ef4afbba,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
a1175804-87ee-455a-b1e5-9c46ef4afbba,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
a1175804-87ee-455a-b1e5-9c46ef4afbba,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
a1175804-87ee-455a-b1e5-9c46ef4afbba,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
a1175804-87ee-455a-b1e5-9c46ef4afbba,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
23b79cea-6d5e-4f78-9653-7d4d9b613d9e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
23b79cea-6d5e-4f78-9653-7d4d9b613d9e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
23b79cea-6d5e-4f78-9653-7d4d9b613d9e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
23b79cea-6d5e-4f78-9653-7d4d9b613d9e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
23b79cea-6d5e-4f78-9653-7d4d9b613d9e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
23b79cea-6d5e-4f78-9653-7d4d9b613d9e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
a9219e02-815e-45a2-9ea0-ac4cf864fbf2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
a9219e02-815e-45a2-9ea0-ac4cf864fbf2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
a9219e02-815e-45a2-9ea0-ac4cf864fbf2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
a9219e02-815e-45a2-9ea0-ac4cf864fbf2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
a9219e02-815e-45a2-9ea0-ac4cf864fbf2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
a9219e02-815e-45a2-9ea0-ac4cf864fbf2,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
fc836e5e-c1c9-4928-a443-aa96409e1819,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.2 Tricarboxylic Acid Cycle (TCA),True,Summary of pathway regulation,,,,
b98942e4-1e12-4e85-af17-81675ddeae43,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
b98942e4-1e12-4e85-af17-81675ddeae43,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
b98942e4-1e12-4e85-af17-81675ddeae43,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
b98942e4-1e12-4e85-af17-81675ddeae43,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
b98942e4-1e12-4e85-af17-81675ddeae43,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
b98942e4-1e12-4e85-af17-81675ddeae43,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
93df16ce-05a3-4390-97d8-33b94520e816,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,FADH2,False,FADH2,,,,
642ae580-8500-4860-b02c-2cba56add6cc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
642ae580-8500-4860-b02c-2cba56add6cc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
642ae580-8500-4860-b02c-2cba56add6cc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
642ae580-8500-4860-b02c-2cba56add6cc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
642ae580-8500-4860-b02c-2cba56add6cc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
642ae580-8500-4860-b02c-2cba56add6cc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
a8a38913-a371-48ab-844a-47cc69e6476b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
a8a38913-a371-48ab-844a-47cc69e6476b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
a8a38913-a371-48ab-844a-47cc69e6476b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
a8a38913-a371-48ab-844a-47cc69e6476b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
a8a38913-a371-48ab-844a-47cc69e6476b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
a8a38913-a371-48ab-844a-47cc69e6476b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
dda8ecee-c131-4087-8678-468d7aca8539,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of the TCA cycle,False,Regulation of the TCA cycle,,,,
efc3d06a-4897-4137-961d-8be54aac8c6c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Throughout the cycle, there are two key regulatory and irreversible steps to be aware of. The first is the conversion of isocitrate to α-ketoglutarate by isocitrate dehydrogenase, and the second is the conversion of α-ketoglutarate to succinyl-CoA by α-ketoglutarate dehydrogenase. The two key regulatory points are:",True,Regulation of the TCA cycle,,,,
d24f523b-dbc5-4058-81d5-19de867b067c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Isocitrate dehydrogenase, which can be activated by Ca2+ and ADP to increase flux through the cycle, and inhibited by NADH, which would suggest adequate energy in the cell.",True,Regulation of the TCA cycle,,,,
2cef0674-70d2-4d0c-adfb-aa944abff047,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Ca2,False,Ca2,,,,
bcba9f79-02f4-4bd8-af3b-68761776a585,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
bcba9f79-02f4-4bd8-af3b-68761776a585,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
bcba9f79-02f4-4bd8-af3b-68761776a585,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
bcba9f79-02f4-4bd8-af3b-68761776a585,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
bcba9f79-02f4-4bd8-af3b-68761776a585,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
bcba9f79-02f4-4bd8-af3b-68761776a585,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
0674e92c-bf8b-44e0-93a6-1ff984cea24c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Malate dehydrogenase can also be inhibited by NADH, however, the reaction is reversible depending on levels of NADH. The oxidation of malate to OAA requires NAD+, and under certain pathological situations the lack of free NAD+ within the mitochondria will reduce the rate of this reaction (this is common in the case of alcohol metabolism).",True,Ca2,,,,
769e382b-4493-4957-bd34-61228dcc16eb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Keep in mind that with the addition of each acetyl-CoA (comprised of 2 carbons) to the TCA cycle, two molecules of CO2 are released, thus there is no net gain or loss of carbons in the cycle. The process moves forward driven by energetics and substrate availability. The pathway can be active in both the fed and fasted states. In the fed state, acetyl-CoA is generated primarily through glucose oxidation. In contrast, in the fasted state acetyl-CoA is generated primarily from β-oxidation, and the majority of acetyl-CoA is used to synthesize ketones.",True,Ca2,,,,
bbe38e2f-4233-4123-ad47-00967f8b2d53,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Table 4.2: Summary of pathway regulation.,True,Ca2,,,,
a0f3960c-37d6-4a27-8622-1dc59b59df98,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.2 References and resources,True,Ca2,,,,
8cd30b35-b5c8-4f01-9071-98752dd90f30,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8cd30b35-b5c8-4f01-9071-98752dd90f30,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8cd30b35-b5c8-4f01-9071-98752dd90f30,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8cd30b35-b5c8-4f01-9071-98752dd90f30,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8cd30b35-b5c8-4f01-9071-98752dd90f30,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8cd30b35-b5c8-4f01-9071-98752dd90f30,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
6865fed9-6cb6-4ee0-93eb-8ee7571962fb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6865fed9-6cb6-4ee0-93eb-8ee7571962fb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6865fed9-6cb6-4ee0-93eb-8ee7571962fb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6865fed9-6cb6-4ee0-93eb-8ee7571962fb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6865fed9-6cb6-4ee0-93eb-8ee7571962fb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6865fed9-6cb6-4ee0-93eb-8ee7571962fb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
56280a32-2096-4292-b0e3-d81d7a1b5bdf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
56280a32-2096-4292-b0e3-d81d7a1b5bdf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
56280a32-2096-4292-b0e3-d81d7a1b5bdf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
56280a32-2096-4292-b0e3-d81d7a1b5bdf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
56280a32-2096-4292-b0e3-d81d7a1b5bdf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
56280a32-2096-4292-b0e3-d81d7a1b5bdf,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
43c2a05d-f08c-4ef1-93e3-cc3a9d4e31be,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
43c2a05d-f08c-4ef1-93e3-cc3a9d4e31be,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
43c2a05d-f08c-4ef1-93e3-cc3a9d4e31be,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
43c2a05d-f08c-4ef1-93e3-cc3a9d4e31be,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
43c2a05d-f08c-4ef1-93e3-cc3a9d4e31be,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
43c2a05d-f08c-4ef1-93e3-cc3a9d4e31be,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
a20c5f37-73c1-4597-85fc-15ca116b23fd,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.3 Electron Transport Chain (ETC),True,Ca2,,,,
27b219b9-971b-4a3e-a1ca-6627180e7ddc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In the production of NADH and FADH2 by the TCA cycle, β-oxidation or glycolysis is funneled directly into the electron transport chain (ETC) where each of these reduced coenzymes will donate two electrons to electron carriers. As the electrons are passed down their oxidation gradient, some of the energy is lost, but much of this energy is used to pump protons into the intermembrane space of the mitochondria.",True,Ca2,,,,
b786884b-a1de-4583-93be-18ced847fd32,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
b786884b-a1de-4583-93be-18ced847fd32,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
b786884b-a1de-4583-93be-18ced847fd32,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
b786884b-a1de-4583-93be-18ced847fd32,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
b786884b-a1de-4583-93be-18ced847fd32,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
b786884b-a1de-4583-93be-18ced847fd32,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
bad771c1-d83d-41ca-8988-296308499c6f,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"There are site specific inhibitors of the ETC to be aware of, and these will disrupt electron flow reducing overall ATP production.",True,Ca2,,,,
3d7aeb11-4a91-44c3-a763-d23bd11a8618,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Inhibitors,False,Inhibitors,,,,
9e351290-ed25-4be9-95dd-27d05919b1f9,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Inhibitors block oxidation and reduce both ATP generation and oxygen consumption; this is in contrast to uncouplers, which disrupt the mitochondrial membrane and reduce ATP production but increase oxygen consumption.",True,Inhibitors,,,,
bdd01f84-3bd7-43bb-ba49-088d65a173d5,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,uncouplers,False,uncouplers,,,,
882e8b36-e303-42d7-a67b-0364eccbc2d8,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"A common inhibitor of the ETC is carbon monoxide; this will bind to Complex IV and therefore halt the passing of electrons. Without electrons passing through the complexes, the pumping of protons is diminished and ATP is not produced. Other common inhibitors are cyanide (Complex IV), rotenone (Complex I), antimycin C (Complex III), and oligomycin, which is a Complex V inhibitor.",True,uncouplers,,,,
86fc3bee-3a8e-46f2-b6fe-e9f8f83c4da5,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Uncouplers,False,Uncouplers,,,,
d05470bd-aeeb-4f5b-b33f-b91710b78ae5,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Uncoupling of the ETC by the addition of agents such as dinitrophenol have different consequences. Uncouplers disrupt the permeability of the inner membrane (either physically or chemically) and dissipate the proton gradient.,True,Uncouplers,,,,
aa5a0be4-cb95-41ec-8dbf-0d43f30d159e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"In these cases, the release of protons across the membrane is coupled with the release of heat, rather than harnessed in the form of a phosphate bond. NADH oxidation continues rapidly, oxygen consumption is increased, and ATP production decreases. Valinomycin is another common uncoupler.",True,Uncouplers,,,,
ada737a5-ae9f-418a-a0ca-8792490d2a0d,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Biological uncoupling through the expression of uncoupling proteins (UPC) is also likely. These proteins form a physical pore within the mitochondrial membrane allowing the proton gradient to equilibrate. In brown fat, this nonshivering thermogenesis is a means of generating heat, and other members of this protein family (UPC) are expressed in various tissues but have similar roles.",True,Uncouplers,,,,
498a81e9-503f-41f3-9eaa-56bfd63d36a8,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,UPC,False,UPC,,,,
77592677-e5dd-4ee3-98eb-fb0ec67359dc,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,nonshivering,False,nonshivering,,,,
6a1b6da2-0616-4f05-8e20-859e6a4c981b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.3 References and resources,True,nonshivering,,,,
2282ae5b-290c-4b9d-8b9f-0d6d2f014702,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Text,False,Text,,,,
35aaea53-e84a-4683-97c4-20c15375f6ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
35aaea53-e84a-4683-97c4-20c15375f6ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
35aaea53-e84a-4683-97c4-20c15375f6ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
35aaea53-e84a-4683-97c4-20c15375f6ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
35aaea53-e84a-4683-97c4-20c15375f6ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
35aaea53-e84a-4683-97c4-20c15375f6ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
c7066105-ee10-4f3c-8c80-fe6a731096ad,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.4 Fatty Acid Synthesis,True,Text,,,,
ac7c090e-aff8-4808-b9b4-584d5899b86c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
ac7c090e-aff8-4808-b9b4-584d5899b86c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
ac7c090e-aff8-4808-b9b4-584d5899b86c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
ac7c090e-aff8-4808-b9b4-584d5899b86c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
ac7c090e-aff8-4808-b9b4-584d5899b86c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
ac7c090e-aff8-4808-b9b4-584d5899b86c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
d3bcd72c-ff62-4dab-8c84-b13faa076297,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The NADPH generated through this process is necessary for fatty acid synthesis. This is one of the primary pathways that produces NADPH, and the other is the oxidative portion of the pentose pathway.",True,Text,,,,
38322525-b9c6-4452-9ff8-4fcf60958d18,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The process of fatty acid synthesis starts with the carboxylation of acetyl-CoA to form malonyl-CoA (figures 4.16 and 4.17). The enzyme involved, acetyl-CoA carboxylase, is the regulatory enzyme for this pathway and requires biotin as a cofactor. After the initial priming of fatty acid synthase with acetyl-CoA, all other carbon units are added to the elongating fatty acid chain in the form of malonyl-CoA. You will see later that this intermediate is also a key inhibitor of β-oxidation.",True,Text,,,,
c304cd0e-47af-41c9-81c3-2fc3effd0480,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
c304cd0e-47af-41c9-81c3-2fc3effd0480,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
c304cd0e-47af-41c9-81c3-2fc3effd0480,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
c304cd0e-47af-41c9-81c3-2fc3effd0480,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
c304cd0e-47af-41c9-81c3-2fc3effd0480,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
c304cd0e-47af-41c9-81c3-2fc3effd0480,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
f1909fef-2df8-4347-ba2b-3b76a750ae49,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,TAGs,False,TAGs,,,,
a77c2b7c-fa85-4ebd-80e7-72eb09d476bb,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,VLDLs,False,VLDLs,,,,
5e7d14ef-af8a-4fd1-bb2c-1ed09d2ad9af,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of fatty acid synthesis,False,Regulation of fatty acid synthesis,,,,
475f728a-5cc6-4dc1-8c11-7bc1c6a508ce,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
475f728a-5cc6-4dc1-8c11-7bc1c6a508ce,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
475f728a-5cc6-4dc1-8c11-7bc1c6a508ce,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
475f728a-5cc6-4dc1-8c11-7bc1c6a508ce,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
475f728a-5cc6-4dc1-8c11-7bc1c6a508ce,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
475f728a-5cc6-4dc1-8c11-7bc1c6a508ce,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
c01831fa-ed9e-4513-b4a8-9a722bcad21f,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Table 4.3: Summary of pathway regulation.,True,Regulation of fatty acid synthesis,,,,
45f5e214-90b1-4aaf-a8a3-a0ae12dd179f,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.4 References and resources,True,Regulation of fatty acid synthesis,,,,
8f53f808-690a-4965-8178-d303f439ef0c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
8f53f808-690a-4965-8178-d303f439ef0c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
8f53f808-690a-4965-8178-d303f439ef0c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
8f53f808-690a-4965-8178-d303f439ef0c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
8f53f808-690a-4965-8178-d303f439ef0c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
8f53f808-690a-4965-8178-d303f439ef0c,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
2da9ee04-a7e4-420b-b542-8304ecd8313e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
2da9ee04-a7e4-420b-b542-8304ecd8313e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
2da9ee04-a7e4-420b-b542-8304ecd8313e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
2da9ee04-a7e4-420b-b542-8304ecd8313e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
2da9ee04-a7e4-420b-b542-8304ecd8313e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
2da9ee04-a7e4-420b-b542-8304ecd8313e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
a3339a39-aacf-40bc-aad9-0274e0d6e284,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
a3339a39-aacf-40bc-aad9-0274e0d6e284,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
a3339a39-aacf-40bc-aad9-0274e0d6e284,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
a3339a39-aacf-40bc-aad9-0274e0d6e284,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
a3339a39-aacf-40bc-aad9-0274e0d6e284,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
a3339a39-aacf-40bc-aad9-0274e0d6e284,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
45aaf6e1-61af-4aab-9312-0d2ac795dd67,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.5 Glycogen Synthesis,True,Regulation of fatty acid synthesis,,,,
092db27a-30bf-416f-b895-ee990b13547b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glycogen synthesis is the process of storing glucose and occurs primarily in the liver and the skeletal muscle. The metabolic pathways in these tissues are similar, but the utility of glycogen stores is different. Briefly, liver glycogen is catabolized primarily in response to elevated glucagon, and the glucose 6-phosphate generated is dephosphorylated and released into circulation. In contrast, muscle glycogen is only used by the muscle itself; muscle lacks glucose 6-phosphatase and glucose 6-phosphate released from muscle glycogen is oxidized in glycolysis. Although discussed here as a point of comparison, glycogenolysis is a fasted state pathway and occurs in response to glucagon and epinephrine. This will be discussed in section 5.1.",True,Regulation of fatty acid synthesis,,,,
a70e1786-d06e-4ae9-80eb-db54ff99e86e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
a70e1786-d06e-4ae9-80eb-db54ff99e86e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
a70e1786-d06e-4ae9-80eb-db54ff99e86e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
a70e1786-d06e-4ae9-80eb-db54ff99e86e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
a70e1786-d06e-4ae9-80eb-db54ff99e86e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
a70e1786-d06e-4ae9-80eb-db54ff99e86e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
ab1b1f6a-d20d-4bcc-acc9-abbde8f25e8b,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,pyrophosphorylase,False,pyrophosphorylase,,,,
01f6e669-6016-44da-aa15-ea4f7f237a42,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,glycogenin,False,glycogenin,,,,
3ab1b856-3ccd-4697-9f09-74093dbdb5ff,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Regulation of glycogen synthesis,False,Regulation of glycogen synthesis,,,,
cb68d20a-e08b-42e6-842e-364579ecc854,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Glycogen synthesis is regulated by a single enzyme, glycogen synthase. This enzyme is primarily regulated through covalent modification. It is active when dephosphorylated and inactive when phosphorylated. The phosphorylation/dephosphorylation is facilitated by glucagon and insulin levels, respectively (table 4.4).",True,Regulation of glycogen synthesis,,,,
137699bf-c8bb-432b-80d5-1c4d12d249d8,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,Table 4.4: Summary of pathway regulation.,True,Regulation of glycogen synthesis,,,,
7d8b61fb-56f9-4b27-a4aa-14a584070e8e,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,4.5 References and resources,True,Regulation of glycogen synthesis,,,,
916b56ea-4560-4a55-8641-06283ff344ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
916b56ea-4560-4a55-8641-06283ff344ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
916b56ea-4560-4a55-8641-06283ff344ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
916b56ea-4560-4a55-8641-06283ff344ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
916b56ea-4560-4a55-8641-06283ff344ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
916b56ea-4560-4a55-8641-06283ff344ea,https://pressbooks.lib.vt.edu/cellbio/,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-5,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
a7a72843-fbc6-4bef-abe3-5f0541149c8b,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),False,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),,,,
6a540eb4-a7bb-49d3-8b64-48d922d6db8d,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Fatty acid synthesis,False,Fatty acid synthesis,,,,
1a878d85-5c8b-40d1-9f03-40d6a391d652,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycogen synthesis,False,Glycogen synthesis,,,,
3c97b212-57de-4283-9ed1-0086e64156da,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,reoxidize,False,reoxidize,,,,
8a740553-7f88-47e1-abf1-645b23539afb,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of glycolysis,False,Regulation of glycolysis,,,,
deae4eb4-33d7-48d0-a36b-1bb73f8d6318,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
deae4eb4-33d7-48d0-a36b-1bb73f8d6318,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
deae4eb4-33d7-48d0-a36b-1bb73f8d6318,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
deae4eb4-33d7-48d0-a36b-1bb73f8d6318,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
deae4eb4-33d7-48d0-a36b-1bb73f8d6318,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
deae4eb4-33d7-48d0-a36b-1bb73f8d6318,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
f1c8f078-5388-4af4-ba7c-c968effc57f0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glucokinase: Glucose to glucose 6-phosphate,False,Glucokinase: Glucose to glucose 6-phosphate,,,,
028f7ffb-e595-4526-9a2d-301dfe349faa,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
028f7ffb-e595-4526-9a2d-301dfe349faa,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
028f7ffb-e595-4526-9a2d-301dfe349faa,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
028f7ffb-e595-4526-9a2d-301dfe349faa,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
028f7ffb-e595-4526-9a2d-301dfe349faa,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
028f7ffb-e595-4526-9a2d-301dfe349faa,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
3aaea88e-c3b2-4f35-8003-0cf309c50f51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,GLUT2,False,GLUT2,,,,
62f6be69-3e17-4205-98a9-aa50a6c3153f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In skeletal muscle, and most other peripheral tissues, glucose is phosphorylated by hexokinase.",True,GLUT2,,,,
cb865c47-1da3-4eca-98cc-632fc4f14ff9,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
cb865c47-1da3-4eca-98cc-632fc4f14ff9,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
cb865c47-1da3-4eca-98cc-632fc4f14ff9,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
cb865c47-1da3-4eca-98cc-632fc4f14ff9,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
cb865c47-1da3-4eca-98cc-632fc4f14ff9,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
cb865c47-1da3-4eca-98cc-632fc4f14ff9,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b0be45b9-f2bd-467e-9340-aaa845ccae38,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of glucokinase and hexokinase,False,Regulation of glucokinase and hexokinase,,,,
008f0f6f-20cc-42a7-93d8-b9fc6ed6f940,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
008f0f6f-20cc-42a7-93d8-b9fc6ed6f940,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
008f0f6f-20cc-42a7-93d8-b9fc6ed6f940,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
008f0f6f-20cc-42a7-93d8-b9fc6ed6f940,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
008f0f6f-20cc-42a7-93d8-b9fc6ed6f940,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
008f0f6f-20cc-42a7-93d8-b9fc6ed6f940,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
b512884e-4624-43e9-8371-7ac5c2a27d42,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,GKRP,False,GKRP,,,,
8330c909-adfd-4b7a-bc51-59f8e6bea6bb,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",False,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
db6cbffb-04e0-4255-9766-fe54adc6134a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Following glucose phosphorylation to glucose 6-phosphate, the glucose 6-phosphate can be used for glycogen synthesis or the pentose phosphate pathway. Substrate that continues through glycolysis is isomerized to fructose 6-phosphate, which is the substrate for the reaction catalyzed by phosphofructokinase 1 (PFK1).",True,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
7ea1404a-5128-41ca-ba34-867ccd1cdaee,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,PFK1,False,PFK1,,,,
f83b7ae6-cc7a-4aca-b237-335bc7b297f4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of phosphofructokinase 1 (PFK1),False,Regulation of phosphofructokinase 1 (PFK1),,,,
c5525992-c0f5-4238-8945-5b3d9aeeddf0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Regulation of phosphofructokinase 1 is primarily through allosteric activation by AMP and fructose 2,6-bisphosphate. High AMP levels would indicate a lack of energy within the cell, and this would increase flux through glycolysis by enhancing the activity of PFK1. PFK1 is also inhibited by citrate and ATP; levels of these compounds are indicative of a high energy state, suggesting there are sufficient oxidation productions and glucose is diverted to storage pathways.",True,Regulation of phosphofructokinase 1 (PFK1),,,,
ab8ed1a6-115b-4488-9467-47e889652e14,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ab8ed1a6-115b-4488-9467-47e889652e14,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ab8ed1a6-115b-4488-9467-47e889652e14,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ab8ed1a6-115b-4488-9467-47e889652e14,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ab8ed1a6-115b-4488-9467-47e889652e14,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ab8ed1a6-115b-4488-9467-47e889652e14,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
7f51bfaf-0553-4a23-a9e7-900d17a624eb,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,PFK2,False,PFK2,,,,
a43a2972-68c7-4405-87ea-f735fd6eaa4d,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,FBP2,False,FBP2,,,,
27f63131-16e5-4f92-9763-9ab413ff1564,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,False,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
d7702909-67d5-439a-93bb-12bc1211c86f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Following the synthesis of fructose 1,6-phosphate, aldolase will cleave this substrate into dihydroxyacetone and glyceraldehyde 3-phosphate. These three carbon compounds will be used to synthesize pyruvate in the final regulatory step of the pathway catalyzed by pyruvate kinase (PK).",True,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
f382f5c4-6dee-4e4f-839a-e0e22f57c9b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of pyruvate kinase (PK),False,Regulation of pyruvate kinase (PK),,,,
e3110cd9-8b5e-4ae6-bc56-210690ca2b46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
e3110cd9-8b5e-4ae6-bc56-210690ca2b46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
e3110cd9-8b5e-4ae6-bc56-210690ca2b46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
e3110cd9-8b5e-4ae6-bc56-210690ca2b46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
e3110cd9-8b5e-4ae6-bc56-210690ca2b46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
e3110cd9-8b5e-4ae6-bc56-210690ca2b46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
fcecdeb2-92fe-4ff6-bda7-8fa98772663c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,phosphoenol,False,phosphoenol,,,,
2bfcf40c-6e2e-4f7b-a64f-2268dde6ad51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Movement of NADH from the cytosol to the mitochondria,False,Movement of NADH from the cytosol to the mitochondria,,,,
f2534112-aac1-46a5-8c88-3c92eede8a89,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The NADH generated in the cytosol by glycolysis must be oxidized back to NAD+ in order to maintain a pool of NAD+ needed for glucose oxidation. As NADH oxidation takes place in the mitochondria, and the membrane is not permeable to NADH, two shuttles are used to move cytosolic NADH into the mitochondria. These processes are a way to get energy out of cytoplasmic NADH into the mitochondria.",True,Movement of NADH from the cytosol to the mitochondria,,,,
01587b6a-3550-4baf-bdab-a8159d0a798d,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Glycerol 3-phosphate shuttle,False,Glycerol 3-phosphate shuttle,,,,
2c817186-fbd9-4b07-bca3-e70f27b26fa3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2c817186-fbd9-4b07-bca3-e70f27b26fa3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2c817186-fbd9-4b07-bca3-e70f27b26fa3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2c817186-fbd9-4b07-bca3-e70f27b26fa3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2c817186-fbd9-4b07-bca3-e70f27b26fa3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2c817186-fbd9-4b07-bca3-e70f27b26fa3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
76646b66-0bc0-4ef7-a275-40d253083fdf,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,dihydroxyacetonephosphate,False,dihydroxyacetonephosphate,,,,
972e0bc6-bab9-4512-8be9-dadffc30a0f3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Malate-aspartate shuttle,False,Malate-aspartate shuttle,,,,
b4cff1f2-4db3-49e3-9961-57867c9350ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
b4cff1f2-4db3-49e3-9961-57867c9350ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
b4cff1f2-4db3-49e3-9961-57867c9350ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
b4cff1f2-4db3-49e3-9961-57867c9350ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
b4cff1f2-4db3-49e3-9961-57867c9350ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
b4cff1f2-4db3-49e3-9961-57867c9350ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
97c343e7-e3ca-4b80-8847-cb8589c09ae2,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,OAA,False,OAA,,,,
6b8ab1e4-8eb2-4e0f-a624-465aeaa4610b,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,canʼt,False,canʼt,,,,
f19f33ef-a7b0-4270-b842-73c4b407a5ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Pyruvate dehydrogenase complex,False,Pyruvate dehydrogenase complex,,,,
152d7629-38bb-48d6-beda-95f7f28d575e,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Under aerobic conditions, the pyruvate produced by glycolysis will be oxidized to acetyl-CoA using the pyruvate dehydrogenase complex (PDC). This enzyme is a key transition point between cytosolic and mitochondrial metabolism. This complex is composed of three subunits, which require the cofactors thiamine pyrophosphate, lipoic acid, and FADH2; NADH is also required for the reaction to move forward. The enzyme is highly regulated by both covalent and allosteric regulation. Deficiencies of the PDC can be recessive or X-linked (depending on the subunit deficient) and present with symptoms of lactic acidosis after consuming a meal high in carbohydrates. This metabolic deficiency can be managed by delivering a ketogenic diet and bypassing glycolysis all together.",True,Pyruvate dehydrogenase complex,,,,
27d9be7e-b47e-4f2d-b3e4-acca14151fe1,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,FADH,False,FADH,,,,
99bf3f5d-a0cc-4ea8-bbd9-3d5a1f3b9c94,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of the pyruvate dehydrogenase complex (PDC),False,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
fad57c1b-179f-4bc5-908d-2b1519e1ef76,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The PDC is regulated by allosteric and covalent regulations. The complex itself can be allosterically activated by pyruvate and NAD+. Elevation of substrate (pyruvate) will enhance flux through this enzyme as will the indication of low energy states as triggered by high NAD+ levels. The PDC is also inhibited by acetyl-CoA and NADH directly. Product inhibition is a very common regulatory mechanism, and high NADH would signal sufficient energy levels, therefore decreasing activity of the PDC.",True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
2de0e80b-3f4a-4ede-9b40-22fe964010b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,The PDC is also regulated through covalent modification. Phosphorylation of the complex will decrease activity of the enzyme.,True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
9bff5c3b-cbcc-4455-9494-c19c8aa2ca21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
9bff5c3b-cbcc-4455-9494-c19c8aa2ca21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
9bff5c3b-cbcc-4455-9494-c19c8aa2ca21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
9bff5c3b-cbcc-4455-9494-c19c8aa2ca21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
9bff5c3b-cbcc-4455-9494-c19c8aa2ca21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
9bff5c3b-cbcc-4455-9494-c19c8aa2ca21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
01017850-033b-48a7-9ab5-3c5948c0457d,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Summary of pathway regulation,False,Summary of pathway regulation,,,,
122c06a3-dd97-4880-b846-f9eb10a067e3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Table 4.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
9967f4f6-d27f-41bb-9d77-b923e57f0296,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.1 References and resources,True,Summary of pathway regulation,,,,
32c898f2-4f08-4674-9acd-daba84a739f4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 6: Bioenergetics and Oxidative Phosphorylation: Section V, VI, Chapter 8: Introduction to Metabolism and Glycolysis, Chapter 9: TCA Cycle and Pyruvate Dehydrogenase Complex: Section IIA, IIB, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section II, IV, V, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
00a9e6f0-0324-4dee-b80e-8a0b6cee39f2,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72–78, 85–89.",True,Summary of pathway regulation,,,,
6c3e1f64-67ba-489a-ab5d-89f5cd8aebc0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 19: Basic Concepts of Regulation: Section IV.A.1.2, Chapter 20: Cellular Bioenergetics, Chapter 22: Generation of ATP from Glucose: Section I.A.B.C, III, Chapter 24: Oxidative Phosphorylation and the ETC: Section I.E, II, III, Chapter 31: Synthesis of Fatty Acids: Section I.A.B, IV, V.",True,Summary of pathway regulation,,,,
f194ee16-c660-40eb-9199-15925c872bdd,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
f194ee16-c660-40eb-9199-15925c872bdd,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
f194ee16-c660-40eb-9199-15925c872bdd,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
f194ee16-c660-40eb-9199-15925c872bdd,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
f194ee16-c660-40eb-9199-15925c872bdd,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
f194ee16-c660-40eb-9199-15925c872bdd,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
8d00bd80-63ad-4cb0-95de-3922069524ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
8d00bd80-63ad-4cb0-95de-3922069524ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
8d00bd80-63ad-4cb0-95de-3922069524ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
8d00bd80-63ad-4cb0-95de-3922069524ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
8d00bd80-63ad-4cb0-95de-3922069524ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
8d00bd80-63ad-4cb0-95de-3922069524ab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
8b65cc78-fd26-4d39-a539-4fa2122ee3e0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
8b65cc78-fd26-4d39-a539-4fa2122ee3e0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
8b65cc78-fd26-4d39-a539-4fa2122ee3e0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
8b65cc78-fd26-4d39-a539-4fa2122ee3e0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
8b65cc78-fd26-4d39-a539-4fa2122ee3e0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
8b65cc78-fd26-4d39-a539-4fa2122ee3e0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
3f721206-ee53-43ef-be22-a010288d1e09,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
3f721206-ee53-43ef-be22-a010288d1e09,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
3f721206-ee53-43ef-be22-a010288d1e09,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
3f721206-ee53-43ef-be22-a010288d1e09,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
3f721206-ee53-43ef-be22-a010288d1e09,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
3f721206-ee53-43ef-be22-a010288d1e09,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
9cc3e251-fdb9-4016-91f2-365f9b30add3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
9cc3e251-fdb9-4016-91f2-365f9b30add3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
9cc3e251-fdb9-4016-91f2-365f9b30add3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
9cc3e251-fdb9-4016-91f2-365f9b30add3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
9cc3e251-fdb9-4016-91f2-365f9b30add3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
9cc3e251-fdb9-4016-91f2-365f9b30add3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
40082cd3-d7a5-43b4-b941-c09862f423ce,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
40082cd3-d7a5-43b4-b941-c09862f423ce,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
40082cd3-d7a5-43b4-b941-c09862f423ce,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
40082cd3-d7a5-43b4-b941-c09862f423ce,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
40082cd3-d7a5-43b4-b941-c09862f423ce,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
40082cd3-d7a5-43b4-b941-c09862f423ce,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
e1410e18-dfc1-4358-854e-d112a45b6b55,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
e1410e18-dfc1-4358-854e-d112a45b6b55,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
e1410e18-dfc1-4358-854e-d112a45b6b55,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
e1410e18-dfc1-4358-854e-d112a45b6b55,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
e1410e18-dfc1-4358-854e-d112a45b6b55,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
e1410e18-dfc1-4358-854e-d112a45b6b55,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
73400ba1-a849-45ef-b130-c35fcced1aa5,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
73400ba1-a849-45ef-b130-c35fcced1aa5,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
73400ba1-a849-45ef-b130-c35fcced1aa5,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
73400ba1-a849-45ef-b130-c35fcced1aa5,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
73400ba1-a849-45ef-b130-c35fcced1aa5,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
73400ba1-a849-45ef-b130-c35fcced1aa5,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
86ad5b23-f364-410d-bd9d-f20d30c56102,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
86ad5b23-f364-410d-bd9d-f20d30c56102,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
86ad5b23-f364-410d-bd9d-f20d30c56102,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
86ad5b23-f364-410d-bd9d-f20d30c56102,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
86ad5b23-f364-410d-bd9d-f20d30c56102,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
86ad5b23-f364-410d-bd9d-f20d30c56102,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e4a64fd5-0ea1-47e5-a918-528d7ac0c756,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.2 Tricarboxylic Acid Cycle (TCA),True,Summary of pathway regulation,,,,
630b3864-ac17-488e-a23b-bdd46dd65bad,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
630b3864-ac17-488e-a23b-bdd46dd65bad,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
630b3864-ac17-488e-a23b-bdd46dd65bad,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
630b3864-ac17-488e-a23b-bdd46dd65bad,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
630b3864-ac17-488e-a23b-bdd46dd65bad,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
630b3864-ac17-488e-a23b-bdd46dd65bad,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
f97c5916-8607-4bb3-b340-32f71cacea90,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,FADH2,False,FADH2,,,,
acc55992-c930-47ee-979d-a40909f5efd4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
acc55992-c930-47ee-979d-a40909f5efd4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
acc55992-c930-47ee-979d-a40909f5efd4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
acc55992-c930-47ee-979d-a40909f5efd4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
acc55992-c930-47ee-979d-a40909f5efd4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
acc55992-c930-47ee-979d-a40909f5efd4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e3befc76-3d89-4809-a4fe-53c8386dca71,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
e3befc76-3d89-4809-a4fe-53c8386dca71,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
e3befc76-3d89-4809-a4fe-53c8386dca71,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
e3befc76-3d89-4809-a4fe-53c8386dca71,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
e3befc76-3d89-4809-a4fe-53c8386dca71,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
e3befc76-3d89-4809-a4fe-53c8386dca71,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
d5b119f9-1423-4383-85a5-6e63458f70d0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of the TCA cycle,False,Regulation of the TCA cycle,,,,
1145155b-aaae-4075-81d4-d72774cbd9e9,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Throughout the cycle, there are two key regulatory and irreversible steps to be aware of. The first is the conversion of isocitrate to α-ketoglutarate by isocitrate dehydrogenase, and the second is the conversion of α-ketoglutarate to succinyl-CoA by α-ketoglutarate dehydrogenase. The two key regulatory points are:",True,Regulation of the TCA cycle,,,,
e1ef036a-4820-4083-af9c-44249286e83b,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Isocitrate dehydrogenase, which can be activated by Ca2+ and ADP to increase flux through the cycle, and inhibited by NADH, which would suggest adequate energy in the cell.",True,Regulation of the TCA cycle,,,,
815f36df-28aa-4e1e-9726-862169f2cd0d,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Ca2,False,Ca2,,,,
e2075dd3-5d61-4203-a9eb-c96f6fcac75f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
e2075dd3-5d61-4203-a9eb-c96f6fcac75f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
e2075dd3-5d61-4203-a9eb-c96f6fcac75f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
e2075dd3-5d61-4203-a9eb-c96f6fcac75f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
e2075dd3-5d61-4203-a9eb-c96f6fcac75f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
e2075dd3-5d61-4203-a9eb-c96f6fcac75f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
ab6cbadb-38ff-45ce-9c47-6d6f08279e48,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Malate dehydrogenase can also be inhibited by NADH, however, the reaction is reversible depending on levels of NADH. The oxidation of malate to OAA requires NAD+, and under certain pathological situations the lack of free NAD+ within the mitochondria will reduce the rate of this reaction (this is common in the case of alcohol metabolism).",True,Ca2,,,,
47b6a603-7c5f-4451-a336-d64a018b7e4b,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Keep in mind that with the addition of each acetyl-CoA (comprised of 2 carbons) to the TCA cycle, two molecules of CO2 are released, thus there is no net gain or loss of carbons in the cycle. The process moves forward driven by energetics and substrate availability. The pathway can be active in both the fed and fasted states. In the fed state, acetyl-CoA is generated primarily through glucose oxidation. In contrast, in the fasted state acetyl-CoA is generated primarily from β-oxidation, and the majority of acetyl-CoA is used to synthesize ketones.",True,Ca2,,,,
caa0855f-76bc-45b4-b7df-72574dde4723,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Table 4.2: Summary of pathway regulation.,True,Ca2,,,,
7a9955be-ecc6-412a-b886-7a258717efe3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.2 References and resources,True,Ca2,,,,
d5cf9350-0621-4676-b378-98f08dd87a46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
d5cf9350-0621-4676-b378-98f08dd87a46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
d5cf9350-0621-4676-b378-98f08dd87a46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
d5cf9350-0621-4676-b378-98f08dd87a46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
d5cf9350-0621-4676-b378-98f08dd87a46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
d5cf9350-0621-4676-b378-98f08dd87a46,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
48c46567-45c2-442a-b1ec-1e072efc51de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
48c46567-45c2-442a-b1ec-1e072efc51de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
48c46567-45c2-442a-b1ec-1e072efc51de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
48c46567-45c2-442a-b1ec-1e072efc51de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
48c46567-45c2-442a-b1ec-1e072efc51de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
48c46567-45c2-442a-b1ec-1e072efc51de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
9eede993-ced0-4f1a-9ece-8dfdcce5a99e,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
9eede993-ced0-4f1a-9ece-8dfdcce5a99e,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
9eede993-ced0-4f1a-9ece-8dfdcce5a99e,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
9eede993-ced0-4f1a-9ece-8dfdcce5a99e,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
9eede993-ced0-4f1a-9ece-8dfdcce5a99e,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
9eede993-ced0-4f1a-9ece-8dfdcce5a99e,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
fb72c22a-9289-4a87-914f-345636a9d7de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
fb72c22a-9289-4a87-914f-345636a9d7de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
fb72c22a-9289-4a87-914f-345636a9d7de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
fb72c22a-9289-4a87-914f-345636a9d7de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
fb72c22a-9289-4a87-914f-345636a9d7de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
fb72c22a-9289-4a87-914f-345636a9d7de,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
e5843d22-4c89-48c6-b218-680a356c318c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.3 Electron Transport Chain (ETC),True,Ca2,,,,
cb148970-e713-45dc-a7bc-f82d9fecdd9b,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In the production of NADH and FADH2 by the TCA cycle, β-oxidation or glycolysis is funneled directly into the electron transport chain (ETC) where each of these reduced coenzymes will donate two electrons to electron carriers. As the electrons are passed down their oxidation gradient, some of the energy is lost, but much of this energy is used to pump protons into the intermembrane space of the mitochondria.",True,Ca2,,,,
d4da3a96-7679-4e48-a531-fde0370730c3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
d4da3a96-7679-4e48-a531-fde0370730c3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
d4da3a96-7679-4e48-a531-fde0370730c3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
d4da3a96-7679-4e48-a531-fde0370730c3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
d4da3a96-7679-4e48-a531-fde0370730c3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
d4da3a96-7679-4e48-a531-fde0370730c3,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
f3cd8952-4441-451c-b9b1-d8920b0674da,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"There are site specific inhibitors of the ETC to be aware of, and these will disrupt electron flow reducing overall ATP production.",True,Ca2,,,,
420140df-a251-4db4-a41f-20cd8555b552,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Inhibitors,False,Inhibitors,,,,
9cd736d4-0615-4f48-9026-3caa4050ef1b,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Inhibitors block oxidation and reduce both ATP generation and oxygen consumption; this is in contrast to uncouplers, which disrupt the mitochondrial membrane and reduce ATP production but increase oxygen consumption.",True,Inhibitors,,,,
fe6ed570-cc56-47e3-b391-152f9cfd2444,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,uncouplers,False,uncouplers,,,,
