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Idiopathic inflammatory myopathy is a group of disorders characterized by inflammation of the muscles used for movement (skeletal muscles). Idiopathic inflammatory myopathy usually appears in adults between ages 40 and 60 or in children between ages 5 and 15, though it can occur at any age. The primary symptom of idiopathic inflammatory myopathy is muscle weakness, which develops gradually over a period of weeks to months or even years. Other symptoms include joint pain and general tiredness (fatigue). There are several forms of idiopathic inflammatory myopathy, including polymyositis, dermatomyositis, and sporadic inclusion body myositis. Polymyositis and dermatomyositis involve weakness of the muscles closest to the center of the body (proximal muscles), such as the muscles of the hips and thighs, upper arms, and neck. People with these forms of idiopathic inflammatory myopathy may find it difficult to climb stairs, get up from a seated position, or lift items above their head. In some cases, muscle weakness may make swallowing or breathing difficult. Polymyositis and dermatomyositis have similar symptoms, but dermatomyositis is distinguished by a reddish or purplish rash on the eyelids, elbows, knees, or knuckles. Sometimes, abnormal calcium deposits form hard, painful bumps under the skin (calcinosis). In sporadic inclusion body myositis, the muscles most affected are those of the wrists and fingers and the front of the thigh. Affected individuals may frequently stumble while walking and find it difficult to grasp items. As in dermatomyositis and polymyositis, swallowing can be difficult. The incidence of idiopathic inflammatory myopathy is approximately 2 to 8 cases per million people each year. For unknown reasons, polymyositis and dermatomyositis are about twice as common in women as in men, while sporadic inclusion body myositis is more common in men. Idiopathic inflammatory myopathy is thought to arise from a combination of genetic and environmental factors. The term "idiopathic" indicates that the specific cause of the disorder is unknown. Researchers have identified variations in several genes that may influence the risk of developing idiopathic inflammatory myopathy. The most commonly associated genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders (such as viruses and bacteria). Each HLA gene has many different normal variations, allowing each person's immune system to react to a wide range of foreign proteins. Specific variations of several HLA genes seem to affect the risk of developing idiopathic inflammatory myopathy. Researchers are studying variations in other genes related to the body's immune function to understand how they contribute to the risk of developing idiopathic inflammatory myopathy. It is likely that specific genetic variations increase a person's risk of developing idiopathic inflammatory myopathy, and then exposure to certain environmental factors triggers the disorder. Infection, exposure to certain medications, and exposure to ultraviolet light (such as sunlight) have been identified as possible environmental triggers, but most risk factors for this condition remain unknown. Additional Information from NCBI Gene: Most cases of idiopathic inflammatory myopathy are sporadic, which means they occur in people with no history of the disorder in their family. However, several people with idiopathic inflammatory myopathy have had close relatives with autoimmune disorders. Autoimmune diseases occur when the immune system malfunctions and attacks the body's tissues and organs. A small percentage of all cases of idiopathic inflammatory myopathy have been reported to run in families; however, the condition does not have a clear pattern of inheritance. Multiple genetic and environmental factors likely play a part in determining the risk of developing this disorder. As a result, inheriting a genetic variation linked with idiopathic inflammatory myopathy does not mean that a person will develop the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to idiopathic inflammatory myopathy ? | Idiopathic inflammatory myopathy is thought to arise from a combination of genetic and environmental factors. The term "idiopathic" indicates that the specific cause of the disorder is unknown. Researchers have identified variations in several genes that may influence the risk of developing idiopathic inflammatory myopathy. The most commonly associated genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders (such as viruses and bacteria). Each HLA gene has many different normal variations, allowing each person's immune system to react to a wide range of foreign proteins. Specific variations of several HLA genes seem to affect the risk of developing idiopathic inflammatory myopathy. Researchers are studying variations in other genes related to the body's immune function to understand how they contribute to the risk of developing idiopathic inflammatory myopathy. It is likely that specific genetic variations increase a person's risk of developing idiopathic inflammatory myopathy, and then exposure to certain environmental factors triggers the disorder. Infection, exposure to certain medications, and exposure to ultraviolet light (such as sunlight) have been identified as possible environmental triggers, but most risk factors for this condition remain unknown. |
Idiopathic inflammatory myopathy is a group of disorders characterized by inflammation of the muscles used for movement (skeletal muscles). Idiopathic inflammatory myopathy usually appears in adults between ages 40 and 60 or in children between ages 5 and 15, though it can occur at any age. The primary symptom of idiopathic inflammatory myopathy is muscle weakness, which develops gradually over a period of weeks to months or even years. Other symptoms include joint pain and general tiredness (fatigue). There are several forms of idiopathic inflammatory myopathy, including polymyositis, dermatomyositis, and sporadic inclusion body myositis. Polymyositis and dermatomyositis involve weakness of the muscles closest to the center of the body (proximal muscles), such as the muscles of the hips and thighs, upper arms, and neck. People with these forms of idiopathic inflammatory myopathy may find it difficult to climb stairs, get up from a seated position, or lift items above their head. In some cases, muscle weakness may make swallowing or breathing difficult. Polymyositis and dermatomyositis have similar symptoms, but dermatomyositis is distinguished by a reddish or purplish rash on the eyelids, elbows, knees, or knuckles. Sometimes, abnormal calcium deposits form hard, painful bumps under the skin (calcinosis). In sporadic inclusion body myositis, the muscles most affected are those of the wrists and fingers and the front of the thigh. Affected individuals may frequently stumble while walking and find it difficult to grasp items. As in dermatomyositis and polymyositis, swallowing can be difficult. The incidence of idiopathic inflammatory myopathy is approximately 2 to 8 cases per million people each year. For unknown reasons, polymyositis and dermatomyositis are about twice as common in women as in men, while sporadic inclusion body myositis is more common in men. Idiopathic inflammatory myopathy is thought to arise from a combination of genetic and environmental factors. The term "idiopathic" indicates that the specific cause of the disorder is unknown. Researchers have identified variations in several genes that may influence the risk of developing idiopathic inflammatory myopathy. The most commonly associated genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders (such as viruses and bacteria). Each HLA gene has many different normal variations, allowing each person's immune system to react to a wide range of foreign proteins. Specific variations of several HLA genes seem to affect the risk of developing idiopathic inflammatory myopathy. Researchers are studying variations in other genes related to the body's immune function to understand how they contribute to the risk of developing idiopathic inflammatory myopathy. It is likely that specific genetic variations increase a person's risk of developing idiopathic inflammatory myopathy, and then exposure to certain environmental factors triggers the disorder. Infection, exposure to certain medications, and exposure to ultraviolet light (such as sunlight) have been identified as possible environmental triggers, but most risk factors for this condition remain unknown. Additional Information from NCBI Gene: Most cases of idiopathic inflammatory myopathy are sporadic, which means they occur in people with no history of the disorder in their family. However, several people with idiopathic inflammatory myopathy have had close relatives with autoimmune disorders. Autoimmune diseases occur when the immune system malfunctions and attacks the body's tissues and organs. A small percentage of all cases of idiopathic inflammatory myopathy have been reported to run in families; however, the condition does not have a clear pattern of inheritance. Multiple genetic and environmental factors likely play a part in determining the risk of developing this disorder. As a result, inheriting a genetic variation linked with idiopathic inflammatory myopathy does not mean that a person will develop the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is idiopathic inflammatory myopathy inherited ? | Most cases of idiopathic inflammatory myopathy are sporadic, which means they occur in people with no history of the disorder in their family. However, several people with idiopathic inflammatory myopathy have had close relatives with autoimmune disorders. Autoimmune diseases occur when the immune system malfunctions and attacks the body's tissues and organs. A small percentage of all cases of idiopathic inflammatory myopathy have been reported to run in families; however, the condition does not have a clear pattern of inheritance. Multiple genetic and environmental factors likely play a part in determining the risk of developing this disorder. As a result, inheriting a genetic variation linked with idiopathic inflammatory myopathy does not mean that a person will develop the condition. |
Idiopathic inflammatory myopathy is a group of disorders characterized by inflammation of the muscles used for movement (skeletal muscles). Idiopathic inflammatory myopathy usually appears in adults between ages 40 and 60 or in children between ages 5 and 15, though it can occur at any age. The primary symptom of idiopathic inflammatory myopathy is muscle weakness, which develops gradually over a period of weeks to months or even years. Other symptoms include joint pain and general tiredness (fatigue). There are several forms of idiopathic inflammatory myopathy, including polymyositis, dermatomyositis, and sporadic inclusion body myositis. Polymyositis and dermatomyositis involve weakness of the muscles closest to the center of the body (proximal muscles), such as the muscles of the hips and thighs, upper arms, and neck. People with these forms of idiopathic inflammatory myopathy may find it difficult to climb stairs, get up from a seated position, or lift items above their head. In some cases, muscle weakness may make swallowing or breathing difficult. Polymyositis and dermatomyositis have similar symptoms, but dermatomyositis is distinguished by a reddish or purplish rash on the eyelids, elbows, knees, or knuckles. Sometimes, abnormal calcium deposits form hard, painful bumps under the skin (calcinosis). In sporadic inclusion body myositis, the muscles most affected are those of the wrists and fingers and the front of the thigh. Affected individuals may frequently stumble while walking and find it difficult to grasp items. As in dermatomyositis and polymyositis, swallowing can be difficult. The incidence of idiopathic inflammatory myopathy is approximately 2 to 8 cases per million people each year. For unknown reasons, polymyositis and dermatomyositis are about twice as common in women as in men, while sporadic inclusion body myositis is more common in men. Idiopathic inflammatory myopathy is thought to arise from a combination of genetic and environmental factors. The term "idiopathic" indicates that the specific cause of the disorder is unknown. Researchers have identified variations in several genes that may influence the risk of developing idiopathic inflammatory myopathy. The most commonly associated genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders (such as viruses and bacteria). Each HLA gene has many different normal variations, allowing each person's immune system to react to a wide range of foreign proteins. Specific variations of several HLA genes seem to affect the risk of developing idiopathic inflammatory myopathy. Researchers are studying variations in other genes related to the body's immune function to understand how they contribute to the risk of developing idiopathic inflammatory myopathy. It is likely that specific genetic variations increase a person's risk of developing idiopathic inflammatory myopathy, and then exposure to certain environmental factors triggers the disorder. Infection, exposure to certain medications, and exposure to ultraviolet light (such as sunlight) have been identified as possible environmental triggers, but most risk factors for this condition remain unknown. Additional Information from NCBI Gene: Most cases of idiopathic inflammatory myopathy are sporadic, which means they occur in people with no history of the disorder in their family. However, several people with idiopathic inflammatory myopathy have had close relatives with autoimmune disorders. Autoimmune diseases occur when the immune system malfunctions and attacks the body's tissues and organs. A small percentage of all cases of idiopathic inflammatory myopathy have been reported to run in families; however, the condition does not have a clear pattern of inheritance. Multiple genetic and environmental factors likely play a part in determining the risk of developing this disorder. As a result, inheriting a genetic variation linked with idiopathic inflammatory myopathy does not mean that a person will develop the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for idiopathic inflammatory myopathy ? | These resources address the diagnosis or management of idiopathic inflammatory myopathy: - Genetic Testing Registry: Idiopathic myopathy - Genetic Testing Registry: Inclusion body myositis - Johns Hopkins Myositis Center: Diagnosis - Johns Hopkins Myositis Center: Treatment - Muscular Dystrophy Association: Facts about Inflammatory Myopathies (Myositis) These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Mitochondrial trifunctional protein deficiency is a rare condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). Signs and symptoms of mitochondrial trifunctional protein deficiency may begin during infancy or later in life. Features that occur during infancy include feeding difficulties, lack of energy (lethargy), low blood sugar (hypoglycemia), weak muscle tone (hypotonia), and liver problems. Infants with this disorder are also at high risk for serious heart problems, breathing difficulties, coma, and sudden death. Signs and symptoms of mitochondrial trifunctional protein deficiency that may begin after infancy include hypotonia, muscle pain, a breakdown of muscle tissue, and a loss of sensation in the extremities (peripheral neuropathy). Problems related to mitochondrial trifunctional protein deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections. Mitochondrial trifunctional protein deficiency is a rare disorder; its incidence is unknown. Mutations in the HADHA and HADHB genes cause mitochondrial trifunctional protein deficiency. These genes each provide instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. This enzyme complex is required to break down (metabolize) a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. Mutations in the HADHA or HADHB genes that cause mitochondrial trifunctional protein deficiency disrupt all three functions of this enzyme complex. Without enough of this enzyme complex, long-chain fatty acids from food and body fat cannot be metabolized and processed. As a result, these fatty acids are not converted to energy, which can lead to some features of this disorder, such as lethargy and hypoglycemia. Long-chain fatty acids or partially metabolized fatty acids may also build up and damage the liver, heart, and muscles. This abnormal buildup causes the other signs and symptoms of mitochondrial trifunctional protein deficiency. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) mitochondrial trifunctional protein deficiency ? | Mitochondrial trifunctional protein deficiency is a rare condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). Signs and symptoms of mitochondrial trifunctional protein deficiency may begin during infancy or later in life. Features that occur during infancy include feeding difficulties, lack of energy (lethargy), low blood sugar (hypoglycemia), weak muscle tone (hypotonia), and liver problems. Infants with this disorder are also at high risk for serious heart problems, breathing difficulties, coma, and sudden death. Signs and symptoms of mitochondrial trifunctional protein deficiency that may begin after infancy include hypotonia, muscle pain, a breakdown of muscle tissue, and a loss of sensation in the extremities (peripheral neuropathy). Problems related to mitochondrial trifunctional protein deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections. |