198d6df6-df68-4449-a145-955a7377d86a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"A common inhibitor of the ETC is carbon monoxide; this will bind to Complex IV and therefore halt the passing of electrons. Without electrons passing through the complexes, the pumping of protons is diminished and ATP is not produced. Other common inhibitors are cyanide (Complex IV), rotenone (Complex I), antimycin C (Complex III), and oligomycin, which is a Complex V inhibitor.",True,uncouplers,,,,
27dae06c-d2be-4160-9037-62bc15b92901,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Uncouplers,False,Uncouplers,,,,
dcfe3409-9fdb-42f5-8d3f-1afeb6e6199c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Uncoupling of the ETC by the addition of agents such as dinitrophenol have different consequences. Uncouplers disrupt the permeability of the inner membrane (either physically or chemically) and dissipate the proton gradient.,True,Uncouplers,,,,
2141a838-9c04-4e5a-a87b-9227c9d96dab,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"In these cases, the release of protons across the membrane is coupled with the release of heat, rather than harnessed in the form of a phosphate bond. NADH oxidation continues rapidly, oxygen consumption is increased, and ATP production decreases. Valinomycin is another common uncoupler.",True,Uncouplers,,,,
5af383a9-1e49-4654-8197-ac4e1c5a8efa,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Biological uncoupling through the expression of uncoupling proteins (UPC) is also likely. These proteins form a physical pore within the mitochondrial membrane allowing the proton gradient to equilibrate. In brown fat, this nonshivering thermogenesis is a means of generating heat, and other members of this protein family (UPC) are expressed in various tissues but have similar roles.",True,Uncouplers,,,,
d4f2799a-785b-410f-bb83-5b42424fabf6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,UPC,False,UPC,,,,
6e79f855-1d4f-43b7-b765-c22327f07bce,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,nonshivering,False,nonshivering,,,,
b27b16c7-e6ac-48a2-89dc-fdbb56dd0cca,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.3 References and resources,True,nonshivering,,,,
5ed5bff6-625c-4b4c-bd1d-2675c50e2684,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Text,False,Text,,,,
68f8ada2-5d56-4c62-84ff-cda9b8932ce0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
68f8ada2-5d56-4c62-84ff-cda9b8932ce0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
68f8ada2-5d56-4c62-84ff-cda9b8932ce0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
68f8ada2-5d56-4c62-84ff-cda9b8932ce0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
68f8ada2-5d56-4c62-84ff-cda9b8932ce0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
68f8ada2-5d56-4c62-84ff-cda9b8932ce0,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
fff50bcb-9f29-4e60-bbc8-63abfe176dd1,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.4 Fatty Acid Synthesis,True,Text,,,,
3c268176-57c1-48d4-abab-3e6a1512782a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
3c268176-57c1-48d4-abab-3e6a1512782a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
3c268176-57c1-48d4-abab-3e6a1512782a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
3c268176-57c1-48d4-abab-3e6a1512782a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
3c268176-57c1-48d4-abab-3e6a1512782a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
3c268176-57c1-48d4-abab-3e6a1512782a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
74cbc9a5-80e5-488e-86f1-4c432a757d42,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The NADPH generated through this process is necessary for fatty acid synthesis. This is one of the primary pathways that produces NADPH, and the other is the oxidative portion of the pentose pathway.",True,Text,,,,
8282f46e-4809-40b0-8225-e8292d7f6a3f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The process of fatty acid synthesis starts with the carboxylation of acetyl-CoA to form malonyl-CoA (figures 4.16 and 4.17). The enzyme involved, acetyl-CoA carboxylase, is the regulatory enzyme for this pathway and requires biotin as a cofactor. After the initial priming of fatty acid synthase with acetyl-CoA, all other carbon units are added to the elongating fatty acid chain in the form of malonyl-CoA. You will see later that this intermediate is also a key inhibitor of β-oxidation.",True,Text,,,,
b79b5abc-bac4-4aa5-8820-720d84ff3070,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
b79b5abc-bac4-4aa5-8820-720d84ff3070,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
b79b5abc-bac4-4aa5-8820-720d84ff3070,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
b79b5abc-bac4-4aa5-8820-720d84ff3070,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
b79b5abc-bac4-4aa5-8820-720d84ff3070,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
b79b5abc-bac4-4aa5-8820-720d84ff3070,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
799d18ca-f89d-4de6-a292-e706eb5cccaf,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,TAGs,False,TAGs,,,,
9100a891-fc16-4b75-88e5-9c46b3dd7048,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,VLDLs,False,VLDLs,,,,
232830e4-ad12-4321-81e2-fca4f2c00f1a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of fatty acid synthesis,False,Regulation of fatty acid synthesis,,,,
43fe0295-aed1-4fe6-89ee-a16bbc1f3d1f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
43fe0295-aed1-4fe6-89ee-a16bbc1f3d1f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
43fe0295-aed1-4fe6-89ee-a16bbc1f3d1f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
43fe0295-aed1-4fe6-89ee-a16bbc1f3d1f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
43fe0295-aed1-4fe6-89ee-a16bbc1f3d1f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
43fe0295-aed1-4fe6-89ee-a16bbc1f3d1f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
d1452a7c-9929-4bcb-870f-944fe08d879a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Table 4.3: Summary of pathway regulation.,True,Regulation of fatty acid synthesis,,,,
f1bf1515-3169-40b1-b13e-88a80b9d660f,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.4 References and resources,True,Regulation of fatty acid synthesis,,,,
c6bdea62-251b-4194-b423-ab2db9107941,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
c6bdea62-251b-4194-b423-ab2db9107941,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
c6bdea62-251b-4194-b423-ab2db9107941,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
c6bdea62-251b-4194-b423-ab2db9107941,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
c6bdea62-251b-4194-b423-ab2db9107941,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
c6bdea62-251b-4194-b423-ab2db9107941,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
3a292566-2a45-4906-a154-6bd654f27e51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3a292566-2a45-4906-a154-6bd654f27e51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3a292566-2a45-4906-a154-6bd654f27e51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3a292566-2a45-4906-a154-6bd654f27e51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3a292566-2a45-4906-a154-6bd654f27e51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3a292566-2a45-4906-a154-6bd654f27e51,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
f33c56cc-eaad-4322-bbcf-fb6c98aeeb21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
f33c56cc-eaad-4322-bbcf-fb6c98aeeb21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
f33c56cc-eaad-4322-bbcf-fb6c98aeeb21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
f33c56cc-eaad-4322-bbcf-fb6c98aeeb21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
f33c56cc-eaad-4322-bbcf-fb6c98aeeb21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
f33c56cc-eaad-4322-bbcf-fb6c98aeeb21,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
fd3d84a6-e738-4e78-bcaa-f15615f8ff24,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.5 Glycogen Synthesis,True,Regulation of fatty acid synthesis,,,,
a1f5eef7-fccc-4435-bb31-3c0ef75801f6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glycogen synthesis is the process of storing glucose and occurs primarily in the liver and the skeletal muscle. The metabolic pathways in these tissues are similar, but the utility of glycogen stores is different. Briefly, liver glycogen is catabolized primarily in response to elevated glucagon, and the glucose 6-phosphate generated is dephosphorylated and released into circulation. In contrast, muscle glycogen is only used by the muscle itself; muscle lacks glucose 6-phosphatase and glucose 6-phosphate released from muscle glycogen is oxidized in glycolysis. Although discussed here as a point of comparison, glycogenolysis is a fasted state pathway and occurs in response to glucagon and epinephrine. This will be discussed in section 5.1.",True,Regulation of fatty acid synthesis,,,,
842aa450-249a-4d0d-9c9a-98d1db6162b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
842aa450-249a-4d0d-9c9a-98d1db6162b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
842aa450-249a-4d0d-9c9a-98d1db6162b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
842aa450-249a-4d0d-9c9a-98d1db6162b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
842aa450-249a-4d0d-9c9a-98d1db6162b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
842aa450-249a-4d0d-9c9a-98d1db6162b6,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
7078d70a-ee8c-4778-8660-b7417688fabf,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,pyrophosphorylase,False,pyrophosphorylase,,,,
d29b41db-8c7d-47a8-b472-8214e5106209,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,glycogenin,False,glycogenin,,,,
830be2fc-177b-45b2-8960-6f19484df60a,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Regulation of glycogen synthesis,False,Regulation of glycogen synthesis,,,,
0f928982-ed4c-4024-9d70-ea31a157d3e4,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Glycogen synthesis is regulated by a single enzyme, glycogen synthase. This enzyme is primarily regulated through covalent modification. It is active when dephosphorylated and inactive when phosphorylated. The phosphorylation/dephosphorylation is facilitated by glucagon and insulin levels, respectively (table 4.4).",True,Regulation of glycogen synthesis,,,,
f85814e1-eed6-463d-bb2d-81c511c90aeb,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,Table 4.4: Summary of pathway regulation.,True,Regulation of glycogen synthesis,,,,
43d83f57-19b9-4b21-8383-49de0c2d7a41,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,4.5 References and resources,True,Regulation of glycogen synthesis,,,,
44c9aeaf-642f-406e-a5a1-5ddc866acf7c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
44c9aeaf-642f-406e-a5a1-5ddc866acf7c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
44c9aeaf-642f-406e-a5a1-5ddc866acf7c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
44c9aeaf-642f-406e-a5a1-5ddc866acf7c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
44c9aeaf-642f-406e-a5a1-5ddc866acf7c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
44c9aeaf-642f-406e-a5a1-5ddc866acf7c,https://pressbooks.lib.vt.edu/cellbio/,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-4,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
9ffa6fb5-d911-40d5-9b3b-12ddef993841,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),False,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),,,,
1ae30827-c26f-419b-8d50-45adc1175921,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Fatty acid synthesis,False,Fatty acid synthesis,,,,
0e091a2d-922b-4dc6-bbdb-cb853cbd79c2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycogen synthesis,False,Glycogen synthesis,,,,
201a2e97-3ee3-42b7-94df-e2811cfcc7b9,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,reoxidize,False,reoxidize,,,,
39a45395-7fae-4c0e-a62a-02ee205c454f,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of glycolysis,False,Regulation of glycolysis,,,,
80767b43-a60c-4641-8d77-e472be1ae239,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
80767b43-a60c-4641-8d77-e472be1ae239,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
80767b43-a60c-4641-8d77-e472be1ae239,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
80767b43-a60c-4641-8d77-e472be1ae239,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
80767b43-a60c-4641-8d77-e472be1ae239,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
80767b43-a60c-4641-8d77-e472be1ae239,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
b93014c2-f4dc-483b-b6a5-abe5a5fbf6bd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glucokinase: Glucose to glucose 6-phosphate,False,Glucokinase: Glucose to glucose 6-phosphate,,,,
bfe52ddf-3b85-4539-b199-9091c5cddc75,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bfe52ddf-3b85-4539-b199-9091c5cddc75,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bfe52ddf-3b85-4539-b199-9091c5cddc75,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bfe52ddf-3b85-4539-b199-9091c5cddc75,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bfe52ddf-3b85-4539-b199-9091c5cddc75,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bfe52ddf-3b85-4539-b199-9091c5cddc75,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
b78def2e-8a68-4725-83b3-548d872b5eef,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,GLUT2,False,GLUT2,,,,
cee77649-94f1-4807-9787-7eb20edebfa2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In skeletal muscle, and most other peripheral tissues, glucose is phosphorylated by hexokinase.",True,GLUT2,,,,
0495f9c5-37b1-4558-a801-c2302c6b0e58,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
0495f9c5-37b1-4558-a801-c2302c6b0e58,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
0495f9c5-37b1-4558-a801-c2302c6b0e58,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
0495f9c5-37b1-4558-a801-c2302c6b0e58,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
0495f9c5-37b1-4558-a801-c2302c6b0e58,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
0495f9c5-37b1-4558-a801-c2302c6b0e58,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
ed3a73da-bb9e-4ccc-aab6-42c91ed346f5,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of glucokinase and hexokinase,False,Regulation of glucokinase and hexokinase,,,,
b2c958a8-e99c-4ff9-8f74-3eca0fe87905,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
b2c958a8-e99c-4ff9-8f74-3eca0fe87905,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
b2c958a8-e99c-4ff9-8f74-3eca0fe87905,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
b2c958a8-e99c-4ff9-8f74-3eca0fe87905,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
b2c958a8-e99c-4ff9-8f74-3eca0fe87905,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
b2c958a8-e99c-4ff9-8f74-3eca0fe87905,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c20ad998-8cd3-49fd-a8a0-56380ea02faf,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,GKRP,False,GKRP,,,,
314c5ca7-6433-4c29-8d31-5263fb9eaf6b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",False,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
199581a3-f5a2-476b-9f10-b2f384bcd90d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Following glucose phosphorylation to glucose 6-phosphate, the glucose 6-phosphate can be used for glycogen synthesis or the pentose phosphate pathway. Substrate that continues through glycolysis is isomerized to fructose 6-phosphate, which is the substrate for the reaction catalyzed by phosphofructokinase 1 (PFK1).",True,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
0dab74af-e595-4fe9-ba95-950e4a58690b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,PFK1,False,PFK1,,,,
87a8a477-c658-46f5-b212-5987f1f5e60a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of phosphofructokinase 1 (PFK1),False,Regulation of phosphofructokinase 1 (PFK1),,,,
dbaaba0c-a70e-4b25-b800-045baf6b8b1a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Regulation of phosphofructokinase 1 is primarily through allosteric activation by AMP and fructose 2,6-bisphosphate. High AMP levels would indicate a lack of energy within the cell, and this would increase flux through glycolysis by enhancing the activity of PFK1. PFK1 is also inhibited by citrate and ATP; levels of these compounds are indicative of a high energy state, suggesting there are sufficient oxidation productions and glucose is diverted to storage pathways.",True,Regulation of phosphofructokinase 1 (PFK1),,,,
05ab8544-b146-466c-a729-722428f32f5d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
05ab8544-b146-466c-a729-722428f32f5d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
05ab8544-b146-466c-a729-722428f32f5d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
05ab8544-b146-466c-a729-722428f32f5d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
05ab8544-b146-466c-a729-722428f32f5d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
05ab8544-b146-466c-a729-722428f32f5d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
d7ab1123-a84f-482a-a72c-1b05ced4cdaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,PFK2,False,PFK2,,,,
8c33cf62-63b1-405d-a5df-98c0d45772a8,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,FBP2,False,FBP2,,,,
33816f03-457f-4190-a5df-59f57141e5a7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,False,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
74909211-f066-4e85-b099-7abcccc949ad,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Following the synthesis of fructose 1,6-phosphate, aldolase will cleave this substrate into dihydroxyacetone and glyceraldehyde 3-phosphate. These three carbon compounds will be used to synthesize pyruvate in the final regulatory step of the pathway catalyzed by pyruvate kinase (PK).",True,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
30113bf4-3b1a-4649-a12f-2789a6e0249b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of pyruvate kinase (PK),False,Regulation of pyruvate kinase (PK),,,,
80241fd2-239f-4d04-bd94-1d1c86e8240b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
80241fd2-239f-4d04-bd94-1d1c86e8240b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
80241fd2-239f-4d04-bd94-1d1c86e8240b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
80241fd2-239f-4d04-bd94-1d1c86e8240b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
80241fd2-239f-4d04-bd94-1d1c86e8240b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
80241fd2-239f-4d04-bd94-1d1c86e8240b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
281e5391-d58f-47d1-941a-fd3fc0b1227b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,phosphoenol,False,phosphoenol,,,,
5f2f3b92-a774-4e82-b6c3-ee12d3ba6bb0,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Movement of NADH from the cytosol to the mitochondria,False,Movement of NADH from the cytosol to the mitochondria,,,,
e698fa10-2445-42ad-afd6-1a3c778c4c62,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The NADH generated in the cytosol by glycolysis must be oxidized back to NAD+ in order to maintain a pool of NAD+ needed for glucose oxidation. As NADH oxidation takes place in the mitochondria, and the membrane is not permeable to NADH, two shuttles are used to move cytosolic NADH into the mitochondria. These processes are a way to get energy out of cytoplasmic NADH into the mitochondria.",True,Movement of NADH from the cytosol to the mitochondria,,,,
151e796d-7cc2-41e7-aeea-5a3a08b245f2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Glycerol 3-phosphate shuttle,False,Glycerol 3-phosphate shuttle,,,,
2b2467ef-1994-41f4-9607-a325d3a14b13,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2b2467ef-1994-41f4-9607-a325d3a14b13,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2b2467ef-1994-41f4-9607-a325d3a14b13,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2b2467ef-1994-41f4-9607-a325d3a14b13,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2b2467ef-1994-41f4-9607-a325d3a14b13,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
2b2467ef-1994-41f4-9607-a325d3a14b13,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
6f56c3fd-558f-417d-8cbc-0b6ddc4d69f5,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,dihydroxyacetonephosphate,False,dihydroxyacetonephosphate,,,,
db383925-ffd0-41d0-ba83-0ab50961c4b7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Malate-aspartate shuttle,False,Malate-aspartate shuttle,,,,
2f65ea12-983c-44fa-871a-62e5d3323dd2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
2f65ea12-983c-44fa-871a-62e5d3323dd2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
2f65ea12-983c-44fa-871a-62e5d3323dd2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
2f65ea12-983c-44fa-871a-62e5d3323dd2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
2f65ea12-983c-44fa-871a-62e5d3323dd2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
2f65ea12-983c-44fa-871a-62e5d3323dd2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
8e2db2af-7270-4f4d-a1d3-ff6deac77eeb,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,OAA,False,OAA,,,,
41dd6ac6-1413-438a-b34d-d63ad988a999,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,canʼt,False,canʼt,,,,
af39b3d4-378c-4357-b7bc-783f461c0320,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Pyruvate dehydrogenase complex,False,Pyruvate dehydrogenase complex,,,,
598f4340-a15a-4a68-9943-72943215aac4,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Under aerobic conditions, the pyruvate produced by glycolysis will be oxidized to acetyl-CoA using the pyruvate dehydrogenase complex (PDC). This enzyme is a key transition point between cytosolic and mitochondrial metabolism. This complex is composed of three subunits, which require the cofactors thiamine pyrophosphate, lipoic acid, and FADH2; NADH is also required for the reaction to move forward. The enzyme is highly regulated by both covalent and allosteric regulation. Deficiencies of the PDC can be recessive or X-linked (depending on the subunit deficient) and present with symptoms of lactic acidosis after consuming a meal high in carbohydrates. This metabolic deficiency can be managed by delivering a ketogenic diet and bypassing glycolysis all together.",True,Pyruvate dehydrogenase complex,,,,
0f082eb7-cb57-475e-98e4-909ec5c0240b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,FADH,False,FADH,,,,
2a133666-a359-4494-94c8-6745852f2d92,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of the pyruvate dehydrogenase complex (PDC),False,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
479775a8-bebf-4ad9-98fc-244a4999330e,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The PDC is regulated by allosteric and covalent regulations. The complex itself can be allosterically activated by pyruvate and NAD+. Elevation of substrate (pyruvate) will enhance flux through this enzyme as will the indication of low energy states as triggered by high NAD+ levels. The PDC is also inhibited by acetyl-CoA and NADH directly. Product inhibition is a very common regulatory mechanism, and high NADH would signal sufficient energy levels, therefore decreasing activity of the PDC.",True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
d1c5b203-5782-4fc8-86ab-45f241a20b14,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,The PDC is also regulated through covalent modification. Phosphorylation of the complex will decrease activity of the enzyme.,True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
ca5db667-e6d7-4c2d-913d-889c762fda38,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ca5db667-e6d7-4c2d-913d-889c762fda38,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ca5db667-e6d7-4c2d-913d-889c762fda38,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ca5db667-e6d7-4c2d-913d-889c762fda38,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ca5db667-e6d7-4c2d-913d-889c762fda38,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ca5db667-e6d7-4c2d-913d-889c762fda38,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
deaa0324-3187-46b9-9756-27c950e30ef0,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Summary of pathway regulation,False,Summary of pathway regulation,,,,
42b5c472-c598-4345-891e-b291253139b5,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Table 4.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
66497449-a95a-47a1-bb3d-1e085d2bcdd7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.1 References and resources,True,Summary of pathway regulation,,,,
18bff842-6d01-478e-a221-0160a307eaa7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 6: Bioenergetics and Oxidative Phosphorylation: Section V, VI, Chapter 8: Introduction to Metabolism and Glycolysis, Chapter 9: TCA Cycle and Pyruvate Dehydrogenase Complex: Section IIA, IIB, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section II, IV, V, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
e24bf784-77e3-422f-a219-95625df93abb,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72–78, 85–89.",True,Summary of pathway regulation,,,,
fc6b1b68-fe0f-4b63-9932-3d7245fcfd08,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 19: Basic Concepts of Regulation: Section IV.A.1.2, Chapter 20: Cellular Bioenergetics, Chapter 22: Generation of ATP from Glucose: Section I.A.B.C, III, Chapter 24: Oxidative Phosphorylation and the ETC: Section I.E, II, III, Chapter 31: Synthesis of Fatty Acids: Section I.A.B, IV, V.",True,Summary of pathway regulation,,,,
305a21e8-84c7-4475-91e4-20f61795f5ae,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
305a21e8-84c7-4475-91e4-20f61795f5ae,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
305a21e8-84c7-4475-91e4-20f61795f5ae,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
305a21e8-84c7-4475-91e4-20f61795f5ae,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
305a21e8-84c7-4475-91e4-20f61795f5ae,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
305a21e8-84c7-4475-91e4-20f61795f5ae,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
05848508-3f1c-4833-8743-fe8af33a3a7d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
05848508-3f1c-4833-8743-fe8af33a3a7d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
05848508-3f1c-4833-8743-fe8af33a3a7d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
05848508-3f1c-4833-8743-fe8af33a3a7d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
05848508-3f1c-4833-8743-fe8af33a3a7d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
05848508-3f1c-4833-8743-fe8af33a3a7d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
b91415f0-e4c9-4d10-9081-d3b728d8aa73,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b91415f0-e4c9-4d10-9081-d3b728d8aa73,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b91415f0-e4c9-4d10-9081-d3b728d8aa73,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b91415f0-e4c9-4d10-9081-d3b728d8aa73,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b91415f0-e4c9-4d10-9081-d3b728d8aa73,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b91415f0-e4c9-4d10-9081-d3b728d8aa73,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
5df9dc70-e998-4981-81d9-84635fd48e19,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
5df9dc70-e998-4981-81d9-84635fd48e19,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
5df9dc70-e998-4981-81d9-84635fd48e19,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
5df9dc70-e998-4981-81d9-84635fd48e19,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
5df9dc70-e998-4981-81d9-84635fd48e19,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
5df9dc70-e998-4981-81d9-84635fd48e19,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba761803-c685-4ea8-9bc7-4855c4999552,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ba761803-c685-4ea8-9bc7-4855c4999552,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ba761803-c685-4ea8-9bc7-4855c4999552,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ba761803-c685-4ea8-9bc7-4855c4999552,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ba761803-c685-4ea8-9bc7-4855c4999552,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
ba761803-c685-4ea8-9bc7-4855c4999552,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
940e6b35-fa75-4c6d-86bc-7615a44745d3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
940e6b35-fa75-4c6d-86bc-7615a44745d3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
940e6b35-fa75-4c6d-86bc-7615a44745d3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
940e6b35-fa75-4c6d-86bc-7615a44745d3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
940e6b35-fa75-4c6d-86bc-7615a44745d3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
940e6b35-fa75-4c6d-86bc-7615a44745d3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
06c9273e-c4c1-4648-a0fe-0b8aba46a282,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
06c9273e-c4c1-4648-a0fe-0b8aba46a282,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
06c9273e-c4c1-4648-a0fe-0b8aba46a282,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
06c9273e-c4c1-4648-a0fe-0b8aba46a282,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
06c9273e-c4c1-4648-a0fe-0b8aba46a282,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
06c9273e-c4c1-4648-a0fe-0b8aba46a282,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
77a49542-180e-45a8-8a14-ff5cae75f349,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
77a49542-180e-45a8-8a14-ff5cae75f349,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
77a49542-180e-45a8-8a14-ff5cae75f349,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
77a49542-180e-45a8-8a14-ff5cae75f349,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
77a49542-180e-45a8-8a14-ff5cae75f349,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
77a49542-180e-45a8-8a14-ff5cae75f349,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
e462cc99-0718-41ec-8c8c-8db4d0d1619a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e462cc99-0718-41ec-8c8c-8db4d0d1619a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e462cc99-0718-41ec-8c8c-8db4d0d1619a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e462cc99-0718-41ec-8c8c-8db4d0d1619a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e462cc99-0718-41ec-8c8c-8db4d0d1619a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e462cc99-0718-41ec-8c8c-8db4d0d1619a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
b1a5e7dc-ff88-4f31-8eee-829ba71d9a38,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.2 Tricarboxylic Acid Cycle (TCA),True,Summary of pathway regulation,,,,
f6d15b1c-626d-4338-90d0-98536b79f334,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
f6d15b1c-626d-4338-90d0-98536b79f334,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
f6d15b1c-626d-4338-90d0-98536b79f334,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
f6d15b1c-626d-4338-90d0-98536b79f334,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
f6d15b1c-626d-4338-90d0-98536b79f334,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
f6d15b1c-626d-4338-90d0-98536b79f334,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
f8c6e440-6f49-4840-84b7-c3fed0c923d3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,FADH2,False,FADH2,,,,
a11bceed-f9da-4510-8c96-8cab6cfb94f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
a11bceed-f9da-4510-8c96-8cab6cfb94f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
a11bceed-f9da-4510-8c96-8cab6cfb94f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
a11bceed-f9da-4510-8c96-8cab6cfb94f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
a11bceed-f9da-4510-8c96-8cab6cfb94f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
a11bceed-f9da-4510-8c96-8cab6cfb94f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
d495ea98-a6f5-453e-8c10-09f742810c45,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
d495ea98-a6f5-453e-8c10-09f742810c45,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
d495ea98-a6f5-453e-8c10-09f742810c45,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
d495ea98-a6f5-453e-8c10-09f742810c45,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
d495ea98-a6f5-453e-8c10-09f742810c45,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
d495ea98-a6f5-453e-8c10-09f742810c45,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
2c8e949b-4dd1-469b-84fc-5377dbe90236,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of the TCA cycle,False,Regulation of the TCA cycle,,,,
6194e99e-872f-47c4-8259-2225fbf18a8d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Throughout the cycle, there are two key regulatory and irreversible steps to be aware of. The first is the conversion of isocitrate to α-ketoglutarate by isocitrate dehydrogenase, and the second is the conversion of α-ketoglutarate to succinyl-CoA by α-ketoglutarate dehydrogenase. The two key regulatory points are:",True,Regulation of the TCA cycle,,,,
e69ac666-db6e-4104-a1d9-a88cd8cff9f3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Isocitrate dehydrogenase, which can be activated by Ca2+ and ADP to increase flux through the cycle, and inhibited by NADH, which would suggest adequate energy in the cell.",True,Regulation of the TCA cycle,,,,
e69ffe5b-f8b6-44e6-a154-8b23990c5c9d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Ca2,False,Ca2,,,,
b624964c-9c23-49aa-b30b-dd8f70a761b1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
b624964c-9c23-49aa-b30b-dd8f70a761b1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
b624964c-9c23-49aa-b30b-dd8f70a761b1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
b624964c-9c23-49aa-b30b-dd8f70a761b1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
b624964c-9c23-49aa-b30b-dd8f70a761b1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
b624964c-9c23-49aa-b30b-dd8f70a761b1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9884d5c0-b0aa-4ee5-999e-676951d5dd9e,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Malate dehydrogenase can also be inhibited by NADH, however, the reaction is reversible depending on levels of NADH. The oxidation of malate to OAA requires NAD+, and under certain pathological situations the lack of free NAD+ within the mitochondria will reduce the rate of this reaction (this is common in the case of alcohol metabolism).",True,Ca2,,,,
86c38427-15d2-4d42-8eee-905d34c24c83,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Keep in mind that with the addition of each acetyl-CoA (comprised of 2 carbons) to the TCA cycle, two molecules of CO2 are released, thus there is no net gain or loss of carbons in the cycle. The process moves forward driven by energetics and substrate availability. The pathway can be active in both the fed and fasted states. In the fed state, acetyl-CoA is generated primarily through glucose oxidation. In contrast, in the fasted state acetyl-CoA is generated primarily from β-oxidation, and the majority of acetyl-CoA is used to synthesize ketones.",True,Ca2,,,,
6df18b1c-d82c-4d94-8a25-b401a4383e06,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Table 4.2: Summary of pathway regulation.,True,Ca2,,,,
83bf6edd-6b32-45cd-a0aa-f40383919cb5,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.2 References and resources,True,Ca2,,,,
383f08e0-66bd-41d4-b13d-2cd14dc350a3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
383f08e0-66bd-41d4-b13d-2cd14dc350a3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
383f08e0-66bd-41d4-b13d-2cd14dc350a3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
383f08e0-66bd-41d4-b13d-2cd14dc350a3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
383f08e0-66bd-41d4-b13d-2cd14dc350a3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
383f08e0-66bd-41d4-b13d-2cd14dc350a3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
6ba86e78-9b57-4da8-9258-ac06079adaaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6ba86e78-9b57-4da8-9258-ac06079adaaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6ba86e78-9b57-4da8-9258-ac06079adaaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6ba86e78-9b57-4da8-9258-ac06079adaaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6ba86e78-9b57-4da8-9258-ac06079adaaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
6ba86e78-9b57-4da8-9258-ac06079adaaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
8dff5382-2af3-4b41-92ef-6a862caecf99,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
8dff5382-2af3-4b41-92ef-6a862caecf99,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
8dff5382-2af3-4b41-92ef-6a862caecf99,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
8dff5382-2af3-4b41-92ef-6a862caecf99,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
8dff5382-2af3-4b41-92ef-6a862caecf99,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
8dff5382-2af3-4b41-92ef-6a862caecf99,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
ef421914-d7c6-4a3c-9c00-7b4a99ba5c67,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
ef421914-d7c6-4a3c-9c00-7b4a99ba5c67,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
ef421914-d7c6-4a3c-9c00-7b4a99ba5c67,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
ef421914-d7c6-4a3c-9c00-7b4a99ba5c67,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
ef421914-d7c6-4a3c-9c00-7b4a99ba5c67,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
ef421914-d7c6-4a3c-9c00-7b4a99ba5c67,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
2f997fda-39b4-45c4-b8dc-77409ada87a6,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.3 Electron Transport Chain (ETC),True,Ca2,,,,
c74b5c4f-0ad8-4240-b729-5b6030fce48d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In the production of NADH and FADH2 by the TCA cycle, β-oxidation or glycolysis is funneled directly into the electron transport chain (ETC) where each of these reduced coenzymes will donate two electrons to electron carriers. As the electrons are passed down their oxidation gradient, some of the energy is lost, but much of this energy is used to pump protons into the intermembrane space of the mitochondria.",True,Ca2,,,,
377c6384-1b28-4194-bf02-cba2c5d0d668,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
377c6384-1b28-4194-bf02-cba2c5d0d668,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
377c6384-1b28-4194-bf02-cba2c5d0d668,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
377c6384-1b28-4194-bf02-cba2c5d0d668,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
377c6384-1b28-4194-bf02-cba2c5d0d668,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
377c6384-1b28-4194-bf02-cba2c5d0d668,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
c377985d-fbe5-4f43-a52e-9ed6a7617ac1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"There are site specific inhibitors of the ETC to be aware of, and these will disrupt electron flow reducing overall ATP production.",True,Ca2,,,,
0e3d45c0-d5fd-47f0-89fd-2df2783f54b4,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Inhibitors,False,Inhibitors,,,,
40b375ef-1ca2-4417-9028-61e79a659398,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Inhibitors block oxidation and reduce both ATP generation and oxygen consumption; this is in contrast to uncouplers, which disrupt the mitochondrial membrane and reduce ATP production but increase oxygen consumption.",True,Inhibitors,,,,
204058f9-6e1e-4c94-8f24-7d539e69a408,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,uncouplers,False,uncouplers,,,,
98bac7ff-43a8-4d64-aa7e-6fc75db7e072,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"A common inhibitor of the ETC is carbon monoxide; this will bind to Complex IV and therefore halt the passing of electrons. Without electrons passing through the complexes, the pumping of protons is diminished and ATP is not produced. Other common inhibitors are cyanide (Complex IV), rotenone (Complex I), antimycin C (Complex III), and oligomycin, which is a Complex V inhibitor.",True,uncouplers,,,,
d8fad589-51ac-4cf1-a9a9-58810f553986,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Uncouplers,False,Uncouplers,,,,
56117003-a22a-4a66-bd60-eac0f5ec9140,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Uncoupling of the ETC by the addition of agents such as dinitrophenol have different consequences. Uncouplers disrupt the permeability of the inner membrane (either physically or chemically) and dissipate the proton gradient.,True,Uncouplers,,,,
52461d96-dd43-4193-b21e-c9c36cca4b01,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"In these cases, the release of protons across the membrane is coupled with the release of heat, rather than harnessed in the form of a phosphate bond. NADH oxidation continues rapidly, oxygen consumption is increased, and ATP production decreases. Valinomycin is another common uncoupler.",True,Uncouplers,,,,
e7deeb6f-bc50-49cf-9448-f711ffb10604,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Biological uncoupling through the expression of uncoupling proteins (UPC) is also likely. These proteins form a physical pore within the mitochondrial membrane allowing the proton gradient to equilibrate. In brown fat, this nonshivering thermogenesis is a means of generating heat, and other members of this protein family (UPC) are expressed in various tissues but have similar roles.",True,Uncouplers,,,,
dbf18629-5d36-4166-b4ed-f4d35be0264e,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,UPC,False,UPC,,,,
ccb1bf72-164f-4eaa-a323-d322cd65cbe2,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,nonshivering,False,nonshivering,,,,
bcb5dc61-b449-495e-9d72-7db50ad848b5,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.3 References and resources,True,nonshivering,,,,
22e170d3-deaf-4ec6-903c-86ed8e6b499a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Text,False,Text,,,,
0ac213d8-cf49-4dc4-acd8-5d1a238cb031,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
0ac213d8-cf49-4dc4-acd8-5d1a238cb031,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
0ac213d8-cf49-4dc4-acd8-5d1a238cb031,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
0ac213d8-cf49-4dc4-acd8-5d1a238cb031,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
0ac213d8-cf49-4dc4-acd8-5d1a238cb031,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
0ac213d8-cf49-4dc4-acd8-5d1a238cb031,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
3cce137e-63e6-4758-9796-19615287ba98,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.4 Fatty Acid Synthesis,True,Text,,,,
2a4fef31-3e76-432e-8977-e3e4f132108a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
2a4fef31-3e76-432e-8977-e3e4f132108a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
2a4fef31-3e76-432e-8977-e3e4f132108a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
2a4fef31-3e76-432e-8977-e3e4f132108a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
2a4fef31-3e76-432e-8977-e3e4f132108a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
2a4fef31-3e76-432e-8977-e3e4f132108a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
7f3be860-48bb-42ca-b69e-0aadcf04ce97,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The NADPH generated through this process is necessary for fatty acid synthesis. This is one of the primary pathways that produces NADPH, and the other is the oxidative portion of the pentose pathway.",True,Text,,,,
74ec03b8-e7dc-4fef-91b6-e6f1cb7007d8,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The process of fatty acid synthesis starts with the carboxylation of acetyl-CoA to form malonyl-CoA (figures 4.16 and 4.17). The enzyme involved, acetyl-CoA carboxylase, is the regulatory enzyme for this pathway and requires biotin as a cofactor. After the initial priming of fatty acid synthase with acetyl-CoA, all other carbon units are added to the elongating fatty acid chain in the form of malonyl-CoA. You will see later that this intermediate is also a key inhibitor of β-oxidation.",True,Text,,,,
d6d98e94-cbf0-45ed-9341-19f1819462f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
d6d98e94-cbf0-45ed-9341-19f1819462f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
d6d98e94-cbf0-45ed-9341-19f1819462f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
d6d98e94-cbf0-45ed-9341-19f1819462f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
d6d98e94-cbf0-45ed-9341-19f1819462f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
d6d98e94-cbf0-45ed-9341-19f1819462f7,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3cbb8525-8e54-44a4-8a32-fb5552e47110,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,TAGs,False,TAGs,,,,
0b24a45f-bae4-49b1-9691-e4a1a68e887a,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,VLDLs,False,VLDLs,,,,
71285511-1eda-489d-87a2-f1efb7d9b93e,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of fatty acid synthesis,False,Regulation of fatty acid synthesis,,,,
80a965a5-b35b-445c-a9a3-d502faa899aa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
80a965a5-b35b-445c-a9a3-d502faa899aa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
80a965a5-b35b-445c-a9a3-d502faa899aa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
80a965a5-b35b-445c-a9a3-d502faa899aa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
80a965a5-b35b-445c-a9a3-d502faa899aa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
80a965a5-b35b-445c-a9a3-d502faa899aa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
17b5c657-621b-4d33-9f9b-fc6f5c1d4a3b,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Table 4.3: Summary of pathway regulation.,True,Regulation of fatty acid synthesis,,,,
77b2eee5-2fec-43d1-90a5-3efea1873d06,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.4 References and resources,True,Regulation of fatty acid synthesis,,,,
89d609a2-c530-4b93-948e-9b677cf392c1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
89d609a2-c530-4b93-948e-9b677cf392c1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
89d609a2-c530-4b93-948e-9b677cf392c1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
89d609a2-c530-4b93-948e-9b677cf392c1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
89d609a2-c530-4b93-948e-9b677cf392c1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
89d609a2-c530-4b93-948e-9b677cf392c1,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
fb5a5bfe-798b-434d-9fe9-6920ddef58bd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
fb5a5bfe-798b-434d-9fe9-6920ddef58bd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
fb5a5bfe-798b-434d-9fe9-6920ddef58bd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
fb5a5bfe-798b-434d-9fe9-6920ddef58bd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
fb5a5bfe-798b-434d-9fe9-6920ddef58bd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
fb5a5bfe-798b-434d-9fe9-6920ddef58bd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
4c7ac5ef-524d-495f-90f3-43648f5b1cdd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
4c7ac5ef-524d-495f-90f3-43648f5b1cdd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
4c7ac5ef-524d-495f-90f3-43648f5b1cdd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
4c7ac5ef-524d-495f-90f3-43648f5b1cdd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
4c7ac5ef-524d-495f-90f3-43648f5b1cdd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
4c7ac5ef-524d-495f-90f3-43648f5b1cdd,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
13cd5171-17e4-423b-851a-1d268a60f717,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.5 Glycogen Synthesis,True,Regulation of fatty acid synthesis,,,,
012ff9d2-aaac-4682-a697-49d3aabf6a42,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glycogen synthesis is the process of storing glucose and occurs primarily in the liver and the skeletal muscle. The metabolic pathways in these tissues are similar, but the utility of glycogen stores is different. Briefly, liver glycogen is catabolized primarily in response to elevated glucagon, and the glucose 6-phosphate generated is dephosphorylated and released into circulation. In contrast, muscle glycogen is only used by the muscle itself; muscle lacks glucose 6-phosphatase and glucose 6-phosphate released from muscle glycogen is oxidized in glycolysis. Although discussed here as a point of comparison, glycogenolysis is a fasted state pathway and occurs in response to glucagon and epinephrine. This will be discussed in section 5.1.",True,Regulation of fatty acid synthesis,,,,
d098e43a-cd04-455e-8aa4-c788a3346469,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d098e43a-cd04-455e-8aa4-c788a3346469,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d098e43a-cd04-455e-8aa4-c788a3346469,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d098e43a-cd04-455e-8aa4-c788a3346469,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d098e43a-cd04-455e-8aa4-c788a3346469,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d098e43a-cd04-455e-8aa4-c788a3346469,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
79caa4d3-f0db-4c7d-a751-0c3f15128694,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,pyrophosphorylase,False,pyrophosphorylase,,,,
e038f0a6-d8bb-4c60-ae85-835c2f69e84d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,glycogenin,False,glycogenin,,,,
45820d9a-fb92-4321-af95-6c54497eecdc,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Regulation of glycogen synthesis,False,Regulation of glycogen synthesis,,,,
26350eb1-bbb4-4ebf-94a3-338855ff9eaa,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Glycogen synthesis is regulated by a single enzyme, glycogen synthase. This enzyme is primarily regulated through covalent modification. It is active when dephosphorylated and inactive when phosphorylated. The phosphorylation/dephosphorylation is facilitated by glucagon and insulin levels, respectively (table 4.4).",True,Regulation of glycogen synthesis,,,,
8ce36cdd-325f-4651-a0b0-9b08634ff4c4,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,Table 4.4: Summary of pathway regulation.,True,Regulation of glycogen synthesis,,,,
bd26b47a-feaf-4cd4-84bc-ea8ff98187c3,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,4.5 References and resources,True,Regulation of glycogen synthesis,,,,