Mitochondrial trifunctional protein deficiency is a rare condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). Signs and symptoms of mitochondrial trifunctional protein deficiency may begin during infancy or later in life. Features that occur during infancy include feeding difficulties, lack of energy (lethargy), low blood sugar (hypoglycemia), weak muscle tone (hypotonia), and liver problems. Infants with this disorder are also at high risk for serious heart problems, breathing difficulties, coma, and sudden death. Signs and symptoms of mitochondrial trifunctional protein deficiency that may begin after infancy include hypotonia, muscle pain, a breakdown of muscle tissue, and a loss of sensation in the extremities (peripheral neuropathy). Problems related to mitochondrial trifunctional protein deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections. Mitochondrial trifunctional protein deficiency is a rare disorder; its incidence is unknown. Mutations in the HADHA and HADHB genes cause mitochondrial trifunctional protein deficiency. These genes each provide instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. This enzyme complex is required to break down (metabolize) a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. Mutations in the HADHA or HADHB genes that cause mitochondrial trifunctional protein deficiency disrupt all three functions of this enzyme complex. Without enough of this enzyme complex, long-chain fatty acids from food and body fat cannot be metabolized and processed. As a result, these fatty acids are not converted to energy, which can lead to some features of this disorder, such as lethargy and hypoglycemia. Long-chain fatty acids or partially metabolized fatty acids may also build up and damage the liver, heart, and muscles. This abnormal buildup causes the other signs and symptoms of mitochondrial trifunctional protein deficiency. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by mitochondrial trifunctional protein deficiency ? | Mitochondrial trifunctional protein deficiency is a rare disorder; its incidence is unknown. |
Mitochondrial trifunctional protein deficiency is a rare condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). Signs and symptoms of mitochondrial trifunctional protein deficiency may begin during infancy or later in life. Features that occur during infancy include feeding difficulties, lack of energy (lethargy), low blood sugar (hypoglycemia), weak muscle tone (hypotonia), and liver problems. Infants with this disorder are also at high risk for serious heart problems, breathing difficulties, coma, and sudden death. Signs and symptoms of mitochondrial trifunctional protein deficiency that may begin after infancy include hypotonia, muscle pain, a breakdown of muscle tissue, and a loss of sensation in the extremities (peripheral neuropathy). Problems related to mitochondrial trifunctional protein deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections. Mitochondrial trifunctional protein deficiency is a rare disorder; its incidence is unknown. Mutations in the HADHA and HADHB genes cause mitochondrial trifunctional protein deficiency. These genes each provide instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. This enzyme complex is required to break down (metabolize) a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. Mutations in the HADHA or HADHB genes that cause mitochondrial trifunctional protein deficiency disrupt all three functions of this enzyme complex. Without enough of this enzyme complex, long-chain fatty acids from food and body fat cannot be metabolized and processed. As a result, these fatty acids are not converted to energy, which can lead to some features of this disorder, such as lethargy and hypoglycemia. Long-chain fatty acids or partially metabolized fatty acids may also build up and damage the liver, heart, and muscles. This abnormal buildup causes the other signs and symptoms of mitochondrial trifunctional protein deficiency. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to mitochondrial trifunctional protein deficiency ? | Mutations in the HADHA and HADHB genes cause mitochondrial trifunctional protein deficiency. These genes each provide instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. This enzyme complex is required to break down (metabolize) a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. Mutations in the HADHA or HADHB genes that cause mitochondrial trifunctional protein deficiency disrupt all three functions of this enzyme complex. Without enough of this enzyme complex, long-chain fatty acids from food and body fat cannot be metabolized and processed. As a result, these fatty acids are not converted to energy, which can lead to some features of this disorder, such as lethargy and hypoglycemia. Long-chain fatty acids or partially metabolized fatty acids may also build up and damage the liver, heart, and muscles. This abnormal buildup causes the other signs and symptoms of mitochondrial trifunctional protein deficiency. |
Mitochondrial trifunctional protein deficiency is a rare condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). Signs and symptoms of mitochondrial trifunctional protein deficiency may begin during infancy or later in life. Features that occur during infancy include feeding difficulties, lack of energy (lethargy), low blood sugar (hypoglycemia), weak muscle tone (hypotonia), and liver problems. Infants with this disorder are also at high risk for serious heart problems, breathing difficulties, coma, and sudden death. Signs and symptoms of mitochondrial trifunctional protein deficiency that may begin after infancy include hypotonia, muscle pain, a breakdown of muscle tissue, and a loss of sensation in the extremities (peripheral neuropathy). Problems related to mitochondrial trifunctional protein deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections. Mitochondrial trifunctional protein deficiency is a rare disorder; its incidence is unknown. Mutations in the HADHA and HADHB genes cause mitochondrial trifunctional protein deficiency. These genes each provide instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. This enzyme complex is required to break down (metabolize) a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. Mutations in the HADHA or HADHB genes that cause mitochondrial trifunctional protein deficiency disrupt all three functions of this enzyme complex. Without enough of this enzyme complex, long-chain fatty acids from food and body fat cannot be metabolized and processed. As a result, these fatty acids are not converted to energy, which can lead to some features of this disorder, such as lethargy and hypoglycemia. Long-chain fatty acids or partially metabolized fatty acids may also build up and damage the liver, heart, and muscles. This abnormal buildup causes the other signs and symptoms of mitochondrial trifunctional protein deficiency. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is mitochondrial trifunctional protein deficiency inherited ? | This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. |
Mitochondrial trifunctional protein deficiency is a rare condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). Signs and symptoms of mitochondrial trifunctional protein deficiency may begin during infancy or later in life. Features that occur during infancy include feeding difficulties, lack of energy (lethargy), low blood sugar (hypoglycemia), weak muscle tone (hypotonia), and liver problems. Infants with this disorder are also at high risk for serious heart problems, breathing difficulties, coma, and sudden death. Signs and symptoms of mitochondrial trifunctional protein deficiency that may begin after infancy include hypotonia, muscle pain, a breakdown of muscle tissue, and a loss of sensation in the extremities (peripheral neuropathy). Problems related to mitochondrial trifunctional protein deficiency can be triggered by periods of fasting or by illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe disorder that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections. Mitochondrial trifunctional protein deficiency is a rare disorder; its incidence is unknown. Mutations in the HADHA and HADHB genes cause mitochondrial trifunctional protein deficiency. These genes each provide instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. This enzyme complex is required to break down (metabolize) a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. Mutations in the HADHA or HADHB genes that cause mitochondrial trifunctional protein deficiency disrupt all three functions of this enzyme complex. Without enough of this enzyme complex, long-chain fatty acids from food and body fat cannot be metabolized and processed. As a result, these fatty acids are not converted to energy, which can lead to some features of this disorder, such as lethargy and hypoglycemia. Long-chain fatty acids or partially metabolized fatty acids may also build up and damage the liver, heart, and muscles. This abnormal buildup causes the other signs and symptoms of mitochondrial trifunctional protein deficiency. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for mitochondrial trifunctional protein deficiency ? | These resources address the diagnosis or management of mitochondrial trifunctional protein deficiency: - Baby's First Test - Genetic Testing Registry: Mitochondrial trifunctional protein deficiency - MedlinePlus Encyclopedia: Hypoglycemia - MedlinePlus Encyclopedia: Peripheral Neuropathy These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Hereditary myopathy with early respiratory failure (HMERF) is an inherited disease that affects muscles used for movement (skeletal muscles) and muscles that are needed for breathing (respiratory muscles). The major signs and symptoms of HMERF usually appear in adulthood, often in the mid-thirties. Among the earliest signs of the condition are breathing problems and difficulty walking. Weakness of the respiratory muscles, particularly the diaphragm (the muscle that separates the organs in the abdomen from those in the chest), causes breathing problems. This weakness worsens over time and can lead to life-threatening respiratory failure. Some affected individuals have weakness of muscles of the lower leg and foot, which makes it difficult to lift the toes while walking, a condition known as foot drop. Other muscles that become weak in people with HMERF include those of the hips, thighs, upper arms, and neck. When viewed under a microscope, muscle fibers from affected individuals contain abnormal structures called cytoplasmic bodies. In many cases, the cytoplasmic bodies are arranged side-by-side in a ring inside the muscle fiber, resembling a necklace (necklace cytoplasmic bodies). HMERF is a rare condition with an unknown prevalence. It has been found in populations worldwide. HMERF is caused by mutations in the TTN gene. This gene provides instructions for making a protein called titin. Titin plays an important role in muscles the body uses for movement (skeletal muscles) and in heart (cardiac) muscle. Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle contraction; they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of its most important jobs is to act as a backbone in these structures, providing structure, flexibility, and stability. Titin also plays a role in chemical signaling and in assembling new sarcomeres. The TTN gene mutations responsible for HMERF lead to the production of an altered version of the titin protein that cannot fold into its normal 3-dimensional shape. Researchers are studying how abnormally folded titin contributes to the muscle damage that underlies the signs and symptoms of HMERF. It is unclear why these effects are usually limited to skeletal muscles and respiratory muscles, and do not involve cardiac muscle. Rarely, people with the characteristic features of HMERF do not have identified mutations in the TTN gene. In these cases, the genetic cause of the condition is unknown. HMERF is typically inherited in an autosomal dominant pattern, which means one copy of the altered TTN gene in each cell is sufficient to cause the disorder. An affected person usually has one parent with the condition. In rare cases, a specific mutation in one copy of the TTN gene leads to mild signs and symptoms of the condition, such as respiratory problems that begin later than is typical in HMERF with no other muscle weakness. However, family members who have the mutation in both copies of the gene have severe features of HMERF. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) hereditary myopathy with early respiratory failure ? | Hereditary myopathy with early respiratory failure (HMERF) is an inherited muscle disease that predominantly affects muscles close to the center of the body (proximal muscles) and muscles that are needed for breathing. The major signs and symptoms of HMERF usually appear in adulthood, on average around age 35. Among the earliest muscles affected in HMERF are the neck flexors, which are muscles at the front of the neck that help hold the head up. Other proximal muscles that become weak in people with HMERF include those of the hips, thighs, and upper arms. Some affected individuals have also reported weakness in muscles of the lower leg and foot called the dorsal foot extensors. HMERF also causes severe weakness in muscles of the chest that are involved in breathing, particularly the diaphragm. This weakness leads to breathing problems and life-threatening respiratory failure. |
Hereditary myopathy with early respiratory failure (HMERF) is an inherited disease that affects muscles used for movement (skeletal muscles) and muscles that are needed for breathing (respiratory muscles). The major signs and symptoms of HMERF usually appear in adulthood, often in the mid-thirties. Among the earliest signs of the condition are breathing problems and difficulty walking. Weakness of the respiratory muscles, particularly the diaphragm (the muscle that separates the organs in the abdomen from those in the chest), causes breathing problems. This weakness worsens over time and can lead to life-threatening respiratory failure. Some affected individuals have weakness of muscles of the lower leg and foot, which makes it difficult to lift the toes while walking, a condition known as foot drop. Other muscles that become weak in people with HMERF include those of the hips, thighs, upper arms, and neck. When viewed under a microscope, muscle fibers from affected individuals contain abnormal structures called cytoplasmic bodies. In many cases, the cytoplasmic bodies are arranged side-by-side in a ring inside the muscle fiber, resembling a necklace (necklace cytoplasmic bodies). HMERF is a rare condition with an unknown prevalence. It has been found in populations worldwide. HMERF is caused by mutations in the TTN gene. This gene provides instructions for making a protein called titin. Titin plays an important role in muscles the body uses for movement (skeletal muscles) and in heart (cardiac) muscle. Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle contraction; they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of its most important jobs is to act as a backbone in these structures, providing structure, flexibility, and stability. Titin also plays a role in chemical signaling and in assembling new sarcomeres. The TTN gene mutations responsible for HMERF lead to the production of an altered version of the titin protein that cannot fold into its normal 3-dimensional shape. Researchers are studying how abnormally folded titin contributes to the muscle damage that underlies the signs and symptoms of HMERF. It is unclear why these effects are usually limited to skeletal muscles and respiratory muscles, and do not involve cardiac muscle. Rarely, people with the characteristic features of HMERF do not have identified mutations in the TTN gene. In these cases, the genetic cause of the condition is unknown. HMERF is typically inherited in an autosomal dominant pattern, which means one copy of the altered TTN gene in each cell is sufficient to cause the disorder. An affected person usually has one parent with the condition. In rare cases, a specific mutation in one copy of the TTN gene leads to mild signs and symptoms of the condition, such as respiratory problems that begin later than is typical in HMERF with no other muscle weakness. However, family members who have the mutation in both copies of the gene have severe features of HMERF. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by hereditary myopathy with early respiratory failure ? | HMERF is a rare condition. It has been reported in several families of Swedish and French descent, and in at least one individual from Italy. |
Hereditary myopathy with early respiratory failure (HMERF) is an inherited disease that affects muscles used for movement (skeletal muscles) and muscles that are needed for breathing (respiratory muscles). The major signs and symptoms of HMERF usually appear in adulthood, often in the mid-thirties. Among the earliest signs of the condition are breathing problems and difficulty walking. Weakness of the respiratory muscles, particularly the diaphragm (the muscle that separates the organs in the abdomen from those in the chest), causes breathing problems. This weakness worsens over time and can lead to life-threatening respiratory failure. Some affected individuals have weakness of muscles of the lower leg and foot, which makes it difficult to lift the toes while walking, a condition known as foot drop. Other muscles that become weak in people with HMERF include those of the hips, thighs, upper arms, and neck. When viewed under a microscope, muscle fibers from affected individuals contain abnormal structures called cytoplasmic bodies. In many cases, the cytoplasmic bodies are arranged side-by-side in a ring inside the muscle fiber, resembling a necklace (necklace cytoplasmic bodies). HMERF is a rare condition with an unknown prevalence. It has been found in populations worldwide. HMERF is caused by mutations in the TTN gene. This gene provides instructions for making a protein called titin. Titin plays an important role in muscles the body uses for movement (skeletal muscles) and in heart (cardiac) muscle. Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle contraction; they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of its most important jobs is to act as a backbone in these structures, providing structure, flexibility, and stability. Titin also plays a role in chemical signaling and in assembling new sarcomeres. The TTN gene mutations responsible for HMERF lead to the production of an altered version of the titin protein that cannot fold into its normal 3-dimensional shape. Researchers are studying how abnormally folded titin contributes to the muscle damage that underlies the signs and symptoms of HMERF. It is unclear why these effects are usually limited to skeletal muscles and respiratory muscles, and do not involve cardiac muscle. Rarely, people with the characteristic features of HMERF do not have identified mutations in the TTN gene. In these cases, the genetic cause of the condition is unknown. HMERF is typically inherited in an autosomal dominant pattern, which means one copy of the altered TTN gene in each cell is sufficient to cause the disorder. An affected person usually has one parent with the condition. In rare cases, a specific mutation in one copy of the TTN gene leads to mild signs and symptoms of the condition, such as respiratory problems that begin later than is typical in HMERF with no other muscle weakness. However, family members who have the mutation in both copies of the gene have severe features of HMERF. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to hereditary myopathy with early respiratory failure ? | HMERF can be caused by a mutation in the TTN gene. This gene provides instructions for making a protein called titin. Titin plays an important role in muscles the body uses for movement (skeletal muscles) and in heart (cardiac) muscle. Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle contraction; they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of its most important jobs is to provide structure, flexibility, and stability to these cell structures. Titin also plays a role in chemical signaling and in assembling new sarcomeres. The TTN gene mutation responsible for HMERF leads to the production of an altered version of the titin protein. Studies suggest that this change may disrupt titin's interactions with other proteins within sarcomeres and interfere with the protein's role in chemical signaling. Consequently, muscle fibers become damaged and weaken over time. It is unclear why these effects are usually limited to proximal muscles and muscles involved in breathing. Some people with the characteristic features of HMERF do not have identified mutations in the TTN gene. In these cases, the genetic cause of the condition is unknown. |
Hereditary myopathy with early respiratory failure (HMERF) is an inherited disease that affects muscles used for movement (skeletal muscles) and muscles that are needed for breathing (respiratory muscles). The major signs and symptoms of HMERF usually appear in adulthood, often in the mid-thirties. Among the earliest signs of the condition are breathing problems and difficulty walking. Weakness of the respiratory muscles, particularly the diaphragm (the muscle that separates the organs in the abdomen from those in the chest), causes breathing problems. This weakness worsens over time and can lead to life-threatening respiratory failure. Some affected individuals have weakness of muscles of the lower leg and foot, which makes it difficult to lift the toes while walking, a condition known as foot drop. Other muscles that become weak in people with HMERF include those of the hips, thighs, upper arms, and neck. When viewed under a microscope, muscle fibers from affected individuals contain abnormal structures called cytoplasmic bodies. In many cases, the cytoplasmic bodies are arranged side-by-side in a ring inside the muscle fiber, resembling a necklace (necklace cytoplasmic bodies). HMERF is a rare condition with an unknown prevalence. It has been found in populations worldwide. HMERF is caused by mutations in the TTN gene. This gene provides instructions for making a protein called titin. Titin plays an important role in muscles the body uses for movement (skeletal muscles) and in heart (cardiac) muscle. Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle contraction; they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of its most important jobs is to act as a backbone in these structures, providing structure, flexibility, and stability. Titin also plays a role in chemical signaling and in assembling new sarcomeres. The TTN gene mutations responsible for HMERF lead to the production of an altered version of the titin protein that cannot fold into its normal 3-dimensional shape. Researchers are studying how abnormally folded titin contributes to the muscle damage that underlies the signs and symptoms of HMERF. It is unclear why these effects are usually limited to skeletal muscles and respiratory muscles, and do not involve cardiac muscle. Rarely, people with the characteristic features of HMERF do not have identified mutations in the TTN gene. In these cases, the genetic cause of the condition is unknown. HMERF is typically inherited in an autosomal dominant pattern, which means one copy of the altered TTN gene in each cell is sufficient to cause the disorder. An affected person usually has one parent with the condition. In rare cases, a specific mutation in one copy of the TTN gene leads to mild signs and symptoms of the condition, such as respiratory problems that begin later than is typical in HMERF with no other muscle weakness. However, family members who have the mutation in both copies of the gene have severe features of HMERF. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is hereditary myopathy with early respiratory failure inherited ? | This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. |
Hereditary myopathy with early respiratory failure (HMERF) is an inherited disease that affects muscles used for movement (skeletal muscles) and muscles that are needed for breathing (respiratory muscles). The major signs and symptoms of HMERF usually appear in adulthood, often in the mid-thirties. Among the earliest signs of the condition are breathing problems and difficulty walking. Weakness of the respiratory muscles, particularly the diaphragm (the muscle that separates the organs in the abdomen from those in the chest), causes breathing problems. This weakness worsens over time and can lead to life-threatening respiratory failure. Some affected individuals have weakness of muscles of the lower leg and foot, which makes it difficult to lift the toes while walking, a condition known as foot drop. Other muscles that become weak in people with HMERF include those of the hips, thighs, upper arms, and neck. When viewed under a microscope, muscle fibers from affected individuals contain abnormal structures called cytoplasmic bodies. In many cases, the cytoplasmic bodies are arranged side-by-side in a ring inside the muscle fiber, resembling a necklace (necklace cytoplasmic bodies). HMERF is a rare condition with an unknown prevalence. It has been found in populations worldwide. HMERF is caused by mutations in the TTN gene. This gene provides instructions for making a protein called titin. Titin plays an important role in muscles the body uses for movement (skeletal muscles) and in heart (cardiac) muscle. Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle contraction; they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of its most important jobs is to act as a backbone in these structures, providing structure, flexibility, and stability. Titin also plays a role in chemical signaling and in assembling new sarcomeres. The TTN gene mutations responsible for HMERF lead to the production of an altered version of the titin protein that cannot fold into its normal 3-dimensional shape. Researchers are studying how abnormally folded titin contributes to the muscle damage that underlies the signs and symptoms of HMERF. It is unclear why these effects are usually limited to skeletal muscles and respiratory muscles, and do not involve cardiac muscle. Rarely, people with the characteristic features of HMERF do not have identified mutations in the TTN gene. In these cases, the genetic cause of the condition is unknown. HMERF is typically inherited in an autosomal dominant pattern, which means one copy of the altered TTN gene in each cell is sufficient to cause the disorder. An affected person usually has one parent with the condition. In rare cases, a specific mutation in one copy of the TTN gene leads to mild signs and symptoms of the condition, such as respiratory problems that begin later than is typical in HMERF with no other muscle weakness. However, family members who have the mutation in both copies of the gene have severe features of HMERF. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for hereditary myopathy with early respiratory failure ? | These resources address the diagnosis or management of HMERF: - Gene Review: Gene Review: Hereditary Myopathy with Early Respiratory Failure (HMERF) - Genetic Testing Registry: Hereditary myopathy with early respiratory failure - National Heart, Lung, and Blood Institute: How Is Respiratory Failure Diagnosed? - National Heart, Lung, and Blood Institute: How Is Respiratory Failure Treated? These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Sjögren-Larsson syndrome is a condition characterized by dry, scaly skin (ichthyosis); neurological problems; and eye problems. These symptoms are apparent by early childhood and usually do not worsen with age. Affected infants tend to be born prematurely. At birth the skin is red (erythema), but later in infancy the skin becomes dry, rough, and scaly with a brownish or yellowish tone. Mild to severe itchiness (pruritus) is also common. These skin abnormalities are generally dispersed over the whole body, most severely affecting the nape of the neck, the torso, and the extremities. The skin of the face is usually not affected. People with this condition may also have neurological signs and symptoms. Most affected individuals have leukoencephalopathy, which is a change in a type of brain tissue called white matter. White matter consists of nerve fibers covered by a substance (myelin) that insulates and protects the nerves. The leukoencephalopathy is thought to contribute to many of the neurological signs and symptoms in people with Sjögren-Larsson syndrome. Most affected individuals have intellectual disability that varies from mild to profound and is usually apparent by early childhood. People with Sjögren-Larsson syndrome have speech difficulties (dysarthria) and delayed speech. Usually they are able to produce only short sentences with poorly formed words. Rarely, people with this condition have normal intelligence. In addition, approximately 40 percent of people with Sjögren-Larsson syndrome have seizures. Children with this condition often experience delayed development of motor skills (such as crawling and walking) due to abnormal muscle stiffness (spasticity) that is typically in their legs and, less commonly, also in their arms. About one-half of people with Sjögren-Larsson syndrome require wheelchair assistance and many others need some form of support to walk. Affected individuals have tiny crystals in the light-sensitive tissue at the back of the eye (retina) that can be seen during an eye exam. Based on their appearance, these retinal crystals are often called glistening white dots. These white dots are usually apparent by early childhood, and it is unclear if they affect normal vision. People with Sjögren-Larsson syndrome may also have nearsightedness (myopia) or an increased sensitivity to light (photophobia). Sjögren-Larsson syndrome was first observed in Sweden, where the prevalence of this condition is 1 per 250,000 individuals. Outside Sweden, the prevalence of this condition is unknown. Mutations in the ALDH3A2 gene cause Sjögren-Larsson syndrome. The ALDH3A2 gene provides instructions for making an enzyme called fatty aldehyde dehydrogenase (FALDH). The FALDH enzyme is part of a multistep process called fatty acid oxidation in which fats are broken down and converted into energy. Specifically, the FALDH enzyme breaks down molecules called fatty aldehydes to fatty acids. ALDH3A2 gene mutations disrupt the normal process of fatty acid oxidation. Most mutations result in the production of a FALDH enzyme that is unable to break down fatty aldehyde molecules. As a result, fats that cannot be broken down build up in cells. Within skin cells, excess fat accumulation can interfere with the formation of membranes that act as protective barriers to control water loss. As a result of the loss of these protective barriers, the skin has difficulty maintaining its water balance, resulting in dry, scaly skin. In the brain, the consequences of excess fat accumulation are unclear, but it is likely that an abundance of fat disrupts the formation of myelin. Myelin is the covering that protects nerves and promotes the efficient transmission of nerve impulses. A lack of myelin can lead to neurological problems such as intellectual disability and walking difficulties. The cause of the eye problems is unclear, but it is also likely related to a disruption in the breakdown of fats. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) Sjgren-Larsson syndrome ? | Sjgren-Larsson syndrome is a condition characterized by dry, scaly skin (ichthyosis); neurological problems; and eye problems. These symptoms are apparent by early childhood and usually do not worsen with age. Affected infants tend to be born prematurely. At birth the skin is red (erythema), but later in infancy the skin becomes dry, rough, and scaly with a brownish or yellowish tone. Mild to severe itchiness (pruritus) is also common. These skin abnormalities are generally dispersed over the whole body, most severely affecting the nape of the neck, the torso, and the extremities. The skin of the face is usually not affected. People with this condition may also have neurological signs and symptoms. Most affected individuals have leukoencephalopathy, which is a change in a type of brain tissue called white matter. White matter consists of nerve fibers covered by a substance (myelin) that insulates and protects the nerves. The leukoencephalopathy is thought to contribute to many of the neurological signs and symptoms in people with Sjgren-Larsson syndrome. Most affected individuals have intellectual disability that varies from mild to profound and is usually apparent by early childhood. People with Sjgren-Larsson syndrome have speech difficulties (dysarthria) and delayed speech. Usually they are able to produce only short sentences with poorly formed words. Rarely, people with this condition have normal intelligence. In addition, approximately 40 percent of people with Sjgren-Larsson syndrome have seizures. Children with this condition often experience delayed development of motor skills (such as crawling and walking) due to abnormal muscle stiffness (spasticity) that is typically in their legs and, less commonly, also in their arms. About one-half of people with Sjgren-Larsson syndrome require wheelchair assistance and many others need some form of support to walk. Affected individuals have tiny crystals in the light-sensitive tissue at the back of the eye (retina) that can be seen during an eye exam. Based on their appearance, these retinal crystals are often called glistening white dots. These white dots are usually apparent by early childhood, and it is unclear if they affect normal vision. People with Sjgren-Larsson syndrome may also have nearsightedness (myopia) or an increased sensitivity to light (photophobia). |
Sjögren-Larsson syndrome is a condition characterized by dry, scaly skin (ichthyosis); neurological problems; and eye problems. These symptoms are apparent by early childhood and usually do not worsen with age. Affected infants tend to be born prematurely. At birth the skin is red (erythema), but later in infancy the skin becomes dry, rough, and scaly with a brownish or yellowish tone. Mild to severe itchiness (pruritus) is also common. These skin abnormalities are generally dispersed over the whole body, most severely affecting the nape of the neck, the torso, and the extremities. The skin of the face is usually not affected. People with this condition may also have neurological signs and symptoms. Most affected individuals have leukoencephalopathy, which is a change in a type of brain tissue called white matter. White matter consists of nerve fibers covered by a substance (myelin) that insulates and protects the nerves. The leukoencephalopathy is thought to contribute to many of the neurological signs and symptoms in people with Sjögren-Larsson syndrome. Most affected individuals have intellectual disability that varies from mild to profound and is usually apparent by early childhood. People with Sjögren-Larsson syndrome have speech difficulties (dysarthria) and delayed speech. Usually they are able to produce only short sentences with poorly formed words. Rarely, people with this condition have normal intelligence. In addition, approximately 40 percent of people with Sjögren-Larsson syndrome have seizures. Children with this condition often experience delayed development of motor skills (such as crawling and walking) due to abnormal muscle stiffness (spasticity) that is typically in their legs and, less commonly, also in their arms. About one-half of people with Sjögren-Larsson syndrome require wheelchair assistance and many others need some form of support to walk. Affected individuals have tiny crystals in the light-sensitive tissue at the back of the eye (retina) that can be seen during an eye exam. Based on their appearance, these retinal crystals are often called glistening white dots. These white dots are usually apparent by early childhood, and it is unclear if they affect normal vision. People with Sjögren-Larsson syndrome may also have nearsightedness (myopia) or an increased sensitivity to light (photophobia). Sjögren-Larsson syndrome was first observed in Sweden, where the prevalence of this condition is 1 per 250,000 individuals. Outside Sweden, the prevalence of this condition is unknown. Mutations in the ALDH3A2 gene cause Sjögren-Larsson syndrome. The ALDH3A2 gene provides instructions for making an enzyme called fatty aldehyde dehydrogenase (FALDH). The FALDH enzyme is part of a multistep process called fatty acid oxidation in which fats are broken down and converted into energy. Specifically, the FALDH enzyme breaks down molecules called fatty aldehydes to fatty acids. ALDH3A2 gene mutations disrupt the normal process of fatty acid oxidation. Most mutations result in the production of a FALDH enzyme that is unable to break down fatty aldehyde molecules. As a result, fats that cannot be broken down build up in cells. Within skin cells, excess fat accumulation can interfere with the formation of membranes that act as protective barriers to control water loss. As a result of the loss of these protective barriers, the skin has difficulty maintaining its water balance, resulting in dry, scaly skin. In the brain, the consequences of excess fat accumulation are unclear, but it is likely that an abundance of fat disrupts the formation of myelin. Myelin is the covering that protects nerves and promotes the efficient transmission of nerve impulses. A lack of myelin can lead to neurological problems such as intellectual disability and walking difficulties. The cause of the eye problems is unclear, but it is also likely related to a disruption in the breakdown of fats. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by Sjgren-Larsson syndrome ? | Sjgren-Larsson syndrome was first observed in Sweden, where the prevalence of this condition is 1 per 250,000 individuals. Outside Sweden, the prevalence of this condition is unknown. |