d978fd0f-c79f-46ac-933b-cc771520869d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d978fd0f-c79f-46ac-933b-cc771520869d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d978fd0f-c79f-46ac-933b-cc771520869d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d978fd0f-c79f-46ac-933b-cc771520869d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d978fd0f-c79f-46ac-933b-cc771520869d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d978fd0f-c79f-46ac-933b-cc771520869d,https://pressbooks.lib.vt.edu/cellbio/,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-3,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
e8a04b7a-41e6-443d-a5d8-ad7c512794d4,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),False,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),,,,
3899f776-44a8-4ca0-ad32-b69d29b65757,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Fatty acid synthesis,False,Fatty acid synthesis,,,,
888cdc06-8064-4b49-9f48-51bed2e2bbab,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycogen synthesis,False,Glycogen synthesis,,,,
984f4589-e026-412d-a4f0-5a9a109339c6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,reoxidize,False,reoxidize,,,,
f102d77e-83be-4be5-b783-fa2e93513f27,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of glycolysis,False,Regulation of glycolysis,,,,
d3175730-7e4e-4bc4-9bdd-e4f8d0f5d756,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d3175730-7e4e-4bc4-9bdd-e4f8d0f5d756,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d3175730-7e4e-4bc4-9bdd-e4f8d0f5d756,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d3175730-7e4e-4bc4-9bdd-e4f8d0f5d756,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d3175730-7e4e-4bc4-9bdd-e4f8d0f5d756,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d3175730-7e4e-4bc4-9bdd-e4f8d0f5d756,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d7c4f98c-fb87-43ba-a1b4-11e0ad00fef8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glucokinase: Glucose to glucose 6-phosphate,False,Glucokinase: Glucose to glucose 6-phosphate,,,,
d9b819b0-70cb-4a3d-a281-1c2bb5049ee8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
d9b819b0-70cb-4a3d-a281-1c2bb5049ee8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
d9b819b0-70cb-4a3d-a281-1c2bb5049ee8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
d9b819b0-70cb-4a3d-a281-1c2bb5049ee8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
d9b819b0-70cb-4a3d-a281-1c2bb5049ee8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
d9b819b0-70cb-4a3d-a281-1c2bb5049ee8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
93669599-8c3b-44c8-81dc-d5a4615679d6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,GLUT2,False,GLUT2,,,,
394752c8-6ab3-4187-a4e7-36d2fabeb42a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In skeletal muscle, and most other peripheral tissues, glucose is phosphorylated by hexokinase.",True,GLUT2,,,,
985d90de-3544-49f3-92b5-9bbeac59bf48,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
985d90de-3544-49f3-92b5-9bbeac59bf48,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
985d90de-3544-49f3-92b5-9bbeac59bf48,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
985d90de-3544-49f3-92b5-9bbeac59bf48,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
985d90de-3544-49f3-92b5-9bbeac59bf48,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
985d90de-3544-49f3-92b5-9bbeac59bf48,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
0f84dea3-59ec-4b53-8de2-2edf74f29b7d,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of glucokinase and hexokinase,False,Regulation of glucokinase and hexokinase,,,,
c6a8afc9-c2f0-4893-853e-10f856db1011,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c6a8afc9-c2f0-4893-853e-10f856db1011,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c6a8afc9-c2f0-4893-853e-10f856db1011,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c6a8afc9-c2f0-4893-853e-10f856db1011,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c6a8afc9-c2f0-4893-853e-10f856db1011,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c6a8afc9-c2f0-4893-853e-10f856db1011,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c45da5fc-2090-4cf8-9b43-57e3726632bd,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,GKRP,False,GKRP,,,,
6b3b95eb-a559-4e66-b377-ed7b3e4cb9e9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",False,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
556e1d48-04d9-4109-9a18-01fb85daa9a9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Following glucose phosphorylation to glucose 6-phosphate, the glucose 6-phosphate can be used for glycogen synthesis or the pentose phosphate pathway. Substrate that continues through glycolysis is isomerized to fructose 6-phosphate, which is the substrate for the reaction catalyzed by phosphofructokinase 1 (PFK1).",True,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
c0693edf-77de-443f-8f72-4f22917541cc,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,PFK1,False,PFK1,,,,
a74d7251-be19-445d-a9c2-948f40646426,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of phosphofructokinase 1 (PFK1),False,Regulation of phosphofructokinase 1 (PFK1),,,,
a0311908-f37d-49fb-9d90-c91f4f1bc539,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Regulation of phosphofructokinase 1 is primarily through allosteric activation by AMP and fructose 2,6-bisphosphate. High AMP levels would indicate a lack of energy within the cell, and this would increase flux through glycolysis by enhancing the activity of PFK1. PFK1 is also inhibited by citrate and ATP; levels of these compounds are indicative of a high energy state, suggesting there are sufficient oxidation productions and glucose is diverted to storage pathways.",True,Regulation of phosphofructokinase 1 (PFK1),,,,
b4282d1f-35cf-433d-a37e-68f1b2a8f3d3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b4282d1f-35cf-433d-a37e-68f1b2a8f3d3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b4282d1f-35cf-433d-a37e-68f1b2a8f3d3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b4282d1f-35cf-433d-a37e-68f1b2a8f3d3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b4282d1f-35cf-433d-a37e-68f1b2a8f3d3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b4282d1f-35cf-433d-a37e-68f1b2a8f3d3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
1ed85b00-92e5-4ade-ac7b-442f4c4bde3b,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,PFK2,False,PFK2,,,,
796146d8-0f7c-44a2-9558-54c6ae862aae,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,FBP2,False,FBP2,,,,
26353a29-1704-41d1-bd5f-71e9621fda1e,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,False,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
6e4d4ed2-eaa5-4c80-b166-91815b3052a6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Following the synthesis of fructose 1,6-phosphate, aldolase will cleave this substrate into dihydroxyacetone and glyceraldehyde 3-phosphate. These three carbon compounds will be used to synthesize pyruvate in the final regulatory step of the pathway catalyzed by pyruvate kinase (PK).",True,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
d51ecebf-96f5-4e51-8092-985ec14c6dbc,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of pyruvate kinase (PK),False,Regulation of pyruvate kinase (PK),,,,
c9fde2b5-f005-4cb0-8d2f-80a251f6d43a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
c9fde2b5-f005-4cb0-8d2f-80a251f6d43a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
c9fde2b5-f005-4cb0-8d2f-80a251f6d43a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
c9fde2b5-f005-4cb0-8d2f-80a251f6d43a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
c9fde2b5-f005-4cb0-8d2f-80a251f6d43a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
c9fde2b5-f005-4cb0-8d2f-80a251f6d43a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9817ead2-9d21-4724-8b7a-ca1913a2fa47,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,phosphoenol,False,phosphoenol,,,,
f82c6d2f-f45d-4e2a-a697-46e4079ba681,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Movement of NADH from the cytosol to the mitochondria,False,Movement of NADH from the cytosol to the mitochondria,,,,
f2db44a5-f173-4536-8b63-db6cdcd0768c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The NADH generated in the cytosol by glycolysis must be oxidized back to NAD+ in order to maintain a pool of NAD+ needed for glucose oxidation. As NADH oxidation takes place in the mitochondria, and the membrane is not permeable to NADH, two shuttles are used to move cytosolic NADH into the mitochondria. These processes are a way to get energy out of cytoplasmic NADH into the mitochondria.",True,Movement of NADH from the cytosol to the mitochondria,,,,
2e9d60ea-ecd3-4431-84ad-ffd4b5584e35,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Glycerol 3-phosphate shuttle,False,Glycerol 3-phosphate shuttle,,,,
4f3345bb-17b0-41db-840d-c643ced2c9d8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
4f3345bb-17b0-41db-840d-c643ced2c9d8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
4f3345bb-17b0-41db-840d-c643ced2c9d8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
4f3345bb-17b0-41db-840d-c643ced2c9d8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
4f3345bb-17b0-41db-840d-c643ced2c9d8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
4f3345bb-17b0-41db-840d-c643ced2c9d8,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
3bcc960a-97a3-4a5e-8f0b-ccfd4568143f,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,dihydroxyacetonephosphate,False,dihydroxyacetonephosphate,,,,
dbbe95e4-6388-486e-aef8-002332fad377,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Malate-aspartate shuttle,False,Malate-aspartate shuttle,,,,
5a48915e-be75-4c68-9d89-d4aebd16640d,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
5a48915e-be75-4c68-9d89-d4aebd16640d,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
5a48915e-be75-4c68-9d89-d4aebd16640d,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
5a48915e-be75-4c68-9d89-d4aebd16640d,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
5a48915e-be75-4c68-9d89-d4aebd16640d,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
5a48915e-be75-4c68-9d89-d4aebd16640d,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
29216548-8a1c-4d05-b0d9-e68b562a4c3e,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,OAA,False,OAA,,,,
ee1d3976-eba3-40fc-a49b-6741c37b1b9a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,canʼt,False,canʼt,,,,
d7727677-93a7-43e1-b11f-eb4e930875cb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Pyruvate dehydrogenase complex,False,Pyruvate dehydrogenase complex,,,,
32bc1ea9-7696-4c01-9ad3-e626a6490670,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Under aerobic conditions, the pyruvate produced by glycolysis will be oxidized to acetyl-CoA using the pyruvate dehydrogenase complex (PDC). This enzyme is a key transition point between cytosolic and mitochondrial metabolism. This complex is composed of three subunits, which require the cofactors thiamine pyrophosphate, lipoic acid, and FADH2; NADH is also required for the reaction to move forward. The enzyme is highly regulated by both covalent and allosteric regulation. Deficiencies of the PDC can be recessive or X-linked (depending on the subunit deficient) and present with symptoms of lactic acidosis after consuming a meal high in carbohydrates. This metabolic deficiency can be managed by delivering a ketogenic diet and bypassing glycolysis all together.",True,Pyruvate dehydrogenase complex,,,,
8ef59ccc-efc8-420e-ab70-40a31585210c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,FADH,False,FADH,,,,
c64be056-bc54-4246-a016-f1a207e15c69,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of the pyruvate dehydrogenase complex (PDC),False,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
ee4745f1-fc41-48a7-9e57-eb3e092b2664,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The PDC is regulated by allosteric and covalent regulations. The complex itself can be allosterically activated by pyruvate and NAD+. Elevation of substrate (pyruvate) will enhance flux through this enzyme as will the indication of low energy states as triggered by high NAD+ levels. The PDC is also inhibited by acetyl-CoA and NADH directly. Product inhibition is a very common regulatory mechanism, and high NADH would signal sufficient energy levels, therefore decreasing activity of the PDC.",True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
d8b333c0-8a36-450d-a827-d63bfcfe5d32,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,The PDC is also regulated through covalent modification. Phosphorylation of the complex will decrease activity of the enzyme.,True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
ac2295de-32d2-420d-b20c-1a16260283ee,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ac2295de-32d2-420d-b20c-1a16260283ee,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ac2295de-32d2-420d-b20c-1a16260283ee,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ac2295de-32d2-420d-b20c-1a16260283ee,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ac2295de-32d2-420d-b20c-1a16260283ee,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
ac2295de-32d2-420d-b20c-1a16260283ee,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
6fd42679-2c51-4cf0-aafd-50064d697806,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Summary of pathway regulation,False,Summary of pathway regulation,,,,
63e09dd9-e239-409c-af72-d5939cb3fa36,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Table 4.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
8113bcd1-644e-441c-8c60-a9f5460e81ca,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.1 References and resources,True,Summary of pathway regulation,,,,
5fa8f4bc-bd06-4e70-9f68-6f21d85ffb33,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 6: Bioenergetics and Oxidative Phosphorylation: Section V, VI, Chapter 8: Introduction to Metabolism and Glycolysis, Chapter 9: TCA Cycle and Pyruvate Dehydrogenase Complex: Section IIA, IIB, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section II, IV, V, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
1c47011f-3b34-4c17-b641-1b29fda0bbac,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72–78, 85–89.",True,Summary of pathway regulation,,,,
a73366f4-5a13-4b79-b84a-d254ac9a08de,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 19: Basic Concepts of Regulation: Section IV.A.1.2, Chapter 20: Cellular Bioenergetics, Chapter 22: Generation of ATP from Glucose: Section I.A.B.C, III, Chapter 24: Oxidative Phosphorylation and the ETC: Section I.E, II, III, Chapter 31: Synthesis of Fatty Acids: Section I.A.B, IV, V.",True,Summary of pathway regulation,,,,
d375d356-cd7b-48b6-87b4-e6885a79e131,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d375d356-cd7b-48b6-87b4-e6885a79e131,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d375d356-cd7b-48b6-87b4-e6885a79e131,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d375d356-cd7b-48b6-87b4-e6885a79e131,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d375d356-cd7b-48b6-87b4-e6885a79e131,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
d375d356-cd7b-48b6-87b4-e6885a79e131,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
54428aea-5213-45a5-9094-e33952179194,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
54428aea-5213-45a5-9094-e33952179194,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
54428aea-5213-45a5-9094-e33952179194,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
54428aea-5213-45a5-9094-e33952179194,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
54428aea-5213-45a5-9094-e33952179194,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
54428aea-5213-45a5-9094-e33952179194,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
3b7abf18-457b-4a6a-8e32-5156513c61f9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
3b7abf18-457b-4a6a-8e32-5156513c61f9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
3b7abf18-457b-4a6a-8e32-5156513c61f9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
3b7abf18-457b-4a6a-8e32-5156513c61f9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
3b7abf18-457b-4a6a-8e32-5156513c61f9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
3b7abf18-457b-4a6a-8e32-5156513c61f9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
cd1c8a7a-7a26-4e1d-84bf-be0dc377eb94,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
cd1c8a7a-7a26-4e1d-84bf-be0dc377eb94,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
cd1c8a7a-7a26-4e1d-84bf-be0dc377eb94,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
cd1c8a7a-7a26-4e1d-84bf-be0dc377eb94,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
cd1c8a7a-7a26-4e1d-84bf-be0dc377eb94,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
cd1c8a7a-7a26-4e1d-84bf-be0dc377eb94,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
89044c95-bd1b-42fc-a93f-2588df01ca29,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
89044c95-bd1b-42fc-a93f-2588df01ca29,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
89044c95-bd1b-42fc-a93f-2588df01ca29,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
89044c95-bd1b-42fc-a93f-2588df01ca29,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
89044c95-bd1b-42fc-a93f-2588df01ca29,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
89044c95-bd1b-42fc-a93f-2588df01ca29,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
7abdc159-d5f3-4b32-9c00-8753171655e9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
7abdc159-d5f3-4b32-9c00-8753171655e9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
7abdc159-d5f3-4b32-9c00-8753171655e9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
7abdc159-d5f3-4b32-9c00-8753171655e9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
7abdc159-d5f3-4b32-9c00-8753171655e9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
7abdc159-d5f3-4b32-9c00-8753171655e9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
deb98a56-db59-4bd2-9857-c83ea79c7ea0,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
deb98a56-db59-4bd2-9857-c83ea79c7ea0,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
deb98a56-db59-4bd2-9857-c83ea79c7ea0,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
deb98a56-db59-4bd2-9857-c83ea79c7ea0,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
deb98a56-db59-4bd2-9857-c83ea79c7ea0,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
deb98a56-db59-4bd2-9857-c83ea79c7ea0,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
a9c49e68-7f53-4f58-8ad3-c113da8337f3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
a9c49e68-7f53-4f58-8ad3-c113da8337f3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
a9c49e68-7f53-4f58-8ad3-c113da8337f3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
a9c49e68-7f53-4f58-8ad3-c113da8337f3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
a9c49e68-7f53-4f58-8ad3-c113da8337f3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
a9c49e68-7f53-4f58-8ad3-c113da8337f3,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
8379aa1a-9b52-4539-98bb-6e69bbd448eb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
8379aa1a-9b52-4539-98bb-6e69bbd448eb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
8379aa1a-9b52-4539-98bb-6e69bbd448eb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
8379aa1a-9b52-4539-98bb-6e69bbd448eb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
8379aa1a-9b52-4539-98bb-6e69bbd448eb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
8379aa1a-9b52-4539-98bb-6e69bbd448eb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
fc2075a2-b6b7-4efb-b0cb-6896ebce0996,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.2 Tricarboxylic Acid Cycle (TCA),True,Summary of pathway regulation,,,,
320f2723-2f35-43e3-9b92-b6cf4f39822a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
320f2723-2f35-43e3-9b92-b6cf4f39822a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
320f2723-2f35-43e3-9b92-b6cf4f39822a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
320f2723-2f35-43e3-9b92-b6cf4f39822a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
320f2723-2f35-43e3-9b92-b6cf4f39822a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
320f2723-2f35-43e3-9b92-b6cf4f39822a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
a583f5b6-18da-4955-8888-99067d19ce30,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,FADH2,False,FADH2,,,,
e61cec12-dee2-47e6-be09-6f4726b83c79,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e61cec12-dee2-47e6-be09-6f4726b83c79,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e61cec12-dee2-47e6-be09-6f4726b83c79,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e61cec12-dee2-47e6-be09-6f4726b83c79,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e61cec12-dee2-47e6-be09-6f4726b83c79,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e61cec12-dee2-47e6-be09-6f4726b83c79,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
cdf502dd-83e6-4f54-a70f-0a44c2d10247,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
cdf502dd-83e6-4f54-a70f-0a44c2d10247,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
cdf502dd-83e6-4f54-a70f-0a44c2d10247,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
cdf502dd-83e6-4f54-a70f-0a44c2d10247,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
cdf502dd-83e6-4f54-a70f-0a44c2d10247,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
cdf502dd-83e6-4f54-a70f-0a44c2d10247,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
7b3da0e5-fe2f-46b4-bea6-2df280822cb5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of the TCA cycle,False,Regulation of the TCA cycle,,,,
3dd0fbda-098a-4e2a-a0f9-c5e991c9d608,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Throughout the cycle, there are two key regulatory and irreversible steps to be aware of. The first is the conversion of isocitrate to α-ketoglutarate by isocitrate dehydrogenase, and the second is the conversion of α-ketoglutarate to succinyl-CoA by α-ketoglutarate dehydrogenase. The two key regulatory points are:",True,Regulation of the TCA cycle,,,,
6025b182-83cb-4d2b-bda4-1d0dca18ea76,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Isocitrate dehydrogenase, which can be activated by Ca2+ and ADP to increase flux through the cycle, and inhibited by NADH, which would suggest adequate energy in the cell.",True,Regulation of the TCA cycle,,,,
1bce2d88-6a22-4cc8-b5fa-d733c7fe7c34,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Ca2,False,Ca2,,,,
6a2a379c-963b-4b25-9676-eb8880b03468,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
6a2a379c-963b-4b25-9676-eb8880b03468,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
6a2a379c-963b-4b25-9676-eb8880b03468,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
6a2a379c-963b-4b25-9676-eb8880b03468,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
6a2a379c-963b-4b25-9676-eb8880b03468,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
6a2a379c-963b-4b25-9676-eb8880b03468,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
28998e80-5bd8-4ef7-b43e-ce63a0ebf939,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Malate dehydrogenase can also be inhibited by NADH, however, the reaction is reversible depending on levels of NADH. The oxidation of malate to OAA requires NAD+, and under certain pathological situations the lack of free NAD+ within the mitochondria will reduce the rate of this reaction (this is common in the case of alcohol metabolism).",True,Ca2,,,,
09c37685-2574-4cfe-9583-207dd275c99e,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Keep in mind that with the addition of each acetyl-CoA (comprised of 2 carbons) to the TCA cycle, two molecules of CO2 are released, thus there is no net gain or loss of carbons in the cycle. The process moves forward driven by energetics and substrate availability. The pathway can be active in both the fed and fasted states. In the fed state, acetyl-CoA is generated primarily through glucose oxidation. In contrast, in the fasted state acetyl-CoA is generated primarily from β-oxidation, and the majority of acetyl-CoA is used to synthesize ketones.",True,Ca2,,,,
d4986493-1a95-4002-9a4d-0b50f6c0222e,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Table 4.2: Summary of pathway regulation.,True,Ca2,,,,
52b5c3ed-11a5-4c72-9693-7b0e48219ec9,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.2 References and resources,True,Ca2,,,,
06c66d35-182d-4399-9946-f7935228a093,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
06c66d35-182d-4399-9946-f7935228a093,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
06c66d35-182d-4399-9946-f7935228a093,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
06c66d35-182d-4399-9946-f7935228a093,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
06c66d35-182d-4399-9946-f7935228a093,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
06c66d35-182d-4399-9946-f7935228a093,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
e38bc5f0-8c79-460e-9203-fb46c2d898cb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e38bc5f0-8c79-460e-9203-fb46c2d898cb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e38bc5f0-8c79-460e-9203-fb46c2d898cb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e38bc5f0-8c79-460e-9203-fb46c2d898cb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e38bc5f0-8c79-460e-9203-fb46c2d898cb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e38bc5f0-8c79-460e-9203-fb46c2d898cb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
5b852882-293a-445c-be07-984d8d884ebd,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
5b852882-293a-445c-be07-984d8d884ebd,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
5b852882-293a-445c-be07-984d8d884ebd,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
5b852882-293a-445c-be07-984d8d884ebd,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
5b852882-293a-445c-be07-984d8d884ebd,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
5b852882-293a-445c-be07-984d8d884ebd,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
8940f69c-1ccd-4ea4-8506-d7c834880de1,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
8940f69c-1ccd-4ea4-8506-d7c834880de1,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
8940f69c-1ccd-4ea4-8506-d7c834880de1,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
8940f69c-1ccd-4ea4-8506-d7c834880de1,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
8940f69c-1ccd-4ea4-8506-d7c834880de1,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
8940f69c-1ccd-4ea4-8506-d7c834880de1,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
6fd17f29-556b-440b-b56f-2de906d93560,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.3 Electron Transport Chain (ETC),True,Ca2,,,,
09261729-c2d3-4b94-a9fe-360f52e8d312,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In the production of NADH and FADH2 by the TCA cycle, β-oxidation or glycolysis is funneled directly into the electron transport chain (ETC) where each of these reduced coenzymes will donate two electrons to electron carriers. As the electrons are passed down their oxidation gradient, some of the energy is lost, but much of this energy is used to pump protons into the intermembrane space of the mitochondria.",True,Ca2,,,,
baa36f51-332e-4386-b5a5-d056688cd34c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
baa36f51-332e-4386-b5a5-d056688cd34c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
baa36f51-332e-4386-b5a5-d056688cd34c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
baa36f51-332e-4386-b5a5-d056688cd34c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
baa36f51-332e-4386-b5a5-d056688cd34c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
baa36f51-332e-4386-b5a5-d056688cd34c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
f95b7430-4b8d-4e28-812b-b2282bf42711,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"There are site specific inhibitors of the ETC to be aware of, and these will disrupt electron flow reducing overall ATP production.",True,Ca2,,,,
f55e8fb4-8aae-4c7a-b38b-ee72b7f6a07c,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Inhibitors,False,Inhibitors,,,,
4b6f98aa-d0d4-439a-8cfe-93ae8508e144,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Inhibitors block oxidation and reduce both ATP generation and oxygen consumption; this is in contrast to uncouplers, which disrupt the mitochondrial membrane and reduce ATP production but increase oxygen consumption.",True,Inhibitors,,,,
1a7a534f-fdd3-45aa-a3b2-da2c2759c18b,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,uncouplers,False,uncouplers,,,,
835a2a6a-2ac1-49bf-adcf-b9ca80fe710a,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"A common inhibitor of the ETC is carbon monoxide; this will bind to Complex IV and therefore halt the passing of electrons. Without electrons passing through the complexes, the pumping of protons is diminished and ATP is not produced. Other common inhibitors are cyanide (Complex IV), rotenone (Complex I), antimycin C (Complex III), and oligomycin, which is a Complex V inhibitor.",True,uncouplers,,,,
06753c53-d067-42e0-a389-dbb670eab960,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Uncouplers,False,Uncouplers,,,,
15bb5f46-f41a-4d1c-b4b2-b75171f256a6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Uncoupling of the ETC by the addition of agents such as dinitrophenol have different consequences. Uncouplers disrupt the permeability of the inner membrane (either physically or chemically) and dissipate the proton gradient.,True,Uncouplers,,,,
961a47c5-535a-46c2-a97f-7a6fb3f81950,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"In these cases, the release of protons across the membrane is coupled with the release of heat, rather than harnessed in the form of a phosphate bond. NADH oxidation continues rapidly, oxygen consumption is increased, and ATP production decreases. Valinomycin is another common uncoupler.",True,Uncouplers,,,,
041e6a05-bb76-4294-9def-22928f5a1789,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Biological uncoupling through the expression of uncoupling proteins (UPC) is also likely. These proteins form a physical pore within the mitochondrial membrane allowing the proton gradient to equilibrate. In brown fat, this nonshivering thermogenesis is a means of generating heat, and other members of this protein family (UPC) are expressed in various tissues but have similar roles.",True,Uncouplers,,,,
01c4770f-fa67-43fe-8d5c-f2a5e064854f,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,UPC,False,UPC,,,,
feecbf49-3c71-4ea9-b046-d474922f6341,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,nonshivering,False,nonshivering,,,,
583b1925-5502-4614-b3aa-8d7ca38299a4,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.3 References and resources,True,nonshivering,,,,
7ce899c8-1718-44e1-82f8-458ddd515cfc,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Text,False,Text,,,,
4c1a7d8e-7ae8-4572-b7e3-64986c6b06a5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
4c1a7d8e-7ae8-4572-b7e3-64986c6b06a5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
4c1a7d8e-7ae8-4572-b7e3-64986c6b06a5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
4c1a7d8e-7ae8-4572-b7e3-64986c6b06a5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
4c1a7d8e-7ae8-4572-b7e3-64986c6b06a5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
4c1a7d8e-7ae8-4572-b7e3-64986c6b06a5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
fcb57815-7e68-4c5a-b75c-06ba4170dfe0,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.4 Fatty Acid Synthesis,True,Text,,,,
5d992709-0b4e-48a2-8a85-8e58871db6d6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
5d992709-0b4e-48a2-8a85-8e58871db6d6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
5d992709-0b4e-48a2-8a85-8e58871db6d6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
5d992709-0b4e-48a2-8a85-8e58871db6d6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
5d992709-0b4e-48a2-8a85-8e58871db6d6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
5d992709-0b4e-48a2-8a85-8e58871db6d6,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
df74f6c6-9641-45d9-a9bf-a9e05f873794,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The NADPH generated through this process is necessary for fatty acid synthesis. This is one of the primary pathways that produces NADPH, and the other is the oxidative portion of the pentose pathway.",True,Text,,,,
4db40c6f-827c-4822-93ca-9983ffe1d768,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The process of fatty acid synthesis starts with the carboxylation of acetyl-CoA to form malonyl-CoA (figures 4.16 and 4.17). The enzyme involved, acetyl-CoA carboxylase, is the regulatory enzyme for this pathway and requires biotin as a cofactor. After the initial priming of fatty acid synthase with acetyl-CoA, all other carbon units are added to the elongating fatty acid chain in the form of malonyl-CoA. You will see later that this intermediate is also a key inhibitor of β-oxidation.",True,Text,,,,
ece5907a-c899-43e7-b35d-118369c0e146,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
ece5907a-c899-43e7-b35d-118369c0e146,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
ece5907a-c899-43e7-b35d-118369c0e146,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
ece5907a-c899-43e7-b35d-118369c0e146,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
ece5907a-c899-43e7-b35d-118369c0e146,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
ece5907a-c899-43e7-b35d-118369c0e146,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
8eea4e9e-b4eb-41c9-998c-cd781e741c52,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,TAGs,False,TAGs,,,,
4bf47b8f-b222-416c-b4fb-8eb02057a405,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,VLDLs,False,VLDLs,,,,
dff62322-0b9a-4082-b16f-66e79e9da7d7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of fatty acid synthesis,False,Regulation of fatty acid synthesis,,,,
0f5b515a-223f-4e3e-8532-5bc5c07d8e90,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0f5b515a-223f-4e3e-8532-5bc5c07d8e90,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0f5b515a-223f-4e3e-8532-5bc5c07d8e90,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0f5b515a-223f-4e3e-8532-5bc5c07d8e90,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0f5b515a-223f-4e3e-8532-5bc5c07d8e90,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0f5b515a-223f-4e3e-8532-5bc5c07d8e90,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
a087697e-6ed9-4af5-a99d-1b5de5be383b,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Table 4.3: Summary of pathway regulation.,True,Regulation of fatty acid synthesis,,,,
fa1238d5-60d3-40c7-97cc-6229c427a308,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.4 References and resources,True,Regulation of fatty acid synthesis,,,,
b0e3eba7-3b66-4249-9311-bf36d81b5137,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b0e3eba7-3b66-4249-9311-bf36d81b5137,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b0e3eba7-3b66-4249-9311-bf36d81b5137,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b0e3eba7-3b66-4249-9311-bf36d81b5137,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b0e3eba7-3b66-4249-9311-bf36d81b5137,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b0e3eba7-3b66-4249-9311-bf36d81b5137,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
423d2a21-b4d0-435a-9279-18b0625e0c88,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
423d2a21-b4d0-435a-9279-18b0625e0c88,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
423d2a21-b4d0-435a-9279-18b0625e0c88,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
423d2a21-b4d0-435a-9279-18b0625e0c88,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
423d2a21-b4d0-435a-9279-18b0625e0c88,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
423d2a21-b4d0-435a-9279-18b0625e0c88,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
5f1546c5-370c-4690-8628-a82a5d4c40f7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
5f1546c5-370c-4690-8628-a82a5d4c40f7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
5f1546c5-370c-4690-8628-a82a5d4c40f7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
5f1546c5-370c-4690-8628-a82a5d4c40f7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
5f1546c5-370c-4690-8628-a82a5d4c40f7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
5f1546c5-370c-4690-8628-a82a5d4c40f7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
bd398da0-1986-4056-b844-3f4eea797415,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.5 Glycogen Synthesis,True,Regulation of fatty acid synthesis,,,,
222fae96-959e-4d76-9782-7e352f1fcd76,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glycogen synthesis is the process of storing glucose and occurs primarily in the liver and the skeletal muscle. The metabolic pathways in these tissues are similar, but the utility of glycogen stores is different. Briefly, liver glycogen is catabolized primarily in response to elevated glucagon, and the glucose 6-phosphate generated is dephosphorylated and released into circulation. In contrast, muscle glycogen is only used by the muscle itself; muscle lacks glucose 6-phosphatase and glucose 6-phosphate released from muscle glycogen is oxidized in glycolysis. Although discussed here as a point of comparison, glycogenolysis is a fasted state pathway and occurs in response to glucagon and epinephrine. This will be discussed in section 5.1.",True,Regulation of fatty acid synthesis,,,,
1c1f2db2-73c4-42fa-9200-0184ee684e00,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
1c1f2db2-73c4-42fa-9200-0184ee684e00,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
1c1f2db2-73c4-42fa-9200-0184ee684e00,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
1c1f2db2-73c4-42fa-9200-0184ee684e00,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
1c1f2db2-73c4-42fa-9200-0184ee684e00,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
1c1f2db2-73c4-42fa-9200-0184ee684e00,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
f53a2f7b-6a64-4928-8e61-43471e32edb4,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,pyrophosphorylase,False,pyrophosphorylase,,,,
caf3fdc4-b4b0-4f36-8f07-5d4b0f378de7,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,glycogenin,False,glycogenin,,,,
8d13bbb1-7120-4629-b917-464b16ac5aed,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Regulation of glycogen synthesis,False,Regulation of glycogen synthesis,,,,
6b280078-3214-46c8-b8d9-953ee88ef5a5,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Glycogen synthesis is regulated by a single enzyme, glycogen synthase. This enzyme is primarily regulated through covalent modification. It is active when dephosphorylated and inactive when phosphorylated. The phosphorylation/dephosphorylation is facilitated by glucagon and insulin levels, respectively (table 4.4).",True,Regulation of glycogen synthesis,,,,
4d301419-0445-467a-b56f-08994c6af9eb,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,Table 4.4: Summary of pathway regulation.,True,Regulation of glycogen synthesis,,,,
bbcc8b7b-52c6-486d-ac07-7f633272c9d2,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,4.5 References and resources,True,Regulation of glycogen synthesis,,,,
cbe57a72-91da-456d-aa3b-4e3ff14d7a28,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
cbe57a72-91da-456d-aa3b-4e3ff14d7a28,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
cbe57a72-91da-456d-aa3b-4e3ff14d7a28,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
cbe57a72-91da-456d-aa3b-4e3ff14d7a28,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
cbe57a72-91da-456d-aa3b-4e3ff14d7a28,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
cbe57a72-91da-456d-aa3b-4e3ff14d7a28,https://pressbooks.lib.vt.edu/cellbio/,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-2,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
9b255528-99ec-49b5-9b2b-f8c40713d0e2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),False,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),,,,
caeba870-57d3-4857-8742-fdcfbb4ed905,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Fatty acid synthesis,False,Fatty acid synthesis,,,,
51e0f1bf-6e0f-4962-ab68-607852b17e76,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycogen synthesis,False,Glycogen synthesis,,,,
7f3b9060-89cb-409d-8b32-d33320232c7e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,reoxidize,False,reoxidize,,,,
dddb7541-3add-46bd-926c-15302817863f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of glycolysis,False,Regulation of glycolysis,,,,
b683d837-1d29-4ec4-b039-b92b9b692e2f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
b683d837-1d29-4ec4-b039-b92b9b692e2f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
b683d837-1d29-4ec4-b039-b92b9b692e2f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
b683d837-1d29-4ec4-b039-b92b9b692e2f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
b683d837-1d29-4ec4-b039-b92b9b692e2f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
b683d837-1d29-4ec4-b039-b92b9b692e2f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
2e8435fd-5c38-478b-a154-8a1fba1f6d1f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glucokinase: Glucose to glucose 6-phosphate,False,Glucokinase: Glucose to glucose 6-phosphate,,,,
f87e7b8c-9f80-421a-a589-15e7d0c06562,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
f87e7b8c-9f80-421a-a589-15e7d0c06562,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
f87e7b8c-9f80-421a-a589-15e7d0c06562,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
f87e7b8c-9f80-421a-a589-15e7d0c06562,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
f87e7b8c-9f80-421a-a589-15e7d0c06562,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
f87e7b8c-9f80-421a-a589-15e7d0c06562,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
ce6b1922-b24a-49af-8510-2a17ef621182,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,GLUT2,False,GLUT2,,,,
cd45b676-a5df-42b9-87ca-2979b4e8c359,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In skeletal muscle, and most other peripheral tissues, glucose is phosphorylated by hexokinase.",True,GLUT2,,,,
b92fe985-6f75-4a2b-a5f2-9de40a4f73c2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b92fe985-6f75-4a2b-a5f2-9de40a4f73c2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b92fe985-6f75-4a2b-a5f2-9de40a4f73c2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b92fe985-6f75-4a2b-a5f2-9de40a4f73c2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b92fe985-6f75-4a2b-a5f2-9de40a4f73c2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
b92fe985-6f75-4a2b-a5f2-9de40a4f73c2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
6670238e-70ea-416a-b858-93e9057df51f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of glucokinase and hexokinase,False,Regulation of glucokinase and hexokinase,,,,
eea6eb17-3827-4691-bd6d-140206c8d4ff,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
eea6eb17-3827-4691-bd6d-140206c8d4ff,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
eea6eb17-3827-4691-bd6d-140206c8d4ff,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
eea6eb17-3827-4691-bd6d-140206c8d4ff,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
eea6eb17-3827-4691-bd6d-140206c8d4ff,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
eea6eb17-3827-4691-bd6d-140206c8d4ff,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
42a21249-f0da-4f65-bb12-90a63d321ba3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,GKRP,False,GKRP,,,,
5258dc88-2a60-411c-ae60-6f3cf51bd7f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",False,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
6efb5a54-0977-44ea-98bd-980b715932cf,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Following glucose phosphorylation to glucose 6-phosphate, the glucose 6-phosphate can be used for glycogen synthesis or the pentose phosphate pathway. Substrate that continues through glycolysis is isomerized to fructose 6-phosphate, which is the substrate for the reaction catalyzed by phosphofructokinase 1 (PFK1).",True,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
cdd9c144-ed04-4175-9723-181cdd12728a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,PFK1,False,PFK1,,,,
b9c182ed-b7e5-4220-ae7f-b4cccc8f200f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of phosphofructokinase 1 (PFK1),False,Regulation of phosphofructokinase 1 (PFK1),,,,
9b583377-6e12-473e-99f3-0ea57de5af1c,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Regulation of phosphofructokinase 1 is primarily through allosteric activation by AMP and fructose 2,6-bisphosphate. High AMP levels would indicate a lack of energy within the cell, and this would increase flux through glycolysis by enhancing the activity of PFK1. PFK1 is also inhibited by citrate and ATP; levels of these compounds are indicative of a high energy state, suggesting there are sufficient oxidation productions and glucose is diverted to storage pathways.",True,Regulation of phosphofructokinase 1 (PFK1),,,,
96843a35-e42f-4ca7-8d69-84b4df9e1e27,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
96843a35-e42f-4ca7-8d69-84b4df9e1e27,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
96843a35-e42f-4ca7-8d69-84b4df9e1e27,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
96843a35-e42f-4ca7-8d69-84b4df9e1e27,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
96843a35-e42f-4ca7-8d69-84b4df9e1e27,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
96843a35-e42f-4ca7-8d69-84b4df9e1e27,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
9b68fa90-32ff-46db-b71d-edfbc1f4e38f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,PFK2,False,PFK2,,,,
21823981-72e2-4442-b9d9-23d7c3b77ff7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,FBP2,False,FBP2,,,,
2c6364ea-0734-4f27-96b8-68bb424ea5e1,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,False,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
d6478f4e-d7a9-4189-b7b7-3da3a0b9200d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Following the synthesis of fructose 1,6-phosphate, aldolase will cleave this substrate into dihydroxyacetone and glyceraldehyde 3-phosphate. These three carbon compounds will be used to synthesize pyruvate in the final regulatory step of the pathway catalyzed by pyruvate kinase (PK).",True,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
207cb294-464c-499e-9bdf-a12cb86b4970,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of pyruvate kinase (PK),False,Regulation of pyruvate kinase (PK),,,,
67480843-c62e-45c6-a002-e1fc36ed7cc9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
67480843-c62e-45c6-a002-e1fc36ed7cc9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
67480843-c62e-45c6-a002-e1fc36ed7cc9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
67480843-c62e-45c6-a002-e1fc36ed7cc9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
67480843-c62e-45c6-a002-e1fc36ed7cc9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
67480843-c62e-45c6-a002-e1fc36ed7cc9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
95d24db8-9ec3-4b02-9b65-7a18f1ba474a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,phosphoenol,False,phosphoenol,,,,
2fb68ec2-c8ab-478b-9fcc-fb318af221a9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Movement of NADH from the cytosol to the mitochondria,False,Movement of NADH from the cytosol to the mitochondria,,,,
5467b016-1f83-4ab9-b087-7c26cbff7279,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The NADH generated in the cytosol by glycolysis must be oxidized back to NAD+ in order to maintain a pool of NAD+ needed for glucose oxidation. As NADH oxidation takes place in the mitochondria, and the membrane is not permeable to NADH, two shuttles are used to move cytosolic NADH into the mitochondria. These processes are a way to get energy out of cytoplasmic NADH into the mitochondria.",True,Movement of NADH from the cytosol to the mitochondria,,,,
75669d0e-3da2-4188-a8ca-ca0b9b64b736,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Glycerol 3-phosphate shuttle,False,Glycerol 3-phosphate shuttle,,,,
9722c832-f518-4027-b74e-ba826a79caa7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
9722c832-f518-4027-b74e-ba826a79caa7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
9722c832-f518-4027-b74e-ba826a79caa7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
9722c832-f518-4027-b74e-ba826a79caa7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
9722c832-f518-4027-b74e-ba826a79caa7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
9722c832-f518-4027-b74e-ba826a79caa7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
a034647b-2ddb-4fb1-9807-c423f7150237,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,dihydroxyacetonephosphate,False,dihydroxyacetonephosphate,,,,
fc8b61b0-842a-42f2-ae4f-1b368b43ca8d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Malate-aspartate shuttle,False,Malate-aspartate shuttle,,,,
695bf0e8-da60-446d-aba9-74211dda61c5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
695bf0e8-da60-446d-aba9-74211dda61c5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
695bf0e8-da60-446d-aba9-74211dda61c5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
695bf0e8-da60-446d-aba9-74211dda61c5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
695bf0e8-da60-446d-aba9-74211dda61c5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
695bf0e8-da60-446d-aba9-74211dda61c5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
28ce3165-5f41-4466-a895-6c511a22ad6a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,OAA,False,OAA,,,,
c747d465-de95-42d9-b747-6fb7f34d76d0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,canʼt,False,canʼt,,,,
9a36b40a-43a7-48a0-993e-7210227cd5db,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Pyruvate dehydrogenase complex,False,Pyruvate dehydrogenase complex,,,,