Sjögren-Larsson syndrome is a condition characterized by dry, scaly skin (ichthyosis); neurological problems; and eye problems. These symptoms are apparent by early childhood and usually do not worsen with age. Affected infants tend to be born prematurely. At birth the skin is red (erythema), but later in infancy the skin becomes dry, rough, and scaly with a brownish or yellowish tone. Mild to severe itchiness (pruritus) is also common. These skin abnormalities are generally dispersed over the whole body, most severely affecting the nape of the neck, the torso, and the extremities. The skin of the face is usually not affected. People with this condition may also have neurological signs and symptoms. Most affected individuals have leukoencephalopathy, which is a change in a type of brain tissue called white matter. White matter consists of nerve fibers covered by a substance (myelin) that insulates and protects the nerves. The leukoencephalopathy is thought to contribute to many of the neurological signs and symptoms in people with Sjögren-Larsson syndrome. Most affected individuals have intellectual disability that varies from mild to profound and is usually apparent by early childhood. People with Sjögren-Larsson syndrome have speech difficulties (dysarthria) and delayed speech. Usually they are able to produce only short sentences with poorly formed words. Rarely, people with this condition have normal intelligence. In addition, approximately 40 percent of people with Sjögren-Larsson syndrome have seizures. Children with this condition often experience delayed development of motor skills (such as crawling and walking) due to abnormal muscle stiffness (spasticity) that is typically in their legs and, less commonly, also in their arms. About one-half of people with Sjögren-Larsson syndrome require wheelchair assistance and many others need some form of support to walk. Affected individuals have tiny crystals in the light-sensitive tissue at the back of the eye (retina) that can be seen during an eye exam. Based on their appearance, these retinal crystals are often called glistening white dots. These white dots are usually apparent by early childhood, and it is unclear if they affect normal vision. People with Sjögren-Larsson syndrome may also have nearsightedness (myopia) or an increased sensitivity to light (photophobia). Sjögren-Larsson syndrome was first observed in Sweden, where the prevalence of this condition is 1 per 250,000 individuals. Outside Sweden, the prevalence of this condition is unknown. Mutations in the ALDH3A2 gene cause Sjögren-Larsson syndrome. The ALDH3A2 gene provides instructions for making an enzyme called fatty aldehyde dehydrogenase (FALDH). The FALDH enzyme is part of a multistep process called fatty acid oxidation in which fats are broken down and converted into energy. Specifically, the FALDH enzyme breaks down molecules called fatty aldehydes to fatty acids. ALDH3A2 gene mutations disrupt the normal process of fatty acid oxidation. Most mutations result in the production of a FALDH enzyme that is unable to break down fatty aldehyde molecules. As a result, fats that cannot be broken down build up in cells. Within skin cells, excess fat accumulation can interfere with the formation of membranes that act as protective barriers to control water loss. As a result of the loss of these protective barriers, the skin has difficulty maintaining its water balance, resulting in dry, scaly skin. In the brain, the consequences of excess fat accumulation are unclear, but it is likely that an abundance of fat disrupts the formation of myelin. Myelin is the covering that protects nerves and promotes the efficient transmission of nerve impulses. A lack of myelin can lead to neurological problems such as intellectual disability and walking difficulties. The cause of the eye problems is unclear, but it is also likely related to a disruption in the breakdown of fats. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to Sjgren-Larsson syndrome ? | Mutations in the ALDH3A2 gene cause Sjgren-Larsson syndrome. The ALDH3A2 gene provides instructions for making an enzyme called fatty aldehyde dehydrogenase (FALDH). The FALDH enzyme is part of a multistep process called fatty acid oxidation in which fats are broken down and converted into energy. Specifically, the FALDH enzyme breaks down molecules called fatty aldehydes to fatty acids. ALDH3A2 gene mutations disrupt the normal process of fatty acid oxidation. Most mutations result in the production of a FALDH enzyme that is unable to break down fatty aldehyde molecules. As a result, fats that cannot be broken down build up in cells. Within skin cells, excess fat accumulation can interfere with the formation of membranes that act as protective barriers to control water loss. As a result of the loss of these protective barriers, the skin has difficulty maintaining its water balance, resulting in dry, scaly skin. In the brain, the consequences of excess fat accumulation are unclear, but it is likely that an abundance of fat disrupts the formation of myelin. Myelin is the covering that protects nerves and promotes the efficient transmission of nerve impulses. A lack of myelin can lead to neurological problems such as intellectual disability and walking difficulties. The cause of the eye problems is unclear, but it is also likely related to a disruption in the breakdown of fats. |
Sjögren-Larsson syndrome is a condition characterized by dry, scaly skin (ichthyosis); neurological problems; and eye problems. These symptoms are apparent by early childhood and usually do not worsen with age. Affected infants tend to be born prematurely. At birth the skin is red (erythema), but later in infancy the skin becomes dry, rough, and scaly with a brownish or yellowish tone. Mild to severe itchiness (pruritus) is also common. These skin abnormalities are generally dispersed over the whole body, most severely affecting the nape of the neck, the torso, and the extremities. The skin of the face is usually not affected. People with this condition may also have neurological signs and symptoms. Most affected individuals have leukoencephalopathy, which is a change in a type of brain tissue called white matter. White matter consists of nerve fibers covered by a substance (myelin) that insulates and protects the nerves. The leukoencephalopathy is thought to contribute to many of the neurological signs and symptoms in people with Sjögren-Larsson syndrome. Most affected individuals have intellectual disability that varies from mild to profound and is usually apparent by early childhood. People with Sjögren-Larsson syndrome have speech difficulties (dysarthria) and delayed speech. Usually they are able to produce only short sentences with poorly formed words. Rarely, people with this condition have normal intelligence. In addition, approximately 40 percent of people with Sjögren-Larsson syndrome have seizures. Children with this condition often experience delayed development of motor skills (such as crawling and walking) due to abnormal muscle stiffness (spasticity) that is typically in their legs and, less commonly, also in their arms. About one-half of people with Sjögren-Larsson syndrome require wheelchair assistance and many others need some form of support to walk. Affected individuals have tiny crystals in the light-sensitive tissue at the back of the eye (retina) that can be seen during an eye exam. Based on their appearance, these retinal crystals are often called glistening white dots. These white dots are usually apparent by early childhood, and it is unclear if they affect normal vision. People with Sjögren-Larsson syndrome may also have nearsightedness (myopia) or an increased sensitivity to light (photophobia). Sjögren-Larsson syndrome was first observed in Sweden, where the prevalence of this condition is 1 per 250,000 individuals. Outside Sweden, the prevalence of this condition is unknown. Mutations in the ALDH3A2 gene cause Sjögren-Larsson syndrome. The ALDH3A2 gene provides instructions for making an enzyme called fatty aldehyde dehydrogenase (FALDH). The FALDH enzyme is part of a multistep process called fatty acid oxidation in which fats are broken down and converted into energy. Specifically, the FALDH enzyme breaks down molecules called fatty aldehydes to fatty acids. ALDH3A2 gene mutations disrupt the normal process of fatty acid oxidation. Most mutations result in the production of a FALDH enzyme that is unable to break down fatty aldehyde molecules. As a result, fats that cannot be broken down build up in cells. Within skin cells, excess fat accumulation can interfere with the formation of membranes that act as protective barriers to control water loss. As a result of the loss of these protective barriers, the skin has difficulty maintaining its water balance, resulting in dry, scaly skin. In the brain, the consequences of excess fat accumulation are unclear, but it is likely that an abundance of fat disrupts the formation of myelin. Myelin is the covering that protects nerves and promotes the efficient transmission of nerve impulses. A lack of myelin can lead to neurological problems such as intellectual disability and walking difficulties. The cause of the eye problems is unclear, but it is also likely related to a disruption in the breakdown of fats. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is Sjgren-Larsson syndrome inherited ? | This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. |
Sjögren-Larsson syndrome is a condition characterized by dry, scaly skin (ichthyosis); neurological problems; and eye problems. These symptoms are apparent by early childhood and usually do not worsen with age. Affected infants tend to be born prematurely. At birth the skin is red (erythema), but later in infancy the skin becomes dry, rough, and scaly with a brownish or yellowish tone. Mild to severe itchiness (pruritus) is also common. These skin abnormalities are generally dispersed over the whole body, most severely affecting the nape of the neck, the torso, and the extremities. The skin of the face is usually not affected. People with this condition may also have neurological signs and symptoms. Most affected individuals have leukoencephalopathy, which is a change in a type of brain tissue called white matter. White matter consists of nerve fibers covered by a substance (myelin) that insulates and protects the nerves. The leukoencephalopathy is thought to contribute to many of the neurological signs and symptoms in people with Sjögren-Larsson syndrome. Most affected individuals have intellectual disability that varies from mild to profound and is usually apparent by early childhood. People with Sjögren-Larsson syndrome have speech difficulties (dysarthria) and delayed speech. Usually they are able to produce only short sentences with poorly formed words. Rarely, people with this condition have normal intelligence. In addition, approximately 40 percent of people with Sjögren-Larsson syndrome have seizures. Children with this condition often experience delayed development of motor skills (such as crawling and walking) due to abnormal muscle stiffness (spasticity) that is typically in their legs and, less commonly, also in their arms. About one-half of people with Sjögren-Larsson syndrome require wheelchair assistance and many others need some form of support to walk. Affected individuals have tiny crystals in the light-sensitive tissue at the back of the eye (retina) that can be seen during an eye exam. Based on their appearance, these retinal crystals are often called glistening white dots. These white dots are usually apparent by early childhood, and it is unclear if they affect normal vision. People with Sjögren-Larsson syndrome may also have nearsightedness (myopia) or an increased sensitivity to light (photophobia). Sjögren-Larsson syndrome was first observed in Sweden, where the prevalence of this condition is 1 per 250,000 individuals. Outside Sweden, the prevalence of this condition is unknown. Mutations in the ALDH3A2 gene cause Sjögren-Larsson syndrome. The ALDH3A2 gene provides instructions for making an enzyme called fatty aldehyde dehydrogenase (FALDH). The FALDH enzyme is part of a multistep process called fatty acid oxidation in which fats are broken down and converted into energy. Specifically, the FALDH enzyme breaks down molecules called fatty aldehydes to fatty acids. ALDH3A2 gene mutations disrupt the normal process of fatty acid oxidation. Most mutations result in the production of a FALDH enzyme that is unable to break down fatty aldehyde molecules. As a result, fats that cannot be broken down build up in cells. Within skin cells, excess fat accumulation can interfere with the formation of membranes that act as protective barriers to control water loss. As a result of the loss of these protective barriers, the skin has difficulty maintaining its water balance, resulting in dry, scaly skin. In the brain, the consequences of excess fat accumulation are unclear, but it is likely that an abundance of fat disrupts the formation of myelin. Myelin is the covering that protects nerves and promotes the efficient transmission of nerve impulses. A lack of myelin can lead to neurological problems such as intellectual disability and walking difficulties. The cause of the eye problems is unclear, but it is also likely related to a disruption in the breakdown of fats. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for Sjgren-Larsson syndrome ? | These resources address the diagnosis or management of Sjgren-Larsson syndrome: - Genetic Testing Registry: Sjgren-Larsson syndrome These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Epidermolysis bullosa simplex is one of a group of genetic conditions called epidermolysis bullosa that cause the skin to be very fragile and to blister easily. Blisters and areas of skin loss (erosions) occur in response to minor injury or friction, such as rubbing or scratching. Epidermolysis bullosa simplex is one of the major forms of epidermolysis bullosa. The signs and symptoms of this condition vary widely among affected individuals. Blistering primarily affects the hands and feet in mild cases, and the blisters usually heal without leaving scars. Severe cases of this condition involve widespread blistering that can lead to infections, dehydration, and other medical problems. Severe cases may be life-threatening in infancy. Researchers have identified four major types of epidermolysis bullosa simplex. Although the types differ in severity, their features overlap significantly, and they are caused by mutations in the same genes. Most researchers now consider the major forms of this condition to be part of a single disorder with a range of signs and symptoms. The mildest form of epidermolysis bullosa simplex, known as the localized type (formerly called the Weber-Cockayne type), is characterized by skin blistering that begins anytime between childhood and adulthood and is usually limited to the hands and feet. Later in life, skin on the palms of the hands and soles of the feet may thicken and harden (hyperkeratosis). The Dowling-Meara type is the most severe form of epidermolysis bullosa simplex. Extensive, severe blistering can occur anywhere on the body, including the inside of the mouth, and blisters may appear in clusters. Blistering is present from birth and tends to improve with age. Affected individuals also experience abnormal nail growth and hyperkeratosis of the palms and soles. Another form of epidermolysis bullosa simplex, known as the other generalized type (formerly called the Koebner type), is associated with widespread blisters that appear at birth or in early infancy. The blistering tends to be less severe than in the Dowling-Meara type. Epidermolysis bullosa simplex with mottled pigmentation is characterized by patches of darker skin on the trunk, arms, and legs that fade in adulthood. This form of the disorder also involves skin blistering from early infancy, hyperkeratosis of the palms and soles, and abnormal nail growth. In addition to the four major types described above, researchers have identified another skin condition related to epidermolysis bullosa simplex, which they call the Ogna type. It is caused by mutations in a gene that is not associated with the other types of epidermolysis bullosa simplex. It is unclear whether the Ogna type is a subtype of epidermolysis bullosa simplex or represents a separate form of epidermolysis bullosa. Several other variants of epidermolysis bullosa simplex have been proposed, but they appear to be very rare. The exact prevalence of epidermolysis bullosa simplex is unknown, but this condition is estimated to affect 1 in 30,000 to 50,000 people. The localized type is the most common form of the condition. The four major types of epidermolysis bullosa simplex can result from mutations in either the KRT5 or KRT14 gene. These genes provide instructions for making proteins called keratin 5 and keratin 14. These tough, fibrous proteins work together to provide strength and resiliency to the outer layer of the skin (the epidermis). Mutations in either the KRT5 or KRT14 gene prevent the keratin proteins from assembling into strong networks, causing cells in the epidermis to become fragile and easily damaged. As a result, the skin is less resistant to friction and minor trauma and blisters easily. In rare cases, no KRT5 or KRT14 gene mutations are identified in people with one of the four major types of epidermolysis bullosa simplex. Mutations in another gene, PLEC, have been associated with the rare Ogna type of epidermolysis bullosa simplex. The PLEC gene provides instructions for making a protein called plectin, which helps attach the epidermis to underlying layers of skin. Researchers are working to determine how PLEC gene mutations lead to the major features of the condition. Epidermolysis bullosa simplex is usually inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Some affected people inherit the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. In rare cases, epidermolysis bullosa simplex is inherited in an autosomal recessive pattern. Autosomal recessive inheritance means the condition results when two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive disorder typically each carry one copy of the altered gene, but do not show signs and symptoms of the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) epidermolysis bullosa simplex ? | Epidermolysis bullosa simplex is one of a group of genetic conditions called epidermolysis bullosa that cause the skin to be very fragile and to blister easily. Blisters and areas of skin loss (erosions) occur in response to minor injury or friction, such as rubbing or scratching. Epidermolysis bullosa simplex is one of the major forms of epidermolysis bullosa. The signs and symptoms of this condition vary widely among affected individuals. Blistering primarily affects the hands and feet in mild cases, and the blisters usually heal without leaving scars. Severe cases of this condition involve widespread blistering that can lead to infections, dehydration, and other medical problems. Severe cases may be life-threatening in infancy. Researchers have identified four major types of epidermolysis bullosa simplex. Although the types differ in severity, their features overlap significantly, and they are caused by mutations in the same genes. Most researchers now consider the major forms of this condition to be part of a single disorder with a range of signs and symptoms. The mildest form of epidermolysis bullosa simplex, known as the localized type (formerly called the Weber-Cockayne type), is characterized by skin blistering that begins anytime between childhood and adulthood and is usually limited to the hands and feet. Later in life, skin on the palms of the hands and soles of the feet may thicken and harden (hyperkeratosis). The Dowling-Meara type is the most severe form of epidermolysis bullosa simplex. Extensive, severe blistering can occur anywhere on the body, including the inside of the mouth, and blisters may appear in clusters. Blistering is present from birth and tends to improve with age. Affected individuals also experience abnormal nail growth and hyperkeratosis of the palms and soles. Another form of epidermolysis bullosa simplex, known as the other generalized type (formerly called the Koebner type), is associated with widespread blisters that appear at birth or in early infancy. The blistering tends to be less severe than in the Dowling-Meara type. Epidermolysis bullosa simplex with mottled pigmentation is characterized by patches of darker skin on the trunk, arms, and legs that fade in adulthood. This form of the disorder also involves skin blistering from early infancy, hyperkeratosis of the palms and soles, and abnormal nail growth. In addition to the four major types described above, researchers have identified another skin condition related to epidermolysis bullosa simplex, which they call the Ogna type. It is caused by mutations in a gene that is not associated with the other types of epidermolysis bullosa simplex. It is unclear whether the Ogna type is a subtype of epidermolysis bullosa simplex or represents a separate form of epidermolysis bullosa. Several other variants of epidermolysis bullosa simplex have been proposed, but they appear to be very rare. |
Epidermolysis bullosa simplex is one of a group of genetic conditions called epidermolysis bullosa that cause the skin to be very fragile and to blister easily. Blisters and areas of skin loss (erosions) occur in response to minor injury or friction, such as rubbing or scratching. Epidermolysis bullosa simplex is one of the major forms of epidermolysis bullosa. The signs and symptoms of this condition vary widely among affected individuals. Blistering primarily affects the hands and feet in mild cases, and the blisters usually heal without leaving scars. Severe cases of this condition involve widespread blistering that can lead to infections, dehydration, and other medical problems. Severe cases may be life-threatening in infancy. Researchers have identified four major types of epidermolysis bullosa simplex. Although the types differ in severity, their features overlap significantly, and they are caused by mutations in the same genes. Most researchers now consider the major forms of this condition to be part of a single disorder with a range of signs and symptoms. The mildest form of epidermolysis bullosa simplex, known as the localized type (formerly called the Weber-Cockayne type), is characterized by skin blistering that begins anytime between childhood and adulthood and is usually limited to the hands and feet. Later in life, skin on the palms of the hands and soles of the feet may thicken and harden (hyperkeratosis). The Dowling-Meara type is the most severe form of epidermolysis bullosa simplex. Extensive, severe blistering can occur anywhere on the body, including the inside of the mouth, and blisters may appear in clusters. Blistering is present from birth and tends to improve with age. Affected individuals also experience abnormal nail growth and hyperkeratosis of the palms and soles. Another form of epidermolysis bullosa simplex, known as the other generalized type (formerly called the Koebner type), is associated with widespread blisters that appear at birth or in early infancy. The blistering tends to be less severe than in the Dowling-Meara type. Epidermolysis bullosa simplex with mottled pigmentation is characterized by patches of darker skin on the trunk, arms, and legs that fade in adulthood. This form of the disorder also involves skin blistering from early infancy, hyperkeratosis of the palms and soles, and abnormal nail growth. In addition to the four major types described above, researchers have identified another skin condition related to epidermolysis bullosa simplex, which they call the Ogna type. It is caused by mutations in a gene that is not associated with the other types of epidermolysis bullosa simplex. It is unclear whether the Ogna type is a subtype of epidermolysis bullosa simplex or represents a separate form of epidermolysis bullosa. Several other variants of epidermolysis bullosa simplex have been proposed, but they appear to be very rare. The exact prevalence of epidermolysis bullosa simplex is unknown, but this condition is estimated to affect 1 in 30,000 to 50,000 people. The localized type is the most common form of the condition. The four major types of epidermolysis bullosa simplex can result from mutations in either the KRT5 or KRT14 gene. These genes provide instructions for making proteins called keratin 5 and keratin 14. These tough, fibrous proteins work together to provide strength and resiliency to the outer layer of the skin (the epidermis). Mutations in either the KRT5 or KRT14 gene prevent the keratin proteins from assembling into strong networks, causing cells in the epidermis to become fragile and easily damaged. As a result, the skin is less resistant to friction and minor trauma and blisters easily. In rare cases, no KRT5 or KRT14 gene mutations are identified in people with one of the four major types of epidermolysis bullosa simplex. Mutations in another gene, PLEC, have been associated with the rare Ogna type of epidermolysis bullosa simplex. The PLEC gene provides instructions for making a protein called plectin, which helps attach the epidermis to underlying layers of skin. Researchers are working to determine how PLEC gene mutations lead to the major features of the condition. Epidermolysis bullosa simplex is usually inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Some affected people inherit the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. In rare cases, epidermolysis bullosa simplex is inherited in an autosomal recessive pattern. Autosomal recessive inheritance means the condition results when two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive disorder typically each carry one copy of the altered gene, but do not show signs and symptoms of the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by epidermolysis bullosa simplex ? | The exact prevalence of epidermolysis bullosa simplex is unknown, but this condition is estimated to affect 1 in 30,000 to 50,000 people. The localized type is the most common form of the condition. |
Epidermolysis bullosa simplex is one of a group of genetic conditions called epidermolysis bullosa that cause the skin to be very fragile and to blister easily. Blisters and areas of skin loss (erosions) occur in response to minor injury or friction, such as rubbing or scratching. Epidermolysis bullosa simplex is one of the major forms of epidermolysis bullosa. The signs and symptoms of this condition vary widely among affected individuals. Blistering primarily affects the hands and feet in mild cases, and the blisters usually heal without leaving scars. Severe cases of this condition involve widespread blistering that can lead to infections, dehydration, and other medical problems. Severe cases may be life-threatening in infancy. Researchers have identified four major types of epidermolysis bullosa simplex. Although the types differ in severity, their features overlap significantly, and they are caused by mutations in the same genes. Most researchers now consider the major forms of this condition to be part of a single disorder with a range of signs and symptoms. The mildest form of epidermolysis bullosa simplex, known as the localized type (formerly called the Weber-Cockayne type), is characterized by skin blistering that begins anytime between childhood and adulthood and is usually limited to the hands and feet. Later in life, skin on the palms of the hands and soles of the feet may thicken and harden (hyperkeratosis). The Dowling-Meara type is the most severe form of epidermolysis bullosa simplex. Extensive, severe blistering can occur anywhere on the body, including the inside of the mouth, and blisters may appear in clusters. Blistering is present from birth and tends to improve with age. Affected individuals also experience abnormal nail growth and hyperkeratosis of the palms and soles. Another form of epidermolysis bullosa simplex, known as the other generalized type (formerly called the Koebner type), is associated with widespread blisters that appear at birth or in early infancy. The blistering tends to be less severe than in the Dowling-Meara type. Epidermolysis bullosa simplex with mottled pigmentation is characterized by patches of darker skin on the trunk, arms, and legs that fade in adulthood. This form of the disorder also involves skin blistering from early infancy, hyperkeratosis of the palms and soles, and abnormal nail growth. In addition to the four major types described above, researchers have identified another skin condition related to epidermolysis bullosa simplex, which they call the Ogna type. It is caused by mutations in a gene that is not associated with the other types of epidermolysis bullosa simplex. It is unclear whether the Ogna type is a subtype of epidermolysis bullosa simplex or represents a separate form of epidermolysis bullosa. Several other variants of epidermolysis bullosa simplex have been proposed, but they appear to be very rare. The exact prevalence of epidermolysis bullosa simplex is unknown, but this condition is estimated to affect 1 in 30,000 to 50,000 people. The localized type is the most common form of the condition. The four major types of epidermolysis bullosa simplex can result from mutations in either the KRT5 or KRT14 gene. These genes provide instructions for making proteins called keratin 5 and keratin 14. These tough, fibrous proteins work together to provide strength and resiliency to the outer layer of the skin (the epidermis). Mutations in either the KRT5 or KRT14 gene prevent the keratin proteins from assembling into strong networks, causing cells in the epidermis to become fragile and easily damaged. As a result, the skin is less resistant to friction and minor trauma and blisters easily. In rare cases, no KRT5 or KRT14 gene mutations are identified in people with one of the four major types of epidermolysis bullosa simplex. Mutations in another gene, PLEC, have been associated with the rare Ogna type of epidermolysis bullosa simplex. The PLEC gene provides instructions for making a protein called plectin, which helps attach the epidermis to underlying layers of skin. Researchers are working to determine how PLEC gene mutations lead to the major features of the condition. Epidermolysis bullosa simplex is usually inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Some affected people inherit the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. In rare cases, epidermolysis bullosa simplex is inherited in an autosomal recessive pattern. Autosomal recessive inheritance means the condition results when two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive disorder typically each carry one copy of the altered gene, but do not show signs and symptoms of the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to epidermolysis bullosa simplex ? | The four major types of epidermolysis bullosa simplex can result from mutations in either the KRT5 or KRT14 gene. These genes provide instructions for making proteins called keratin 5 and keratin 14. These tough, fibrous proteins work together to provide strength and resiliency to the outer layer of the skin (the epidermis). Mutations in either the KRT5 or KRT14 gene prevent the keratin proteins from assembling into strong networks, causing cells in the epidermis to become fragile and easily damaged. As a result, the skin is less resistant to friction and minor trauma and blisters easily. In rare cases, no KRT5 or KRT14 gene mutations are identified in people with one of the four major types of epidermolysis bullosa simplex. Mutations in another gene, PLEC, have been associated with the rare Ogna type of epidermolysis bullosa simplex. The PLEC gene provides instructions for making a protein called plectin, which helps attach the epidermis to underlying layers of skin. Researchers are working to determine how PLEC gene mutations lead to the major features of the condition. |
Epidermolysis bullosa simplex is one of a group of genetic conditions called epidermolysis bullosa that cause the skin to be very fragile and to blister easily. Blisters and areas of skin loss (erosions) occur in response to minor injury or friction, such as rubbing or scratching. Epidermolysis bullosa simplex is one of the major forms of epidermolysis bullosa. The signs and symptoms of this condition vary widely among affected individuals. Blistering primarily affects the hands and feet in mild cases, and the blisters usually heal without leaving scars. Severe cases of this condition involve widespread blistering that can lead to infections, dehydration, and other medical problems. Severe cases may be life-threatening in infancy. Researchers have identified four major types of epidermolysis bullosa simplex. Although the types differ in severity, their features overlap significantly, and they are caused by mutations in the same genes. Most researchers now consider the major forms of this condition to be part of a single disorder with a range of signs and symptoms. The mildest form of epidermolysis bullosa simplex, known as the localized type (formerly called the Weber-Cockayne type), is characterized by skin blistering that begins anytime between childhood and adulthood and is usually limited to the hands and feet. Later in life, skin on the palms of the hands and soles of the feet may thicken and harden (hyperkeratosis). The Dowling-Meara type is the most severe form of epidermolysis bullosa simplex. Extensive, severe blistering can occur anywhere on the body, including the inside of the mouth, and blisters may appear in clusters. Blistering is present from birth and tends to improve with age. Affected individuals also experience abnormal nail growth and hyperkeratosis of the palms and soles. Another form of epidermolysis bullosa simplex, known as the other generalized type (formerly called the Koebner type), is associated with widespread blisters that appear at birth or in early infancy. The blistering tends to be less severe than in the Dowling-Meara type. Epidermolysis bullosa simplex with mottled pigmentation is characterized by patches of darker skin on the trunk, arms, and legs that fade in adulthood. This form of the disorder also involves skin blistering from early infancy, hyperkeratosis of the palms and soles, and abnormal nail growth. In addition to the four major types described above, researchers have identified another skin condition related to epidermolysis bullosa simplex, which they call the Ogna type. It is caused by mutations in a gene that is not associated with the other types of epidermolysis bullosa simplex. It is unclear whether the Ogna type is a subtype of epidermolysis bullosa simplex or represents a separate form of epidermolysis bullosa. Several other variants of epidermolysis bullosa simplex have been proposed, but they appear to be very rare. The exact prevalence of epidermolysis bullosa simplex is unknown, but this condition is estimated to affect 1 in 30,000 to 50,000 people. The localized type is the most common form of the condition. The four major types of epidermolysis bullosa simplex can result from mutations in either the KRT5 or KRT14 gene. These genes provide instructions for making proteins called keratin 5 and keratin 14. These tough, fibrous proteins work together to provide strength and resiliency to the outer layer of the skin (the epidermis). Mutations in either the KRT5 or KRT14 gene prevent the keratin proteins from assembling into strong networks, causing cells in the epidermis to become fragile and easily damaged. As a result, the skin is less resistant to friction and minor trauma and blisters easily. In rare cases, no KRT5 or KRT14 gene mutations are identified in people with one of the four major types of epidermolysis bullosa simplex. Mutations in another gene, PLEC, have been associated with the rare Ogna type of epidermolysis bullosa simplex. The PLEC gene provides instructions for making a protein called plectin, which helps attach the epidermis to underlying layers of skin. Researchers are working to determine how PLEC gene mutations lead to the major features of the condition. Epidermolysis bullosa simplex is usually inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Some affected people inherit the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. In rare cases, epidermolysis bullosa simplex is inherited in an autosomal recessive pattern. Autosomal recessive inheritance means the condition results when two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive disorder typically each carry one copy of the altered gene, but do not show signs and symptoms of the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is epidermolysis bullosa simplex inherited ? | Epidermolysis bullosa simplex is usually inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Some affected people inherit the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. In rare cases, epidermolysis bullosa simplex is inherited in an autosomal recessive pattern. Autosomal recessive inheritance means the condition results when two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive disorder typically each carry one copy of the altered gene, but do not show signs and symptoms of the disorder. |