b3966936-97d3-48e8-a2c9-32edc21843a3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Under aerobic conditions, the pyruvate produced by glycolysis will be oxidized to acetyl-CoA using the pyruvate dehydrogenase complex (PDC). This enzyme is a key transition point between cytosolic and mitochondrial metabolism. This complex is composed of three subunits, which require the cofactors thiamine pyrophosphate, lipoic acid, and FADH2; NADH is also required for the reaction to move forward. The enzyme is highly regulated by both covalent and allosteric regulation. Deficiencies of the PDC can be recessive or X-linked (depending on the subunit deficient) and present with symptoms of lactic acidosis after consuming a meal high in carbohydrates. This metabolic deficiency can be managed by delivering a ketogenic diet and bypassing glycolysis all together.",True,Pyruvate dehydrogenase complex,,,,
08535f04-5552-48b2-acba-49fc8bdc2e8a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,FADH,False,FADH,,,,
04957e4b-fac4-4a0b-9270-f9a929dad4d2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of the pyruvate dehydrogenase complex (PDC),False,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
ffca75f6-ded7-493c-9bca-f11742574ccd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The PDC is regulated by allosteric and covalent regulations. The complex itself can be allosterically activated by pyruvate and NAD+. Elevation of substrate (pyruvate) will enhance flux through this enzyme as will the indication of low energy states as triggered by high NAD+ levels. The PDC is also inhibited by acetyl-CoA and NADH directly. Product inhibition is a very common regulatory mechanism, and high NADH would signal sufficient energy levels, therefore decreasing activity of the PDC.",True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
3eabd1ef-5f21-4206-9814-0de780daa964,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,The PDC is also regulated through covalent modification. Phosphorylation of the complex will decrease activity of the enzyme.,True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
0a405cfb-5c58-45a8-a3f4-bb76e75611ae,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
0a405cfb-5c58-45a8-a3f4-bb76e75611ae,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
0a405cfb-5c58-45a8-a3f4-bb76e75611ae,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
0a405cfb-5c58-45a8-a3f4-bb76e75611ae,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
0a405cfb-5c58-45a8-a3f4-bb76e75611ae,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
0a405cfb-5c58-45a8-a3f4-bb76e75611ae,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
f292f0dd-2d16-4f3b-aadf-48a6ee2aa907,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Summary of pathway regulation,False,Summary of pathway regulation,,,,
e065459c-645d-4f79-959a-aad9b4325d40,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Table 4.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
0a6890e2-de2f-4ae6-826b-1a01a2e5bf8c,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.1 References and resources,True,Summary of pathway regulation,,,,
d67cf161-a93c-455c-97a6-871b711f59bd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 6: Bioenergetics and Oxidative Phosphorylation: Section V, VI, Chapter 8: Introduction to Metabolism and Glycolysis, Chapter 9: TCA Cycle and Pyruvate Dehydrogenase Complex: Section IIA, IIB, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section II, IV, V, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
bd2fb08f-b7e3-4b87-9bfd-dc9fa7d7e0ca,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72–78, 85–89.",True,Summary of pathway regulation,,,,
ff3688bc-29ff-42f2-b2da-3cbb343dae36,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 19: Basic Concepts of Regulation: Section IV.A.1.2, Chapter 20: Cellular Bioenergetics, Chapter 22: Generation of ATP from Glucose: Section I.A.B.C, III, Chapter 24: Oxidative Phosphorylation and the ETC: Section I.E, II, III, Chapter 31: Synthesis of Fatty Acids: Section I.A.B, IV, V.",True,Summary of pathway regulation,,,,
420f59aa-4086-4c3d-b8e2-2833d8cbd027,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
420f59aa-4086-4c3d-b8e2-2833d8cbd027,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
420f59aa-4086-4c3d-b8e2-2833d8cbd027,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
420f59aa-4086-4c3d-b8e2-2833d8cbd027,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
420f59aa-4086-4c3d-b8e2-2833d8cbd027,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
420f59aa-4086-4c3d-b8e2-2833d8cbd027,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
2605530d-0f9f-4c4d-8a30-3caba677b900,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
2605530d-0f9f-4c4d-8a30-3caba677b900,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
2605530d-0f9f-4c4d-8a30-3caba677b900,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
2605530d-0f9f-4c4d-8a30-3caba677b900,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
2605530d-0f9f-4c4d-8a30-3caba677b900,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
2605530d-0f9f-4c4d-8a30-3caba677b900,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
730506b9-93f5-4550-936e-15d5858d523a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
730506b9-93f5-4550-936e-15d5858d523a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
730506b9-93f5-4550-936e-15d5858d523a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
730506b9-93f5-4550-936e-15d5858d523a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
730506b9-93f5-4550-936e-15d5858d523a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
730506b9-93f5-4550-936e-15d5858d523a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
2d53142e-83f7-436d-9528-9c84881c2c38,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
2d53142e-83f7-436d-9528-9c84881c2c38,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
2d53142e-83f7-436d-9528-9c84881c2c38,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
2d53142e-83f7-436d-9528-9c84881c2c38,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
2d53142e-83f7-436d-9528-9c84881c2c38,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
2d53142e-83f7-436d-9528-9c84881c2c38,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
b15f317d-83fe-4790-9354-010d230e47f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b15f317d-83fe-4790-9354-010d230e47f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b15f317d-83fe-4790-9354-010d230e47f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b15f317d-83fe-4790-9354-010d230e47f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b15f317d-83fe-4790-9354-010d230e47f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
b15f317d-83fe-4790-9354-010d230e47f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
1cf77d32-429e-4c5d-b5c9-15eba8bfcae0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
1cf77d32-429e-4c5d-b5c9-15eba8bfcae0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
1cf77d32-429e-4c5d-b5c9-15eba8bfcae0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
1cf77d32-429e-4c5d-b5c9-15eba8bfcae0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
1cf77d32-429e-4c5d-b5c9-15eba8bfcae0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
1cf77d32-429e-4c5d-b5c9-15eba8bfcae0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
abdafa41-83ab-4d0c-9cdd-079764ad8bc0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
abdafa41-83ab-4d0c-9cdd-079764ad8bc0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
abdafa41-83ab-4d0c-9cdd-079764ad8bc0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
abdafa41-83ab-4d0c-9cdd-079764ad8bc0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
abdafa41-83ab-4d0c-9cdd-079764ad8bc0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
abdafa41-83ab-4d0c-9cdd-079764ad8bc0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
38bb3df1-5ae7-45c0-be35-20977d26c6b3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
38bb3df1-5ae7-45c0-be35-20977d26c6b3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
38bb3df1-5ae7-45c0-be35-20977d26c6b3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
38bb3df1-5ae7-45c0-be35-20977d26c6b3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
38bb3df1-5ae7-45c0-be35-20977d26c6b3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
38bb3df1-5ae7-45c0-be35-20977d26c6b3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
16c65967-c4ce-4314-a8f7-ec73da8f674b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
16c65967-c4ce-4314-a8f7-ec73da8f674b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
16c65967-c4ce-4314-a8f7-ec73da8f674b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
16c65967-c4ce-4314-a8f7-ec73da8f674b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
16c65967-c4ce-4314-a8f7-ec73da8f674b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
16c65967-c4ce-4314-a8f7-ec73da8f674b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
916337a6-4432-476a-9663-e436510c09f3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.2 Tricarboxylic Acid Cycle (TCA),True,Summary of pathway regulation,,,,
921e2673-a7cc-4a50-992e-6f5dc1958899,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
921e2673-a7cc-4a50-992e-6f5dc1958899,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
921e2673-a7cc-4a50-992e-6f5dc1958899,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
921e2673-a7cc-4a50-992e-6f5dc1958899,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
921e2673-a7cc-4a50-992e-6f5dc1958899,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
921e2673-a7cc-4a50-992e-6f5dc1958899,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
d4c9c95a-9d58-42ed-8010-0a53bce0946c,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,FADH2,False,FADH2,,,,
387338c8-88f0-4ff8-a620-dab68a9982ce,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
387338c8-88f0-4ff8-a620-dab68a9982ce,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
387338c8-88f0-4ff8-a620-dab68a9982ce,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
387338c8-88f0-4ff8-a620-dab68a9982ce,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
387338c8-88f0-4ff8-a620-dab68a9982ce,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
387338c8-88f0-4ff8-a620-dab68a9982ce,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
60ade046-cbe5-4999-a262-a6c6d630b03b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
60ade046-cbe5-4999-a262-a6c6d630b03b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
60ade046-cbe5-4999-a262-a6c6d630b03b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
60ade046-cbe5-4999-a262-a6c6d630b03b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
60ade046-cbe5-4999-a262-a6c6d630b03b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
60ade046-cbe5-4999-a262-a6c6d630b03b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
61662f34-2fe1-4344-9125-e4062797ed00,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of the TCA cycle,False,Regulation of the TCA cycle,,,,
97f35b0b-200f-4cb4-bdbf-269d3d7c4816,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Throughout the cycle, there are two key regulatory and irreversible steps to be aware of. The first is the conversion of isocitrate to α-ketoglutarate by isocitrate dehydrogenase, and the second is the conversion of α-ketoglutarate to succinyl-CoA by α-ketoglutarate dehydrogenase. The two key regulatory points are:",True,Regulation of the TCA cycle,,,,
057a7e4b-9967-423c-b854-cb4c9571349a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Isocitrate dehydrogenase, which can be activated by Ca2+ and ADP to increase flux through the cycle, and inhibited by NADH, which would suggest adequate energy in the cell.",True,Regulation of the TCA cycle,,,,
f18527af-63cd-4e3e-9d46-91dc380197ce,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Ca2,False,Ca2,,,,
0d24e2dc-2042-404f-825e-febc154eff44,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
0d24e2dc-2042-404f-825e-febc154eff44,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
0d24e2dc-2042-404f-825e-febc154eff44,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
0d24e2dc-2042-404f-825e-febc154eff44,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
0d24e2dc-2042-404f-825e-febc154eff44,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
0d24e2dc-2042-404f-825e-febc154eff44,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
135279b3-58c1-46d0-b958-3fd098468b1a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Malate dehydrogenase can also be inhibited by NADH, however, the reaction is reversible depending on levels of NADH. The oxidation of malate to OAA requires NAD+, and under certain pathological situations the lack of free NAD+ within the mitochondria will reduce the rate of this reaction (this is common in the case of alcohol metabolism).",True,Ca2,,,,
141f80d6-1ae3-47f1-8fe9-ed614a2dbf05,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Keep in mind that with the addition of each acetyl-CoA (comprised of 2 carbons) to the TCA cycle, two molecules of CO2 are released, thus there is no net gain or loss of carbons in the cycle. The process moves forward driven by energetics and substrate availability. The pathway can be active in both the fed and fasted states. In the fed state, acetyl-CoA is generated primarily through glucose oxidation. In contrast, in the fasted state acetyl-CoA is generated primarily from β-oxidation, and the majority of acetyl-CoA is used to synthesize ketones.",True,Ca2,,,,
4fbf3757-aa2a-4d78-8405-7cb23e67792f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Table 4.2: Summary of pathway regulation.,True,Ca2,,,,
d785358d-0a72-46c7-aafa-fba8a633c7b5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.2 References and resources,True,Ca2,,,,
8d5a8dd1-0f5f-43e6-8096-0b63156a3f3d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8d5a8dd1-0f5f-43e6-8096-0b63156a3f3d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8d5a8dd1-0f5f-43e6-8096-0b63156a3f3d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8d5a8dd1-0f5f-43e6-8096-0b63156a3f3d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8d5a8dd1-0f5f-43e6-8096-0b63156a3f3d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
8d5a8dd1-0f5f-43e6-8096-0b63156a3f3d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
53e498b4-5b75-4876-9de3-f093d7d8d895,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
53e498b4-5b75-4876-9de3-f093d7d8d895,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
53e498b4-5b75-4876-9de3-f093d7d8d895,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
53e498b4-5b75-4876-9de3-f093d7d8d895,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
53e498b4-5b75-4876-9de3-f093d7d8d895,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
53e498b4-5b75-4876-9de3-f093d7d8d895,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
bb54e58e-52f1-4023-8d61-295fe73a3788,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
bb54e58e-52f1-4023-8d61-295fe73a3788,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
bb54e58e-52f1-4023-8d61-295fe73a3788,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
bb54e58e-52f1-4023-8d61-295fe73a3788,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
bb54e58e-52f1-4023-8d61-295fe73a3788,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
bb54e58e-52f1-4023-8d61-295fe73a3788,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
f6924436-bb1a-4678-8d03-8c4470604c08,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
f6924436-bb1a-4678-8d03-8c4470604c08,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
f6924436-bb1a-4678-8d03-8c4470604c08,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
f6924436-bb1a-4678-8d03-8c4470604c08,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
f6924436-bb1a-4678-8d03-8c4470604c08,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
f6924436-bb1a-4678-8d03-8c4470604c08,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
828d7be1-25ee-412a-a1e5-9a00abfeb5a0,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.3 Electron Transport Chain (ETC),True,Ca2,,,,
011ea6cb-3809-44fb-bfc2-1fde7d655366,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In the production of NADH and FADH2 by the TCA cycle, β-oxidation or glycolysis is funneled directly into the electron transport chain (ETC) where each of these reduced coenzymes will donate two electrons to electron carriers. As the electrons are passed down their oxidation gradient, some of the energy is lost, but much of this energy is used to pump protons into the intermembrane space of the mitochondria.",True,Ca2,,,,
60cf8c4e-797e-4184-8349-32cfeb3e6ecc,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
60cf8c4e-797e-4184-8349-32cfeb3e6ecc,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
60cf8c4e-797e-4184-8349-32cfeb3e6ecc,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
60cf8c4e-797e-4184-8349-32cfeb3e6ecc,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
60cf8c4e-797e-4184-8349-32cfeb3e6ecc,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
60cf8c4e-797e-4184-8349-32cfeb3e6ecc,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
9a66156b-35f1-48c9-91d8-8f880f637c9f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"There are site specific inhibitors of the ETC to be aware of, and these will disrupt electron flow reducing overall ATP production.",True,Ca2,,,,
f029998a-cd2f-4ee5-ba02-7238c6797e07,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Inhibitors,False,Inhibitors,,,,
e191ee41-d81f-4900-9305-69d26a4c920b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Inhibitors block oxidation and reduce both ATP generation and oxygen consumption; this is in contrast to uncouplers, which disrupt the mitochondrial membrane and reduce ATP production but increase oxygen consumption.",True,Inhibitors,,,,
af9bb33b-031c-4213-a37b-5ccacf481cf3,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,uncouplers,False,uncouplers,,,,
1077646d-b5ee-40a8-9727-a3745444fcb5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"A common inhibitor of the ETC is carbon monoxide; this will bind to Complex IV and therefore halt the passing of electrons. Without electrons passing through the complexes, the pumping of protons is diminished and ATP is not produced. Other common inhibitors are cyanide (Complex IV), rotenone (Complex I), antimycin C (Complex III), and oligomycin, which is a Complex V inhibitor.",True,uncouplers,,,,
7fcae649-248c-40f3-b63c-b19760aba45d,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Uncouplers,False,Uncouplers,,,,
e967d12e-be07-4dd8-bf34-26109447129f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Uncoupling of the ETC by the addition of agents such as dinitrophenol have different consequences. Uncouplers disrupt the permeability of the inner membrane (either physically or chemically) and dissipate the proton gradient.,True,Uncouplers,,,,
b61ce7d0-4407-4cc9-901a-32fbb9fd76e7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"In these cases, the release of protons across the membrane is coupled with the release of heat, rather than harnessed in the form of a phosphate bond. NADH oxidation continues rapidly, oxygen consumption is increased, and ATP production decreases. Valinomycin is another common uncoupler.",True,Uncouplers,,,,
30a616d9-7cfb-4e9d-ade1-5a02bba37850,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Biological uncoupling through the expression of uncoupling proteins (UPC) is also likely. These proteins form a physical pore within the mitochondrial membrane allowing the proton gradient to equilibrate. In brown fat, this nonshivering thermogenesis is a means of generating heat, and other members of this protein family (UPC) are expressed in various tissues but have similar roles.",True,Uncouplers,,,,
b170de4d-af19-40b4-9873-9b8288acc321,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,UPC,False,UPC,,,,
bb5ad97c-d4d4-473d-87cb-8109f7575072,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,nonshivering,False,nonshivering,,,,
995192af-c31d-4852-bf65-06fc7a5136f4,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.3 References and resources,True,nonshivering,,,,
e7e85a5b-6a6e-44e8-8bf8-9608eb72eb4c,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Text,False,Text,,,,
51bae9ae-ec62-4578-abc3-1d87bf30238f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
51bae9ae-ec62-4578-abc3-1d87bf30238f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
51bae9ae-ec62-4578-abc3-1d87bf30238f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
51bae9ae-ec62-4578-abc3-1d87bf30238f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
51bae9ae-ec62-4578-abc3-1d87bf30238f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
51bae9ae-ec62-4578-abc3-1d87bf30238f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
09420054-8395-4c6a-ab45-599f0a7df369,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.4 Fatty Acid Synthesis,True,Text,,,,
b1e5f131-050b-439b-9071-84444f383787,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b1e5f131-050b-439b-9071-84444f383787,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b1e5f131-050b-439b-9071-84444f383787,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b1e5f131-050b-439b-9071-84444f383787,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b1e5f131-050b-439b-9071-84444f383787,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
b1e5f131-050b-439b-9071-84444f383787,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
64f959a6-ff4b-4a39-a8f2-efaedfa211f9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The NADPH generated through this process is necessary for fatty acid synthesis. This is one of the primary pathways that produces NADPH, and the other is the oxidative portion of the pentose pathway.",True,Text,,,,
f01b8143-a539-48fc-9b28-2d5931c06cf5,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The process of fatty acid synthesis starts with the carboxylation of acetyl-CoA to form malonyl-CoA (figures 4.16 and 4.17). The enzyme involved, acetyl-CoA carboxylase, is the regulatory enzyme for this pathway and requires biotin as a cofactor. After the initial priming of fatty acid synthase with acetyl-CoA, all other carbon units are added to the elongating fatty acid chain in the form of malonyl-CoA. You will see later that this intermediate is also a key inhibitor of β-oxidation.",True,Text,,,,
921c4ddc-e53f-4426-accc-e133f1576db4,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
921c4ddc-e53f-4426-accc-e133f1576db4,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
921c4ddc-e53f-4426-accc-e133f1576db4,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
921c4ddc-e53f-4426-accc-e133f1576db4,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
921c4ddc-e53f-4426-accc-e133f1576db4,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
921c4ddc-e53f-4426-accc-e133f1576db4,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
24eda7f0-2043-428c-85d9-4695deb54e1e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,TAGs,False,TAGs,,,,
2fe9386e-fdea-434c-989a-46a3f10204a7,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,VLDLs,False,VLDLs,,,,
2771af3f-d554-4f90-9ff6-1fe55c951463,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of fatty acid synthesis,False,Regulation of fatty acid synthesis,,,,
e23d555e-0456-4cf2-8d7b-37217c604c14,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e23d555e-0456-4cf2-8d7b-37217c604c14,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e23d555e-0456-4cf2-8d7b-37217c604c14,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e23d555e-0456-4cf2-8d7b-37217c604c14,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e23d555e-0456-4cf2-8d7b-37217c604c14,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e23d555e-0456-4cf2-8d7b-37217c604c14,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
935e8a3f-db8c-436c-8590-29861e112ca2,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Table 4.3: Summary of pathway regulation.,True,Regulation of fatty acid synthesis,,,,
384b3ce8-ca39-4e18-bfcb-1c59789c262f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.4 References and resources,True,Regulation of fatty acid synthesis,,,,
91d98cc5-5ef0-410b-bc67-ea4fcc574c68,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
91d98cc5-5ef0-410b-bc67-ea4fcc574c68,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
91d98cc5-5ef0-410b-bc67-ea4fcc574c68,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
91d98cc5-5ef0-410b-bc67-ea4fcc574c68,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
91d98cc5-5ef0-410b-bc67-ea4fcc574c68,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
91d98cc5-5ef0-410b-bc67-ea4fcc574c68,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
55c88bdb-485c-4086-9395-29a1fb7ddc74,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
55c88bdb-485c-4086-9395-29a1fb7ddc74,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
55c88bdb-485c-4086-9395-29a1fb7ddc74,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
55c88bdb-485c-4086-9395-29a1fb7ddc74,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
55c88bdb-485c-4086-9395-29a1fb7ddc74,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
55c88bdb-485c-4086-9395-29a1fb7ddc74,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
e4b63eb4-860c-4258-8840-9f4474d03a4e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e4b63eb4-860c-4258-8840-9f4474d03a4e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e4b63eb4-860c-4258-8840-9f4474d03a4e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e4b63eb4-860c-4258-8840-9f4474d03a4e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e4b63eb4-860c-4258-8840-9f4474d03a4e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
e4b63eb4-860c-4258-8840-9f4474d03a4e,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
8cac4e74-8061-4391-b791-8915bb8e3a7f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.5 Glycogen Synthesis,True,Regulation of fatty acid synthesis,,,,
edb7f9ea-bd0d-4bfb-87be-dc74e7221b6f,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glycogen synthesis is the process of storing glucose and occurs primarily in the liver and the skeletal muscle. The metabolic pathways in these tissues are similar, but the utility of glycogen stores is different. Briefly, liver glycogen is catabolized primarily in response to elevated glucagon, and the glucose 6-phosphate generated is dephosphorylated and released into circulation. In contrast, muscle glycogen is only used by the muscle itself; muscle lacks glucose 6-phosphatase and glucose 6-phosphate released from muscle glycogen is oxidized in glycolysis. Although discussed here as a point of comparison, glycogenolysis is a fasted state pathway and occurs in response to glucagon and epinephrine. This will be discussed in section 5.1.",True,Regulation of fatty acid synthesis,,,,
d4a54136-6b53-4d13-becc-668d7e14f1cd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d4a54136-6b53-4d13-becc-668d7e14f1cd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d4a54136-6b53-4d13-becc-668d7e14f1cd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d4a54136-6b53-4d13-becc-668d7e14f1cd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d4a54136-6b53-4d13-becc-668d7e14f1cd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
d4a54136-6b53-4d13-becc-668d7e14f1cd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
1a873343-dc29-429a-bdb7-400b88af216b,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,pyrophosphorylase,False,pyrophosphorylase,,,,
8adc0e5a-b91d-4955-bfe1-c9da1de56a8a,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,glycogenin,False,glycogenin,,,,
a8b654b5-394e-4802-8dde-93db541d93c8,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Regulation of glycogen synthesis,False,Regulation of glycogen synthesis,,,,
dfb37ba5-bacd-4ba9-8785-07e1cace34ec,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Glycogen synthesis is regulated by a single enzyme, glycogen synthase. This enzyme is primarily regulated through covalent modification. It is active when dephosphorylated and inactive when phosphorylated. The phosphorylation/dephosphorylation is facilitated by glucagon and insulin levels, respectively (table 4.4).",True,Regulation of glycogen synthesis,,,,
d45f5190-0c2b-47c1-bf51-80398c6321cd,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,Table 4.4: Summary of pathway regulation.,True,Regulation of glycogen synthesis,,,,
af71b0ed-5f23-40e2-bc2e-651058b71745,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,4.5 References and resources,True,Regulation of glycogen synthesis,,,,
bbcc53c4-62f5-434c-9a78-3a537bc568e9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
bbcc53c4-62f5-434c-9a78-3a537bc568e9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
bbcc53c4-62f5-434c-9a78-3a537bc568e9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
bbcc53c4-62f5-434c-9a78-3a537bc568e9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
bbcc53c4-62f5-434c-9a78-3a537bc568e9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
bbcc53c4-62f5-434c-9a78-3a537bc568e9,https://pressbooks.lib.vt.edu/cellbio/,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/#chapter-65-section-1,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
ac2f1c9c-72a7-42a5-a16e-7c84b5c5d12f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),False,Tricarboxylic acid cycle (TCA) and electron transport chain (ETC),,,,
4f679bd6-3f9d-4e1c-8aef-a7db5613afb5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Fatty acid synthesis,False,Fatty acid synthesis,,,,
b150cde5-a15d-409d-9037-62cc97e58e0e,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycogen synthesis,False,Glycogen synthesis,,,,
2d5079dc-9e99-4a4b-a261-141f2f7c59de,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,reoxidize,False,reoxidize,,,,
4e76a23a-d1da-4121-aaef-640d3326ecbc,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of glycolysis,False,Regulation of glycolysis,,,,
67909e82-ab86-4fdd-b555-3020ca1fb7e5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
67909e82-ab86-4fdd-b555-3020ca1fb7e5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
67909e82-ab86-4fdd-b555-3020ca1fb7e5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
67909e82-ab86-4fdd-b555-3020ca1fb7e5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
67909e82-ab86-4fdd-b555-3020ca1fb7e5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
67909e82-ab86-4fdd-b555-3020ca1fb7e5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycolysis in the liver has three primary regulated and irreversible steps (figure 4.1).,True,Regulation of glycolysis,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
95498e14-b139-451f-baa7-119a77386da5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glucokinase: Glucose to glucose 6-phosphate,False,Glucokinase: Glucose to glucose 6-phosphate,,,,
bc5dacb4-ea6b-4019-9d87-8f777acb1eb3,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bc5dacb4-ea6b-4019-9d87-8f777acb1eb3,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bc5dacb4-ea6b-4019-9d87-8f777acb1eb3,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bc5dacb4-ea6b-4019-9d87-8f777acb1eb3,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bc5dacb4-ea6b-4019-9d87-8f777acb1eb3,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
bc5dacb4-ea6b-4019-9d87-8f777acb1eb3,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In the liver, glucose is taken up through an insulin-independent process mediated by GLUT2 transporters. Following this, glucose must be phosphorylated to be trapped in the cell. The phosphorylation of glucose to glucose 6-phosphate is catalyzed by glucokinase (figure 4.2) in the liver.",True,Glucokinase: Glucose to glucose 6-phosphate,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
852f0522-e694-4423-b1f5-5e94892e08b7,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,GLUT2,False,GLUT2,,,,
792eb267-ae36-4181-b115-e0a9be5b11b1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In skeletal muscle, and most other peripheral tissues, glucose is phosphorylated by hexokinase.",True,GLUT2,,,,
dbdb0af2-57cd-4328-92a4-28eb12de84f2,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
dbdb0af2-57cd-4328-92a4-28eb12de84f2,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
dbdb0af2-57cd-4328-92a4-28eb12de84f2,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
dbdb0af2-57cd-4328-92a4-28eb12de84f2,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
dbdb0af2-57cd-4328-92a4-28eb12de84f2,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
dbdb0af2-57cd-4328-92a4-28eb12de84f2,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glucokinase and hexokinase perform the same reaction but have very different enzyme kinetics. Glucokinase (in the liver) has a higher Km (lower affinity for glucose) when compared to hexokinase. In the liver, this enzyme will phosphorylate glucose only when glucose concentrations are high such as in the fed state. Glucokinase also has a high Vmax and is therefore not rapidly saturated. This allows for continuous glucose uptake when glucose levels are high allowing for glucose storage and the rapid removal of glucose from circulation, minimizing the likelihood of hyperglycemia. In contrast, hexokinase has a lower Km and a high affinity for glucose (figure 4.3). This enzyme becomes rapidly saturated over a very small range of glucose concentrations.",True,GLUT2,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
09b45da7-8bd3-4006-840a-8ba302302b73,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of glucokinase and hexokinase,False,Regulation of glucokinase and hexokinase,,,,
ba46a9eb-c28c-4787-9dd8-25da88f26853,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba46a9eb-c28c-4787-9dd8-25da88f26853,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba46a9eb-c28c-4787-9dd8-25da88f26853,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba46a9eb-c28c-4787-9dd8-25da88f26853,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba46a9eb-c28c-4787-9dd8-25da88f26853,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
ba46a9eb-c28c-4787-9dd8-25da88f26853,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Hexokinase is regulated through feedback inhibition where glucose 6-phosphate will compete with glucose for substrate binding. On the other hand, glucokinase is regulated through an alternative mechanism involving the glucokinase regulatory binding protein (GKRP). This protein will bind glucokinase and trap it in the nucleus. When glucose is high, glucokinase is released into the cytosol to phosphorylate glucose. As fructose 6-phosphate levels increase, this will inhibit the glucokinase reaction by enhancing the rebinding of glucokinase to GKRP, trapping it in the nucleus (figure 4.4).",True,Regulation of glucokinase and hexokinase,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
20e22353-2f28-4cb2-88fb-7ec2521714e0,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,GKRP,False,GKRP,,,,
85fbefd7-473b-4a43-92a0-8df54629e7de,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",False,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
9454ff5c-3a0c-4196-9870-73ad02b56a9e,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Following glucose phosphorylation to glucose 6-phosphate, the glucose 6-phosphate can be used for glycogen synthesis or the pentose phosphate pathway. Substrate that continues through glycolysis is isomerized to fructose 6-phosphate, which is the substrate for the reaction catalyzed by phosphofructokinase 1 (PFK1).",True,"Phosphofructokinase 1 (PFK1): Fructose 6-phosphate to fructose 1,6-bisphosphate",,,,
a2b0d5e8-4c73-4548-8f9b-f4d66c85da0e,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,PFK1,False,PFK1,,,,
3eb5e743-02c6-4b44-9719-d5ddec350919,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of phosphofructokinase 1 (PFK1),False,Regulation of phosphofructokinase 1 (PFK1),,,,
c1478ffb-7ae6-457f-9f13-d5bac9476984,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Regulation of phosphofructokinase 1 is primarily through allosteric activation by AMP and fructose 2,6-bisphosphate. High AMP levels would indicate a lack of energy within the cell, and this would increase flux through glycolysis by enhancing the activity of PFK1. PFK1 is also inhibited by citrate and ATP; levels of these compounds are indicative of a high energy state, suggesting there are sufficient oxidation productions and glucose is diverted to storage pathways.",True,Regulation of phosphofructokinase 1 (PFK1),,,,
f497cd6c-a494-46a0-8f45-296449ae53ef,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
f497cd6c-a494-46a0-8f45-296449ae53ef,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
f497cd6c-a494-46a0-8f45-296449ae53ef,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
f497cd6c-a494-46a0-8f45-296449ae53ef,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
f497cd6c-a494-46a0-8f45-296449ae53ef,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
f497cd6c-a494-46a0-8f45-296449ae53ef,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Fructose 2,6-bisphosphate is an important regulator of glycolysis, formed by a shunt in the glycolytic pathway. When there is an excess of fructose 6-phosphate in the cell, this substrate is accepted by phosphofructokinase 2 (PFK2) and converted to fructose 2,6-bisphosphate. This compound, fructose 2,6-bisphosphate, functions as an allosteric activator of PFK1. Additionally, PFK2 can be regulated by covalent modification such as phosphorylation. PFK2 is a bifunctional enzyme and only functions as a kinase when insulin is high and it is dephosphorylated. Under fasted conditions, when glucagon is high, this leads to the phosphorylation and inactivation of PFK2; when the enzyme is phosphorylated, it functions as a phosphatase and is referred to as fructose 2,6-bisphosphatase (FBP2) (figure 4.5).",True,Regulation of phosphofructokinase 1 (PFK1),Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
f970328c-769f-4b02-98fd-cf5ea4c1241c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,PFK2,False,PFK2,,,,
37880d3e-ebf0-4428-8ff2-ff66e3ce2681,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,FBP2,False,FBP2,,,,
ed3960fe-7505-4ff0-915a-8437e57e51f5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,False,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
29ac5e35-1a35-4148-a0c6-7e3b34a4942b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Following the synthesis of fructose 1,6-phosphate, aldolase will cleave this substrate into dihydroxyacetone and glyceraldehyde 3-phosphate. These three carbon compounds will be used to synthesize pyruvate in the final regulatory step of the pathway catalyzed by pyruvate kinase (PK).",True,Pyruvate kinase: Phosphoenol pyruvate to pyruvate,,,,
77506372-8507-4745-99da-ad6554180af6,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of pyruvate kinase (PK),False,Regulation of pyruvate kinase (PK),,,,
9a0bcea9-bd30-4a98-96dc-e16a10c2e3d9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9a0bcea9-bd30-4a98-96dc-e16a10c2e3d9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9a0bcea9-bd30-4a98-96dc-e16a10c2e3d9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9a0bcea9-bd30-4a98-96dc-e16a10c2e3d9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9a0bcea9-bd30-4a98-96dc-e16a10c2e3d9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
9a0bcea9-bd30-4a98-96dc-e16a10c2e3d9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The final regulatory step of glycolysis is the reaction catalyzed by pyruvate kinase. The enzyme converts phosphoenol pyruvate (PEP) to pyruvate. PK can be regulated by phosphorylation and allosteric means. PK is subject to feed-forward activation by fructose 1,6-bisphosphate, which allosterically activates the enzyme, increasing flux in the downward direction. As energy levels in the cell increase, ATP levels will reduce enzyme activity through allosteric inhibition (figure 4.6). PK can also be regulated through phosphorylation. Similar to PFK2, PK is dephosphorylated and active in the fed state but phosphorylated during the fasted state, which renders the enzyme inactive; the phosphorylation is glucagon mediated.",True,Regulation of pyruvate kinase (PK),Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
80791d22-cfc3-443c-9e6f-89715e339b4c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,phosphoenol,False,phosphoenol,,,,
0d6a041b-2b38-4469-acc9-832ce720e5e2,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Movement of NADH from the cytosol to the mitochondria,False,Movement of NADH from the cytosol to the mitochondria,,,,
3a4beda9-b549-4c17-99d8-eaf16558434b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The NADH generated in the cytosol by glycolysis must be oxidized back to NAD+ in order to maintain a pool of NAD+ needed for glucose oxidation. As NADH oxidation takes place in the mitochondria, and the membrane is not permeable to NADH, two shuttles are used to move cytosolic NADH into the mitochondria. These processes are a way to get energy out of cytoplasmic NADH into the mitochondria.",True,Movement of NADH from the cytosol to the mitochondria,,,,
3ec55a8b-5ab2-4e92-8d15-59dbe52e9db3,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Glycerol 3-phosphate shuttle,False,Glycerol 3-phosphate shuttle,,,,
03d2c5e0-d3a5-44de-bdb0-167827699940,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
03d2c5e0-d3a5-44de-bdb0-167827699940,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
03d2c5e0-d3a5-44de-bdb0-167827699940,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
03d2c5e0-d3a5-44de-bdb0-167827699940,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
03d2c5e0-d3a5-44de-bdb0-167827699940,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
03d2c5e0-d3a5-44de-bdb0-167827699940,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The glycerol 3-phosphate shuttle is the major shuttle used in most tissues to move NADH from the cytosol to the mitochondria for oxidation. In this pathway, NAD+ is regenerated by glycerol 3-phosphate dehydrogenase, which transfers electrons from NADH to dihydroxyacetonephosphate to generate glycerol 3-phosphate. Glycerol 3-phosphate can diffuse across the mitochondrial membrane where it will donate electrons to membrane bound FAD (bound to succinate dehydrogenase) (figure 4.7).",True,Glycerol 3-phosphate shuttle,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
513189c9-549f-40d0-ae58-c4d3ae35befb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,dihydroxyacetonephosphate,False,dihydroxyacetonephosphate,,,,
dc45c1c8-bd30-499e-a31c-8c1a8483b21a,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Malate-aspartate shuttle,False,Malate-aspartate shuttle,,,,
e161142e-1412-4516-9870-b98541bdc89f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
e161142e-1412-4516-9870-b98541bdc89f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
e161142e-1412-4516-9870-b98541bdc89f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
e161142e-1412-4516-9870-b98541bdc89f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
e161142e-1412-4516-9870-b98541bdc89f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
e161142e-1412-4516-9870-b98541bdc89f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Many tissues also contain the malate-aspartate shuttle, which can also carry cytosolic NADH into the mitochondria. Cytosolic NADH is used to reduce oxaloacetate (OAA) to malate, which can cross the mitochondrial membrane. Once inside the mitochondria, malate can be oxidized to OAA to produce NADH. OAA canʼt pass through the mitochondrial membrane, so it requires transamination to aspartate, which can be shuttled into the cytosol to regenerate the cycle (figure 4.8).",True,Malate-aspartate shuttle,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
54977377-82a7-4ea4-ae4f-30091821c1b9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,OAA,False,OAA,,,,
4405d37c-3016-40c6-8aae-38064e17de6d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,canʼt,False,canʼt,,,,
e9377b4f-fab8-451c-a440-954db3e72620,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Pyruvate dehydrogenase complex,False,Pyruvate dehydrogenase complex,,,,
9a9bc82c-7bd4-422e-bcdb-d0846408bb31,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Under aerobic conditions, the pyruvate produced by glycolysis will be oxidized to acetyl-CoA using the pyruvate dehydrogenase complex (PDC). This enzyme is a key transition point between cytosolic and mitochondrial metabolism. This complex is composed of three subunits, which require the cofactors thiamine pyrophosphate, lipoic acid, and FADH2; NADH is also required for the reaction to move forward. The enzyme is highly regulated by both covalent and allosteric regulation. Deficiencies of the PDC can be recessive or X-linked (depending on the subunit deficient) and present with symptoms of lactic acidosis after consuming a meal high in carbohydrates. This metabolic deficiency can be managed by delivering a ketogenic diet and bypassing glycolysis all together.",True,Pyruvate dehydrogenase complex,,,,
7ca2a751-1859-4c41-a7d4-ae55b406b67b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,FADH,False,FADH,,,,
824cc8ca-32fb-4b5b-9409-6404db9356e4,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of the pyruvate dehydrogenase complex (PDC),False,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
882ac3dc-0d77-43e0-94e7-72581850105e,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The PDC is regulated by allosteric and covalent regulations. The complex itself can be allosterically activated by pyruvate and NAD+. Elevation of substrate (pyruvate) will enhance flux through this enzyme as will the indication of low energy states as triggered by high NAD+ levels. The PDC is also inhibited by acetyl-CoA and NADH directly. Product inhibition is a very common regulatory mechanism, and high NADH would signal sufficient energy levels, therefore decreasing activity of the PDC.",True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
961859bf-2bc2-44e3-971a-0d2184063be8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,The PDC is also regulated through covalent modification. Phosphorylation of the complex will decrease activity of the enzyme.,True,Regulation of the pyruvate dehydrogenase complex (PDC),,,,
e825d794-1ebf-4055-a5ec-a4090f905e5d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e825d794-1ebf-4055-a5ec-a4090f905e5d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e825d794-1ebf-4055-a5ec-a4090f905e5d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e825d794-1ebf-4055-a5ec-a4090f905e5d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e825d794-1ebf-4055-a5ec-a4090f905e5d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
e825d794-1ebf-4055-a5ec-a4090f905e5d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,The enzyme responsible for phosphorylation of the PDC is pyruvate dehydrogenase kinase. The kinase is regulated inversely to the PDC (figure 4.9). The kinase is most active when acetyl-CoA and NADH are high. These compounds will stimulate the kinase to phosphorylate and inactivate the PDC. The PDC can be dephosphorylated by a calcium-mediated phosphatase.,True,Regulation of the pyruvate dehydrogenase complex (PDC),Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
b578364b-bc8d-4523-9afe-c1eb882580aa,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Summary of pathway regulation,False,Summary of pathway regulation,,,,
6b543438-fc80-490f-8e65-e35010d5d41a,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Table 4.1: Summary of pathway regulation.,True,Summary of pathway regulation,,,,
d49e7533-1901-4e27-8c58-19330c19ce6e,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.1 References and resources,True,Summary of pathway regulation,,,,
d078b631-627e-4155-aafd-8284875d963c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 6: Bioenergetics and Oxidative Phosphorylation: Section V, VI, Chapter 8: Introduction to Metabolism and Glycolysis, Chapter 9: TCA Cycle and Pyruvate Dehydrogenase Complex: Section IIA, IIB, Chapter 11: Glycogen Metabolism: Section V, VI, Chapter 16: Fatty Acid Ketone Body and TAG Metabolism: Section II, IV, V, Chapter 23: Metabolic Effect of Insulin and Glucagon, Chapter 25: Diabetes Mellitus.",True,Summary of pathway regulation,,,,
a4e02974-4f67-4da4-9c9a-fc963177fdc0,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 72–78, 85–89.",True,Summary of pathway regulation,,,,
853f294b-867b-4f00-934b-7bfa66052d5a,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 19: Basic Concepts of Regulation: Section IV.A.1.2, Chapter 20: Cellular Bioenergetics, Chapter 22: Generation of ATP from Glucose: Section I.A.B.C, III, Chapter 24: Oxidative Phosphorylation and the ETC: Section I.E, II, III, Chapter 31: Synthesis of Fatty Acids: Section I.A.B, IV, V.",True,Summary of pathway regulation,,,,
54cfe6bd-9688-4811-bbdf-ac7bd12bd124,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
54cfe6bd-9688-4811-bbdf-ac7bd12bd124,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
54cfe6bd-9688-4811-bbdf-ac7bd12bd124,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
54cfe6bd-9688-4811-bbdf-ac7bd12bd124,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
54cfe6bd-9688-4811-bbdf-ac7bd12bd124,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
54cfe6bd-9688-4811-bbdf-ac7bd12bd124,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.1 Summary of glycolysis… 2021. https://archive.org/details/4.1_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.1,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
862df962-a324-4325-be35-6af834ad4e43,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
862df962-a324-4325-be35-6af834ad4e43,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
862df962-a324-4325-be35-6af834ad4e43,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
862df962-a324-4325-be35-6af834ad4e43,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
862df962-a324-4325-be35-6af834ad4e43,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
862df962-a324-4325-be35-6af834ad4e43,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.2 Regulatory step committed by hexo or glucokinase… 2021. https://archive.org/details/4.2_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.2,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
d8568e0a-9009-4353-92ae-7d644270aab9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
d8568e0a-9009-4353-92ae-7d644270aab9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
d8568e0a-9009-4353-92ae-7d644270aab9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
d8568e0a-9009-4353-92ae-7d644270aab9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
d8568e0a-9009-4353-92ae-7d644270aab9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
d8568e0a-9009-4353-92ae-7d644270aab9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.3 Comparison of glucokinase and hexokinase kinetics. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 154. Figure 9.4 A comparison between hexokinase I and glucokinase. 2017.",True,Summary of pathway regulation,Figure 4.3,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
758fd923-9c6c-4342-93dc-bab6f119a8b9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
758fd923-9c6c-4342-93dc-bab6f119a8b9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
758fd923-9c6c-4342-93dc-bab6f119a8b9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
758fd923-9c6c-4342-93dc-bab6f119a8b9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
758fd923-9c6c-4342-93dc-bab6f119a8b9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
758fd923-9c6c-4342-93dc-bab6f119a8b9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.4 Regulation of glucokinase by glucokinase regulatory protein. 2021. https://archive.org/details/4.4_20210924. CC BY 4.0. Added ion channel by Léa Lortal from Noun Project and sphere by Pablo Rozenberg from Noun Project.",True,Summary of pathway regulation,Figure 4.4,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
c4bb571b-bce5-46f0-9be0-d21b893849e1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
c4bb571b-bce5-46f0-9be0-d21b893849e1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
c4bb571b-bce5-46f0-9be0-d21b893849e1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
c4bb571b-bce5-46f0-9be0-d21b893849e1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
c4bb571b-bce5-46f0-9be0-d21b893849e1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
c4bb571b-bce5-46f0-9be0-d21b893849e1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.5 Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2. 2021. https://archive.org/details/4.5-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.5,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
fd5673b3-3c61-407b-96fd-ce74ecb8a421,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
fd5673b3-3c61-407b-96fd-ce74ecb8a421,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
fd5673b3-3c61-407b-96fd-ce74ecb8a421,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
fd5673b3-3c61-407b-96fd-ce74ecb8a421,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
fd5673b3-3c61-407b-96fd-ce74ecb8a421,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
fd5673b3-3c61-407b-96fd-ce74ecb8a421,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.6 Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate. 2021. https://archive.org/details/4.6-new. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.6,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
1825cbb7-99d0-4265-9e7f-5ca03a8657bb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
1825cbb7-99d0-4265-9e7f-5ca03a8657bb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
1825cbb7-99d0-4265-9e7f-5ca03a8657bb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
1825cbb7-99d0-4265-9e7f-5ca03a8657bb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
1825cbb7-99d0-4265-9e7f-5ca03a8657bb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
1825cbb7-99d0-4265-9e7f-5ca03a8657bb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.7 Glycerol 3-phosphate shuttle. 2021. https://archive.org/details/4.7_20210924. CC BY 4.0. Added ion channel by Léa Lortal from the Noun Project.",True,Summary of pathway regulation,Figure 4.7,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
48d806f0-9162-4df3-ad5f-87c681eeb857,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
48d806f0-9162-4df3-ad5f-87c681eeb857,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
48d806f0-9162-4df3-ad5f-87c681eeb857,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
48d806f0-9162-4df3-ad5f-87c681eeb857,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
48d806f0-9162-4df3-ad5f-87c681eeb857,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
48d806f0-9162-4df3-ad5f-87c681eeb857,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.8 Malate-aspartate shuttle. 2021. https://archive.org/details/4.8_20210924. CC BY 4.0.",True,Summary of pathway regulation,Figure 4.8,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
d4df5868-3b3d-4e6f-8b7c-b38e997411af,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
d4df5868-3b3d-4e6f-8b7c-b38e997411af,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
d4df5868-3b3d-4e6f-8b7c-b38e997411af,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
d4df5868-3b3d-4e6f-8b7c-b38e997411af,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
d4df5868-3b3d-4e6f-8b7c-b38e997411af,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
d4df5868-3b3d-4e6f-8b7c-b38e997411af,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.9 Regulation of the PDC. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 471. Figure 23.15 Regulation of pyruvate dehydroenase complex (PDC). 2017.",True,Summary of pathway regulation,Figure 4.9,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
4943dd01-8d79-42da-bb8f-b2ede9410553,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.2 Tricarboxylic Acid Cycle (TCA),True,Summary of pathway regulation,,,,
683b2d96-e5f8-4d8c-b349-6e7f4c4b813d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
683b2d96-e5f8-4d8c-b349-6e7f4c4b813d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
683b2d96-e5f8-4d8c-b349-6e7f4c4b813d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
683b2d96-e5f8-4d8c-b349-6e7f4c4b813d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
683b2d96-e5f8-4d8c-b349-6e7f4c4b813d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
683b2d96-e5f8-4d8c-b349-6e7f4c4b813d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The TCA cycle is responsible for generating over half of the ATP from the oxidation of fuels. This is primarily because the substrate for the TCA cycle, acetyl-CoA, is generated by the oxidation of fatty acids, glucose, amino acids, and ketone bodies. With each turn of the TCA cycle, there is a net production of three NADH, FADH2, two CO2, and one GTP for every acetyl-CoA that enters (figure 4.10).",True,Summary of pathway regulation,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
07a40a16-de02-4779-983f-335a1f28e7a1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,FADH2,False,FADH2,,,,
e91370cc-d553-45c1-bddd-7c249c57be03,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e91370cc-d553-45c1-bddd-7c249c57be03,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e91370cc-d553-45c1-bddd-7c249c57be03,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e91370cc-d553-45c1-bddd-7c249c57be03,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e91370cc-d553-45c1-bddd-7c249c57be03,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
e91370cc-d553-45c1-bddd-7c249c57be03,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The other major role of the TCA cycle is to provide substrates for other synthetic pathways. Malate is shuttled out of the TCA cycle and used as a substrate for gluconeogenesis and oxaloacetate (OAA) and α-ketoglutarate are used as substrates for amino acid synthesis. Through transamination reactions, these two keto-acids can be converted into aspartate and glutamate, respectively. α-ketoglutarate is also a key substrate for the synthesis of neurotransmitters, and succinyl-CoA is the substrate for heme synthesis. Citrate is also a key compound as it is both an intermediate of the TCA cycle and can be shuttled into the cytosol to provide acetyl-CoA for both cholesterol and fatty acid synthesis (figure 4.11).",True,FADH2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
32be9702-6ba8-4664-9351-daa09aebd42b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
32be9702-6ba8-4664-9351-daa09aebd42b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
32be9702-6ba8-4664-9351-daa09aebd42b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
32be9702-6ba8-4664-9351-daa09aebd42b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
32be9702-6ba8-4664-9351-daa09aebd42b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
32be9702-6ba8-4664-9351-daa09aebd42b,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In order to maintain a pool of TCA cycle intermediates, as substrates are removed from the cycle, there are several key reactions (anaplerotic reactions) that are responsible for the addition of intermediates. These reactions are illustrated in figure 4.12. Notice all of these reactions add carbon back to the cycle from amino acids (reactions 1, 2, 3, 4, 5). These will become very important in the discussion of gluconeogenesis where these substrates will provide the majority of carbon for glucose production. Odd chain fatty acid oxidation can also provide carbon in the from of propionyl-CoA (3) although this is not a primary source of TCA cycle intermediates.",True,FADH2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
d6e28a25-1390-4eb2-aa34-6bb4a300a8a9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of the TCA cycle,False,Regulation of the TCA cycle,,,,
de35e27c-1a57-4a20-8d15-c50d6185d8e9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Throughout the cycle, there are two key regulatory and irreversible steps to be aware of. The first is the conversion of isocitrate to α-ketoglutarate by isocitrate dehydrogenase, and the second is the conversion of α-ketoglutarate to succinyl-CoA by α-ketoglutarate dehydrogenase. The two key regulatory points are:",True,Regulation of the TCA cycle,,,,
60b64a3a-fb70-49df-a196-c3727f267461,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Isocitrate dehydrogenase, which can be activated by Ca2+ and ADP to increase flux through the cycle, and inhibited by NADH, which would suggest adequate energy in the cell.",True,Regulation of the TCA cycle,,,,
010f4890-031e-49d6-abec-fda3bef88cea,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Ca2,False,Ca2,,,,
9ddccea9-330b-4729-95ff-1b0b148fa903,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9ddccea9-330b-4729-95ff-1b0b148fa903,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9ddccea9-330b-4729-95ff-1b0b148fa903,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9ddccea9-330b-4729-95ff-1b0b148fa903,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9ddccea9-330b-4729-95ff-1b0b148fa903,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9ddccea9-330b-4729-95ff-1b0b148fa903,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Likewise, α-ketoglutarate dehydrogenase can be activated by Ca2+ and inhibited by NADH (and succinyl-CoA) (figure 4.13).",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
21c41024-e217-4444-b6d8-928ca2c4f393,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Malate dehydrogenase can also be inhibited by NADH, however, the reaction is reversible depending on levels of NADH. The oxidation of malate to OAA requires NAD+, and under certain pathological situations the lack of free NAD+ within the mitochondria will reduce the rate of this reaction (this is common in the case of alcohol metabolism).",True,Ca2,,,,
1a461f85-02d8-4979-be14-4d28ac08c9db,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Keep in mind that with the addition of each acetyl-CoA (comprised of 2 carbons) to the TCA cycle, two molecules of CO2 are released, thus there is no net gain or loss of carbons in the cycle. The process moves forward driven by energetics and substrate availability. The pathway can be active in both the fed and fasted states. In the fed state, acetyl-CoA is generated primarily through glucose oxidation. In contrast, in the fasted state acetyl-CoA is generated primarily from β-oxidation, and the majority of acetyl-CoA is used to synthesize ketones.",True,Ca2,,,,
bd96b555-1568-4863-93b2-2137956516d9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Table 4.2: Summary of pathway regulation.,True,Ca2,,,,
01f80963-a135-40f6-977b-3b4f31cc970c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.2 References and resources,True,Ca2,,,,
66173c5e-055c-40d0-9a52-bf20b42d0286,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
66173c5e-055c-40d0-9a52-bf20b42d0286,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
66173c5e-055c-40d0-9a52-bf20b42d0286,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
66173c5e-055c-40d0-9a52-bf20b42d0286,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
66173c5e-055c-40d0-9a52-bf20b42d0286,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
66173c5e-055c-40d0-9a52-bf20b42d0286,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.10 Overview of the TCA cycle. 2021. https://archive.org/details/4.10-new. CC BY 4.0.",True,Ca2,Figure 4.10,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
907eaa62-407b-4154-8e97-f7bc0d4d5517,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
907eaa62-407b-4154-8e97-f7bc0d4d5517,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
907eaa62-407b-4154-8e97-f7bc0d4d5517,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
907eaa62-407b-4154-8e97-f7bc0d4d5517,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
907eaa62-407b-4154-8e97-f7bc0d4d5517,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
907eaa62-407b-4154-8e97-f7bc0d4d5517,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.11 Substrates produced by the TCA cycle. 2021. https://archive.org/details/4.11_20210924. CC BY 4.0.",True,Ca2,Figure 4.11,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
f5864d84-b703-4210-8a15-69968e8512ee,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
f5864d84-b703-4210-8a15-69968e8512ee,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
f5864d84-b703-4210-8a15-69968e8512ee,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
f5864d84-b703-4210-8a15-69968e8512ee,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
f5864d84-b703-4210-8a15-69968e8512ee,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
f5864d84-b703-4210-8a15-69968e8512ee,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.12 Anaplerotic reactions of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 473. Figure 23.18 Major anaplerotic pathways of the tricarboxylic acid (TCA) cycle. 2017.",True,Ca2,Figure 4.12,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
9dd23f6d-f07d-446b-a450-a02feb868396,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9dd23f6d-f07d-446b-a450-a02feb868396,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9dd23f6d-f07d-446b-a450-a02feb868396,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9dd23f6d-f07d-446b-a450-a02feb868396,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9dd23f6d-f07d-446b-a450-a02feb868396,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
9dd23f6d-f07d-446b-a450-a02feb868396,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Lieberman M, Peet A. Figure 4.13 Regulation of the TCA cycle. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 468. Figure 23.11 Major regulatory interaction in the tricarboxylic acid (TCA) cycle. 2017. Added ion channel by Léa Lortal from the Noun Project.",True,Ca2,Figure 4.13,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
a4369cee-e321-4d82-a39a-2c5160294b36,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.3 Electron Transport Chain (ETC),True,Ca2,,,,
c665938f-3ad0-4922-a5e3-f8fa65b3d7c5,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In the production of NADH and FADH2 by the TCA cycle, β-oxidation or glycolysis is funneled directly into the electron transport chain (ETC) where each of these reduced coenzymes will donate two electrons to electron carriers. As the electrons are passed down their oxidation gradient, some of the energy is lost, but much of this energy is used to pump protons into the intermembrane space of the mitochondria.",True,Ca2,,,,
7a60ae69-c9bc-4b0a-939f-330da7ae45bd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
7a60ae69-c9bc-4b0a-939f-330da7ae45bd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
7a60ae69-c9bc-4b0a-939f-330da7ae45bd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
7a60ae69-c9bc-4b0a-939f-330da7ae45bd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
7a60ae69-c9bc-4b0a-939f-330da7ae45bd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
7a60ae69-c9bc-4b0a-939f-330da7ae45bd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The process of oxidative phosphorylation (figure 4.14) involves the coupling of electron transfer with the pumping of protons to generate an electrochemical gradient across the mitochondrial membrane. With the exception of CoQ all proteins are bound to the mitochondria membrane, and electrons are passed between metal containing cytochromes. Complex I and Complex II function in parallel (rather than series) with each other having preference for NADH or FADH2, respectively. Complex II (succinate dehydrogenase) is not required for oxidative phosphorylation because it does not span the mitochondrial membrane (figure 4.14). Electrons are passed down an electrochemical gradient, and molecular oxygen is the final electron acceptor (molecular oxygen).",True,Ca2,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
74e66668-a5f2-46f8-be21-49e714479974,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"There are site specific inhibitors of the ETC to be aware of, and these will disrupt electron flow reducing overall ATP production.",True,Ca2,,,,
21285f49-60d3-42a6-bab1-0ac1577756a1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Inhibitors,False,Inhibitors,,,,
b3043bcd-a9fe-4e08-8a14-65ea7e7a72c9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Inhibitors block oxidation and reduce both ATP generation and oxygen consumption; this is in contrast to uncouplers, which disrupt the mitochondrial membrane and reduce ATP production but increase oxygen consumption.",True,Inhibitors,,,,
c21f3d43-fce2-4ed7-ace0-703a2235cf0c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,uncouplers,False,uncouplers,,,,
8faabea8-d321-4dcb-87fc-028989aedd86,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"A common inhibitor of the ETC is carbon monoxide; this will bind to Complex IV and therefore halt the passing of electrons. Without electrons passing through the complexes, the pumping of protons is diminished and ATP is not produced. Other common inhibitors are cyanide (Complex IV), rotenone (Complex I), antimycin C (Complex III), and oligomycin, which is a Complex V inhibitor.",True,uncouplers,,,,
b189699b-9501-41af-9898-ae23a43b3b5f,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Uncouplers,False,Uncouplers,,,,
72735c23-0f20-4dee-b70c-b3975761f9ce,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Uncoupling of the ETC by the addition of agents such as dinitrophenol have different consequences. Uncouplers disrupt the permeability of the inner membrane (either physically or chemically) and dissipate the proton gradient.,True,Uncouplers,,,,
d4484952-6358-4e48-8317-d01b272b7c54,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"In these cases, the release of protons across the membrane is coupled with the release of heat, rather than harnessed in the form of a phosphate bond. NADH oxidation continues rapidly, oxygen consumption is increased, and ATP production decreases. Valinomycin is another common uncoupler.",True,Uncouplers,,,,
58609730-2b6d-47bd-80e8-d37aa169fe6c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Biological uncoupling through the expression of uncoupling proteins (UPC) is also likely. These proteins form a physical pore within the mitochondrial membrane allowing the proton gradient to equilibrate. In brown fat, this nonshivering thermogenesis is a means of generating heat, and other members of this protein family (UPC) are expressed in various tissues but have similar roles.",True,Uncouplers,,,,
f2b6c0d6-8c98-417f-8bf7-194715f11c3d,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,UPC,False,UPC,,,,
03422c9c-4cce-406a-a302-17c871266671,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,nonshivering,False,nonshivering,,,,
cb4235b2-f175-48ea-9414-f449a48b8ea7,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.3 References and resources,True,nonshivering,,,,
4c36d3cd-84ba-4379-b372-61df05001a75,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Text,False,Text,,,,
3ccaf2d9-2f77-4690-8a37-2ff65b2db524,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
3ccaf2d9-2f77-4690-8a37-2ff65b2db524,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
3ccaf2d9-2f77-4690-8a37-2ff65b2db524,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
3ccaf2d9-2f77-4690-8a37-2ff65b2db524,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
3ccaf2d9-2f77-4690-8a37-2ff65b2db524,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
3ccaf2d9-2f77-4690-8a37-2ff65b2db524,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.14 Overview of the electron transport chain (ETC). 2021. https://archive.org/details/4.14_20210924. CC BY 4.0.",True,Text,Figure 4.14,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
e2bb89e4-5ba3-46da-965d-085599ad9776,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.4 Fatty Acid Synthesis,True,Text,,,,
6d3741ad-e9b0-4ca9-a29f-4893923098cb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
6d3741ad-e9b0-4ca9-a29f-4893923098cb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
6d3741ad-e9b0-4ca9-a29f-4893923098cb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
6d3741ad-e9b0-4ca9-a29f-4893923098cb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
6d3741ad-e9b0-4ca9-a29f-4893923098cb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
6d3741ad-e9b0-4ca9-a29f-4893923098cb,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids is an anabolic pathway that occurs in the cytosol under fed conditions. As glucose is taken up by the liver and the flux through the TCA cycle increases, excess citrate is removed via the citrate shuttle. Once in the cytosol, citrate is cleaved by citrate lyase back into oxaloacetate (OAA) and acetyl-CoA. The OAA can be reduced to malate by cytosolic malate dehydrogenase and decarboxylated by malic enzyme producing pyruvate and NADPH (figure 4.15).",True,Text,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
48d04a54-3708-4dc8-9c9c-83324b8dac10,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The NADPH generated through this process is necessary for fatty acid synthesis. This is one of the primary pathways that produces NADPH, and the other is the oxidative portion of the pentose pathway.",True,Text,,,,
8f028c14-6117-4a34-bcd6-2ecd74c5e30c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The process of fatty acid synthesis starts with the carboxylation of acetyl-CoA to form malonyl-CoA (figures 4.16 and 4.17). The enzyme involved, acetyl-CoA carboxylase, is the regulatory enzyme for this pathway and requires biotin as a cofactor. After the initial priming of fatty acid synthase with acetyl-CoA, all other carbon units are added to the elongating fatty acid chain in the form of malonyl-CoA. You will see later that this intermediate is also a key inhibitor of β-oxidation.",True,Text,,,,
3cb6db44-80bd-4a80-ab67-7ea6287c3a81,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3cb6db44-80bd-4a80-ab67-7ea6287c3a81,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3cb6db44-80bd-4a80-ab67-7ea6287c3a81,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3cb6db44-80bd-4a80-ab67-7ea6287c3a81,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3cb6db44-80bd-4a80-ab67-7ea6287c3a81,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
3cb6db44-80bd-4a80-ab67-7ea6287c3a81,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"The synthesis of fatty acids by fatty acid synthase initially starts with the transfer of an acetyl moiety from acetyl-CoA to the acyl carrier protein within fatty acid synthase. Malonyl-CoA is added to the acetyl group and decarboxylated to form a four-carbon β-keto chain. From here, the fatty acid chain is elongated through a series of dehydration and reduction reactions, which use NADPH as a reducing agent. The final product is palmitate, a C-16 molecule (figure 4.16). Fatty acids are not stored in the liver and must be packaged into VLDL particles for transport to peripheral tissues for storage. To produce VLDL particles, the newly synthesized fatty acids are packaged into triacylglycerols (TAGs). TAG synthesis can take place in both the liver and adipose tissue. Synthesis requires glycerol 3-phosphate, which can be derived from glycolysis or from the phosphorylation of glycerol using glycerol kinase in the liver. Three fatty acyl-CoA groups react with the glycerol 3-phosphate to form a TAG. TAGs, along with cholesterol, are packaged into VLDLs distributed into circulation (section 6.2).",True,Text,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
17357f3b-9131-47c4-9bd8-892bbe201c31,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,TAGs,False,TAGs,,,,
0791af3b-2cae-4157-ba45-a9cd1ad725e0,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,VLDLs,False,VLDLs,,,,
6edecec4-cb50-42bb-b27e-5e31566444ec,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of fatty acid synthesis,False,Regulation of fatty acid synthesis,,,,
0a1a942a-1fea-4260-9cc6-2c29ea32a9f1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0a1a942a-1fea-4260-9cc6-2c29ea32a9f1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0a1a942a-1fea-4260-9cc6-2c29ea32a9f1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0a1a942a-1fea-4260-9cc6-2c29ea32a9f1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0a1a942a-1fea-4260-9cc6-2c29ea32a9f1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
0a1a942a-1fea-4260-9cc6-2c29ea32a9f1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Acetyl-CoA carboxylase is the regulatory enzyme for fatty acid synthesis. This enzyme is regulated both allosterically and through covalent modification. It is allosterically activated by high levels of citrate and inhibited by its product, fatty acyl-CoA. It can also be inhibited by elevated levels of glucagon, epinephrine, and adenosine monophosphate (AMP)-activated protein kinase phosphorylation. Insulin will stimulate the dephosphorylation and activation of the enzyme such that it can be active in the fed state (figure 4.17).",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
4fee1540-1630-47a2-bdbe-1165120294ef,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Table 4.3: Summary of pathway regulation.,True,Regulation of fatty acid synthesis,,,,
12aee5c7-cba3-4e95-b9ea-ae0a58d5e1e0,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.4 References and resources,True,Regulation of fatty acid synthesis,,,,
65550461-858e-4f29-9988-fd6d45019ae8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
65550461-858e-4f29-9988-fd6d45019ae8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
65550461-858e-4f29-9988-fd6d45019ae8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
65550461-858e-4f29-9988-fd6d45019ae8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
65550461-858e-4f29-9988-fd6d45019ae8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
65550461-858e-4f29-9988-fd6d45019ae8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.15 Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis. 2021. https://archive.org/details/4.15-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.15,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
492bc604-73f3-46e8-b946-1c46a2ad2c61,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
492bc604-73f3-46e8-b946-1c46a2ad2c61,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
492bc604-73f3-46e8-b946-1c46a2ad2c61,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
492bc604-73f3-46e8-b946-1c46a2ad2c61,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
492bc604-73f3-46e8-b946-1c46a2ad2c61,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
492bc604-73f3-46e8-b946-1c46a2ad2c61,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.16 Fatty acid synthesis is an iterative process which begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase, following this activation, carbons are added to the growing chain in the form of malonyl-CoA. 2021. https://archive.org/details/4.16_20210924. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.16,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
d93be59c-cb4d-4f7f-a61b-4db8499d99c9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
d93be59c-cb4d-4f7f-a61b-4db8499d99c9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
d93be59c-cb4d-4f7f-a61b-4db8499d99c9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
d93be59c-cb4d-4f7f-a61b-4db8499d99c9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
d93be59c-cb4d-4f7f-a61b-4db8499d99c9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
d93be59c-cb4d-4f7f-a61b-4db8499d99c9,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.17 Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol. 2021. https://archive.org/details/4.17-new. CC BY 4.0.",True,Regulation of fatty acid synthesis,Figure 4.17,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
047a51b3-be93-48bb-a83f-d81fecc9d236,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.5 Glycogen Synthesis,True,Regulation of fatty acid synthesis,,,,
26859049-56f7-4661-8daa-d0b1363f9bdf,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glycogen synthesis is the process of storing glucose and occurs primarily in the liver and the skeletal muscle. The metabolic pathways in these tissues are similar, but the utility of glycogen stores is different. Briefly, liver glycogen is catabolized primarily in response to elevated glucagon, and the glucose 6-phosphate generated is dephosphorylated and released into circulation. In contrast, muscle glycogen is only used by the muscle itself; muscle lacks glucose 6-phosphatase and glucose 6-phosphate released from muscle glycogen is oxidized in glycolysis. Although discussed here as a point of comparison, glycogenolysis is a fasted state pathway and occurs in response to glucagon and epinephrine. This will be discussed in section 5.1.",True,Regulation of fatty acid synthesis,,,,
e15e055f-581c-4224-a939-8a230f924abd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
e15e055f-581c-4224-a939-8a230f924abd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
e15e055f-581c-4224-a939-8a230f924abd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
e15e055f-581c-4224-a939-8a230f924abd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
e15e055f-581c-4224-a939-8a230f924abd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
e15e055f-581c-4224-a939-8a230f924abd,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Initially glucose 6-phosphate, is isomerized to glucose 1-phosphate. UDP-glucose pyrophosphorylase synthesizes UDP-glucose from glucose 1-phosphate and UTP, and this is the source of all the glycosyl residues added to the growing glycogen chain (figure 4.18). Glycogen synthase is the regulatory enzyme for the pathway and is responsible for linking glycosyl residues in a 1,4 linkage. The reaction typically occurs on existing glycogen stores; however, in the absence of any stored glycogen the reaction can occur on the protein primer, glycogenin.",True,Regulation of fatty acid synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
b5810817-bc1e-4d18-8268-b100dcba1c65,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,pyrophosphorylase,False,pyrophosphorylase,,,,
136681b7-acc5-480d-867d-22e03fecd9a1,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,glycogenin,False,glycogenin,,,,
d7c07d92-5227-4967-a1c8-b9a71b0e0ac8,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Regulation of glycogen synthesis,False,Regulation of glycogen synthesis,,,,
b575abdc-2e6d-4cb8-a565-24dbca25fe8c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Glycogen synthesis is regulated by a single enzyme, glycogen synthase. This enzyme is primarily regulated through covalent modification. It is active when dephosphorylated and inactive when phosphorylated. The phosphorylation/dephosphorylation is facilitated by glucagon and insulin levels, respectively (table 4.4).",True,Regulation of glycogen synthesis,,,,
c3bcfbaa-bae4-4972-8d76-012a264d2e6c,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,Table 4.4: Summary of pathway regulation.,True,Regulation of glycogen synthesis,,,,
3072a4d3-8c2d-4c5f-a967-e05899c16476,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,4.5 References and resources,True,Regulation of glycogen synthesis,,,,
8e27fe75-29ef-4d0c-8889-acd4affd4f33,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.5 Glycogen Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
8e27fe75-29ef-4d0c-8889-acd4affd4f33,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.4 Fatty Acid Synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
8e27fe75-29ef-4d0c-8889-acd4affd4f33,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.3 Electron Transport Chain (ETC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
8e27fe75-29ef-4d0c-8889-acd4affd4f33,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.2 Tricarboxylic Acid Cycle (TCA),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
8e27fe75-29ef-4d0c-8889-acd4affd4f33,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4.1 Glycolysis and the Pyruvate Dehydrogenase Complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
8e27fe75-29ef-4d0c-8889-acd4affd4f33,https://pressbooks.lib.vt.edu/cellbio/,4. Fuel for Now,https://pressbooks.lib.vt.edu/cellbio/chapter/fuel-for-now/,"Grey, Kindred, Figure 4.18 Glycogen synthesis. 2021. https://archive.org/details/4.18_20210924. CC BY 4.0.",True,Regulation of glycogen synthesis,Figure 4.18,4. Fuel for Now,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
bc891e5d-544c-4ae2-8bc4-11035afc9b7b,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"The ratios of these hormones in circulation will dictate the activity of specific metabolic pathways that control glucose homeostasis in a range of 80 mg/dL to 120 mg/dL. There are many other hormones (thyroid hormone, growth hormone, etc.) and adipokines (adiponectin, leptin, etc.) that can influence glucose homeostasis, as well as neural mechanisms that control higher level functions such as hunger and satiety. These will not be the focus of this section.",True,Regulation of glycogen synthesis,,,,
1a370c0c-9602-43fc-9def-02a710caa224,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,adipokines,False,adipokines,,,,
e51b8490-2194-4f6c-ae5b-d5617a3aca38,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Fed state metabolism,False,Fed state metabolism,,,,
b6d2cfa0-de95-4c60-ac0f-7faaf4605c00,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"In the fed state, or postprandial, elevated glucose levels trigger the release of insulin from the pancreas. As insulin levels rise, there is an increase in glucose uptake, oxidation, and storage in peripheral tissues as well as increases in other anabolic pathways.",True,Fed state metabolism,,,,
b30fe9bd-725d-4d25-9e4a-1607efcc11bb,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Under these conditions, most tissues (liver, skeletal muscle, adipose, brain, and red blood cells) will increase glucose uptake and oxidation (table 3.1 and figure 3.1).",True,Fed state metabolism,Figure 3.1,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
b30fe9bd-725d-4d25-9e4a-1607efcc11bb,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Under these conditions, most tissues (liver, skeletal muscle, adipose, brain, and red blood cells) will increase glucose uptake and oxidation (table 3.1 and figure 3.1).",True,Fed state metabolism,Figure 3.1,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
5291e1f8-19cf-4b9e-a7e3-ae3a3b9a0b12,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Each tissue will take up glucose in the fed state using one of the glucose transporters (GLUT) known to facilitate glucose transport across the plasma membrane. This family of proteins can be broadly categorized as insulin-independent and insulin-dependent transporters.,True,Fed state metabolism,,,,
cf50ecaa-17fd-479a-8744-0cfbce1e3920,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Table 3.1: Summary table of fuels used in the fed state and uptake methods for important tissues.,True,Fed state metabolism,,,,
2cc487a3-6e23-48e8-8f48-882d0cb9ab1c,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Insulin-independent glucose uptake,False,Insulin-independent glucose uptake,,,,
2b0a480e-0f67-4f70-a826-a623e5ffd33a,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"The brain and red blood cells will always preferentially oxidize glucose regardless of hormone levels. Consequently, both tissues have a prevalence of GLUT1 transporters on the cell membrane. GLUT1 is present on the blood brain barrier, while GLUT3 is predominant on the brain. GLUT1 has a lower Km (higher affinity) for glucose, ensuring glucose transport to these important tissues. Likewise, glucose uptake in the liver is also insulin-independent and is facilitated by GLUT2 transporters. The pancreas also predominantly expresses GLUT1 and is able to take up glucose in this manner.",True,Insulin-independent glucose uptake,,,,
af75bf7a-1c6f-4141-9afb-838477deeddf,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,GLUT1,False,GLUT1,,,,
5d8536c8-555d-4749-a694-84e10ffc7d7b,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,GLUT3,False,GLUT3,,,,
2bcbb302-1c79-4aab-8c0a-6924152685c9,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Red blood cell metabolism,False,Red blood cell metabolism,,,,
e46608a0-0184-45f4-b150-6e00b029c121,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"The red blood cell lacks mitochondria, therefore it oxidizes glucose under both fed and fasted conditions. Glucose can be oxidized by:",True,Red blood cell metabolism,,,,
a987741e-4ca1-434d-aa64-977f6ab2bdd2,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Brain metabolism,False,Brain metabolism,,,,
7e813d7f-4218-437a-83bf-0a73da02b3d8,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,The brain will preferentially oxidize glucose under most conditions with the exception of starvation states.,True,Brain metabolism,,,,
930616f2-f3a8-43c5-9832-ef0c7336478b,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Liver metabolism,False,Liver metabolism,,,,
130ada33-1bbd-4224-96c0-120eefb0d066,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"In the liver, glucose is taken up in an insulin-independent manner, and the activity of the following processes increased in the fed state are summarized in figure 3.1 and tables 3.1 and 3.2.",True,Liver metabolism,Figure 3.1,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
130ada33-1bbd-4224-96c0-120eefb0d066,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"In the liver, glucose is taken up in an insulin-independent manner, and the activity of the following processes increased in the fed state are summarized in figure 3.1 and tables 3.1 and 3.2.",True,Liver metabolism,Figure 3.1,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
89d7c5e2-c42d-4482-a7dc-50b8d3cfdbc3,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Insulin-dependent glucose uptake,False,Insulin-dependent glucose uptake,,,,
f57166cd-eaf6-4f74-88a3-bd8219cb2a8a,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"In contrast, the skeletal muscle and adipose tissues require insulin for glucose uptake. GLUT4 is the primary glucose transporter on these tissues, and in the absence of insulin this transporter is predominantly bound to intracellular vesicles. When the cell receives a signal (via insulin binding the insulin receptor), this cell signaling event allows the GLUT4 containing vesicles to fuse with the plasma membrane where it will facilitate glucose uptake.",True,Insulin-dependent glucose uptake,,,,
ee3183ef-d873-4053-b5d4-f88896b3331b,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Skeletal muscle metabolism,False,Skeletal muscle metabolism,,,,
7b3ba56f-a2fb-4776-aae2-8413f3bba03b,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,The skeletal muscle will increase uptake of both amino acids and glucose under fed conditions.,True,Skeletal muscle metabolism,,,,
9a3eabcc-8982-46d1-9722-6fe15a07e10e,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Adipose metabolism,False,Adipose metabolism,,,,
6698c1e5-cb67-467f-bcee-e6a69aaa9081,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"In the adipose tissue, glucose as well as dietary fat and cholesterol (transported as chylomicrons; section 6.2) are taken up by the adipose tissue. Glucose has several potential fates described below, while dietary fat is stored as triacylglycerol.",True,Adipose metabolism,,,,
1ba233f8-0ef3-4639-9513-6a555aa243eb,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Table 3.2: Summary of metabolism during the fed state.,True,Adipose metabolism,,,,
bca2dec5-653b-4ace-84ed-6645d2d6d695,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Fasted state metabolism,False,Fasted state metabolism,,,,
7a3ec35d-40b2-4690-9234-1ee40ac510d9,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Approximately two hours after a meal, the decrease in serum glucose levels will lead to decreased insulin production in the pancreas. At this point in fasted state metabolism, the insulin to glucagon ratio becomes  less than 1 (insulin low; glucagon high) with an additional increase of cortisol and epinephrine. Under these conditions tissues will transition to utilizing alternative fuels for energy as a means of maintaining glucose homeostasis. Fasted state metabolism will have limited impact on the oxidation of glucose by the brain and red blood cells, but it will lead to an increase in fatty acid oxidation by both the skeletal muscle and the liver (figure 3.6). The fatty acids oxidized by these tissues are released through the process of epinephrine-mediated lipolysis from the adipose. In the fasted state, the liver will primarily release glucose using both gluconeogenesis and glycogenolysis for the maintenance of blood glucose.",True,Fasted state metabolism,Figure 3.6,,,
301f19d4-f160-4e83-9ec8-21cb3ddbeddf,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Table 3.3: Summary table of fuels used in the fasted state and the pathways providing the fuel source.,True,Fasted state metabolism,,,,
d919abd4-f28c-4e7d-b184-33b754662fdd,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"The primary role of the liver in the fasted state is to synthesize and release glucose. To facilitate this task, the liver will use circulating free fatty acids as the primary fuel source to generate energy (ATP) for these homeostatic processes. (These processes are summarized in figure 3.2 and tables 3.3 and 3.4)",True,Fasted state metabolism,Figure 3.2,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
d919abd4-f28c-4e7d-b184-33b754662fdd,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"The primary role of the liver in the fasted state is to synthesize and release glucose. To facilitate this task, the liver will use circulating free fatty acids as the primary fuel source to generate energy (ATP) for these homeostatic processes. (These processes are summarized in figure 3.2 and tables 3.3 and 3.4)",True,Fasted state metabolism,Figure 3.2,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
3b9f1182-e156-4062-8117-dfb0515afdb0,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"The red blood cell lacks mitochondria, therefore it oxidizes glucose under both fed and fasted conditions. The metabolism of this tissue remains largely unchanged.",True,Fasted state metabolism,,,,
51c87026-5818-40cb-8807-fa467ae336a6,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"The brain will oxidize glucose under most conditions with the exception of starvation states. Under normal fasting conditions, although ketones will be synthesized, the brain will not transition to utilizing them as a predominant source of fuel until extended fasting has occurred (days).",True,Fasted state metabolism,,,,
ff9e2a78-f6bc-4d5f-9a95-1119a4863e17,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,The skeletal muscle will increase uptake of fatty acids and ketones.,True,Fasted state metabolism,,,,
db1d6849-6e4a-4ee1-929a-184801a22236,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,The most important process in the adipose tissue during the fasted state is lipolysis.,True,Fasted state metabolism,,,,
c23f64eb-49f7-42d1-bbe7-77d0485d3a7f,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Table 3.4: Summary of metabolism during the fasted state.,True,Fasted state metabolism,,,,
874810fd-adc1-498c-8a3a-347765c6e50e,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,3.1 References and resources,True,Fasted state metabolism,,,,
fc45a092-3e09-4c54-8fb6-958af0bd3fd7,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 24: Fed Fast Cycle.",True,Fasted state metabolism,,,,
6d7664aa-702b-428d-aaad-63c5b00529a8,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 91, 324–325",True,Fasted state metabolism,,,,
8bf5d57b-757e-48a7-a512-455bfd798753,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,.,False,.,,,,
c2bbdb21-b5e1-4528-a6a9-a1bad9ad1f07,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Lieberman, M., A. and Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 3: The Fasted State.",True,.,,,,
965ffb94-bc92-413a-afc2-1300b985d8f5,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,Arm muscles anatomical. Public domain. From wpclipart.,True,.,,,,
9d13f4aa-25c0-445f-b11d-f94ae6ae08fb,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Gregory D, Marshall D, Fat cells. CC BY 4.0. From Welcome Collection.",True,.,,,,
c16eb070-c654-4256-a642-9d4963705f13,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Grey, Kindred, Figure 3.1: Overview of fed state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Brain by Maxicons from the Noun Project, and Muscle by Laymik from the Noun Project.",True,.,Figure 3.1,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
c16eb070-c654-4256-a642-9d4963705f13,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Grey, Kindred, Figure 3.1: Overview of fed state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Brain by Maxicons from the Noun Project, and Muscle by Laymik from the Noun Project.",True,.,Figure 3.1,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
70a209b5-5fde-4cde-812d-3d2349b2d10b,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Grey, Kindred, Figure 3.2: Overview of fasted state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from Noun Project, Brain by Maxicons from Noun Project, Muscle by Laymik from Noun Project, red blood cells by Lucas Helle from Noun Project.",True,.,Figure 3.2,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
70a209b5-5fde-4cde-812d-3d2349b2d10b,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Grey, Kindred, Figure 3.2: Overview of fasted state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from Noun Project, Brain by Maxicons from Noun Project, Muscle by Laymik from Noun Project, red blood cells by Lucas Helle from Noun Project.",True,.,Figure 3.2,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
bc7274da-04ec-46ec-aa32-da7e47ca1335,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"Häggström M, Liver (transparent). Public domain. From Wikimedia Commons.",True,.,,,,
0d3fb0a9-624e-4f35-bf53-b9ef91a26fa3,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"LadyofHats, Osmotic pressure on blood cells diagram. Public domain. From Wikimedia Commons.",True,.,,,,
076a2dd4-b999-43af-b419-f2a26fc58cdb,https://pressbooks.lib.vt.edu/cellbio/,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/#chapter-62-section-1,"_DJ_, Human brain on white background. 2005. CC BY-SA 2.0. From Flickr.",True,.,,,,
b98c00cc-ab82-4460-987e-41ae2cbe4dd8,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"The ratios of these hormones in circulation will dictate the activity of specific metabolic pathways that control glucose homeostasis in a range of 80 mg/dL to 120 mg/dL. There are many other hormones (thyroid hormone, growth hormone, etc.) and adipokines (adiponectin, leptin, etc.) that can influence glucose homeostasis, as well as neural mechanisms that control higher level functions such as hunger and satiety. These will not be the focus of this section.",True,.,,,,
203e0baf-fb47-40d4-ab18-393591b3f5d3,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,adipokines,False,adipokines,,,,
bf9d88ee-a0eb-4d50-9208-149e7c4d995e,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Fed state metabolism,False,Fed state metabolism,,,,
7b090500-a469-4614-9d3b-5bf0c2cdb3b4,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"In the fed state, or postprandial, elevated glucose levels trigger the release of insulin from the pancreas. As insulin levels rise, there is an increase in glucose uptake, oxidation, and storage in peripheral tissues as well as increases in other anabolic pathways.",True,Fed state metabolism,,,,