Epidermolysis bullosa simplex is one of a group of genetic conditions called epidermolysis bullosa that cause the skin to be very fragile and to blister easily. Blisters and areas of skin loss (erosions) occur in response to minor injury or friction, such as rubbing or scratching. Epidermolysis bullosa simplex is one of the major forms of epidermolysis bullosa. The signs and symptoms of this condition vary widely among affected individuals. Blistering primarily affects the hands and feet in mild cases, and the blisters usually heal without leaving scars. Severe cases of this condition involve widespread blistering that can lead to infections, dehydration, and other medical problems. Severe cases may be life-threatening in infancy. Researchers have identified four major types of epidermolysis bullosa simplex. Although the types differ in severity, their features overlap significantly, and they are caused by mutations in the same genes. Most researchers now consider the major forms of this condition to be part of a single disorder with a range of signs and symptoms. The mildest form of epidermolysis bullosa simplex, known as the localized type (formerly called the Weber-Cockayne type), is characterized by skin blistering that begins anytime between childhood and adulthood and is usually limited to the hands and feet. Later in life, skin on the palms of the hands and soles of the feet may thicken and harden (hyperkeratosis). The Dowling-Meara type is the most severe form of epidermolysis bullosa simplex. Extensive, severe blistering can occur anywhere on the body, including the inside of the mouth, and blisters may appear in clusters. Blistering is present from birth and tends to improve with age. Affected individuals also experience abnormal nail growth and hyperkeratosis of the palms and soles. Another form of epidermolysis bullosa simplex, known as the other generalized type (formerly called the Koebner type), is associated with widespread blisters that appear at birth or in early infancy. The blistering tends to be less severe than in the Dowling-Meara type. Epidermolysis bullosa simplex with mottled pigmentation is characterized by patches of darker skin on the trunk, arms, and legs that fade in adulthood. This form of the disorder also involves skin blistering from early infancy, hyperkeratosis of the palms and soles, and abnormal nail growth. In addition to the four major types described above, researchers have identified another skin condition related to epidermolysis bullosa simplex, which they call the Ogna type. It is caused by mutations in a gene that is not associated with the other types of epidermolysis bullosa simplex. It is unclear whether the Ogna type is a subtype of epidermolysis bullosa simplex or represents a separate form of epidermolysis bullosa. Several other variants of epidermolysis bullosa simplex have been proposed, but they appear to be very rare. The exact prevalence of epidermolysis bullosa simplex is unknown, but this condition is estimated to affect 1 in 30,000 to 50,000 people. The localized type is the most common form of the condition. The four major types of epidermolysis bullosa simplex can result from mutations in either the KRT5 or KRT14 gene. These genes provide instructions for making proteins called keratin 5 and keratin 14. These tough, fibrous proteins work together to provide strength and resiliency to the outer layer of the skin (the epidermis). Mutations in either the KRT5 or KRT14 gene prevent the keratin proteins from assembling into strong networks, causing cells in the epidermis to become fragile and easily damaged. As a result, the skin is less resistant to friction and minor trauma and blisters easily. In rare cases, no KRT5 or KRT14 gene mutations are identified in people with one of the four major types of epidermolysis bullosa simplex. Mutations in another gene, PLEC, have been associated with the rare Ogna type of epidermolysis bullosa simplex. The PLEC gene provides instructions for making a protein called plectin, which helps attach the epidermis to underlying layers of skin. Researchers are working to determine how PLEC gene mutations lead to the major features of the condition. Epidermolysis bullosa simplex is usually inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Some affected people inherit the mutation from one affected parent. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. In rare cases, epidermolysis bullosa simplex is inherited in an autosomal recessive pattern. Autosomal recessive inheritance means the condition results when two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive disorder typically each carry one copy of the altered gene, but do not show signs and symptoms of the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for epidermolysis bullosa simplex ? | These resources address the diagnosis or management of epidermolysis bullosa simplex: - Dystrophic Epidermolysis Bullosa Research Association (DebRA) of America: Wound Care - Epidermolysis Bullosa Center, Cincinnati Children's Hospital Medical Center - Gene Review: Gene Review: Epidermolysis Bullosa Simplex - Genetic Testing Registry: Epidermolysis bullosa simplex - Genetic Testing Registry: Epidermolysis bullosa simplex with mottled pigmentation - Genetic Testing Registry: Epidermolysis bullosa simplex, Cockayne-Touraine type - Genetic Testing Registry: Epidermolysis bullosa simplex, Koebner type - Genetic Testing Registry: Epidermolysis bullosa simplex, Ogna type - Genetic Testing Registry: Epidermolysis bullosa simplex, autosomal recessive - MedlinePlus Encyclopedia: Epidermolysis Bullosa These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Hypochondrogenesis is a rare, severe disorder of bone growth. This condition is characterized by a small body, short limbs, and abnormal bone formation (ossification) in the spine and pelvis. Affected infants have short arms and legs, a small chest with short ribs, and underdeveloped lungs. Bones in the skull develop normally, but the bones of the spine (vertebrae) and pelvis do not harden (ossify) properly. The face appears flat and oval-shaped, with widely spaced eyes, a small chin, and, in some cases, an opening in the roof of the mouth called a cleft palate. Individuals with hypochondrogenesis have an enlarged abdomen and may have a condition called hydrops fetalis in which excess fluid builds up in the body before birth. As a result of these serious health problems, some affected fetuses do not survive to term. Infants born with hypochondrogenesis usually die at birth or shortly thereafter from respiratory failure. Babies who live past the newborn period are usually reclassified as having spondyloepiphyseal dysplasia congenita, a related but milder disorder that similarly affects bone development. Hypochondrogenesis and achondrogenesis, type 2 (a similar skeletal disorder) together affect 1 in 40,000 to 60,000 newborns. Hypochondrogenesis is one of the most severe conditions in a spectrum of disorders caused by mutations in the COL2A1 gene. This gene provides instructions for making a protein that forms type II collagen. This type of collagen is found mostly in the clear gel that fills the eyeball (the vitreous) and in cartilage. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is essential for the normal development of bones and other connective tissues that form the body's supportive framework. Mutations in the COL2A1 gene interfere with the assembly of type II collagen molecules, which prevents bones and other connective tissues from developing properly. Hypochondrogenesis is considered an autosomal dominant disorder because one copy of the altered gene in each cell is sufficient to cause the condition. It is caused by new mutations in the COL2A1 gene and occurs in people with no history of the disorder in their family. This condition is not passed on to the next generation because affected individuals do not live long enough to have children. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) hypochondrogenesis ? | Hypochondrogenesis is a rare, severe disorder of bone growth. This condition is characterized by a small body, short limbs, and abnormal bone formation (ossification) in the spine and pelvis. Affected infants have short arms and legs, a small chest with short ribs, and underdeveloped lungs. Bones in the skull develop normally, but the bones of the spine (vertebrae) and pelvis do not harden (ossify) properly. The face appears flat and oval-shaped, with widely spaced eyes, a small chin, and, in some cases, an opening in the roof of the mouth called a cleft palate. Individuals with hypochondrogenesis have an enlarged abdomen and may have a condition called hydrops fetalis in which excess fluid builds up in the body before birth. As a result of these serious health problems, some affected fetuses do not survive to term. Infants born with hypochondrogenesis usually die at birth or shortly thereafter from respiratory failure. Babies who live past the newborn period are usually reclassified as having spondyloepiphyseal dysplasia congenita, a related but milder disorder that similarly affects bone development. |
Hypochondrogenesis is a rare, severe disorder of bone growth. This condition is characterized by a small body, short limbs, and abnormal bone formation (ossification) in the spine and pelvis. Affected infants have short arms and legs, a small chest with short ribs, and underdeveloped lungs. Bones in the skull develop normally, but the bones of the spine (vertebrae) and pelvis do not harden (ossify) properly. The face appears flat and oval-shaped, with widely spaced eyes, a small chin, and, in some cases, an opening in the roof of the mouth called a cleft palate. Individuals with hypochondrogenesis have an enlarged abdomen and may have a condition called hydrops fetalis in which excess fluid builds up in the body before birth. As a result of these serious health problems, some affected fetuses do not survive to term. Infants born with hypochondrogenesis usually die at birth or shortly thereafter from respiratory failure. Babies who live past the newborn period are usually reclassified as having spondyloepiphyseal dysplasia congenita, a related but milder disorder that similarly affects bone development. Hypochondrogenesis and achondrogenesis, type 2 (a similar skeletal disorder) together affect 1 in 40,000 to 60,000 newborns. Hypochondrogenesis is one of the most severe conditions in a spectrum of disorders caused by mutations in the COL2A1 gene. This gene provides instructions for making a protein that forms type II collagen. This type of collagen is found mostly in the clear gel that fills the eyeball (the vitreous) and in cartilage. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is essential for the normal development of bones and other connective tissues that form the body's supportive framework. Mutations in the COL2A1 gene interfere with the assembly of type II collagen molecules, which prevents bones and other connective tissues from developing properly. Hypochondrogenesis is considered an autosomal dominant disorder because one copy of the altered gene in each cell is sufficient to cause the condition. It is caused by new mutations in the COL2A1 gene and occurs in people with no history of the disorder in their family. This condition is not passed on to the next generation because affected individuals do not live long enough to have children. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by hypochondrogenesis ? | Hypochondrogenesis and achondrogenesis, type 2 (a similar skeletal disorder) together affect 1 in 40,000 to 60,000 newborns. |
Hypochondrogenesis is a rare, severe disorder of bone growth. This condition is characterized by a small body, short limbs, and abnormal bone formation (ossification) in the spine and pelvis. Affected infants have short arms and legs, a small chest with short ribs, and underdeveloped lungs. Bones in the skull develop normally, but the bones of the spine (vertebrae) and pelvis do not harden (ossify) properly. The face appears flat and oval-shaped, with widely spaced eyes, a small chin, and, in some cases, an opening in the roof of the mouth called a cleft palate. Individuals with hypochondrogenesis have an enlarged abdomen and may have a condition called hydrops fetalis in which excess fluid builds up in the body before birth. As a result of these serious health problems, some affected fetuses do not survive to term. Infants born with hypochondrogenesis usually die at birth or shortly thereafter from respiratory failure. Babies who live past the newborn period are usually reclassified as having spondyloepiphyseal dysplasia congenita, a related but milder disorder that similarly affects bone development. Hypochondrogenesis and achondrogenesis, type 2 (a similar skeletal disorder) together affect 1 in 40,000 to 60,000 newborns. Hypochondrogenesis is one of the most severe conditions in a spectrum of disorders caused by mutations in the COL2A1 gene. This gene provides instructions for making a protein that forms type II collagen. This type of collagen is found mostly in the clear gel that fills the eyeball (the vitreous) and in cartilage. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is essential for the normal development of bones and other connective tissues that form the body's supportive framework. Mutations in the COL2A1 gene interfere with the assembly of type II collagen molecules, which prevents bones and other connective tissues from developing properly. Hypochondrogenesis is considered an autosomal dominant disorder because one copy of the altered gene in each cell is sufficient to cause the condition. It is caused by new mutations in the COL2A1 gene and occurs in people with no history of the disorder in their family. This condition is not passed on to the next generation because affected individuals do not live long enough to have children. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to hypochondrogenesis ? | Hypochondrogenesis is one of the most severe conditions in a spectrum of disorders caused by mutations in the COL2A1 gene. This gene provides instructions for making a protein that forms type II collagen. This type of collagen is found mostly in the clear gel that fills the eyeball (the vitreous) and in cartilage. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is essential for the normal development of bones and other connective tissues that form the body's supportive framework. Mutations in the COL2A1 gene interfere with the assembly of type II collagen molecules, which prevents bones and other connective tissues from developing properly. |
Hypochondrogenesis is a rare, severe disorder of bone growth. This condition is characterized by a small body, short limbs, and abnormal bone formation (ossification) in the spine and pelvis. Affected infants have short arms and legs, a small chest with short ribs, and underdeveloped lungs. Bones in the skull develop normally, but the bones of the spine (vertebrae) and pelvis do not harden (ossify) properly. The face appears flat and oval-shaped, with widely spaced eyes, a small chin, and, in some cases, an opening in the roof of the mouth called a cleft palate. Individuals with hypochondrogenesis have an enlarged abdomen and may have a condition called hydrops fetalis in which excess fluid builds up in the body before birth. As a result of these serious health problems, some affected fetuses do not survive to term. Infants born with hypochondrogenesis usually die at birth or shortly thereafter from respiratory failure. Babies who live past the newborn period are usually reclassified as having spondyloepiphyseal dysplasia congenita, a related but milder disorder that similarly affects bone development. Hypochondrogenesis and achondrogenesis, type 2 (a similar skeletal disorder) together affect 1 in 40,000 to 60,000 newborns. Hypochondrogenesis is one of the most severe conditions in a spectrum of disorders caused by mutations in the COL2A1 gene. This gene provides instructions for making a protein that forms type II collagen. This type of collagen is found mostly in the clear gel that fills the eyeball (the vitreous) and in cartilage. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is essential for the normal development of bones and other connective tissues that form the body's supportive framework. Mutations in the COL2A1 gene interfere with the assembly of type II collagen molecules, which prevents bones and other connective tissues from developing properly. Hypochondrogenesis is considered an autosomal dominant disorder because one copy of the altered gene in each cell is sufficient to cause the condition. It is caused by new mutations in the COL2A1 gene and occurs in people with no history of the disorder in their family. This condition is not passed on to the next generation because affected individuals do not live long enough to have children. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is hypochondrogenesis inherited ? | Hypochondrogenesis is considered an autosomal dominant disorder because one copy of the altered gene in each cell is sufficient to cause the condition. It is caused by new mutations in the COL2A1 gene and occurs in people with no history of the disorder in their family. This condition is not passed on to the next generation because affected individuals do not live long enough to have children. |