f34f9351-7977-4b6b-b2df-3888d9865508,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Under these conditions, most tissues (liver, skeletal muscle, adipose, brain, and red blood cells) will increase glucose uptake and oxidation (table 3.1 and figure 3.1).",True,Fed state metabolism,Figure 3.1,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
f34f9351-7977-4b6b-b2df-3888d9865508,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Under these conditions, most tissues (liver, skeletal muscle, adipose, brain, and red blood cells) will increase glucose uptake and oxidation (table 3.1 and figure 3.1).",True,Fed state metabolism,Figure 3.1,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
5202ba51-21f0-4e45-89f1-5652ba8e32b2,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Each tissue will take up glucose in the fed state using one of the glucose transporters (GLUT) known to facilitate glucose transport across the plasma membrane. This family of proteins can be broadly categorized as insulin-independent and insulin-dependent transporters.,True,Fed state metabolism,,,,
56575fe0-3762-416c-ae8f-56da62415921,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Table 3.1: Summary table of fuels used in the fed state and uptake methods for important tissues.,True,Fed state metabolism,,,,
66195239-202e-44fa-b624-aae9e9b915a2,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Insulin-independent glucose uptake,False,Insulin-independent glucose uptake,,,,
309ab2a3-d387-420f-aa79-d2d14e9806b7,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"The brain and red blood cells will always preferentially oxidize glucose regardless of hormone levels. Consequently, both tissues have a prevalence of GLUT1 transporters on the cell membrane. GLUT1 is present on the blood brain barrier, while GLUT3 is predominant on the brain. GLUT1 has a lower Km (higher affinity) for glucose, ensuring glucose transport to these important tissues. Likewise, glucose uptake in the liver is also insulin-independent and is facilitated by GLUT2 transporters. The pancreas also predominantly expresses GLUT1 and is able to take up glucose in this manner.",True,Insulin-independent glucose uptake,,,,
7f2452fd-7a2e-48ed-bf5d-2e3ca86b352f,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,GLUT1,False,GLUT1,,,,
d5dc64b3-5db0-4c94-8e54-5b88dab58143,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,GLUT3,False,GLUT3,,,,
548bd340-6f6f-4443-85b5-7cdcf2ef86d9,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Red blood cell metabolism,False,Red blood cell metabolism,,,,
5362c5de-76ef-4b22-b350-88334a01a7e5,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"The red blood cell lacks mitochondria, therefore it oxidizes glucose under both fed and fasted conditions. Glucose can be oxidized by:",True,Red blood cell metabolism,,,,
b8a69ed7-effa-4153-90e8-cf25bbc1f63a,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Brain metabolism,False,Brain metabolism,,,,
43024971-0bcc-4496-bcfd-6a7f6c092bdd,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,The brain will preferentially oxidize glucose under most conditions with the exception of starvation states.,True,Brain metabolism,,,,
7e6364f5-adae-494c-bc36-8dbcee290b4e,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Liver metabolism,False,Liver metabolism,,,,
798885a1-80c1-42c3-a440-a18ced7e6a12,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"In the liver, glucose is taken up in an insulin-independent manner, and the activity of the following processes increased in the fed state are summarized in figure 3.1 and tables 3.1 and 3.2.",True,Liver metabolism,Figure 3.1,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
798885a1-80c1-42c3-a440-a18ced7e6a12,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"In the liver, glucose is taken up in an insulin-independent manner, and the activity of the following processes increased in the fed state are summarized in figure 3.1 and tables 3.1 and 3.2.",True,Liver metabolism,Figure 3.1,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
95541f29-2f2d-4886-9fee-c5731efb0277,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Insulin-dependent glucose uptake,False,Insulin-dependent glucose uptake,,,,
f2fa5790-0bdc-4786-b980-82a3ac36e28d,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"In contrast, the skeletal muscle and adipose tissues require insulin for glucose uptake. GLUT4 is the primary glucose transporter on these tissues, and in the absence of insulin this transporter is predominantly bound to intracellular vesicles. When the cell receives a signal (via insulin binding the insulin receptor), this cell signaling event allows the GLUT4 containing vesicles to fuse with the plasma membrane where it will facilitate glucose uptake.",True,Insulin-dependent glucose uptake,,,,
c08443bd-ab43-4e88-817c-7c8c52f1ce48,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Skeletal muscle metabolism,False,Skeletal muscle metabolism,,,,
8146a5c0-4dba-4556-a349-85f6bd82e464,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,The skeletal muscle will increase uptake of both amino acids and glucose under fed conditions.,True,Skeletal muscle metabolism,,,,
a858b333-c2e2-4039-9eda-06a366b2c243,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Adipose metabolism,False,Adipose metabolism,,,,
a6c3dd09-e627-448b-8c23-2191bee43c40,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"In the adipose tissue, glucose as well as dietary fat and cholesterol (transported as chylomicrons; section 6.2) are taken up by the adipose tissue. Glucose has several potential fates described below, while dietary fat is stored as triacylglycerol.",True,Adipose metabolism,,,,
a4b5cf4a-8410-47f3-9ef3-17975efc64d4,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Table 3.2: Summary of metabolism during the fed state.,True,Adipose metabolism,,,,
4f68334b-a08e-48e5-9b1a-cc55e5205620,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Fasted state metabolism,False,Fasted state metabolism,,,,
bff6040b-b61b-455d-9fa2-d127198e62b1,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Approximately two hours after a meal, the decrease in serum glucose levels will lead to decreased insulin production in the pancreas. At this point in fasted state metabolism, the insulin to glucagon ratio becomes  less than 1 (insulin low; glucagon high) with an additional increase of cortisol and epinephrine. Under these conditions tissues will transition to utilizing alternative fuels for energy as a means of maintaining glucose homeostasis. Fasted state metabolism will have limited impact on the oxidation of glucose by the brain and red blood cells, but it will lead to an increase in fatty acid oxidation by both the skeletal muscle and the liver (figure 3.6). The fatty acids oxidized by these tissues are released through the process of epinephrine-mediated lipolysis from the adipose. In the fasted state, the liver will primarily release glucose using both gluconeogenesis and glycogenolysis for the maintenance of blood glucose.",True,Fasted state metabolism,Figure 3.6,,,
989f63e2-90a0-4868-b04a-76bf9583d253,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Table 3.3: Summary table of fuels used in the fasted state and the pathways providing the fuel source.,True,Fasted state metabolism,,,,
58fb48e2-4ba3-4750-a823-789458811bd5,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"The primary role of the liver in the fasted state is to synthesize and release glucose. To facilitate this task, the liver will use circulating free fatty acids as the primary fuel source to generate energy (ATP) for these homeostatic processes. (These processes are summarized in figure 3.2 and tables 3.3 and 3.4)",True,Fasted state metabolism,Figure 3.2,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
58fb48e2-4ba3-4750-a823-789458811bd5,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"The primary role of the liver in the fasted state is to synthesize and release glucose. To facilitate this task, the liver will use circulating free fatty acids as the primary fuel source to generate energy (ATP) for these homeostatic processes. (These processes are summarized in figure 3.2 and tables 3.3 and 3.4)",True,Fasted state metabolism,Figure 3.2,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
ee26e68f-b519-47ca-9b2c-59d963051c2f,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"The red blood cell lacks mitochondria, therefore it oxidizes glucose under both fed and fasted conditions. The metabolism of this tissue remains largely unchanged.",True,Fasted state metabolism,,,,
76852ea1-eb21-46d0-a61d-d143cef50063,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"The brain will oxidize glucose under most conditions with the exception of starvation states. Under normal fasting conditions, although ketones will be synthesized, the brain will not transition to utilizing them as a predominant source of fuel until extended fasting has occurred (days).",True,Fasted state metabolism,,,,
0fc0aff2-db58-42f2-b619-8fb5bf83ab18,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,The skeletal muscle will increase uptake of fatty acids and ketones.,True,Fasted state metabolism,,,,
b6227c76-fa9c-4fbe-8ac2-e439c6fe3a46,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,The most important process in the adipose tissue during the fasted state is lipolysis.,True,Fasted state metabolism,,,,
da4d4b5b-e7fd-46f6-9eaa-7601d77f4bca,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Table 3.4: Summary of metabolism during the fasted state.,True,Fasted state metabolism,,,,
0a102d10-6e04-4780-9206-0de1f1b43775,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,3.1 References and resources,True,Fasted state metabolism,,,,
fb717fa3-42ec-444b-82c2-4d22138e4744,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 24: Fed Fast Cycle.",True,Fasted state metabolism,,,,
4634c06f-3b0d-4b1a-92ac-5eaf602c4088,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 91, 324–325",True,Fasted state metabolism,,,,
9a5baf37-da19-4fd7-8a69-c0d86a00f837,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,.,False,.,,,,
83ded96c-8a6c-4665-8d60-17cd79d2ae96,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Lieberman, M., A. and Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 2: The Fed or Absorptive State, Chapter 3: The Fasted State.",True,.,,,,
e5571e43-5c47-4df4-872c-5ebc0189e2ae,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,Arm muscles anatomical. Public domain. From wpclipart.,True,.,,,,
3478c85f-6816-4260-b7ec-66661f9f6b6c,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Gregory D, Marshall D, Fat cells. CC BY 4.0. From Welcome Collection.",True,.,,,,
5840ec35-c06b-4907-9b28-81cade337a21,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Grey, Kindred, Figure 3.1: Overview of fed state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Brain by Maxicons from the Noun Project, and Muscle by Laymik from the Noun Project.",True,.,Figure 3.1,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
5840ec35-c06b-4907-9b28-81cade337a21,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Grey, Kindred, Figure 3.1: Overview of fed state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from the Noun Project, Brain by Maxicons from the Noun Project, and Muscle by Laymik from the Noun Project.",True,.,Figure 3.1,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
febcae07-ff8f-450b-8a39-456496670731,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Grey, Kindred, Figure 3.2: Overview of fasted state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from Noun Project, Brain by Maxicons from Noun Project, Muscle by Laymik from Noun Project, red blood cells by Lucas Helle from Noun Project.",True,.,Figure 3.2,3.1 Fed and Fasted States,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
febcae07-ff8f-450b-8a39-456496670731,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Grey, Kindred, Figure 3.2: Overview of fasted state metabolism. 2021. CC BY 4.0. Added Liver by Liam Mitchell from Noun Project, Brain by Maxicons from Noun Project, Muscle by Laymik from Noun Project, red blood cells by Lucas Helle from Noun Project.",True,.,Figure 3.2,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
e84e3712-01cc-453b-b2b9-c9adce28804c,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"Häggström M, Liver (transparent). Public domain. From Wikimedia Commons.",True,.,,,,
ca1b5bd6-8ac6-4b65-84c2-8baad1c3ae4e,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"LadyofHats, Osmotic pressure on blood cells diagram. Public domain. From Wikimedia Commons.",True,.,,,,
db5e8bcd-eaa8-4e5a-9845-981273ef5e9f,https://pressbooks.lib.vt.edu/cellbio/,3. Fed and Fasted State,https://pressbooks.lib.vt.edu/cellbio/chapter/fed-and-fasted-state/,"_DJ_, Human brain on white background. 2005. CC BY-SA 2.0. From Flickr.",True,.,,,,
09319bf1-e82b-4d7b-8f69-9c09b9a9ab70,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"As a clinician, your first indication of changes to these cellular components will be illustrated by the signs and symptoms of your patient. Following this generalized assessment, you will begin to dissect out a clinical diagnosis by interpreting basic lab values. Each of these elements are indicative of molecular changes ultimately leading to the presentation you are challenged with.",True,.,,,,
b825122b-ef67-44f8-8e43-40a5e90d9718,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"How to read a CMP both clinically and biochemically will help hone the skills of diagnosis and maintenance of health status in patients. Additional laboratory tests such as a lipid profile, blood lactate, or urinalysis may also be ordered to supplement information from the CMP.",True,.,,,,
95e43085-48dc-43bf-a6ab-0f3aeeccbabb,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Deviations in any of these values can help determine changes in substrate availability, cofactors, and vitamin or enzymatic deficiencies. It will also help you better understand how biochemical pathways can influence clinical signs and symptoms.",True,.,,,,
d6c002eb-ddd7-4c03-823a-768a7f492eaf,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Comprehensive metabolic panel,False,Comprehensive metabolic panel,,,,
94863da8-63a0-4832-a39f-5516972e8ce1,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,A CMP is often administered as part of a routine physical exam or for monitoring of specific conditions that impact kidney and liver functions. The results include the following tests (table 2.1):,True,Comprehensive metabolic panel,,,,
72ebdf9d-ebe1-4f56-95c6-1c661012d0e1,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Table 2.1: Normal values for a typical comprehensive metabolic panel. These values will be given to you when evaluating information.,True,Comprehensive metabolic panel,,,,
aacd505b-e140-4ceb-a8ec-2f3adbe88638,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Glucose – This energy source for the body is maintained in a very narrow range. Metabolic pathways are in place to balance both glucose uptake and glucose output to keep this value constant. Glucose homeostasis is regulated hormonally, and deviations from normal values could suggest metabolic or hormonal deficiencies (chapter 4 and chapter 5).",True,Comprehensive metabolic panel,,,,
bd2a6f95-3f87-4981-9631-87e491969a0d,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Calcium – This is one of the most important minerals in the body; it is essential for the proper functioning of muscles, nerves, and cardiac tissue. It is a cofactor in processes such as blood clotting and bone formation. Other vitamins also play key roles in these pathways (vitamin K in clotting and vitamin D in bone formation), so understanding this value may give insights into other potential deficiencies.",True,Comprehensive metabolic panel,,,,
e3c72633-4362-4149-b4f5-1ba7aa8ce719,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Proteins,False,Proteins,,,,
9743942b-f920-468d-911f-ab9cb31abfa4,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Albumin – Albumin is a major serum protein produced in the liver and is a nonspecific carrier of many lipid soluble vitamins and other hydrophobic compounds. It is also essential for maintaining oncotic pressure. Decreases in serum albumin may be suggestive of nutritional deficiencies or changes in plasma volume as well as poor liver function. Therefore accessibility of lipid soluble vitamins, minerals, and hormones may be diminished secondarily to a decrease in albumin.",True,Proteins,,,,
086a839e-4b69-4c78-8292-939ca60bdb14,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Total protein – Like serum albumin, a measure of total serum protein is useful to evaluate malnutrition or more chronic disorders such as inflammatory bowel disease. Increased production of immunoglobulins could also be detected here and would be indicative of chronic illness.",True,Proteins,,,,
6d599948-d766-4acc-81bc-02e0c00d2e7e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Electrolytes,False,Electrolytes,,,,
c93cedc3-030a-4def-9315-a419c3a88e44,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Sodium – Sodium is vital to normal body processes, including nerve and muscle function. Hyponatremia can be suggestive of illness, diarrhea, or malnutrition, while hypernatremia is most often caused by an increased loss of water (dehydration) potentially due to endocrine disorders such as Cushing syndrome or diabetes insipidus.",True,Electrolytes,,,,
4d30ac8d-ebe1-4e09-8860-feb8b785b761,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Potassium – Potassium is critical for cardiac function, and although hypo or hyperkalemia can be indicative of a variety of disorders, it can be a critical indicator of maintenance of diabetes. Unmanaged diabetic individuals may present with hyperkalemia, however, inappropriate insulin administration will increase potassium uptake. Therefore poor management can cause a sudden drop in potassium (hypokalemia) leading to cardiac dysfunction.",True,Electrolytes,,,,
8fb42423-6d50-4a78-8a61-2bf26f054087,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"CO2 (carbon dioxide, bicarbonate) – CO2 is produced from several oxidative pathways and is removed in the form of bicarbonate or through hemoglobin transport. Elevation of CO2 could suggest a renal, respiratory, and/or metabolic concern, and additional laboratory values would need to be assessed to determine the root cause. These may include blood lactate, blood urea nitrogen (BUN), as well as arteriole blood gasses (ABG).",True,Electrolytes,,,,
d8263b54-4459-44f8-868e-d7f920a53309,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Chloride – Chloride is a negatively charged ion that works with other electrolytes (potassium, sodium, and bicarbonate) to help regulate both fluid and acid–base (pH) balance in the body. Chloride and electrolyte tests may help diagnose the cause of signs and symptoms such as prolonged vomiting, diarrhea, weakness, and difficulty breathing (respiratory distress).",True,Electrolytes,,,,
cdb34a11-a276-437b-8c0c-926d4210c128,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Kidney tests,False,Kidney tests,,,,
62eaaebc-5409-44a0-9db5-40d8fac26129,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Blood urea nitrogen (BUN) – Urea is a waste product of amino acid metabolism filtered out of the blood by the kidneys. It is a primary means of nitrogen disposal, and conditions that affect the kidneys have the potential to affect the amount of urea in the blood. This value is also indicative of deficiencies in amino acid metabolism, or changes in urea cycle activity or protein catabolism (section 5.3).",True,Kidney tests,,,,
00b5473c-c08b-4827-a2c2-1d6ba1cf6420,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Creatinine – This waste product is produced in the muscles and filtered out by the kidneys. Urinary levels of creatinine are a good indicator of how the kidneys are working.,True,Kidney tests,,,,
bb9a63fb-9e75-49a4-8f0b-c34c2fd04eb2,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Liver tests,False,Liver tests,,,,
daa4f6b2-27c6-4e7f-85af-54bbb05c2bc6,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Alkaline phosphatase (ALP) – ALP is an enzyme found in the liver and other tissues such as bone. Elevated levels of ALP are most commonly caused by liver disease or other pathologies that increase cell damage leading to the release of ALP in the blood. Other disorders that impact bone growth may also increase ALP.,True,Liver tests,,,,
f92bf38c-fbce-49d1-9a3d-39875bdced7f,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Alanine amino transferase (ALT) – ALT is an enzyme found predominantly in the liver and kidney. It is important in movement of ammonia (through the process of transamination) in tissues, and an elevation of ALT in circulation suggests liver damage (or potentially muscle damage) (section 5.3).",True,Liver tests,,,,
4115f0c6-83ee-419c-898e-f77232222093,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Aspartate amino transferase (AST) – AST is also a transferase needed in nitrogen metabolism found especially within the heart and liver. It is also a useful test for detecting liver damage. The ratio of ALT/AST can be used to distinguish between disorders such as alcoholic versus nonalcoholic fatty liver disease (section 5.3).,True,Liver tests,,,,
a63aa7ac-62b9-44e4-8fca-6ee7a595a39b,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a63aa7ac-62b9-44e4-8fca-6ee7a595a39b,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a63aa7ac-62b9-44e4-8fca-6ee7a595a39b,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
784afc1b-84ff-42ac-b2ec-48bb41c9a34e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Lipid profile,False,Lipid profile,,,,
7665c87b-e221-4d0a-ba45-3a8de4115f17,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,A lipid profile (table 2.2) is often used to assess risk of developing cardiovascular disease (CVD) or to monitor the effectiveness of a dietary or pharmacological intervention.,True,Lipid profile,,,,
00ea3713-8bd5-414a-9463-a10cc23dede7,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Table 2.2: Desirable (optimal) values for lipids. Ranges of intermediate and high can also be found for these values.,True,Lipid profile,,,,
72fc4503-6cb6-415d-b410-e80bb1bb61a3,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Total cholesterol – This measurement takes in to account various forms of cholesterol in circulation. It is the total of high-density lipoprotein (HDL), low-density lipoprotein (LDL), and 20 percent of the triglyceride measurement. This is key to determining your cholesterol ratio (total/HDL), which should be below 5 with an ideal ratio being 3.5.",True,Lipid profile,,,,
bace3fd2-13df-4b1b-be29-ce733d33caaf,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,High-density lipoprotein cholesterol (HDL-C) – HDL is predominantly involved in reverse cholesterol transport because it removes excess cholesterol from peripheral tissues and carries it to the liver for removal or use. It has several key interactions with very low-density lipid (VLDL) particles in circulation that assist in lipid metabolism.,True,Lipid profile,,,,
2f240bf3-7961-4474-9c18-bec0e0b77227,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Low-density lipoprotein cholesterol (LDL-C) – LDL is often called “bad cholesterol” because it can deposit excess cholesterol in walls of blood vessels, which can contribute to atherosclerosis.",True,Lipid profile,,,,
e582f60e-d05a-4652-bdae-26bde2d36346,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Triglycerides – This is a measurement of circulating triacylglycerols (TAG), which are primarily transported by VLDL particles. TAG levels should be less than 150 mg/dL, and increased TAG may suggest endocrine deficiencies or metabolic defects.",True,Lipid profile,,,,
d4ae984c-aa01-45b8-887c-b5865d6e9ad4,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Variations of normal in a lipid profile could be suggestive of heritable disorders, poor diet, or lipid uptake, decreased lipid storage, or excessive synthesis. The combination of these values will help determine what aspect of lipid metabolism is altered (chapter 6).",True,Lipid profile,,,,
885b0608-3022-40d7-9918-60cc0b9afd42,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Lactate,False,Lactate,,,,
a1bd4d19-e758-479c-b85d-67408c03c539,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
a1bd4d19-e758-479c-b85d-67408c03c539,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
a1bd4d19-e758-479c-b85d-67408c03c539,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
45dceea9-79a6-4eb8-810c-1a580808d0c6,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Urinalysis (includes a visual, chemical, and microscopic exam)",False,"Urinalysis (includes a visual, chemical, and microscopic exam)",,,,
70563ba5-d1af-4eab-9b1c-2352bf89c4f2,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Visual exam and the microscopic exam,False,Visual exam and the microscopic exam,,,,
89e70f7b-4232-472a-a080-d20abfbbd233,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Although both the visual and microscopic exam are very essential components to this analysis, these will not be focused on here. The color of urine can vary, most often shades of yellow, from very pale or colorless to very dark or amber. Red-colored urine can also occur when blood is present; yellow-brown or greenish-brown urine may be a sign of bilirubin in the urine. Urine clarity refers to how clear the urine is. This could be defined as: clear, slightly cloudy, cloudy, or turbid. “Normal” urine can be clear or cloudy.",True,Visual exam and the microscopic exam,,,,
37b9dae7-b6b1-462d-bf3e-5e7a2fc408a9,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"A microscopic examination will typically be done when there are abnormal findings on the physical or chemical examination. Cells and other substances that may be seen include the following: red blood cells (RBCs), white blood cells (WBCs), epithelial cells, bacteria, yeast and parasites, trichomonas, casts, and crystals. If the crystals are from substances that are not normally in the urine, they are considered “abnormal.” Abnormal crystals may indicate an abnormal metabolic process. Some of these include: calcium carbonate, cystine, tyrosine, and leucine. Urinary presence of some amino acids can be suggestive of amino acid metabolic disorders (chapter 8).",True,Visual exam and the microscopic exam,,,,
6a3e89e7-6482-4156-8cb2-cc677c7e7e3a,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Chemical exam,False,Chemical exam,,,,
ce24cf01-6e56-475f-ae30-bb941c7cf876,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Much like the CMP, the chemical analysis of a urine sample can be very indicative of biochemical derangement. A review of the following components is helpful in making a clinical diagnosis.",True,Chemical exam,,,,
4bcad1ae-be4c-4d76-836b-cd4eb5389dd2,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Specific gravity (SG) – Specific gravity is a measure of urine concentration. This test simply indicates how concentrated the urine is.,True,Chemical exam,,,,
1b479ebf-4bca-4639-9cd6-439b3140713b,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"pH – Urine is typically slightly acidic, about pH 6, but can range from 4.5 to 8. The kidneys play an important role in maintaining the acid–base balance of the body. Therefore, any condition that produces acids or bases in the body, such as acidosis or alkalosis, or the ingestion of acidic or basic foods, can directly affect urine pH.",True,Chemical exam,,,,
c87a34d8-6da0-46d6-b0c6-daa20cee8c31,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Protein – The protein test provides an estimate of the amount of albumin in the urine. Normally, there should be no protein (or a small amount of protein) in the urine. When urine protein is elevated, a person has a condition called proteinuria; this could be caused by a variety of health conditions. Healthy people can have temporary or persistent proteinuria due to stress, exercise, fever, aspirin therapy, or exposure to cold, for example.",True,Chemical exam,,,,
9c043a93-dccb-484a-8440-73a46cb3b574,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Glucose – Glucose is normally not present in urine. When glucose is present, the condition is called glucosuria. This condition can result from either an excessively high glucose level in the blood, such as may be seen in individuals with uncontrolled diabetes. Other reducing sugars, galactose or fructose, may also be present in the urine if a metabolic deficiency occurs (section 9.1).",True,Chemical exam,,,,
ede3c16b-b3ed-45a5-9a41-c0c14b960abf,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Some other conditions that can cause glucosuria include hormonal disorders, liver disease, medications, and pregnancy. When glucosuria occurs, other tests such as a fasting blood glucose test are usually performed to further identify the specific cause.",True,Chemical exam,,,,
a66690ff-d6b3-44b4-bd16-c6cbe0989de2,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Ketones – Ketones are also not normally found in the urine. They are intermediate products of fat metabolism and can be produced when an individual does not eat enough carbohydrates such as in fasting conditions or high-protein diets. When carbohydrates are not available, the body metabolizes fat to generate ATP for baseline metabolic function. Strenuous exercise, exposure to cold, frequent, prolonged vomiting, and several digestive system diseases can also increase fat metabolism, resulting in ketonuria (section 5.2).",True,Chemical exam,,,,
127df023-2b3f-4243-ab01-2ea54fc5bff2,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"In a person who has diabetes, ketones in urine may be an early indication of insufficient insulin. Insufficient insulin response can result in impaired glucose oxidation and consequently results in aberrant fat metabolism. Oxidation of fatty acids provides substrate for ketogenesis, which can cause ketosis and potentially progress to ketoacidosis, a form of metabolic acidosis. Excess ketones and glucose are dumped into the urine by the kidneys in an effort to flush them from the body.",True,Chemical exam,,,,
33e94050-5429-46b5-a7c5-4355b5f2a04c,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Hemoglobin and myoglobin – The presence of hemoglobin in urine indicates blood in the urine (known as hematuria).,True,Chemical exam,,,,
89d4adf9-953d-4c40-a578-b8b5712967fa,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"A small number of RBCs are normally present in urine, however, as these numbers elevate, this will result in a positive test result. These results are interpreted with the microscopic exam. For example, a positive test result here with no visible RBCs in the urine would suggest the presence of myoglobin only, which could be due to strenuous exercise or muscle damage.",True,Chemical exam,,,,
5d289da4-a41d-411c-a7e7-3ba2460ebe28,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Leukocyte esterase – Leukocyte esterase is an enzyme present in most white blood cells (WBCs). A few white blood cells are normally present in urine, however, when the number of WBCs in urine increases significantly, this screening test will become positive. When this test is positive and/or the WBC count in urine is high, it may indicate that there is inflammation in the urinary tract or kidneys.",True,Chemical exam,,,,
aeea09c1-77a7-40c9-9800-c26633a1fa81,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Nitrite – Many normal bacteria can convert nitrate (normally present in urine) to nitrite (not normally present in urine). When bacteria are present in the urinary tract, they can cause a urinary tract infection, which could be diagnosed by a positive nitrite test result.",True,Chemical exam,,,,
e4e951cc-30ca-4a6e-9aff-9c28261beecd,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
e4e951cc-30ca-4a6e-9aff-9c28261beecd,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
e4e951cc-30ca-4a6e-9aff-9c28261beecd,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
7c9d42da-a575-4c7d-a0fe-f52ec5a95263,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Urobilinogen – Urobilinogen is normally present in urine in low concentrations. It is formed in the intestine from bilirubin, and a portion of it is absorbed back into the blood. Positive test results may indicate liver diseases such as viral hepatitis, cirrhosis, liver damage due to drugs or toxic substances, or conditions associated with increased RBC destruction (hemolytic anemia).",True,Chemical exam,,,,
b80f87cd-8fad-4be6-a728-69888ef213f0,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,2.1 References and resources,True,Chemical exam,,,,
c0c291bb-e400-4f98-a6be-34061f2e62df,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 27: Nutrition: Overview, Chapter 28: Micronutrients: Vitamins, Chapter 29: Micronutrients: Minerals.",True,Chemical exam,,,,
76290482-5ce0-4971-afb3-8f886f36028c,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 65–71.",True,Chemical exam,,,,
a5590281-2483-46ef-b4eb-0d18a0e7e03a,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a5590281-2483-46ef-b4eb-0d18a0e7e03a,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a5590281-2483-46ef-b4eb-0d18a0e7e03a,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
d827bfec-32e8-4515-966e-30ab672a709e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
d827bfec-32e8-4515-966e-30ab672a709e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
d827bfec-32e8-4515-966e-30ab672a709e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
9c9775e7-db3b-493a-9bc5-0e883cc64b13,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,2.2 Vitamins as Coenzymes,True,Chemical exam,,,,
2bafdd01-40eb-445f-94f6-f967cf8b05a9,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Nutritional basics,False,Nutritional basics,,,,
98ca8eef-56d5-4229-8d4b-1ead8c894809,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Many of the metabolic enzymes discussed in this course require essential coenzymes for optimal activity. An individual’s nutritional status has the potential to greatly influence their ability to efficiently oxidize fuels, and this can lead to deviations from clinical norms or illness, which would be illustrated on an individual’s CMP.",True,Nutritional basics,,,,
7d297b1a-1d2a-40e6-b3f4-eb8672394ed2,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"It is important to be aware of the presentation of these nutritional deficiencies as they can manifest as hypoglycemia, different types of anemia, or physiological symptoms.",True,Nutritional basics,,,,
bb2f8429-10b6-4933-9386-a2b3ae3ddef1,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Overview,False,Overview,,,,
b81eb85b-c146-401e-b30f-08e0ee0e1935,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Vitamins are organic compounds that, for the most part, we cannot synthesize through endogenous metabolism in adequate quantities (with the exceptions of vitamins B3, D, and K). To address these nutritional needs, we must consume vitamins as part of a balanced diet or supplement through a variety of mechanisms. Below are some key aspects of the roles vitamins play within metabolism and common symptoms associated with deficiencies (table 2.3).",True,Overview,,,,
9136f140-e832-4d8e-b2d6-0cbdcd9c71d9,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Water-soluble vitamins,False,Water-soluble vitamins,,,,
85c101b1-92de-454d-9375-24e21972f210,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Fat-soluble vitamins,False,Fat-soluble vitamins,,,,
68db61d2-3ff8-4ac8-90c5-14cebc982a59,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Folic acid,False,Folic acid,,,,
cf8c5c59-99fb-4032-b1ee-4180b289288e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Folic acid deficiency is a relatively common vitamin deficiency in the United States, presenting routinely as macrocytic anemia.",True,Folic acid,,,,
c0253e06-7e9e-434c-9247-02ecca2dbe66,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Cobalamin (vitamin B12),False,Cobalamin (vitamin B12),,,,
fa18d09a-dd16-43d0-b410-a6587c6a8231,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Vitamin B12 is required in humans for two essential enzymatic reactions.,True,Cobalamin (vitamin B12),,,,
8fabf47f-cebf-451c-8fae-499b7d16975d,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Ascorbic acid (vitamin C),False,Ascorbic acid (vitamin C),,,,
4bcb546d-b71e-49ba-9785-921a8fed0ae9,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,The active form of vitamin C is ascorbic acid.,False,The active form of vitamin C is ascorbic acid.,,,,
945e69cf-d8b6-43a7-b6e9-de1f13923660,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Pyridoxine (vitamin B6),False,Pyridoxine (vitamin B6),,,,
1368d3c4-b8cd-4298-b7ca-a4fd64a73f7e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Vitamin B6 is a term that encompasses all derivatives of pyridine including: pyridoxine, pyridoxal, and pyridoxamine.",True,Pyridoxine (vitamin B6),,,,
878e3379-9567-412a-bcf5-c836050e9286,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,6,False,6,,,,
fc0f7378-6a23-4e04-ab8a-3a6a0f56a683,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Thiamine (vitamin B1),False,Thiamine (vitamin B1),,,,
9744df18-4dea-440e-a569-78eb43db0ee9,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Thiamine pyrophosphate (TPP) is the biologically active form of thiamine and is generated by the transfer of a pyrophosphate group from adenosine triphosphate (ATP) to thiamine.,True,Thiamine (vitamin B1),,,,
0da3c9f3-9c79-48ee-a821-f129d8d7bc43,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Niacin (vitamin B3),False,Niacin (vitamin B3),,,,
542eae86-7ca9-45ad-99d9-2e1b47337945,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Niacin, or nicotinic acid, is a substituted pyridine derivative. The biologically active coenzyme forms are nicotinamide adenine dinucleotide (NAD+) and its phosphorylated derivative, nicotinamide adenine dinucleotide phosphate (NADP+).",True,Niacin (vitamin B3),,,,
74cfa167-ec90-4d5f-9fc0-cee2a6c86b24,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Riboflavin (vitamin B2),False,Riboflavin (vitamin B2),,,,
11e9f87c-075e-4d61-b78f-932bd01637e8,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"The two biologically active forms of B2 are flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), formed by the transfer of an adenosine monophosphate moiety from ATP to FMN.",True,Riboflavin (vitamin B2),,,,
d76a09f2-67b5-448d-9186-c8b03f012cb3,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Biotin (vitamin B7),False,Biotin (vitamin B7),,,,
8bab6572-dd22-44c1-b730-25e4c9ae6d0f,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Biotin is a coenzyme in carboxylation reactions, in which it serves as a carrier of activated carbon dioxide (coenzyme for acetylCoA carboxylase and pyruvate carboxylase).",True,Biotin (vitamin B7),,,,
fb7fdb64-ae38-4bd1-afa3-726eade802f5,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Pantothenic acid,False,Pantothenic acid,,,,
c9b5758e-2fa0-4d21-ade2-505747224ed5,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Pantothenic acid is a component of CoA, which functions in the transfer of acyl groups.",True,Pantothenic acid,,,,
a62e33c8-bb22-4161-a6c5-b5ae33b08140,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Vitamin A,False,Vitamin A,,,,
55bb746c-5703-48d4-a3fa-c02b1da1cda6,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,The retinoids are a family of molecules that are related to dietary retinol (vitamin A).,True,Vitamin A,,,,
d71bbaa3-7137-4164-bd15-263dda4919e0,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Vitamin D,False,Vitamin D,,,,
3164502f-2bec-49b5-a34f-1f00113a2217,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,The D vitamins are a group of sterols that have a hormone-like function.,True,Vitamin D,,,,
1917b3b6-35de-4874-be77-f878201f5a7b,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Vitamin K,False,Vitamin K,,,,
5ac1300b-6eab-4fd5-a76e-b463d71f07a1,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Vitamin E,False,Vitamin E,,,,
71f6a5a5-710d-4d43-85c2-a42a1256d074,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"The E vitamins consist of eight naturally occurring tocopherols, of which α-tocopherol is the most active.",True,Vitamin E,,,,
bb971741-2573-4d93-8f43-24df36d876b3,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Table 2.3: Summary table of vitamins.,True,Vitamin E,,,,
3dc8df1b-1d07-4179-9723-3fdaa67ca43f,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,2.2 References and resources,True,Vitamin E,,,,
c0b98084-557d-45f7-9560-3a44623e0e7a,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Text,False,Text,,,,
175d5875-6f06-4038-8540-99d328f4cc0e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
175d5875-6f06-4038-8540-99d328f4cc0e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
175d5875-6f06-4038-8540-99d328f4cc0e,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
1e01a86f-7701-468c-a38e-8505aaaae41d,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
1e01a86f-7701-468c-a38e-8505aaaae41d,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
1e01a86f-7701-468c-a38e-8505aaaae41d,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
0144333f-2d71-4df1-8017-91c71de54226,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,Tables,False,Tables,,,,
2b57c575-c182-45ac-8825-0adb3ee5bfde,https://pressbooks.lib.vt.edu/cellbio/,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-2,"Table 2.3 adapted from Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017.",True,Tables,,,,
8648af8d-3ed5-47dd-a5c8-e60adc06acb2,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"As a clinician, your first indication of changes to these cellular components will be illustrated by the signs and symptoms of your patient. Following this generalized assessment, you will begin to dissect out a clinical diagnosis by interpreting basic lab values. Each of these elements are indicative of molecular changes ultimately leading to the presentation you are challenged with.",True,Tables,,,,
e5303269-e112-4f28-b8b4-db95606e41db,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"How to read a CMP both clinically and biochemically will help hone the skills of diagnosis and maintenance of health status in patients. Additional laboratory tests such as a lipid profile, blood lactate, or urinalysis may also be ordered to supplement information from the CMP.",True,Tables,,,,
0e53fc27-0944-4762-baae-d555819eea54,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Deviations in any of these values can help determine changes in substrate availability, cofactors, and vitamin or enzymatic deficiencies. It will also help you better understand how biochemical pathways can influence clinical signs and symptoms.",True,Tables,,,,
300b5e35-ebb6-48b0-92dc-c36c9e258e85,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Comprehensive metabolic panel,False,Comprehensive metabolic panel,,,,
36f7a5d5-ba3d-45b4-bff0-f456112fcb8f,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,A CMP is often administered as part of a routine physical exam or for monitoring of specific conditions that impact kidney and liver functions. The results include the following tests (table 2.1):,True,Comprehensive metabolic panel,,,,
72316b7a-3235-4f77-a9c4-4cb65dbc83d0,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Table 2.1: Normal values for a typical comprehensive metabolic panel. These values will be given to you when evaluating information.,True,Comprehensive metabolic panel,,,,
e4e3e5a5-6621-44b4-9537-d2b38f2bdb4b,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Glucose – This energy source for the body is maintained in a very narrow range. Metabolic pathways are in place to balance both glucose uptake and glucose output to keep this value constant. Glucose homeostasis is regulated hormonally, and deviations from normal values could suggest metabolic or hormonal deficiencies (chapter 4 and chapter 5).",True,Comprehensive metabolic panel,,,,
5f754342-460d-4384-a71e-0c2faf0daf26,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Calcium – This is one of the most important minerals in the body; it is essential for the proper functioning of muscles, nerves, and cardiac tissue. It is a cofactor in processes such as blood clotting and bone formation. Other vitamins also play key roles in these pathways (vitamin K in clotting and vitamin D in bone formation), so understanding this value may give insights into other potential deficiencies.",True,Comprehensive metabolic panel,,,,
14327e77-dab5-4bf8-9007-809acfb8f0f4,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Proteins,False,Proteins,,,,
e1c4e4c3-44f9-436e-b4aa-4b8b07560f8f,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Albumin – Albumin is a major serum protein produced in the liver and is a nonspecific carrier of many lipid soluble vitamins and other hydrophobic compounds. It is also essential for maintaining oncotic pressure. Decreases in serum albumin may be suggestive of nutritional deficiencies or changes in plasma volume as well as poor liver function. Therefore accessibility of lipid soluble vitamins, minerals, and hormones may be diminished secondarily to a decrease in albumin.",True,Proteins,,,,
daa598c6-9608-487f-a361-5861729ccf8d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Total protein – Like serum albumin, a measure of total serum protein is useful to evaluate malnutrition or more chronic disorders such as inflammatory bowel disease. Increased production of immunoglobulins could also be detected here and would be indicative of chronic illness.",True,Proteins,,,,
a1a00c76-cfd0-4fd1-aad0-07c785afa74a,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Electrolytes,False,Electrolytes,,,,
a74027f4-843b-49ca-a32b-08715ce3d6e6,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Sodium – Sodium is vital to normal body processes, including nerve and muscle function. Hyponatremia can be suggestive of illness, diarrhea, or malnutrition, while hypernatremia is most often caused by an increased loss of water (dehydration) potentially due to endocrine disorders such as Cushing syndrome or diabetes insipidus.",True,Electrolytes,,,,
d2085234-264b-4ef6-91df-1e0c99a5aad3,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Potassium – Potassium is critical for cardiac function, and although hypo or hyperkalemia can be indicative of a variety of disorders, it can be a critical indicator of maintenance of diabetes. Unmanaged diabetic individuals may present with hyperkalemia, however, inappropriate insulin administration will increase potassium uptake. Therefore poor management can cause a sudden drop in potassium (hypokalemia) leading to cardiac dysfunction.",True,Electrolytes,,,,
09e0ef7f-4005-4510-9145-241e7794f120,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"CO2 (carbon dioxide, bicarbonate) – CO2 is produced from several oxidative pathways and is removed in the form of bicarbonate or through hemoglobin transport. Elevation of CO2 could suggest a renal, respiratory, and/or metabolic concern, and additional laboratory values would need to be assessed to determine the root cause. These may include blood lactate, blood urea nitrogen (BUN), as well as arteriole blood gasses (ABG).",True,Electrolytes,,,,
0dc52165-58e9-4292-ab1f-9666171b65c7,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Chloride – Chloride is a negatively charged ion that works with other electrolytes (potassium, sodium, and bicarbonate) to help regulate both fluid and acid–base (pH) balance in the body. Chloride and electrolyte tests may help diagnose the cause of signs and symptoms such as prolonged vomiting, diarrhea, weakness, and difficulty breathing (respiratory distress).",True,Electrolytes,,,,
1589cde9-ec8f-439a-a122-7e76aff434ba,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Kidney tests,False,Kidney tests,,,,
da19d572-45d6-4e0e-acb4-890f7b9f6ba2,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Blood urea nitrogen (BUN) – Urea is a waste product of amino acid metabolism filtered out of the blood by the kidneys. It is a primary means of nitrogen disposal, and conditions that affect the kidneys have the potential to affect the amount of urea in the blood. This value is also indicative of deficiencies in amino acid metabolism, or changes in urea cycle activity or protein catabolism (section 5.3).",True,Kidney tests,,,,
ca9e1192-3122-49ac-baa0-60ea970af802,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Creatinine – This waste product is produced in the muscles and filtered out by the kidneys. Urinary levels of creatinine are a good indicator of how the kidneys are working.,True,Kidney tests,,,,
035731bf-2f5b-4c5e-9fd8-4ce651062bd7,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Liver tests,False,Liver tests,,,,
66f7400a-bacc-4970-a5dd-120b82913a67,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Alkaline phosphatase (ALP) – ALP is an enzyme found in the liver and other tissues such as bone. Elevated levels of ALP are most commonly caused by liver disease or other pathologies that increase cell damage leading to the release of ALP in the blood. Other disorders that impact bone growth may also increase ALP.,True,Liver tests,,,,
584f7524-c0f0-4868-a4eb-1658d6eaa20f,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Alanine amino transferase (ALT) – ALT is an enzyme found predominantly in the liver and kidney. It is important in movement of ammonia (through the process of transamination) in tissues, and an elevation of ALT in circulation suggests liver damage (or potentially muscle damage) (section 5.3).",True,Liver tests,,,,
e83f4290-b862-419f-8016-0d40b7d16fb8,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Aspartate amino transferase (AST) – AST is also a transferase needed in nitrogen metabolism found especially within the heart and liver. It is also a useful test for detecting liver damage. The ratio of ALT/AST can be used to distinguish between disorders such as alcoholic versus nonalcoholic fatty liver disease (section 5.3).,True,Liver tests,,,,
a826dad6-9e5f-4d34-98bb-0a5c0fe2e0ba,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a826dad6-9e5f-4d34-98bb-0a5c0fe2e0ba,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a826dad6-9e5f-4d34-98bb-0a5c0fe2e0ba,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
b699d706-baeb-4f11-b25c-ba4bcbbd3048,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Lipid profile,False,Lipid profile,,,,
e75f1c70-fbd5-41e4-b72f-5dbe6a7bff5c,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,A lipid profile (table 2.2) is often used to assess risk of developing cardiovascular disease (CVD) or to monitor the effectiveness of a dietary or pharmacological intervention.,True,Lipid profile,,,,
116e542d-7701-4d77-9751-046050deac33,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Table 2.2: Desirable (optimal) values for lipids. Ranges of intermediate and high can also be found for these values.,True,Lipid profile,,,,
bdf71b7a-88ea-42b9-a409-cfd850b3653a,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Total cholesterol – This measurement takes in to account various forms of cholesterol in circulation. It is the total of high-density lipoprotein (HDL), low-density lipoprotein (LDL), and 20 percent of the triglyceride measurement. This is key to determining your cholesterol ratio (total/HDL), which should be below 5 with an ideal ratio being 3.5.",True,Lipid profile,,,,
c4c46aba-b10e-468e-84ca-44d094cc52bc,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,High-density lipoprotein cholesterol (HDL-C) – HDL is predominantly involved in reverse cholesterol transport because it removes excess cholesterol from peripheral tissues and carries it to the liver for removal or use. It has several key interactions with very low-density lipid (VLDL) particles in circulation that assist in lipid metabolism.,True,Lipid profile,,,,
2c1796e0-e5a7-40f3-9f79-f995478b191f,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Low-density lipoprotein cholesterol (LDL-C) – LDL is often called “bad cholesterol” because it can deposit excess cholesterol in walls of blood vessels, which can contribute to atherosclerosis.",True,Lipid profile,,,,
bac857e0-a70b-49fe-92cc-c91eb1af48c3,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Triglycerides – This is a measurement of circulating triacylglycerols (TAG), which are primarily transported by VLDL particles. TAG levels should be less than 150 mg/dL, and increased TAG may suggest endocrine deficiencies or metabolic defects.",True,Lipid profile,,,,
0a9b08f4-89dd-4ee6-bf41-f649d8b2f1d7,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Variations of normal in a lipid profile could be suggestive of heritable disorders, poor diet, or lipid uptake, decreased lipid storage, or excessive synthesis. The combination of these values will help determine what aspect of lipid metabolism is altered (chapter 6).",True,Lipid profile,,,,
d47c3ec5-b8af-4162-823e-3428fb5cd9e8,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Lactate,False,Lactate,,,,
b9591b0a-aa42-4351-b936-523c6c6b8458,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
b9591b0a-aa42-4351-b936-523c6c6b8458,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
b9591b0a-aa42-4351-b936-523c6c6b8458,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
2148dbac-3d0d-4690-aa79-c93da595b16b,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Urinalysis (includes a visual, chemical, and microscopic exam)",False,"Urinalysis (includes a visual, chemical, and microscopic exam)",,,,
9a5a1ed7-1779-450c-9d3e-46aacc9d6735,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Visual exam and the microscopic exam,False,Visual exam and the microscopic exam,,,,
2e249ca8-24e4-491d-a096-fa9549b2f4be,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Although both the visual and microscopic exam are very essential components to this analysis, these will not be focused on here. The color of urine can vary, most often shades of yellow, from very pale or colorless to very dark or amber. Red-colored urine can also occur when blood is present; yellow-brown or greenish-brown urine may be a sign of bilirubin in the urine. Urine clarity refers to how clear the urine is. This could be defined as: clear, slightly cloudy, cloudy, or turbid. “Normal” urine can be clear or cloudy.",True,Visual exam and the microscopic exam,,,,
6b0d888c-02c1-499c-81d2-2c8825b63d06,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"A microscopic examination will typically be done when there are abnormal findings on the physical or chemical examination. Cells and other substances that may be seen include the following: red blood cells (RBCs), white blood cells (WBCs), epithelial cells, bacteria, yeast and parasites, trichomonas, casts, and crystals. If the crystals are from substances that are not normally in the urine, they are considered “abnormal.” Abnormal crystals may indicate an abnormal metabolic process. Some of these include: calcium carbonate, cystine, tyrosine, and leucine. Urinary presence of some amino acids can be suggestive of amino acid metabolic disorders (chapter 8).",True,Visual exam and the microscopic exam,,,,
3f36602c-f8f0-4261-999f-d217de037ef6,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Chemical exam,False,Chemical exam,,,,
5506f6a1-db3a-4e81-8c24-4f1f496d192a,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Much like the CMP, the chemical analysis of a urine sample can be very indicative of biochemical derangement. A review of the following components is helpful in making a clinical diagnosis.",True,Chemical exam,,,,
d3ed5811-c2ca-44ca-a5e4-2bf48a55d6da,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Specific gravity (SG) – Specific gravity is a measure of urine concentration. This test simply indicates how concentrated the urine is.,True,Chemical exam,,,,
1468b982-4369-4478-a38f-4e0a4c4b6223,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"pH – Urine is typically slightly acidic, about pH 6, but can range from 4.5 to 8. The kidneys play an important role in maintaining the acid–base balance of the body. Therefore, any condition that produces acids or bases in the body, such as acidosis or alkalosis, or the ingestion of acidic or basic foods, can directly affect urine pH.",True,Chemical exam,,,,
1be69cd8-df7b-4f16-bab9-ac8b130acc6e,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Protein – The protein test provides an estimate of the amount of albumin in the urine. Normally, there should be no protein (or a small amount of protein) in the urine. When urine protein is elevated, a person has a condition called proteinuria; this could be caused by a variety of health conditions. Healthy people can have temporary or persistent proteinuria due to stress, exercise, fever, aspirin therapy, or exposure to cold, for example.",True,Chemical exam,,,,
39bfd682-cedf-417f-b0b5-b39a3b877556,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Glucose – Glucose is normally not present in urine. When glucose is present, the condition is called glucosuria. This condition can result from either an excessively high glucose level in the blood, such as may be seen in individuals with uncontrolled diabetes. Other reducing sugars, galactose or fructose, may also be present in the urine if a metabolic deficiency occurs (section 9.1).",True,Chemical exam,,,,
1ef096cd-eff1-4283-9378-c0fa5e2019f8,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Some other conditions that can cause glucosuria include hormonal disorders, liver disease, medications, and pregnancy. When glucosuria occurs, other tests such as a fasting blood glucose test are usually performed to further identify the specific cause.",True,Chemical exam,,,,
4a30ed86-9922-4b40-985d-52ae3e21bffe,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Ketones – Ketones are also not normally found in the urine. They are intermediate products of fat metabolism and can be produced when an individual does not eat enough carbohydrates such as in fasting conditions or high-protein diets. When carbohydrates are not available, the body metabolizes fat to generate ATP for baseline metabolic function. Strenuous exercise, exposure to cold, frequent, prolonged vomiting, and several digestive system diseases can also increase fat metabolism, resulting in ketonuria (section 5.2).",True,Chemical exam,,,,
b5557f88-6013-4a7e-bdf8-b6585c54402b,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"In a person who has diabetes, ketones in urine may be an early indication of insufficient insulin. Insufficient insulin response can result in impaired glucose oxidation and consequently results in aberrant fat metabolism. Oxidation of fatty acids provides substrate for ketogenesis, which can cause ketosis and potentially progress to ketoacidosis, a form of metabolic acidosis. Excess ketones and glucose are dumped into the urine by the kidneys in an effort to flush them from the body.",True,Chemical exam,,,,
d8e84c0c-531b-45a8-b134-ae03a063c08d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Hemoglobin and myoglobin – The presence of hemoglobin in urine indicates blood in the urine (known as hematuria).,True,Chemical exam,,,,
2b63182e-6b88-4f00-840d-b1929f9006a8,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"A small number of RBCs are normally present in urine, however, as these numbers elevate, this will result in a positive test result. These results are interpreted with the microscopic exam. For example, a positive test result here with no visible RBCs in the urine would suggest the presence of myoglobin only, which could be due to strenuous exercise or muscle damage.",True,Chemical exam,,,,
cdc4c20e-6c76-42ef-80d8-7ec24aa715c1,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Leukocyte esterase – Leukocyte esterase is an enzyme present in most white blood cells (WBCs). A few white blood cells are normally present in urine, however, when the number of WBCs in urine increases significantly, this screening test will become positive. When this test is positive and/or the WBC count in urine is high, it may indicate that there is inflammation in the urinary tract or kidneys.",True,Chemical exam,,,,
4571d5b5-e22f-435b-826c-19d673aafdf0,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Nitrite – Many normal bacteria can convert nitrate (normally present in urine) to nitrite (not normally present in urine). When bacteria are present in the urinary tract, they can cause a urinary tract infection, which could be diagnosed by a positive nitrite test result.",True,Chemical exam,,,,
c7c28693-ef26-47ac-8ab5-6f4d2b11f73e,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
c7c28693-ef26-47ac-8ab5-6f4d2b11f73e,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
c7c28693-ef26-47ac-8ab5-6f4d2b11f73e,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
222880cd-6e8e-4d44-97db-fbccdc529a12,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Urobilinogen – Urobilinogen is normally present in urine in low concentrations. It is formed in the intestine from bilirubin, and a portion of it is absorbed back into the blood. Positive test results may indicate liver diseases such as viral hepatitis, cirrhosis, liver damage due to drugs or toxic substances, or conditions associated with increased RBC destruction (hemolytic anemia).",True,Chemical exam,,,,
ec680de5-f07b-43c7-aa70-1c82aca3a32f,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,2.1 References and resources,True,Chemical exam,,,,
5366db64-2949-42dd-b0e0-4c97dc7f1e3d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 27: Nutrition: Overview, Chapter 28: Micronutrients: Vitamins, Chapter 29: Micronutrients: Minerals.",True,Chemical exam,,,,
a66a3d60-64da-4905-b205-9cc13654a183,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 65–71.",True,Chemical exam,,,,
a2f72ef8-f61f-4036-a6bc-d758e7af2384,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a2f72ef8-f61f-4036-a6bc-d758e7af2384,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
a2f72ef8-f61f-4036-a6bc-d758e7af2384,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
d365aad6-7f47-4c30-9bee-77f1132305e2,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
d365aad6-7f47-4c30-9bee-77f1132305e2,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
d365aad6-7f47-4c30-9bee-77f1132305e2,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
964dbcab-fb09-4699-be06-e5e5ac8e0c5b,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,2.2 Vitamins as Coenzymes,True,Chemical exam,,,,
b0180cea-beb3-4d81-a128-bb20b9fc7c39,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Nutritional basics,False,Nutritional basics,,,,
3e81b2ed-b54c-40eb-847d-92844abd8044,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Many of the metabolic enzymes discussed in this course require essential coenzymes for optimal activity. An individual’s nutritional status has the potential to greatly influence their ability to efficiently oxidize fuels, and this can lead to deviations from clinical norms or illness, which would be illustrated on an individual’s CMP.",True,Nutritional basics,,,,
50a73eaf-7b53-4501-a836-869f2db0472f,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"It is important to be aware of the presentation of these nutritional deficiencies as they can manifest as hypoglycemia, different types of anemia, or physiological symptoms.",True,Nutritional basics,,,,
685ec16a-65b8-489c-a2e9-441064499494,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Overview,False,Overview,,,,
24189c82-44a1-4abd-b294-c49a0620e9b0,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Vitamins are organic compounds that, for the most part, we cannot synthesize through endogenous metabolism in adequate quantities (with the exceptions of vitamins B3, D, and K). To address these nutritional needs, we must consume vitamins as part of a balanced diet or supplement through a variety of mechanisms. Below are some key aspects of the roles vitamins play within metabolism and common symptoms associated with deficiencies (table 2.3).",True,Overview,,,,
f56ac9e7-442b-4559-afec-2cde124b3803,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Water-soluble vitamins,False,Water-soluble vitamins,,,,
d846bd92-afde-464d-9f8e-4b301627d384,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Fat-soluble vitamins,False,Fat-soluble vitamins,,,,
787721cd-865f-4660-b105-0416b8da39ad,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Folic acid,False,Folic acid,,,,
844595a8-15ad-4a14-83fa-6fea0af0823b,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Folic acid deficiency is a relatively common vitamin deficiency in the United States, presenting routinely as macrocytic anemia.",True,Folic acid,,,,
94414981-b929-4437-8ae5-743a4e91f62d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Cobalamin (vitamin B12),False,Cobalamin (vitamin B12),,,,
8bb6dd44-7a2a-40cf-8692-0400bdfdc7d5,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Vitamin B12 is required in humans for two essential enzymatic reactions.,True,Cobalamin (vitamin B12),,,,
893cfd8d-ea27-462f-86fd-fe87b4160777,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Ascorbic acid (vitamin C),False,Ascorbic acid (vitamin C),,,,
69f7e51a-5eeb-4dfc-8bed-cb43967c6ab6,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,The active form of vitamin C is ascorbic acid.,False,The active form of vitamin C is ascorbic acid.,,,,
8745e940-ef3a-4a18-87ee-ad11d26a4d78,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Pyridoxine (vitamin B6),False,Pyridoxine (vitamin B6),,,,
80baa88a-84b9-4ec9-946d-117f001f9a46,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Vitamin B6 is a term that encompasses all derivatives of pyridine including: pyridoxine, pyridoxal, and pyridoxamine.",True,Pyridoxine (vitamin B6),,,,
0c5c8b2e-1251-49f4-b779-256dc1d8ee09,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,6,False,6,,,,
d41fe3c2-060c-41c8-832e-2dcf2389a940,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Thiamine (vitamin B1),False,Thiamine (vitamin B1),,,,
876b9e10-b21f-43bd-a97d-200f5121e83c,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Thiamine pyrophosphate (TPP) is the biologically active form of thiamine and is generated by the transfer of a pyrophosphate group from adenosine triphosphate (ATP) to thiamine.,True,Thiamine (vitamin B1),,,,
7408a3dc-1924-4ec0-9899-2be43759c562,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Niacin (vitamin B3),False,Niacin (vitamin B3),,,,
0ce9e7c7-bab7-45a4-951a-f9809ce0d3a1,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Niacin, or nicotinic acid, is a substituted pyridine derivative. The biologically active coenzyme forms are nicotinamide adenine dinucleotide (NAD+) and its phosphorylated derivative, nicotinamide adenine dinucleotide phosphate (NADP+).",True,Niacin (vitamin B3),,,,
4caf3ea0-1ace-424f-97d7-995747dde901,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Riboflavin (vitamin B2),False,Riboflavin (vitamin B2),,,,
1631e44a-d935-41bd-90a6-06f037c477fc,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"The two biologically active forms of B2 are flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), formed by the transfer of an adenosine monophosphate moiety from ATP to FMN.",True,Riboflavin (vitamin B2),,,,
194298de-d167-4c6e-9f85-50d4f180eff2,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Biotin (vitamin B7),False,Biotin (vitamin B7),,,,
82e67fe1-400e-46ca-af4b-31712964396d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Biotin is a coenzyme in carboxylation reactions, in which it serves as a carrier of activated carbon dioxide (coenzyme for acetylCoA carboxylase and pyruvate carboxylase).",True,Biotin (vitamin B7),,,,
648261ec-029b-4534-bed5-81084697c20a,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Pantothenic acid,False,Pantothenic acid,,,,
d18327d9-52da-435d-97f7-b536870adc36,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Pantothenic acid is a component of CoA, which functions in the transfer of acyl groups.",True,Pantothenic acid,,,,
c13846ce-c043-4758-8442-145c4c6f44d7,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Vitamin A,False,Vitamin A,,,,
ad0d3f4d-6826-4a08-baf4-756c87184517,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,The retinoids are a family of molecules that are related to dietary retinol (vitamin A).,True,Vitamin A,,,,
21821644-00bc-48bf-944e-ba3215ac22c3,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Vitamin D,False,Vitamin D,,,,
fff6ff82-5e26-462d-9198-577129a79a80,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,The D vitamins are a group of sterols that have a hormone-like function.,True,Vitamin D,,,,
6f6b5a60-613f-4150-8179-fcf8abfc7dab,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Vitamin K,False,Vitamin K,,,,
89b3f231-518c-4acf-82b3-cfa5ba02d39a,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Vitamin E,False,Vitamin E,,,,
0b72ab03-932b-4bb7-8089-2826f8b8b7fd,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"The E vitamins consist of eight naturally occurring tocopherols, of which α-tocopherol is the most active.",True,Vitamin E,,,,
8070c503-fa20-4a8d-b60a-8b54b6246cc4,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Table 2.3: Summary table of vitamins.,True,Vitamin E,,,,
b6217073-a144-4e80-a0ce-e86a98b6d9c7,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,2.2 References and resources,True,Vitamin E,,,,
23e426b2-e93c-4521-a3c9-3b2e6ab1c9c2,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Text,False,Text,,,,
3497d1b9-6bf0-46cc-a9c2-5009d334ae6d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
3497d1b9-6bf0-46cc-a9c2-5009d334ae6d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
3497d1b9-6bf0-46cc-a9c2-5009d334ae6d,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
2b48aeff-ecd6-43bc-b524-4591954b1156,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
2b48aeff-ecd6-43bc-b524-4591954b1156,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
2b48aeff-ecd6-43bc-b524-4591954b1156,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
a741570f-6de9-4468-9c2e-2f2f1db8d280,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,Tables,False,Tables,,,,
fbae55e1-0ea3-4ca7-8fd4-d3e172cce53a,https://pressbooks.lib.vt.edu/cellbio/,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/#chapter-22-section-1,"Table 2.3 adapted from Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017.",True,Tables,,,,
fd2a3fb5-d9b7-4623-99d0-bc46b16181dd,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"As a clinician, your first indication of changes to these cellular components will be illustrated by the signs and symptoms of your patient. Following this generalized assessment, you will begin to dissect out a clinical diagnosis by interpreting basic lab values. Each of these elements are indicative of molecular changes ultimately leading to the presentation you are challenged with.",True,Tables,,,,
987fbce1-f7aa-48c2-bcd2-6859f64f34cf,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"How to read a CMP both clinically and biochemically will help hone the skills of diagnosis and maintenance of health status in patients. Additional laboratory tests such as a lipid profile, blood lactate, or urinalysis may also be ordered to supplement information from the CMP.",True,Tables,,,,
303ff1da-baa6-47f9-b423-bf1afb453560,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Deviations in any of these values can help determine changes in substrate availability, cofactors, and vitamin or enzymatic deficiencies. It will also help you better understand how biochemical pathways can influence clinical signs and symptoms.",True,Tables,,,,
d37b131f-cd54-45de-a3ae-263225658df6,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Comprehensive metabolic panel,False,Comprehensive metabolic panel,,,,
fedea9cd-a918-4d2b-804b-c8a4aa9c0d77,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,A CMP is often administered as part of a routine physical exam or for monitoring of specific conditions that impact kidney and liver functions. The results include the following tests (table 2.1):,True,Comprehensive metabolic panel,,,,
61a84758-a279-41e7-84ca-7e74518f994f,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Table 2.1: Normal values for a typical comprehensive metabolic panel. These values will be given to you when evaluating information.,True,Comprehensive metabolic panel,,,,
9562bc4d-4534-4caa-8037-4058ed82b0ef,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Glucose – This energy source for the body is maintained in a very narrow range. Metabolic pathways are in place to balance both glucose uptake and glucose output to keep this value constant. Glucose homeostasis is regulated hormonally, and deviations from normal values could suggest metabolic or hormonal deficiencies (chapter 4 and chapter 5).",True,Comprehensive metabolic panel,,,,
9cc174ef-b253-4b23-8199-be9fb215423a,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Calcium – This is one of the most important minerals in the body; it is essential for the proper functioning of muscles, nerves, and cardiac tissue. It is a cofactor in processes such as blood clotting and bone formation. Other vitamins also play key roles in these pathways (vitamin K in clotting and vitamin D in bone formation), so understanding this value may give insights into other potential deficiencies.",True,Comprehensive metabolic panel,,,,
bd379828-789e-4941-9915-e371becf1791,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Proteins,False,Proteins,,,,
7f62b4d8-e4e8-486e-9c49-e77c3ff3876d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Albumin – Albumin is a major serum protein produced in the liver and is a nonspecific carrier of many lipid soluble vitamins and other hydrophobic compounds. It is also essential for maintaining oncotic pressure. Decreases in serum albumin may be suggestive of nutritional deficiencies or changes in plasma volume as well as poor liver function. Therefore accessibility of lipid soluble vitamins, minerals, and hormones may be diminished secondarily to a decrease in albumin.",True,Proteins,,,,
2dd89441-cb0d-4bf4-bc82-282a2278a76b,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Total protein – Like serum albumin, a measure of total serum protein is useful to evaluate malnutrition or more chronic disorders such as inflammatory bowel disease. Increased production of immunoglobulins could also be detected here and would be indicative of chronic illness.",True,Proteins,,,,
e44c35c7-2c32-4acc-b249-5bb970d31bb5,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Electrolytes,False,Electrolytes,,,,
dbfe4018-0e66-41c6-a8ed-b2bdd2e7c971,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Sodium – Sodium is vital to normal body processes, including nerve and muscle function. Hyponatremia can be suggestive of illness, diarrhea, or malnutrition, while hypernatremia is most often caused by an increased loss of water (dehydration) potentially due to endocrine disorders such as Cushing syndrome or diabetes insipidus.",True,Electrolytes,,,,
b151485d-1a67-4e72-bad8-7499a1b46c1a,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Potassium – Potassium is critical for cardiac function, and although hypo or hyperkalemia can be indicative of a variety of disorders, it can be a critical indicator of maintenance of diabetes. Unmanaged diabetic individuals may present with hyperkalemia, however, inappropriate insulin administration will increase potassium uptake. Therefore poor management can cause a sudden drop in potassium (hypokalemia) leading to cardiac dysfunction.",True,Electrolytes,,,,
fbc05da5-c534-41bd-8388-a0db61bdeb6d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"CO2 (carbon dioxide, bicarbonate) – CO2 is produced from several oxidative pathways and is removed in the form of bicarbonate or through hemoglobin transport. Elevation of CO2 could suggest a renal, respiratory, and/or metabolic concern, and additional laboratory values would need to be assessed to determine the root cause. These may include blood lactate, blood urea nitrogen (BUN), as well as arteriole blood gasses (ABG).",True,Electrolytes,,,,
7dcebed2-228f-4d73-b706-58ac1c20ba84,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Chloride – Chloride is a negatively charged ion that works with other electrolytes (potassium, sodium, and bicarbonate) to help regulate both fluid and acid–base (pH) balance in the body. Chloride and electrolyte tests may help diagnose the cause of signs and symptoms such as prolonged vomiting, diarrhea, weakness, and difficulty breathing (respiratory distress).",True,Electrolytes,,,,
a00c9b90-020f-451f-ab37-a408250e2159,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Kidney tests,False,Kidney tests,,,,
bcde02b7-b7c8-497f-b331-16ad6c7b63d8,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Blood urea nitrogen (BUN) – Urea is a waste product of amino acid metabolism filtered out of the blood by the kidneys. It is a primary means of nitrogen disposal, and conditions that affect the kidneys have the potential to affect the amount of urea in the blood. This value is also indicative of deficiencies in amino acid metabolism, or changes in urea cycle activity or protein catabolism (section 5.3).",True,Kidney tests,,,,
ff2080e9-1fd3-4001-a448-4b8d61520832,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Creatinine – This waste product is produced in the muscles and filtered out by the kidneys. Urinary levels of creatinine are a good indicator of how the kidneys are working.,True,Kidney tests,,,,
08355f70-9e25-4645-8343-3caaa4ed34f8,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Liver tests,False,Liver tests,,,,
3a603e2b-d691-4e05-80e1-1a356353ea32,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Alkaline phosphatase (ALP) – ALP is an enzyme found in the liver and other tissues such as bone. Elevated levels of ALP are most commonly caused by liver disease or other pathologies that increase cell damage leading to the release of ALP in the blood. Other disorders that impact bone growth may also increase ALP.,True,Liver tests,,,,
9c1c18e0-a8ce-4819-a2ae-98c9d6383ddc,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Alanine amino transferase (ALT) – ALT is an enzyme found predominantly in the liver and kidney. It is important in movement of ammonia (through the process of transamination) in tissues, and an elevation of ALT in circulation suggests liver damage (or potentially muscle damage) (section 5.3).",True,Liver tests,,,,
f829e610-6521-4e0b-9a71-8d943ba7ecf5,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Aspartate amino transferase (AST) – AST is also a transferase needed in nitrogen metabolism found especially within the heart and liver. It is also a useful test for detecting liver damage. The ratio of ALT/AST can be used to distinguish between disorders such as alcoholic versus nonalcoholic fatty liver disease (section 5.3).,True,Liver tests,,,,
61cedbca-44f1-4bae-9d73-5b57527d86f4,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
61cedbca-44f1-4bae-9d73-5b57527d86f4,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
61cedbca-44f1-4bae-9d73-5b57527d86f4,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Bilirubin – Bilirubin is a waste product produced by the degradation of heme. Heme degradation within the liver is a normal part of red blood cell turnover, but elevated bilirubin could also be indicative of excessive hemolysis (due to deficiencies in NAPDH or increased oxidative stress) or biliary obstructions. Bilirubin values can be reported as direct (conjugated) or indirect (unconjugated) bilirubin. As conjugation takes place in the liver, decreased conjugated bilirubin or increased unconjugated bilirubin would suggest liver dysfunction (figure 2.1).",True,Liver tests,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
725b50e3-2f44-4c47-90ac-e4b6c7664c79,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Lipid profile,False,Lipid profile,,,,
e96543e5-c926-4f71-a05a-2761a1ffdbc8,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,A lipid profile (table 2.2) is often used to assess risk of developing cardiovascular disease (CVD) or to monitor the effectiveness of a dietary or pharmacological intervention.,True,Lipid profile,,,,
9ccaff9d-07a0-4cce-ae8c-7dd7fe0d7fee,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Table 2.2: Desirable (optimal) values for lipids. Ranges of intermediate and high can also be found for these values.,True,Lipid profile,,,,
a379540d-9210-4aef-8b89-332e31038a87,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Total cholesterol – This measurement takes in to account various forms of cholesterol in circulation. It is the total of high-density lipoprotein (HDL), low-density lipoprotein (LDL), and 20 percent of the triglyceride measurement. This is key to determining your cholesterol ratio (total/HDL), which should be below 5 with an ideal ratio being 3.5.",True,Lipid profile,,,,
3b2a561b-07a6-47f9-a80b-641f387e92e0,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,High-density lipoprotein cholesterol (HDL-C) – HDL is predominantly involved in reverse cholesterol transport because it removes excess cholesterol from peripheral tissues and carries it to the liver for removal or use. It has several key interactions with very low-density lipid (VLDL) particles in circulation that assist in lipid metabolism.,True,Lipid profile,,,,
c43b2e30-c54a-46fb-882d-7c589f51588d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Low-density lipoprotein cholesterol (LDL-C) – LDL is often called “bad cholesterol” because it can deposit excess cholesterol in walls of blood vessels, which can contribute to atherosclerosis.",True,Lipid profile,,,,
e6f568df-4097-4d7c-a5c7-4d120459c99d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Triglycerides – This is a measurement of circulating triacylglycerols (TAG), which are primarily transported by VLDL particles. TAG levels should be less than 150 mg/dL, and increased TAG may suggest endocrine deficiencies or metabolic defects.",True,Lipid profile,,,,
79e2fc6b-6aae-4276-9e25-f05f9721adfe,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Variations of normal in a lipid profile could be suggestive of heritable disorders, poor diet, or lipid uptake, decreased lipid storage, or excessive synthesis. The combination of these values will help determine what aspect of lipid metabolism is altered (chapter 6).",True,Lipid profile,,,,
07120320-14fc-4f4f-a99e-eaa5e2bc0258,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Lactate,False,Lactate,,,,
4d81b93d-dd28-4eee-ae5c-76571e3dfb93,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
4d81b93d-dd28-4eee-ae5c-76571e3dfb93,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
4d81b93d-dd28-4eee-ae5c-76571e3dfb93,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Serum lactate levels may also be measured in conjunction with a complete metabolic panel. Serum lactate should be negligible under normal conditions, however, elevated lactate could be suggestive of excessive anaerobic metabolism, such as is the case in intense exercise or deficiency in oxygen transport caused by ischemic injury. This could also be caused by inappropriate diversion of substrate such as is the case in some enzymatic deficiencies (pyruvate dehydrogenase deficiency) or changes in NADH levels (figure 2.2).",True,Lactate,Figure 2.2,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
f8ad0a7d-4de3-4bdb-b10e-1054357db5d3,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Urinalysis (includes a visual, chemical, and microscopic exam)",False,"Urinalysis (includes a visual, chemical, and microscopic exam)",,,,
00d8b977-f1b9-45de-abc5-6d5ca8ec76c8,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Visual exam and the microscopic exam,False,Visual exam and the microscopic exam,,,,
2d3d53e6-79c3-4f01-96c2-6a6ad9612abd,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Although both the visual and microscopic exam are very essential components to this analysis, these will not be focused on here. The color of urine can vary, most often shades of yellow, from very pale or colorless to very dark or amber. Red-colored urine can also occur when blood is present; yellow-brown or greenish-brown urine may be a sign of bilirubin in the urine. Urine clarity refers to how clear the urine is. This could be defined as: clear, slightly cloudy, cloudy, or turbid. “Normal” urine can be clear or cloudy.",True,Visual exam and the microscopic exam,,,,
c1c083b8-679e-435c-a902-a00582171b17,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"A microscopic examination will typically be done when there are abnormal findings on the physical or chemical examination. Cells and other substances that may be seen include the following: red blood cells (RBCs), white blood cells (WBCs), epithelial cells, bacteria, yeast and parasites, trichomonas, casts, and crystals. If the crystals are from substances that are not normally in the urine, they are considered “abnormal.” Abnormal crystals may indicate an abnormal metabolic process. Some of these include: calcium carbonate, cystine, tyrosine, and leucine. Urinary presence of some amino acids can be suggestive of amino acid metabolic disorders (chapter 8).",True,Visual exam and the microscopic exam,,,,
cbffe06e-a6b3-446d-8ada-c7b52634f4b6,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Chemical exam,False,Chemical exam,,,,
51930fd3-1627-4884-a121-549df201b78a,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Much like the CMP, the chemical analysis of a urine sample can be very indicative of biochemical derangement. A review of the following components is helpful in making a clinical diagnosis.",True,Chemical exam,,,,
c48f16aa-7eee-4860-8151-3d4b8bf71c85,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Specific gravity (SG) – Specific gravity is a measure of urine concentration. This test simply indicates how concentrated the urine is.,True,Chemical exam,,,,
21777b90-17ef-4652-bbc7-9cd3221a2e74,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"pH – Urine is typically slightly acidic, about pH 6, but can range from 4.5 to 8. The kidneys play an important role in maintaining the acid–base balance of the body. Therefore, any condition that produces acids or bases in the body, such as acidosis or alkalosis, or the ingestion of acidic or basic foods, can directly affect urine pH.",True,Chemical exam,,,,
d7e45fe8-0dc2-4a5c-a396-4bf621a0be10,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Protein – The protein test provides an estimate of the amount of albumin in the urine. Normally, there should be no protein (or a small amount of protein) in the urine. When urine protein is elevated, a person has a condition called proteinuria; this could be caused by a variety of health conditions. Healthy people can have temporary or persistent proteinuria due to stress, exercise, fever, aspirin therapy, or exposure to cold, for example.",True,Chemical exam,,,,
f8c800e6-ad78-45fd-a614-8c05430fd5b0,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Glucose – Glucose is normally not present in urine. When glucose is present, the condition is called glucosuria. This condition can result from either an excessively high glucose level in the blood, such as may be seen in individuals with uncontrolled diabetes. Other reducing sugars, galactose or fructose, may also be present in the urine if a metabolic deficiency occurs (section 9.1).",True,Chemical exam,,,,
79ce912b-7c33-4f19-b60a-4fd816ceb1fd,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Some other conditions that can cause glucosuria include hormonal disorders, liver disease, medications, and pregnancy. When glucosuria occurs, other tests such as a fasting blood glucose test are usually performed to further identify the specific cause.",True,Chemical exam,,,,
d91bd840-4ad0-4bf0-a684-1de55f31fd48,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Ketones – Ketones are also not normally found in the urine. They are intermediate products of fat metabolism and can be produced when an individual does not eat enough carbohydrates such as in fasting conditions or high-protein diets. When carbohydrates are not available, the body metabolizes fat to generate ATP for baseline metabolic function. Strenuous exercise, exposure to cold, frequent, prolonged vomiting, and several digestive system diseases can also increase fat metabolism, resulting in ketonuria (section 5.2).",True,Chemical exam,,,,
4990773d-9464-4dbb-9290-46fc1556c55f,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"In a person who has diabetes, ketones in urine may be an early indication of insufficient insulin. Insufficient insulin response can result in impaired glucose oxidation and consequently results in aberrant fat metabolism. Oxidation of fatty acids provides substrate for ketogenesis, which can cause ketosis and potentially progress to ketoacidosis, a form of metabolic acidosis. Excess ketones and glucose are dumped into the urine by the kidneys in an effort to flush them from the body.",True,Chemical exam,,,,
9185056c-3110-459c-aa13-7d379c996246,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Hemoglobin and myoglobin – The presence of hemoglobin in urine indicates blood in the urine (known as hematuria).,True,Chemical exam,,,,
5856b9ad-0db2-4ec9-ab11-652b113d5ba3,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"A small number of RBCs are normally present in urine, however, as these numbers elevate, this will result in a positive test result. These results are interpreted with the microscopic exam. For example, a positive test result here with no visible RBCs in the urine would suggest the presence of myoglobin only, which could be due to strenuous exercise or muscle damage.",True,Chemical exam,,,,
08dfbdb7-ecfe-4413-b16c-c803204ad317,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Leukocyte esterase – Leukocyte esterase is an enzyme present in most white blood cells (WBCs). A few white blood cells are normally present in urine, however, when the number of WBCs in urine increases significantly, this screening test will become positive. When this test is positive and/or the WBC count in urine is high, it may indicate that there is inflammation in the urinary tract or kidneys.",True,Chemical exam,,,,
b7db0347-92c0-4e90-9dec-9135c53568b0,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Nitrite – Many normal bacteria can convert nitrate (normally present in urine) to nitrite (not normally present in urine). When bacteria are present in the urinary tract, they can cause a urinary tract infection, which could be diagnosed by a positive nitrite test result.",True,Chemical exam,,,,
0ac0ef3e-34f6-41aa-b913-5fbcd4428115,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
0ac0ef3e-34f6-41aa-b913-5fbcd4428115,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
0ac0ef3e-34f6-41aa-b913-5fbcd4428115,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Bilirubin – Bilirubin is not present in the urine of healthy individuals (figure 2.1). The presence of bilirubin in urine is an early indicator of liver disease and can occur before clinical symptoms such as jaundice develop. Only conjugated bilirubin is present in the urine.,True,Chemical exam,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
709429f7-c7a1-45e9-9b3b-ec7e1355f3ed,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Urobilinogen – Urobilinogen is normally present in urine in low concentrations. It is formed in the intestine from bilirubin, and a portion of it is absorbed back into the blood. Positive test results may indicate liver diseases such as viral hepatitis, cirrhosis, liver damage due to drugs or toxic substances, or conditions associated with increased RBC destruction (hemolytic anemia).",True,Chemical exam,,,,
9e9909b5-8454-46de-9ba2-49f6c14d154b,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,2.1 References and resources,True,Chemical exam,,,,
163fa5eb-d158-4c38-826c-0a08ba305970,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 27: Nutrition: Overview, Chapter 28: Micronutrients: Vitamins, Chapter 29: Micronutrients: Minerals.",True,Chemical exam,,,,
be88f49f-16a7-4bf7-827e-c7ad70dcb06a,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Le, T., and V. Bhushan. First Aid for the USMLE Step 1, 29th ed. New York: McGraw Hill Education, 2018, 65–71.",True,Chemical exam,,,,
ab0c08ff-ed98-4a84-9b0d-82f8eec08909,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
ab0c08ff-ed98-4a84-9b0d-82f8eec08909,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
ab0c08ff-ed98-4a84-9b0d-82f8eec08909,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.1 Heme degradation. 2021. https://archive.org/details/2.2_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.1,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
981c9143-4405-4e31-85a6-44dbc5538302,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
981c9143-4405-4e31-85a6-44dbc5538302,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
981c9143-4405-4e31-85a6-44dbc5538302,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.2 Reaction catalyzed by lactate dehydrogenase. 2021. https://archive.org/details/2.4_20210924. CC BY 4.0.",True,Chemical exam,Figure 2.2,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
5d765ac7-7c1e-44ac-b424-003b505ad1e9,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,2.2 Vitamins as Coenzymes,True,Chemical exam,,,,
8983e3ea-5020-41f8-8199-ca5b7fa15638,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Nutritional basics,False,Nutritional basics,,,,
043351bf-e937-41ff-938b-38335b4f1288,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Many of the metabolic enzymes discussed in this course require essential coenzymes for optimal activity. An individual’s nutritional status has the potential to greatly influence their ability to efficiently oxidize fuels, and this can lead to deviations from clinical norms or illness, which would be illustrated on an individual’s CMP.",True,Nutritional basics,,,,
49e5c119-4e0f-469c-a63f-296d7c4b2a95,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"It is important to be aware of the presentation of these nutritional deficiencies as they can manifest as hypoglycemia, different types of anemia, or physiological symptoms.",True,Nutritional basics,,,,
95246dbe-e497-4608-bf49-dfd86b6b6730,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Overview,False,Overview,,,,
40e32c3c-d959-4abb-a43b-e826c6a56bf5,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Vitamins are organic compounds that, for the most part, we cannot synthesize through endogenous metabolism in adequate quantities (with the exceptions of vitamins B3, D, and K). To address these nutritional needs, we must consume vitamins as part of a balanced diet or supplement through a variety of mechanisms. Below are some key aspects of the roles vitamins play within metabolism and common symptoms associated with deficiencies (table 2.3).",True,Overview,,,,
a26edb58-737c-4306-b415-51ef73eb0a07,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Water-soluble vitamins,False,Water-soluble vitamins,,,,
c8bd963d-d1fc-4ea6-9fab-71642f4bd9ef,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Fat-soluble vitamins,False,Fat-soluble vitamins,,,,
bc52a9d1-d6c5-4154-a49f-e77c18032f0d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Folic acid,False,Folic acid,,,,
e7023a35-23f1-4c81-8cb6-fa1fea894ab3,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Folic acid deficiency is a relatively common vitamin deficiency in the United States, presenting routinely as macrocytic anemia.",True,Folic acid,,,,
d88a560b-7278-472a-aea9-b5276712d767,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Cobalamin (vitamin B12),False,Cobalamin (vitamin B12),,,,
927e72b6-3e61-49e3-83cf-f1ee2fc9336d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Vitamin B12 is required in humans for two essential enzymatic reactions.,True,Cobalamin (vitamin B12),,,,
cc2798f1-da12-4e89-b989-e913c0de69c2,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Ascorbic acid (vitamin C),False,Ascorbic acid (vitamin C),,,,
2285fa1a-9596-4f38-a268-0e7a3ba38107,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,The active form of vitamin C is ascorbic acid.,False,The active form of vitamin C is ascorbic acid.,,,,
416b0755-9d82-4eae-b519-299ab27f1db1,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Pyridoxine (vitamin B6),False,Pyridoxine (vitamin B6),,,,
a46c560a-9ac3-495f-ba18-8f11d796bc17,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Vitamin B6 is a term that encompasses all derivatives of pyridine including: pyridoxine, pyridoxal, and pyridoxamine.",True,Pyridoxine (vitamin B6),,,,
47c8a331-2aa9-4acc-9a74-8af6c635b2b2,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,6,False,6,,,,
56ec28ad-38fd-4dae-9ffb-0e8146bceefb,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Thiamine (vitamin B1),False,Thiamine (vitamin B1),,,,
f7af2a81-6899-4591-9ebe-125adf278966,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Thiamine pyrophosphate (TPP) is the biologically active form of thiamine and is generated by the transfer of a pyrophosphate group from adenosine triphosphate (ATP) to thiamine.,True,Thiamine (vitamin B1),,,,
eb1f5aa1-1c0a-4107-849b-5ced1a024e4c,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Niacin (vitamin B3),False,Niacin (vitamin B3),,,,
9119fbea-9738-48ce-8028-96aa3a6e0828,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Niacin, or nicotinic acid, is a substituted pyridine derivative. The biologically active coenzyme forms are nicotinamide adenine dinucleotide (NAD+) and its phosphorylated derivative, nicotinamide adenine dinucleotide phosphate (NADP+).",True,Niacin (vitamin B3),,,,
337e51c9-033a-4eab-a012-2b31517c3321,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Riboflavin (vitamin B2),False,Riboflavin (vitamin B2),,,,
addb06a9-ea51-4330-aae1-ab40c402f173,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"The two biologically active forms of B2 are flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), formed by the transfer of an adenosine monophosphate moiety from ATP to FMN.",True,Riboflavin (vitamin B2),,,,
bbb69af9-7364-461e-abde-3a755007124e,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Biotin (vitamin B7),False,Biotin (vitamin B7),,,,
c5d35e54-b7c1-4abe-a4ff-34d13a8ffd6e,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Biotin is a coenzyme in carboxylation reactions, in which it serves as a carrier of activated carbon dioxide (coenzyme for acetylCoA carboxylase and pyruvate carboxylase).",True,Biotin (vitamin B7),,,,
177d1b03-4f71-4d42-8711-11322c67129b,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Pantothenic acid,False,Pantothenic acid,,,,
c994e277-97b2-41d6-a28f-b9fb2e9ea766,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Pantothenic acid is a component of CoA, which functions in the transfer of acyl groups.",True,Pantothenic acid,,,,