Hypochondrogenesis is a rare, severe disorder of bone growth. This condition is characterized by a small body, short limbs, and abnormal bone formation (ossification) in the spine and pelvis. Affected infants have short arms and legs, a small chest with short ribs, and underdeveloped lungs. Bones in the skull develop normally, but the bones of the spine (vertebrae) and pelvis do not harden (ossify) properly. The face appears flat and oval-shaped, with widely spaced eyes, a small chin, and, in some cases, an opening in the roof of the mouth called a cleft palate. Individuals with hypochondrogenesis have an enlarged abdomen and may have a condition called hydrops fetalis in which excess fluid builds up in the body before birth. As a result of these serious health problems, some affected fetuses do not survive to term. Infants born with hypochondrogenesis usually die at birth or shortly thereafter from respiratory failure. Babies who live past the newborn period are usually reclassified as having spondyloepiphyseal dysplasia congenita, a related but milder disorder that similarly affects bone development. Hypochondrogenesis and achondrogenesis, type 2 (a similar skeletal disorder) together affect 1 in 40,000 to 60,000 newborns. Hypochondrogenesis is one of the most severe conditions in a spectrum of disorders caused by mutations in the COL2A1 gene. This gene provides instructions for making a protein that forms type II collagen. This type of collagen is found mostly in the clear gel that fills the eyeball (the vitreous) and in cartilage. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is essential for the normal development of bones and other connective tissues that form the body's supportive framework. Mutations in the COL2A1 gene interfere with the assembly of type II collagen molecules, which prevents bones and other connective tissues from developing properly. Hypochondrogenesis is considered an autosomal dominant disorder because one copy of the altered gene in each cell is sufficient to cause the condition. It is caused by new mutations in the COL2A1 gene and occurs in people with no history of the disorder in their family. This condition is not passed on to the next generation because affected individuals do not live long enough to have children. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for hypochondrogenesis ? | These resources address the diagnosis or management of hypochondrogenesis: - Genetic Testing Registry: Hypochondrogenesis - MedlinePlus Encyclopedia: Achondrogenesis These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Amelogenesis imperfecta is a disorder of tooth development. This condition causes teeth to be unusually small, discolored, pitted or grooved, and prone to rapid wear and breakage. Other dental abnormalities are also possible. These defects, which vary among affected individuals, can affect both primary (baby) teeth and permanent (adult) teeth. Researchers have described at least 14 forms of amelogenesis imperfecta. These types are distinguished by their specific dental abnormalities and by their pattern of inheritance. Additionally, amelogenesis imperfecta can occur alone without any other signs and symptoms or it can occur as part of a syndrome that affects multiple parts of the body. The exact incidence of amelogenesis imperfecta is uncertain. Estimates vary widely, from 1 in 700 people in northern Sweden to 1 in 14,000 people in the United States. Mutations in the AMELX, ENAM, MMP20, and FAM83H genes can cause amelogenesis imperfecta. The AMELX, ENAM, and MMP20 genes provide instructions for making proteins that are essential for normal tooth development. Most of these proteins are involved in the formation of enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. Although the function of the protein produced from the FAM83H gene is unknown, it is also believed to be involved in the formation of enamel. Mutations in any of these genes result in altered protein structure or prevent the production of any protein. As a result, tooth enamel is abnormally thin or soft and may have a yellow or brown color. Teeth with defective enamel are weak and easily damaged. Mutations in the genes described above account for only about half of all cases of the condition, with FAM83H gene mutations causing the majority of these cases. In the remaining cases, the genetic cause has not been identified. Researchers are working to find mutations in other genes that are involved in this disorder. Additional Information from NCBI Gene: Amelogenesis imperfecta can have different inheritance patterns depending on the gene that is altered. Many cases are caused by mutations in the FAM83H gene and are inherited in an autosomal dominant pattern. This type of inheritance means one copy of the altered gene in each cell is sufficient to cause the disorder. Some cases caused by mutations in the ENAM gene also have an autosomal dominant inheritance pattern. Amelogenesis imperfecta can also be inherited in an autosomal recessive pattern; this form of the disorder can result from mutations in the ENAM or MMP20 gene. Autosomal recessive inheritance means two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. About 5 percent of amelogenesis imperfecta cases are caused by mutations in the AMELX gene and are inherited in an X-linked pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. In most cases, males with X-linked amelogenesis imperfecta experience more severe dental abnormalities than females with this form of this condition. Other cases of amelogenesis imperfecta result from new gene mutations and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) amelogenesis imperfecta ? | Amelogenesis imperfecta is a disorder of tooth development. This condition causes teeth to be unusually small, discolored, pitted or grooved, and prone to rapid wear and breakage. Other dental abnormalities are also possible. These defects, which vary among affected individuals, can affect both primary (baby) teeth and permanent (adult) teeth. Researchers have described at least 14 forms of amelogenesis imperfecta. These types are distinguished by their specific dental abnormalities and by their pattern of inheritance. Additionally, amelogenesis imperfecta can occur alone without any other signs and symptoms or it can occur as part of a syndrome that affects multiple parts of the body. |
Amelogenesis imperfecta is a disorder of tooth development. This condition causes teeth to be unusually small, discolored, pitted or grooved, and prone to rapid wear and breakage. Other dental abnormalities are also possible. These defects, which vary among affected individuals, can affect both primary (baby) teeth and permanent (adult) teeth. Researchers have described at least 14 forms of amelogenesis imperfecta. These types are distinguished by their specific dental abnormalities and by their pattern of inheritance. Additionally, amelogenesis imperfecta can occur alone without any other signs and symptoms or it can occur as part of a syndrome that affects multiple parts of the body. The exact incidence of amelogenesis imperfecta is uncertain. Estimates vary widely, from 1 in 700 people in northern Sweden to 1 in 14,000 people in the United States. Mutations in the AMELX, ENAM, MMP20, and FAM83H genes can cause amelogenesis imperfecta. The AMELX, ENAM, and MMP20 genes provide instructions for making proteins that are essential for normal tooth development. Most of these proteins are involved in the formation of enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. Although the function of the protein produced from the FAM83H gene is unknown, it is also believed to be involved in the formation of enamel. Mutations in any of these genes result in altered protein structure or prevent the production of any protein. As a result, tooth enamel is abnormally thin or soft and may have a yellow or brown color. Teeth with defective enamel are weak and easily damaged. Mutations in the genes described above account for only about half of all cases of the condition, with FAM83H gene mutations causing the majority of these cases. In the remaining cases, the genetic cause has not been identified. Researchers are working to find mutations in other genes that are involved in this disorder. Additional Information from NCBI Gene: Amelogenesis imperfecta can have different inheritance patterns depending on the gene that is altered. Many cases are caused by mutations in the FAM83H gene and are inherited in an autosomal dominant pattern. This type of inheritance means one copy of the altered gene in each cell is sufficient to cause the disorder. Some cases caused by mutations in the ENAM gene also have an autosomal dominant inheritance pattern. Amelogenesis imperfecta can also be inherited in an autosomal recessive pattern; this form of the disorder can result from mutations in the ENAM or MMP20 gene. Autosomal recessive inheritance means two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. About 5 percent of amelogenesis imperfecta cases are caused by mutations in the AMELX gene and are inherited in an X-linked pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. In most cases, males with X-linked amelogenesis imperfecta experience more severe dental abnormalities than females with this form of this condition. Other cases of amelogenesis imperfecta result from new gene mutations and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by amelogenesis imperfecta ? | The exact incidence of amelogenesis imperfecta is uncertain. Estimates vary widely, from 1 in 700 people in northern Sweden to 1 in 14,000 people in the United States. |
Amelogenesis imperfecta is a disorder of tooth development. This condition causes teeth to be unusually small, discolored, pitted or grooved, and prone to rapid wear and breakage. Other dental abnormalities are also possible. These defects, which vary among affected individuals, can affect both primary (baby) teeth and permanent (adult) teeth. Researchers have described at least 14 forms of amelogenesis imperfecta. These types are distinguished by their specific dental abnormalities and by their pattern of inheritance. Additionally, amelogenesis imperfecta can occur alone without any other signs and symptoms or it can occur as part of a syndrome that affects multiple parts of the body. The exact incidence of amelogenesis imperfecta is uncertain. Estimates vary widely, from 1 in 700 people in northern Sweden to 1 in 14,000 people in the United States. Mutations in the AMELX, ENAM, MMP20, and FAM83H genes can cause amelogenesis imperfecta. The AMELX, ENAM, and MMP20 genes provide instructions for making proteins that are essential for normal tooth development. Most of these proteins are involved in the formation of enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. Although the function of the protein produced from the FAM83H gene is unknown, it is also believed to be involved in the formation of enamel. Mutations in any of these genes result in altered protein structure or prevent the production of any protein. As a result, tooth enamel is abnormally thin or soft and may have a yellow or brown color. Teeth with defective enamel are weak and easily damaged. Mutations in the genes described above account for only about half of all cases of the condition, with FAM83H gene mutations causing the majority of these cases. In the remaining cases, the genetic cause has not been identified. Researchers are working to find mutations in other genes that are involved in this disorder. Additional Information from NCBI Gene: Amelogenesis imperfecta can have different inheritance patterns depending on the gene that is altered. Many cases are caused by mutations in the FAM83H gene and are inherited in an autosomal dominant pattern. This type of inheritance means one copy of the altered gene in each cell is sufficient to cause the disorder. Some cases caused by mutations in the ENAM gene also have an autosomal dominant inheritance pattern. Amelogenesis imperfecta can also be inherited in an autosomal recessive pattern; this form of the disorder can result from mutations in the ENAM or MMP20 gene. Autosomal recessive inheritance means two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. About 5 percent of amelogenesis imperfecta cases are caused by mutations in the AMELX gene and are inherited in an X-linked pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. In most cases, males with X-linked amelogenesis imperfecta experience more severe dental abnormalities than females with this form of this condition. Other cases of amelogenesis imperfecta result from new gene mutations and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to amelogenesis imperfecta ? | Mutations in the AMELX, ENAM, MMP20, and FAM83H genes can cause amelogenesis imperfecta. The AMELX, ENAM, and MMP20 genes provide instructions for making proteins that are essential for normal tooth development. Most of these proteins are involved in the formation of enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. Although the function of the protein produced from the FAM83H gene is unknown, it is also believed to be involved in the formation of enamel. Mutations in any of these genes result in altered protein structure or prevent the production of any protein. As a result, tooth enamel is abnormally thin or soft and may have a yellow or brown color. Teeth with defective enamel are weak and easily damaged. Mutations in the genes described above account for only about half of all cases of the condition, with FAM83H gene mutations causing the majority of these cases. In the remaining cases, the genetic cause has not been identified. Researchers are working to find mutations in other genes that are involved in this disorder. |
Amelogenesis imperfecta is a disorder of tooth development. This condition causes teeth to be unusually small, discolored, pitted or grooved, and prone to rapid wear and breakage. Other dental abnormalities are also possible. These defects, which vary among affected individuals, can affect both primary (baby) teeth and permanent (adult) teeth. Researchers have described at least 14 forms of amelogenesis imperfecta. These types are distinguished by their specific dental abnormalities and by their pattern of inheritance. Additionally, amelogenesis imperfecta can occur alone without any other signs and symptoms or it can occur as part of a syndrome that affects multiple parts of the body. The exact incidence of amelogenesis imperfecta is uncertain. Estimates vary widely, from 1 in 700 people in northern Sweden to 1 in 14,000 people in the United States. Mutations in the AMELX, ENAM, MMP20, and FAM83H genes can cause amelogenesis imperfecta. The AMELX, ENAM, and MMP20 genes provide instructions for making proteins that are essential for normal tooth development. Most of these proteins are involved in the formation of enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. Although the function of the protein produced from the FAM83H gene is unknown, it is also believed to be involved in the formation of enamel. Mutations in any of these genes result in altered protein structure or prevent the production of any protein. As a result, tooth enamel is abnormally thin or soft and may have a yellow or brown color. Teeth with defective enamel are weak and easily damaged. Mutations in the genes described above account for only about half of all cases of the condition, with FAM83H gene mutations causing the majority of these cases. In the remaining cases, the genetic cause has not been identified. Researchers are working to find mutations in other genes that are involved in this disorder. Additional Information from NCBI Gene: Amelogenesis imperfecta can have different inheritance patterns depending on the gene that is altered. Many cases are caused by mutations in the FAM83H gene and are inherited in an autosomal dominant pattern. This type of inheritance means one copy of the altered gene in each cell is sufficient to cause the disorder. Some cases caused by mutations in the ENAM gene also have an autosomal dominant inheritance pattern. Amelogenesis imperfecta can also be inherited in an autosomal recessive pattern; this form of the disorder can result from mutations in the ENAM or MMP20 gene. Autosomal recessive inheritance means two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. About 5 percent of amelogenesis imperfecta cases are caused by mutations in the AMELX gene and are inherited in an X-linked pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. In most cases, males with X-linked amelogenesis imperfecta experience more severe dental abnormalities than females with this form of this condition. Other cases of amelogenesis imperfecta result from new gene mutations and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is amelogenesis imperfecta inherited ? | Amelogenesis imperfecta can have different inheritance patterns depending on the gene that is altered. Many cases are caused by mutations in the FAM83H gene and are inherited in an autosomal dominant pattern. This type of inheritance means one copy of the altered gene in each cell is sufficient to cause the disorder. Some cases caused by mutations in the ENAM gene also have an autosomal dominant inheritance pattern. Amelogenesis imperfecta can also be inherited in an autosomal recessive pattern; this form of the disorder can result from mutations in the ENAM or MMP20 gene. Autosomal recessive inheritance means two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. About 5 percent of amelogenesis imperfecta cases are caused by mutations in the AMELX gene and are inherited in an X-linked pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. In most cases, males with X-linked amelogenesis imperfecta experience more severe dental abnormalities than females with this form of this condition. Other cases of amelogenesis imperfecta result from new gene mutations and occur in people with no history of the disorder in their family. |