d1f1cbd3-3d43-490e-8330-4ad9a78a94de,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Vitamin A,False,Vitamin A,,,,
6cf44cf3-dd2f-4937-a983-1dccafef9bf4,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,The retinoids are a family of molecules that are related to dietary retinol (vitamin A).,True,Vitamin A,,,,
01e0bac9-8b90-43d1-972e-37da05e8d05f,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Vitamin D,False,Vitamin D,,,,
72071479-96e6-4b6f-9c53-d12c1b483d3d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,The D vitamins are a group of sterols that have a hormone-like function.,True,Vitamin D,,,,
57f3132f-1a3f-459d-acf7-bb8c96c2c1ae,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Vitamin K,False,Vitamin K,,,,
1802b8c5-5e37-4cdc-b81c-5f2795318c92,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Vitamin E,False,Vitamin E,,,,
668fed4a-6d49-4f50-9c8b-dde073f4fbf4,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"The E vitamins consist of eight naturally occurring tocopherols, of which α-tocopherol is the most active.",True,Vitamin E,,,,
d2311149-7fe3-4ae9-a0bb-8d716692b84d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Table 2.3: Summary table of vitamins.,True,Vitamin E,,,,
3793d18f-458b-4099-85ba-a8b3a866fc1b,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,2.2 References and resources,True,Vitamin E,,,,
c0d1fb0b-7a53-47a3-8f07-823ef98f095b,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Text,False,Text,,,,
acedac93-958d-4f3a-9825-de0bb7faf1ee,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
acedac93-958d-4f3a-9825-de0bb7faf1ee,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
acedac93-958d-4f3a-9825-de0bb7faf1ee,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Ferrier D. Figure 2.3 Mechanism of action of Vitamin A. Adapted under Fair Use from Figure 28.20 Action of the retinoids. Lippincott Illustrated Reviews Biochemistry. 7th Ed. pp388. 2017. Chemical structure by Henry Jakubowski.,True,Text,Figure 2.3,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
a5b018db-3073-4cd5-9962-b9c75b53e86d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2.2 Vitamins as Coenzymes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
a5b018db-3073-4cd5-9962-b9c75b53e86d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2.1 Laboratory Values and Biochemical Correlates,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
a5b018db-3073-4cd5-9962-b9c75b53e86d,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Grey, Kindred, Figure 2.4 Vitamin K stimulates the maturation of clotting factors. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/2.6_20210924. CC BY 4.0.",True,Text,Figure 2.4,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
747e56c1-6aa9-4819-a1a5-82428730e78a,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,Tables,False,Tables,,,,
75eff301-6813-49f7-a2e2-0b3b4e8f6cfb,https://pressbooks.lib.vt.edu/cellbio/,2. Basic Laboratory Measurements,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-2/,"Table 2.3 adapted from Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017.",True,Tables,,,,
a1b327f8-105f-4455-970f-d5dc431708e5,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Tables,Figure 1.2,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
a1b327f8-105f-4455-970f-d5dc431708e5,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Tables,Figure 1.2,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
a1b327f8-105f-4455-970f-d5dc431708e5,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Tables,Figure 1.2,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
27099d91-541a-4f2d-8c75-4d2e09c8c189,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Although it is not essential to memorize the structures of the amino acids, a strong understanding of their general characteristics will be very helpful.",True,Tables,,,,
9599b7e9-7626-409c-ac4a-63ecec96f3b2,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Amino acid functional groups,False,Amino acid functional groups,,,,
773278cc-edac-4e37-8eed-467ba86fa526,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The primary sequence of a protein is determined by the amino acids in the chain and how these individual units function as a group. More generally, amino acids can be characterized as polar or nonpolar. These fundamental characteristics will determine where the residue resides within the protein (surface or core, within a transmembrane domain or part of the active site) and how the amino acid contributes to folding and catalysis.",True,Amino acid functional groups,,,,
14044f42-421d-4c7f-8ce3-e4db6b107dde,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,transmembrane,False,transmembrane,,,,
6c7ddaec-85ba-4273-8fca-ec0a04f7b1bb,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Nonpolar residues,False,Nonpolar residues,,,,
e48b711e-c6d8-47f6-b238-31f03ee0af61,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Nonpolar amino acids can be further divided into: uncharged (aromatic and nonpolar aliphatic) and sulfur-containing groups. Nonpolar uncharged side chains do not gain or lose protons or participate in hydrogen or ionic bonding. These amino acids typically cluster in the internal regions of a protein, away from the aqueous interface. The exception to this is if these amino acids are present as part of a membrane-bound protein, and in this case, the amino acids may be exposed in the transmembrane region. Proline is also of note, as it forms an unconventional peptide bond and will add a kink in the primary structure of a protein. Sulfur-containing amino acids can participate in disulfide linkages, which are used to stabilize interactions between peptide chains or tertiary structures.",True,Nonpolar residues,,,,
8411dbb1-2c5d-43ae-b935-afecba8bf108,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Polar residues,False,Polar residues,,,,
da24e3df-cc71-4f69-bb99-2a6f76add162,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Amino acids with uncharged polar R-groups may participate in hydrogen bonding and undergo modifications such as phosphorylation. Tyrosine, serine, and threonine all have a hydroxyl group within the R-group, and they can also be readily modified by kinase-mediated phosphorylation.",True,Polar residues,,,,
5ab9aa34-36fb-487e-8f7a-3e9dab933477,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Some amino acids are charged at a physiological pH and can be acidic or basic. These side chains may donate or accept protons, respectively, and the most notable charged amino acid is histidine, which can function as a buffer at a physiological pH.",True,Polar residues,,,,
3067974d-a013-43af-804d-759c9295e62c,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,1.1 References and resources,True,Polar residues,,,,
9bbc330e-7628-4a8a-bea3-1277e24382d9,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 1: Amino Acids, Chapter 2: Protein Structure.",True,Polar residues,,,,
71e8030c-0f45-4b0d-81e8-5f3946e34f17,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 6: Amino Acids in Proteins, Chapter 8: Enzymes as Catalysts, Chapter 9: Regulation of Enzymes.",True,Polar residues,,,,
baa9817f-68cf-497a-a055-208345f9013d,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
baa9817f-68cf-497a-a055-208345f9013d,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
baa9817f-68cf-497a-a055-208345f9013d,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
3f26d77f-fdc8-463f-a56f-2c88db821656,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
3f26d77f-fdc8-463f-a56f-2c88db821656,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
3f26d77f-fdc8-463f-a56f-2c88db821656,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
8cda99ef-1df2-4d64-b8aa-1bd12ce5ebb6,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,1.2 Enzyme Kinetics,True,Polar residues,,,,
22762992-8159-4f33-a756-379751eb176b,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Many translated proteins are also enzymes with a specific metabolic function within the cell. Enzymes help reduce the amount of transition state energy required for a reaction to move forward through several mechanisms:,True,Polar residues,,,,
fc64a696-874c-4f51-9e7e-6ed6c917d9b4,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
fc64a696-874c-4f51-9e7e-6ed6c917d9b4,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
fc64a696-874c-4f51-9e7e-6ed6c917d9b4,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
7a3d5064-3a17-423e-9b8c-b79ccc4c312b,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
7a3d5064-3a17-423e-9b8c-b79ccc4c312b,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
7a3d5064-3a17-423e-9b8c-b79ccc4c312b,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
6285275b-cc7f-4a99-bd01-83bda78e0599,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The Michaelis‒Menten model contains simplifying assumptions (substrate binding is in equilibrium, formation of [P] is irreversible, [E] and [ES] are the only enzyme forms).",True,Polar residues,,,,
94624dd8-fa14-4520-8520-4e57fa1a595f,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
94624dd8-fa14-4520-8520-4e57fa1a595f,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
94624dd8-fa14-4520-8520-4e57fa1a595f,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
84716669-2ba4-4746-80b1-bedb9468cbaf,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Factors influencing enzyme kinetics,False,Factors influencing enzyme kinetics,,,,
6812fc38-a908-4dad-b3fd-64d2788cea57,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The catalytic properties of enzymes, and consequently their activity, are influenced by numerous factors, which all must be optimized and controlled if activity measurements are to be performed in a useful and reproducible fashion. These factors include physical quantities (temperature or pressure), the chemical properties of the solution (pH or ionic strength), and the concentrations of all relevant substrates, cofactors, coenzymes, and inhibitors. The role of cofactors (inorganic) or coenzymes (organic) is often to accept or donate electrons in a reaction or to temporarily stabilize the substrate in the course of the reaction. Depending on the type of interaction with the enzyme, a distinction is made between soluble coenzymes and prosthetic groups.",True,Factors influencing enzyme kinetics,,,,
a7e50404-f32b-4b2f-9897-30d30182ccec,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Enzyme regulation,False,Enzyme regulation,,,,
2459bef7-3000-401f-8c52-b871865d52be,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Competitive and noncompetitive inhibition,False,Competitive and noncompetitive inhibition,,,,
317eef11-b243-409d-b803-09d325fcf076,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Enzymes can be inhibited or activated by interference from other compounds. These will influence the reaction by changing the Km or Vmax of the reaction. Most enzyme inhibitors act reversibly and do not cause permanent changes in the enzyme. However, there are also irreversible inhibitors that modify the target enzyme covalently and permanently. These are termed suicide inhibitors.",True,Competitive and noncompetitive inhibition,,,,
6bc8407e-1cd5-43e6-9062-b1c9d6228070,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Inhibitors can be categorized as competitive or noncompetitive, and this can be determined by comparing the kinetics of the normal versus inhibited reactions.",True,Competitive and noncompetitive inhibition,,,,
c7133a99-dec0-452c-b2dc-6761ba41d6b7,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
c7133a99-dec0-452c-b2dc-6761ba41d6b7,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
c7133a99-dec0-452c-b2dc-6761ba41d6b7,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
167e2378-7373-44d7-a45a-5b93386604c8,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
167e2378-7373-44d7-a45a-5b93386604c8,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
167e2378-7373-44d7-a45a-5b93386604c8,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
f47737b8-f52a-4656-a8d8-d4c7f1d1a83f,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
f47737b8-f52a-4656-a8d8-d4c7f1d1a83f,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
f47737b8-f52a-4656-a8d8-d4c7f1d1a83f,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
6c119a48-8a71-4829-8dad-8379395ead8c,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Allosteric regulation,False,Allosteric regulation,,,,
c7afc137-694b-48fa-bf4a-6672386ff072,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
c7afc137-694b-48fa-bf4a-6672386ff072,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
c7afc137-694b-48fa-bf4a-6672386ff072,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
c7afc137-694b-48fa-bf4a-6672386ff072,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
c7afc137-694b-48fa-bf4a-6672386ff072,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
c7afc137-694b-48fa-bf4a-6672386ff072,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
a0f3c348-ebc3-4b53-86a1-40420b507ddc,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Similar to noncompetitive inhibitors, allosteric effectors will bind sites alternative to the active site. Allosteric activators typically stabilize the relaxed conformation of an enzyme (R), and increase the rate of substrate binding of the subsequent subunits. This is called cooperativity. In contrast, allosteric inhibitors will stabilize the tense (T) conformation of a protein and will increase substrate off (release) rate. The best example of this is with oxygen binding to hemoglobin, which has a quaternary structure with four binding sites for oxygen.",True,Allosteric regulation,,,,
3f916fb4-68dc-45fc-a328-1a76af9aed3a,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Enzyme regulation through covalent modification,False,Enzyme regulation through covalent modification,,,,
8ffb1a30-885f-4d37-b074-10e483377aef,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Enzyme function can also be modified through covalent modification such as phosphorylation. These are typically post-translational modifications that can take place in the golgi or through kinase-mediated interactions. For example, glycogen phosphorylase requires phosphorylation for activation. Phosphorylation will be an integral means of regulation of enzymes during metabolic pathways.",True,Enzyme regulation through covalent modification,,,,
54a1a09f-23f0-4caa-a5ec-295c6db6d200,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,1.2 References and resources,True,Enzyme regulation through covalent modification,,,,
ddc3cf8d-292a-4953-b91e-4f2fdfe86689,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,Text,False,Text,,,,
70247e3f-bb1b-442d-9697-34335c63dba1,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
70247e3f-bb1b-442d-9697-34335c63dba1,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
70247e3f-bb1b-442d-9697-34335c63dba1,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
8c5504b4-2266-4922-8ca6-8cb36b4a358d,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
8c5504b4-2266-4922-8ca6-8cb36b4a358d,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
8c5504b4-2266-4922-8ca6-8cb36b4a358d,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
b94332c2-5c5c-4241-8320-167fa2151c12,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
b94332c2-5c5c-4241-8320-167fa2151c12,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
b94332c2-5c5c-4241-8320-167fa2151c12,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
34677d70-0970-4bc8-be24-8ead6dd4a18b,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
34677d70-0970-4bc8-be24-8ead6dd4a18b,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
34677d70-0970-4bc8-be24-8ead6dd4a18b,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
686b93bc-5742-447c-9446-3005dead833a,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
686b93bc-5742-447c-9446-3005dead833a,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
686b93bc-5742-447c-9446-3005dead833a,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
686b93bc-5742-447c-9446-3005dead833a,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
686b93bc-5742-447c-9446-3005dead833a,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
686b93bc-5742-447c-9446-3005dead833a,https://pressbooks.lib.vt.edu/cellbio/,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-2,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
7aac71af-4ffd-4efe-8c98-072dd31226ac,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Text,Figure 1.2,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
7aac71af-4ffd-4efe-8c98-072dd31226ac,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Text,Figure 1.2,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
7aac71af-4ffd-4efe-8c98-072dd31226ac,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Text,Figure 1.2,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
e6c1de69-0853-4b22-8c56-ce4522c68f73,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Although it is not essential to memorize the structures of the amino acids, a strong understanding of their general characteristics will be very helpful.",True,Text,,,,
9ea81f51-c1ef-4782-afcf-63efcce12657,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Amino acid functional groups,False,Amino acid functional groups,,,,
791a9f47-d78a-47f9-a2ee-71548509c09e,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The primary sequence of a protein is determined by the amino acids in the chain and how these individual units function as a group. More generally, amino acids can be characterized as polar or nonpolar. These fundamental characteristics will determine where the residue resides within the protein (surface or core, within a transmembrane domain or part of the active site) and how the amino acid contributes to folding and catalysis.",True,Amino acid functional groups,,,,
3b09ae30-3ffc-4e44-8051-281d70d17e63,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,transmembrane,False,transmembrane,,,,
0cfde941-8149-45ae-809a-cc70dee3e764,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Nonpolar residues,False,Nonpolar residues,,,,
d2614301-dab4-4f17-a5c0-53fab55345bf,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Nonpolar amino acids can be further divided into: uncharged (aromatic and nonpolar aliphatic) and sulfur-containing groups. Nonpolar uncharged side chains do not gain or lose protons or participate in hydrogen or ionic bonding. These amino acids typically cluster in the internal regions of a protein, away from the aqueous interface. The exception to this is if these amino acids are present as part of a membrane-bound protein, and in this case, the amino acids may be exposed in the transmembrane region. Proline is also of note, as it forms an unconventional peptide bond and will add a kink in the primary structure of a protein. Sulfur-containing amino acids can participate in disulfide linkages, which are used to stabilize interactions between peptide chains or tertiary structures.",True,Nonpolar residues,,,,
c5dc1f56-51cb-4887-bf93-64c4575eecdc,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Polar residues,False,Polar residues,,,,
2b8cb2d9-bb93-46cf-9261-497df7842437,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Amino acids with uncharged polar R-groups may participate in hydrogen bonding and undergo modifications such as phosphorylation. Tyrosine, serine, and threonine all have a hydroxyl group within the R-group, and they can also be readily modified by kinase-mediated phosphorylation.",True,Polar residues,,,,
378f12f3-70b3-47be-898d-b549204de365,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Some amino acids are charged at a physiological pH and can be acidic or basic. These side chains may donate or accept protons, respectively, and the most notable charged amino acid is histidine, which can function as a buffer at a physiological pH.",True,Polar residues,,,,
13c275c8-d452-4db2-8609-e40d8507da27,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,1.1 References and resources,True,Polar residues,,,,
17d0e816-c0c0-41b2-ae72-d47dd9812534,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 1: Amino Acids, Chapter 2: Protein Structure.",True,Polar residues,,,,
10093e98-1481-4945-89d9-b40e74e183be,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 6: Amino Acids in Proteins, Chapter 8: Enzymes as Catalysts, Chapter 9: Regulation of Enzymes.",True,Polar residues,,,,
79a4e503-2239-488c-8a13-77d5a2469ef0,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
79a4e503-2239-488c-8a13-77d5a2469ef0,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
79a4e503-2239-488c-8a13-77d5a2469ef0,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
2db0826b-a1c5-4dda-b015-139eb54f798e,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
2db0826b-a1c5-4dda-b015-139eb54f798e,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
2db0826b-a1c5-4dda-b015-139eb54f798e,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
a90ac5e3-8f20-47a1-9626-f4a60e08e69e,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,1.2 Enzyme Kinetics,True,Polar residues,,,,
44a8e593-879a-4db3-a25c-3684cbf52a32,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Many translated proteins are also enzymes with a specific metabolic function within the cell. Enzymes help reduce the amount of transition state energy required for a reaction to move forward through several mechanisms:,True,Polar residues,,,,
c2e64954-f259-4285-ab48-cdbee653aa68,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
c2e64954-f259-4285-ab48-cdbee653aa68,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
c2e64954-f259-4285-ab48-cdbee653aa68,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
88b96878-78b1-4a01-b23f-c98b7d841089,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
88b96878-78b1-4a01-b23f-c98b7d841089,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
88b96878-78b1-4a01-b23f-c98b7d841089,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
2c8489ae-5a2e-488b-be68-fcc01bd9f9b6,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The Michaelis‒Menten model contains simplifying assumptions (substrate binding is in equilibrium, formation of [P] is irreversible, [E] and [ES] are the only enzyme forms).",True,Polar residues,,,,
7a163a06-1cb7-4c72-b09c-44c392914dad,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
7a163a06-1cb7-4c72-b09c-44c392914dad,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
7a163a06-1cb7-4c72-b09c-44c392914dad,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
a90c8f81-fe32-482e-8c58-51031ff2b0dc,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Factors influencing enzyme kinetics,False,Factors influencing enzyme kinetics,,,,
6291f75a-f2d6-444c-9f47-e796a2ec1b40,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The catalytic properties of enzymes, and consequently their activity, are influenced by numerous factors, which all must be optimized and controlled if activity measurements are to be performed in a useful and reproducible fashion. These factors include physical quantities (temperature or pressure), the chemical properties of the solution (pH or ionic strength), and the concentrations of all relevant substrates, cofactors, coenzymes, and inhibitors. The role of cofactors (inorganic) or coenzymes (organic) is often to accept or donate electrons in a reaction or to temporarily stabilize the substrate in the course of the reaction. Depending on the type of interaction with the enzyme, a distinction is made between soluble coenzymes and prosthetic groups.",True,Factors influencing enzyme kinetics,,,,
67376bda-f5ab-4e3d-b92a-63f71f2ca23d,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Enzyme regulation,False,Enzyme regulation,,,,
8ddc8e06-8f39-47d5-8729-7680f67cbc2d,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Competitive and noncompetitive inhibition,False,Competitive and noncompetitive inhibition,,,,
27eea032-2d8a-4728-a4b6-f7aebe5744e8,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Enzymes can be inhibited or activated by interference from other compounds. These will influence the reaction by changing the Km or Vmax of the reaction. Most enzyme inhibitors act reversibly and do not cause permanent changes in the enzyme. However, there are also irreversible inhibitors that modify the target enzyme covalently and permanently. These are termed suicide inhibitors.",True,Competitive and noncompetitive inhibition,,,,
70a2f8d4-8f9c-4ae2-9707-edbb19574d94,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Inhibitors can be categorized as competitive or noncompetitive, and this can be determined by comparing the kinetics of the normal versus inhibited reactions.",True,Competitive and noncompetitive inhibition,,,,
c19d06f7-4a0f-4c00-a476-f5fb67882a9a,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
c19d06f7-4a0f-4c00-a476-f5fb67882a9a,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
c19d06f7-4a0f-4c00-a476-f5fb67882a9a,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
55b6ae91-c259-480d-893e-9ee5e6d9eed4,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
55b6ae91-c259-480d-893e-9ee5e6d9eed4,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
55b6ae91-c259-480d-893e-9ee5e6d9eed4,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
b8bb9ee3-2bb3-4c29-8fd9-995890c1e7c1,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
b8bb9ee3-2bb3-4c29-8fd9-995890c1e7c1,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
b8bb9ee3-2bb3-4c29-8fd9-995890c1e7c1,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
94eebc16-3b66-4e5d-91a8-4733461161ab,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Allosteric regulation,False,Allosteric regulation,,,,
6329925e-6928-4b3d-8969-cd8c46247ff7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
6329925e-6928-4b3d-8969-cd8c46247ff7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
6329925e-6928-4b3d-8969-cd8c46247ff7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
6329925e-6928-4b3d-8969-cd8c46247ff7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
6329925e-6928-4b3d-8969-cd8c46247ff7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
6329925e-6928-4b3d-8969-cd8c46247ff7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
2b0dde10-a49a-4d00-9455-8214c91fbf74,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Similar to noncompetitive inhibitors, allosteric effectors will bind sites alternative to the active site. Allosteric activators typically stabilize the relaxed conformation of an enzyme (R), and increase the rate of substrate binding of the subsequent subunits. This is called cooperativity. In contrast, allosteric inhibitors will stabilize the tense (T) conformation of a protein and will increase substrate off (release) rate. The best example of this is with oxygen binding to hemoglobin, which has a quaternary structure with four binding sites for oxygen.",True,Allosteric regulation,,,,
ecaf6aad-43c7-4158-aee9-f8b5342b3486,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Enzyme regulation through covalent modification,False,Enzyme regulation through covalent modification,,,,
acd78a3e-e17c-46f2-8001-076b519bd5be,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Enzyme function can also be modified through covalent modification such as phosphorylation. These are typically post-translational modifications that can take place in the golgi or through kinase-mediated interactions. For example, glycogen phosphorylase requires phosphorylation for activation. Phosphorylation will be an integral means of regulation of enzymes during metabolic pathways.",True,Enzyme regulation through covalent modification,,,,
1a125375-4a46-4ca1-b0bd-bb3b0e577bcb,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,1.2 References and resources,True,Enzyme regulation through covalent modification,,,,
092bd58c-8d30-40ef-bb5e-1af281841efd,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,Text,False,Text,,,,
eb6abdc6-6fad-4f02-a5de-670c94591b58,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
eb6abdc6-6fad-4f02-a5de-670c94591b58,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
eb6abdc6-6fad-4f02-a5de-670c94591b58,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
d2a3af6d-8f43-471e-92f1-113df83bbde7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
d2a3af6d-8f43-471e-92f1-113df83bbde7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
d2a3af6d-8f43-471e-92f1-113df83bbde7,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
5012d44a-76d6-46b5-9ad1-ed4a10e89dd3,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
5012d44a-76d6-46b5-9ad1-ed4a10e89dd3,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
5012d44a-76d6-46b5-9ad1-ed4a10e89dd3,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
db6bd140-6484-48c7-8e00-af010b0fda9f,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
db6bd140-6484-48c7-8e00-af010b0fda9f,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
db6bd140-6484-48c7-8e00-af010b0fda9f,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
b4e6a504-8944-4ac4-a24a-c5f29f59cb08,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
b4e6a504-8944-4ac4-a24a-c5f29f59cb08,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
b4e6a504-8944-4ac4-a24a-c5f29f59cb08,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
b4e6a504-8944-4ac4-a24a-c5f29f59cb08,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
b4e6a504-8944-4ac4-a24a-c5f29f59cb08,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
b4e6a504-8944-4ac4-a24a-c5f29f59cb08,https://pressbooks.lib.vt.edu/cellbio/,1.1  Amino Acids,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/#chapter-5-section-1,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
ab4419a5-5d82-47e5-a26c-43e134386f22,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Text,Figure 1.2,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
ab4419a5-5d82-47e5-a26c-43e134386f22,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Text,Figure 1.2,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
ab4419a5-5d82-47e5-a26c-43e134386f22,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Amino acids can be grouped largely by the functionality of their R-group (figure 1.2).,True,Text,Figure 1.2,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
89373c0a-5e99-41b6-b5be-20542c30ad1f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Although it is not essential to memorize the structures of the amino acids, a strong understanding of their general characteristics will be very helpful.",True,Text,,,,
59c623eb-880b-40dd-bc66-2d85f26ee105,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Amino acid functional groups,False,Amino acid functional groups,,,,
11f35f4f-ee40-49e6-97bd-ae8b5e2c2e09,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The primary sequence of a protein is determined by the amino acids in the chain and how these individual units function as a group. More generally, amino acids can be characterized as polar or nonpolar. These fundamental characteristics will determine where the residue resides within the protein (surface or core, within a transmembrane domain or part of the active site) and how the amino acid contributes to folding and catalysis.",True,Amino acid functional groups,,,,
2859acff-55f7-4ea2-aadc-adbf7c93b721,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,transmembrane,False,transmembrane,,,,
532d896b-c738-4cdd-91d2-45078554dfbd,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Nonpolar residues,False,Nonpolar residues,,,,
bb6a2b6c-f4bb-4828-80e4-eb4ca3911696,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Nonpolar amino acids can be further divided into: uncharged (aromatic and nonpolar aliphatic) and sulfur-containing groups. Nonpolar uncharged side chains do not gain or lose protons or participate in hydrogen or ionic bonding. These amino acids typically cluster in the internal regions of a protein, away from the aqueous interface. The exception to this is if these amino acids are present as part of a membrane-bound protein, and in this case, the amino acids may be exposed in the transmembrane region. Proline is also of note, as it forms an unconventional peptide bond and will add a kink in the primary structure of a protein. Sulfur-containing amino acids can participate in disulfide linkages, which are used to stabilize interactions between peptide chains or tertiary structures.",True,Nonpolar residues,,,,
087f2a46-948e-49c2-b53c-6d6a44a98237,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Polar residues,False,Polar residues,,,,
80fa6f77-bda1-428d-9883-dc51d6d938ef,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Amino acids with uncharged polar R-groups may participate in hydrogen bonding and undergo modifications such as phosphorylation. Tyrosine, serine, and threonine all have a hydroxyl group within the R-group, and they can also be readily modified by kinase-mediated phosphorylation.",True,Polar residues,,,,
5f8f4cb4-1dd6-4c1d-b897-f3c3af41de6d,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Some amino acids are charged at a physiological pH and can be acidic or basic. These side chains may donate or accept protons, respectively, and the most notable charged amino acid is histidine, which can function as a buffer at a physiological pH.",True,Polar residues,,,,
2e91c27c-9717-4df4-a0f8-3079471215a3,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,1.1 References and resources,True,Polar residues,,,,
d8ad69fe-471f-4a9f-872b-c466dc288d98,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Ferrier, D. R., ed. Lippincott Illustrated Reviews: Biochemistry, 7th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2017, Chapter 1: Amino Acids, Chapter 2: Protein Structure.",True,Polar residues,,,,
a052b4d7-594b-4231-9458-d55b46c6a4ee,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman, M., and A. Peet, eds. Marks’ Basic Medical Biochemistry: A Clinical Approach, 5th ed. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins, 2018, Chapter 6: Amino Acids in Proteins, Chapter 8: Enzymes as Catalysts, Chapter 9: Regulation of Enzymes.",True,Polar residues,,,,
00fc6444-9904-410b-9d33-eef0c19df00b,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
00fc6444-9904-410b-9d33-eef0c19df00b,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
00fc6444-9904-410b-9d33-eef0c19df00b,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.1 Basic structure of amino acids and ionization. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.1_20210924. CC BY 4.0.",True,Polar residues,Figure 1.1,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
f4470457-fcdc-4b82-bdc7-5e99e215d838,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
f4470457-fcdc-4b82-bdc7-5e99e215d838,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
f4470457-fcdc-4b82-bdc7-5e99e215d838,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.2 Chart of amino acids. 2021. Chemical structure by Henry Jakubowski. https://archive.org/details/1.2_20210924. CC BY 4.0.",True,Polar residues,Figure 1.2,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
b1ee9aef-9d94-4643-a7a8-91fb92ab8483,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,1.2 Enzyme Kinetics,True,Polar residues,,,,
a36b4f95-83fb-4dc0-ad09-e32b4b72f94d,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Many translated proteins are also enzymes with a specific metabolic function within the cell. Enzymes help reduce the amount of transition state energy required for a reaction to move forward through several mechanisms:,True,Polar residues,,,,
ec3c805f-72cc-4042-9fc8-60368e17e070,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
ec3c805f-72cc-4042-9fc8-60368e17e070,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
ec3c805f-72cc-4042-9fc8-60368e17e070,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The kinetics of enzyme-catalyzed reactions is mainly determined by the properties of the catalyst. Like all catalysts, the enzyme [E] creates a new reaction pathway. Initially, the substrate [S] is bound to the free enzyme [ES] (figure 1.3).",True,Polar residues,Figure 1.3,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
f94cd11b-36c9-49e5-9a31-8436088a1a8a,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
f94cd11b-36c9-49e5-9a31-8436088a1a8a,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
f94cd11b-36c9-49e5-9a31-8436088a1a8a,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The rate of this enzyme reaction can be described by the Michaelis–Menten equation, which relates the the initial velocity (vi) to the concentration of substrate [S] and the two parameters Km and Vmax. The Vmax is defined as the maximal velocity that can be achieved at an infinite substrate concentration, while the Km is defined as the substrate concentration needed to reach 1/2 Vmax. The Michaelis constant (Km) characterizes the affinity of the enzyme for a substrate. A high affinity of the enzyme for a substrate therefore leads to a low Km value, and vice versa (figure 1.4).",True,Polar residues,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
fd099b49-c1a8-43f3-bb26-a24f7806e611,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The Michaelis‒Menten model contains simplifying assumptions (substrate binding is in equilibrium, formation of [P] is irreversible, [E] and [ES] are the only enzyme forms).",True,Polar residues,,,,
3e4704aa-baaf-4230-8fdc-bace55de5233,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
3e4704aa-baaf-4230-8fdc-bace55de5233,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
3e4704aa-baaf-4230-8fdc-bace55de5233,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Since vi approaches Vmax asymptotically, it is difficult to read off reliable values for Vmax or Km from diagrams plotting v against [S] (figure 1.4). To alleviate this issue, the Michaelis‒Menten equation can be arranged in such a way that the measured points lie on a straight line. In the Lineweaver‒Burk plot, 1/v is plotted against 1/[S]. The intersections of the line of best fit with the axes then produce 1/Vmax and −1/Km (figure 1.5).",True,Polar residues,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
9fcc2acd-9dbf-4bd3-b0b9-2bc2aceb8f0a,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Factors influencing enzyme kinetics,False,Factors influencing enzyme kinetics,,,,
4547b52c-5a0c-4cd4-b7aa-d3c6e8d35a52,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The catalytic properties of enzymes, and consequently their activity, are influenced by numerous factors, which all must be optimized and controlled if activity measurements are to be performed in a useful and reproducible fashion. These factors include physical quantities (temperature or pressure), the chemical properties of the solution (pH or ionic strength), and the concentrations of all relevant substrates, cofactors, coenzymes, and inhibitors. The role of cofactors (inorganic) or coenzymes (organic) is often to accept or donate electrons in a reaction or to temporarily stabilize the substrate in the course of the reaction. Depending on the type of interaction with the enzyme, a distinction is made between soluble coenzymes and prosthetic groups.",True,Factors influencing enzyme kinetics,,,,
ad9ee45e-8cf8-4a2a-b271-56989aac606d,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Enzyme regulation,False,Enzyme regulation,,,,
d5c366dc-a0d5-41ce-ab8f-8fdaf825f238,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Competitive and noncompetitive inhibition,False,Competitive and noncompetitive inhibition,,,,
dd25ebce-412d-433a-ba36-d65a1c58b1a0,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Enzymes can be inhibited or activated by interference from other compounds. These will influence the reaction by changing the Km or Vmax of the reaction. Most enzyme inhibitors act reversibly and do not cause permanent changes in the enzyme. However, there are also irreversible inhibitors that modify the target enzyme covalently and permanently. These are termed suicide inhibitors.",True,Competitive and noncompetitive inhibition,,,,
30d984ad-b36b-4193-9d36-bd4123cadc6c,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Inhibitors can be categorized as competitive or noncompetitive, and this can be determined by comparing the kinetics of the normal versus inhibited reactions.",True,Competitive and noncompetitive inhibition,,,,
57746a7b-4c51-42ce-96d6-ad12f07d48d2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
57746a7b-4c51-42ce-96d6-ad12f07d48d2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
57746a7b-4c51-42ce-96d6-ad12f07d48d2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Competitive inhibitors bind the enzyme at the active site and compete with the substrate for binding. Many function as substrate analogs. In the presence of the inhibitor, a higher substrate concentration is therefore needed to achieve a half-maximum rate; the Michaelis constant Km increases. When substrate concentrations are elevated, this will ultimately displace the inhibitor, and Vmax will be reached. The maximum rate, Vmax, is therefore not influenced by competitive inhibitors. In this case, there is no change on Vmax as competition can be overcome by increasing the concentration of substrate, but there is an increase in the apparent Km, as a greater substrate concentration is needed to reach Vmax (figure 1.6(a)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
13075a93-57f0-483e-998f-b7b3681de5b5,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
13075a93-57f0-483e-998f-b7b3681de5b5,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
13075a93-57f0-483e-998f-b7b3681de5b5,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"In contrast, noncompetitive inhibitors bind the enzyme on a site alternative to the substrate binding site, and therefore its effects cannot be overcome by increasing the substrate. In this case, Km remains unchanged, but kcat (the rate of product formation), and thus Vmax, decreases. Irreversible inhibitors usually result in a noncompetitive type of inhibition because the concentration of active enzyme [E] decreases (figure 1.6(b)).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
e4702843-3678-4951-9783-86ee6a25eded,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
e4702843-3678-4951-9783-86ee6a25eded,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
e4702843-3678-4951-9783-86ee6a25eded,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The action of inhibitors can be illustrated clearly in the Lineweaver‒Burk plot. In this type of plot, the intercept of the approximation lines with the y-axis corresponds to 1/Vmax, while the x-axis intercept gives the value of −1/Km. This is why the straight lines obtained in the absence (blue) and presence of a competitive inhibitor (A, red) intersect on the y-axis (1/ Vmax), unchanged), while noncompetitive inhibitors (B, red) result in a straight line with a higher y-intercept but unchanged x-intercept (1/Vmax) increased, Km) unchanged) (figure 1.6).",True,Competitive and noncompetitive inhibition,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
b9728f5d-4c99-44a8-a85f-36657344044f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Allosteric regulation,False,Allosteric regulation,,,,
149dc445-b3aa-47c4-ba01-717c4257f90f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
149dc445-b3aa-47c4-ba01-717c4257f90f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
149dc445-b3aa-47c4-ba01-717c4257f90f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
149dc445-b3aa-47c4-ba01-717c4257f90f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
149dc445-b3aa-47c4-ba01-717c4257f90f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
149dc445-b3aa-47c4-ba01-717c4257f90f,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"The Michaelis‒Menten model of enzyme catalysis assumes that the enzymeʼs spatial structure does not alter with substrate binding. However, many enzymes are present in various conformations, which have different catalytic properties. Allosteric enzymes can be recognized by their S-shaped (sigmoidal) saturation curves, which cannot be described using the Michaelis‒Menten equation. In allosteric enzymes, the binding efficiency initially rises with increasing [S], because the free enzyme is present in a low-affinity conformation, which is gradually converted into a higher-affinity form. It is only at high [S] values that a lack of free binding sites becomes noticeable and the binding efficiency decreases again. The affinity of allosteric enzymes is therefore not constant, but depends on the type and concentration of the ligand. Inhibitors and activators (effectors) influence the activity of allosteric enzymes by stabilizing certain conformations. These effects play an important part in regulating metabolism (figure 1.7).",True,Allosteric regulation,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
4e891c26-9fa1-4a20-b420-15ee477af906,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Similar to noncompetitive inhibitors, allosteric effectors will bind sites alternative to the active site. Allosteric activators typically stabilize the relaxed conformation of an enzyme (R), and increase the rate of substrate binding of the subsequent subunits. This is called cooperativity. In contrast, allosteric inhibitors will stabilize the tense (T) conformation of a protein and will increase substrate off (release) rate. The best example of this is with oxygen binding to hemoglobin, which has a quaternary structure with four binding sites for oxygen.",True,Allosteric regulation,,,,
7638a31c-eb66-4991-bffa-4a2f014a9f68,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Enzyme regulation through covalent modification,False,Enzyme regulation through covalent modification,,,,
ee6f9f63-ccff-4bb6-bf13-aebb20f9f528,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Enzyme function can also be modified through covalent modification such as phosphorylation. These are typically post-translational modifications that can take place in the golgi or through kinase-mediated interactions. For example, glycogen phosphorylase requires phosphorylation for activation. Phosphorylation will be an integral means of regulation of enzymes during metabolic pathways.",True,Enzyme regulation through covalent modification,,,,
6981f5fb-c570-4587-a201-20237cbaf98d,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,1.2 References and resources,True,Enzyme regulation through covalent modification,,,,
6179354d-5eca-4aff-9a2d-af8a72c677e6,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,Text,False,Text,,,,
3537df75-e4d9-4173-8fef-f8d05a009aab,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
3537df75-e4d9-4173-8fef-f8d05a009aab,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
3537df75-e4d9-4173-8fef-f8d05a009aab,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Grey, Kindred, Figure 1.3 Basics of enzyme kinetics. 2021. https://archive.org/details/1.3_20210924. CC BY 4.0.",True,Text,Figure 1.3,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
9e48d2df-1331-4e36-8e4b-bbd73101c3fb,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
9e48d2df-1331-4e36-8e4b-bbd73101c3fb,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
9e48d2df-1331-4e36-8e4b-bbd73101c3fb,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.4 Graphical representation of the Michaelis-Menten equation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 152. Figure 9.2 A graph of the Michaelis-Menten equation. 2017.",True,Text,Figure 1.4,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
d1b91952-a9cc-48a6-8a32-e36fa6afd69a,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
d1b91952-a9cc-48a6-8a32-e36fa6afd69a,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
d1b91952-a9cc-48a6-8a32-e36fa6afd69a,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.5 Lineweaver-Burk plot to illustrate Km and Vmax. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 153. Figure 9.3 The Lineweaver-Burk transformation for the Michaelis-Menten equation. 2017.",True,Text,Figure 1.5,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
8d88f724-ca82-47c5-a347-314d4d3aee20,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
8d88f724-ca82-47c5-a347-314d4d3aee20,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
8d88f724-ca82-47c5-a347-314d4d3aee20,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.6 Competitive vs. noncompetitive inhibition. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 156. Figure 9.6 Lineweaver-Burk plots of competitive and purenoncompetitive inhibition. 2017.",True,Text,Figure 1.6,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
9896182f-c348-443d-9bc5-0a95d5bb73f2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
9896182f-c348-443d-9bc5-0a95d5bb73f2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.2 Enzyme Kinetics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
9896182f-c348-443d-9bc5-0a95d5bb73f2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
9896182f-c348-443d-9bc5-0a95d5bb73f2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1.1  Amino Acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
9896182f-c348-443d-9bc5-0a95d5bb73f2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
9896182f-c348-443d-9bc5-0a95d5bb73f2,https://pressbooks.lib.vt.edu/cellbio/,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/cellbio/chapter/chapter-1/,"Lieberman M, Peet A. Figure 1.7 Allosteric enzyme regulation. Adapted under Fair Use from Marks’ Basic Medical Biochemistry. 5th Ed. pp 157. Figure 9.8 Activators and inhibitors of an allosteric enzyme (simplified model). 2017.",True,Text,Figure 1.7,1. Biochemistry Basics,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.