Amelogenesis imperfecta is a disorder of tooth development. This condition causes teeth to be unusually small, discolored, pitted or grooved, and prone to rapid wear and breakage. Other dental abnormalities are also possible. These defects, which vary among affected individuals, can affect both primary (baby) teeth and permanent (adult) teeth. Researchers have described at least 14 forms of amelogenesis imperfecta. These types are distinguished by their specific dental abnormalities and by their pattern of inheritance. Additionally, amelogenesis imperfecta can occur alone without any other signs and symptoms or it can occur as part of a syndrome that affects multiple parts of the body. The exact incidence of amelogenesis imperfecta is uncertain. Estimates vary widely, from 1 in 700 people in northern Sweden to 1 in 14,000 people in the United States. Mutations in the AMELX, ENAM, MMP20, and FAM83H genes can cause amelogenesis imperfecta. The AMELX, ENAM, and MMP20 genes provide instructions for making proteins that are essential for normal tooth development. Most of these proteins are involved in the formation of enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. Although the function of the protein produced from the FAM83H gene is unknown, it is also believed to be involved in the formation of enamel. Mutations in any of these genes result in altered protein structure or prevent the production of any protein. As a result, tooth enamel is abnormally thin or soft and may have a yellow or brown color. Teeth with defective enamel are weak and easily damaged. Mutations in the genes described above account for only about half of all cases of the condition, with FAM83H gene mutations causing the majority of these cases. In the remaining cases, the genetic cause has not been identified. Researchers are working to find mutations in other genes that are involved in this disorder. Additional Information from NCBI Gene: Amelogenesis imperfecta can have different inheritance patterns depending on the gene that is altered. Many cases are caused by mutations in the FAM83H gene and are inherited in an autosomal dominant pattern. This type of inheritance means one copy of the altered gene in each cell is sufficient to cause the disorder. Some cases caused by mutations in the ENAM gene also have an autosomal dominant inheritance pattern. Amelogenesis imperfecta can also be inherited in an autosomal recessive pattern; this form of the disorder can result from mutations in the ENAM or MMP20 gene. Autosomal recessive inheritance means two copies of the gene in each cell are altered. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. About 5 percent of amelogenesis imperfecta cases are caused by mutations in the AMELX gene and are inherited in an X-linked pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. In most cases, males with X-linked amelogenesis imperfecta experience more severe dental abnormalities than females with this form of this condition. Other cases of amelogenesis imperfecta result from new gene mutations and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for amelogenesis imperfecta ? | These resources address the diagnosis or management of amelogenesis imperfecta: - Genetic Testing Registry: Amelogenesis imperfecta - hypoplastic autosomal dominant - local - Genetic Testing Registry: Amelogenesis imperfecta, hypocalcification type - Genetic Testing Registry: Amelogenesis imperfecta, type 1E - Genetic Testing Registry: Amelogenesis imperfecta, type IC - MedlinePlus Encyclopedia: Amelogenesis imperfecta - MedlinePlus Encyclopedia: Tooth - Abnormal Colors These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Laryngo-onycho-cutaneous (LOC) syndrome is a disorder that leads to abnormalities of the voicebox (laryngo-), finger- and toenails (onycho-), and skin (cutaneous). Many of the condition's signs and symptoms are related to the abnormal growth of granulation tissue in different parts of the body. This red, bumpy tissue is normally produced during wound healing and is usually replaced by skin cells as healing continues. However, in people with LOC syndrome, this tissue grows even when there is no major injury. One of the first symptoms in infants with LOC syndrome is a hoarse cry due to ulcers or overgrowth of granulation tissue in the voicebox (the larynx). Excess granulation tissue can also block the airways, leading to life-threatening breathing problems; as a result many affected individuals do not survive past childhood. In LOC syndrome, granulation tissue also grows in the eyes, specifically the conjunctiva, which are the moist tissues that line the eyelids and the white part of the eyes. Affected individuals often have impairment or complete loss of vision due to the tissue overgrowth. Another common feature of LOC syndrome is missing patches of skin (cutaneous erosions). The erosions heal slowly and may become infected. People with LOC syndrome can also have malformed nails and small, abnormal teeth. The hard, white material that forms the protective outer layer of each tooth (enamel) is thin, which contributes to frequent cavities. LOC syndrome is typically considered a subtype of another skin condition called junctional epidermolysis bullosa, which is characterized by fragile skin that blisters easily. While individuals with junctional epidermolysis bullosa can have some of the features of LOC syndrome, they do not usually have overgrowth of granulation tissue in the conjunctiva. LOC syndrome is a rare disorder that primarily affects families of Punjabi background from India and Pakistan, although the condition has also been reported in one family from Iran. LOC syndrome is caused by mutations in the LAMA3 gene, which provides instructions for making one part (subunit) of a protein called laminin 332. This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. The laminin 332 protein plays an important role in strengthening and stabilizing the skin by helping to attach the top layer of skin (the epidermis) to underlying layers. Studies suggest that laminin 332 is also involved in wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The mutations involved in LOC syndrome alter the structure of one version of the alpha subunit of laminin 332 (called alpha-3a). Laminins made with the altered subunit cannot effectively attach the epidermis to underlying layers of skin or regulate wound healing. These abnormalities of laminin 332 cause the cutaneous erosions and overgrowth of granulation tissue that are characteristic of LOC syndrome. The inability of laminin 332 to perform its other functions leads to the nail and tooth abnormalities that occur in this condition. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) laryngo-onycho-cutaneous syndrome ? | Laryngo-onycho-cutaneous (LOC) syndrome is a disorder that leads to abnormalities of the voicebox (laryngo-), finger- and toenails (onycho-), and skin (cutaneous). Many of the condition's signs and symptoms are related to the abnormal growth of granulation tissue in different parts of the body. This red, bumpy tissue is normally produced during wound healing and is usually replaced by skin cells as healing continues. However, in people with LOC syndrome, this tissue grows even when there is no major injury. One of the first symptoms in infants with LOC syndrome is a hoarse cry due to ulcers or overgrowth of granulation tissue in the voicebox (the larynx). Excess granulation tissue can also block the airways, leading to life-threatening breathing problems; as a result many affected individuals do not survive past childhood. In LOC syndrome, granulation tissue also grows in the eyes, specifically the conjunctiva, which are the moist tissues that line the eyelids and the white part of the eyes. Affected individuals often have impairment or complete loss of vision due to the tissue overgrowth. Another common feature of LOC syndrome is missing patches of skin (cutaneous erosions). The erosions heal slowly and may become infected. People with LOC syndrome can also have malformed nails and small, abnormal teeth. The hard, white material that forms the protective outer layer of each tooth (enamel) is thin, which contributes to frequent cavities. LOC syndrome is typically considered a subtype of another skin condition called junctional epidermolysis bullosa, which is characterized by fragile skin that blisters easily. While individuals with junctional epidermolysis bullosa can have some of the features of LOC syndrome, they do not usually have overgrowth of granulation tissue in the conjunctiva. |
Laryngo-onycho-cutaneous (LOC) syndrome is a disorder that leads to abnormalities of the voicebox (laryngo-), finger- and toenails (onycho-), and skin (cutaneous). Many of the condition's signs and symptoms are related to the abnormal growth of granulation tissue in different parts of the body. This red, bumpy tissue is normally produced during wound healing and is usually replaced by skin cells as healing continues. However, in people with LOC syndrome, this tissue grows even when there is no major injury. One of the first symptoms in infants with LOC syndrome is a hoarse cry due to ulcers or overgrowth of granulation tissue in the voicebox (the larynx). Excess granulation tissue can also block the airways, leading to life-threatening breathing problems; as a result many affected individuals do not survive past childhood. In LOC syndrome, granulation tissue also grows in the eyes, specifically the conjunctiva, which are the moist tissues that line the eyelids and the white part of the eyes. Affected individuals often have impairment or complete loss of vision due to the tissue overgrowth. Another common feature of LOC syndrome is missing patches of skin (cutaneous erosions). The erosions heal slowly and may become infected. People with LOC syndrome can also have malformed nails and small, abnormal teeth. The hard, white material that forms the protective outer layer of each tooth (enamel) is thin, which contributes to frequent cavities. LOC syndrome is typically considered a subtype of another skin condition called junctional epidermolysis bullosa, which is characterized by fragile skin that blisters easily. While individuals with junctional epidermolysis bullosa can have some of the features of LOC syndrome, they do not usually have overgrowth of granulation tissue in the conjunctiva. LOC syndrome is a rare disorder that primarily affects families of Punjabi background from India and Pakistan, although the condition has also been reported in one family from Iran. LOC syndrome is caused by mutations in the LAMA3 gene, which provides instructions for making one part (subunit) of a protein called laminin 332. This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. The laminin 332 protein plays an important role in strengthening and stabilizing the skin by helping to attach the top layer of skin (the epidermis) to underlying layers. Studies suggest that laminin 332 is also involved in wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The mutations involved in LOC syndrome alter the structure of one version of the alpha subunit of laminin 332 (called alpha-3a). Laminins made with the altered subunit cannot effectively attach the epidermis to underlying layers of skin or regulate wound healing. These abnormalities of laminin 332 cause the cutaneous erosions and overgrowth of granulation tissue that are characteristic of LOC syndrome. The inability of laminin 332 to perform its other functions leads to the nail and tooth abnormalities that occur in this condition. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by laryngo-onycho-cutaneous syndrome ? | LOC syndrome is a rare disorder that primarily affects families of Punjabi background from India and Pakistan, although the condition has also been reported in one family from Iran. |
Laryngo-onycho-cutaneous (LOC) syndrome is a disorder that leads to abnormalities of the voicebox (laryngo-), finger- and toenails (onycho-), and skin (cutaneous). Many of the condition's signs and symptoms are related to the abnormal growth of granulation tissue in different parts of the body. This red, bumpy tissue is normally produced during wound healing and is usually replaced by skin cells as healing continues. However, in people with LOC syndrome, this tissue grows even when there is no major injury. One of the first symptoms in infants with LOC syndrome is a hoarse cry due to ulcers or overgrowth of granulation tissue in the voicebox (the larynx). Excess granulation tissue can also block the airways, leading to life-threatening breathing problems; as a result many affected individuals do not survive past childhood. In LOC syndrome, granulation tissue also grows in the eyes, specifically the conjunctiva, which are the moist tissues that line the eyelids and the white part of the eyes. Affected individuals often have impairment or complete loss of vision due to the tissue overgrowth. Another common feature of LOC syndrome is missing patches of skin (cutaneous erosions). The erosions heal slowly and may become infected. People with LOC syndrome can also have malformed nails and small, abnormal teeth. The hard, white material that forms the protective outer layer of each tooth (enamel) is thin, which contributes to frequent cavities. LOC syndrome is typically considered a subtype of another skin condition called junctional epidermolysis bullosa, which is characterized by fragile skin that blisters easily. While individuals with junctional epidermolysis bullosa can have some of the features of LOC syndrome, they do not usually have overgrowth of granulation tissue in the conjunctiva. LOC syndrome is a rare disorder that primarily affects families of Punjabi background from India and Pakistan, although the condition has also been reported in one family from Iran. LOC syndrome is caused by mutations in the LAMA3 gene, which provides instructions for making one part (subunit) of a protein called laminin 332. This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. The laminin 332 protein plays an important role in strengthening and stabilizing the skin by helping to attach the top layer of skin (the epidermis) to underlying layers. Studies suggest that laminin 332 is also involved in wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The mutations involved in LOC syndrome alter the structure of one version of the alpha subunit of laminin 332 (called alpha-3a). Laminins made with the altered subunit cannot effectively attach the epidermis to underlying layers of skin or regulate wound healing. These abnormalities of laminin 332 cause the cutaneous erosions and overgrowth of granulation tissue that are characteristic of LOC syndrome. The inability of laminin 332 to perform its other functions leads to the nail and tooth abnormalities that occur in this condition. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to laryngo-onycho-cutaneous syndrome ? | LOC syndrome is caused by mutations in the LAMA3 gene, which provides instructions for making one part (subunit) of a protein called laminin 332. This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. The laminin 332 protein plays an important role in strengthening and stabilizing the skin by helping to attach the top layer of skin (the epidermis) to underlying layers. Studies suggest that laminin 332 is also involved in wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The mutations involved in LOC syndrome alter the structure of one version of the alpha subunit of laminin 332 (called alpha-3a). Laminins made with the altered subunit cannot effectively attach the epidermis to underlying layers of skin or regulate wound healing. These abnormalities of laminin 332 cause the cutaneous erosions and overgrowth of granulation tissue that are characteristic of LOC syndrome. The inability of laminin 332 to perform its other functions leads to the nail and tooth abnormalities that occur in this condition. |
Laryngo-onycho-cutaneous (LOC) syndrome is a disorder that leads to abnormalities of the voicebox (laryngo-), finger- and toenails (onycho-), and skin (cutaneous). Many of the condition's signs and symptoms are related to the abnormal growth of granulation tissue in different parts of the body. This red, bumpy tissue is normally produced during wound healing and is usually replaced by skin cells as healing continues. However, in people with LOC syndrome, this tissue grows even when there is no major injury. One of the first symptoms in infants with LOC syndrome is a hoarse cry due to ulcers or overgrowth of granulation tissue in the voicebox (the larynx). Excess granulation tissue can also block the airways, leading to life-threatening breathing problems; as a result many affected individuals do not survive past childhood. In LOC syndrome, granulation tissue also grows in the eyes, specifically the conjunctiva, which are the moist tissues that line the eyelids and the white part of the eyes. Affected individuals often have impairment or complete loss of vision due to the tissue overgrowth. Another common feature of LOC syndrome is missing patches of skin (cutaneous erosions). The erosions heal slowly and may become infected. People with LOC syndrome can also have malformed nails and small, abnormal teeth. The hard, white material that forms the protective outer layer of each tooth (enamel) is thin, which contributes to frequent cavities. LOC syndrome is typically considered a subtype of another skin condition called junctional epidermolysis bullosa, which is characterized by fragile skin that blisters easily. While individuals with junctional epidermolysis bullosa can have some of the features of LOC syndrome, they do not usually have overgrowth of granulation tissue in the conjunctiva. LOC syndrome is a rare disorder that primarily affects families of Punjabi background from India and Pakistan, although the condition has also been reported in one family from Iran. LOC syndrome is caused by mutations in the LAMA3 gene, which provides instructions for making one part (subunit) of a protein called laminin 332. This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. The laminin 332 protein plays an important role in strengthening and stabilizing the skin by helping to attach the top layer of skin (the epidermis) to underlying layers. Studies suggest that laminin 332 is also involved in wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The mutations involved in LOC syndrome alter the structure of one version of the alpha subunit of laminin 332 (called alpha-3a). Laminins made with the altered subunit cannot effectively attach the epidermis to underlying layers of skin or regulate wound healing. These abnormalities of laminin 332 cause the cutaneous erosions and overgrowth of granulation tissue that are characteristic of LOC syndrome. The inability of laminin 332 to perform its other functions leads to the nail and tooth abnormalities that occur in this condition. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is laryngo-onycho-cutaneous syndrome inherited ? | This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. |
Laryngo-onycho-cutaneous (LOC) syndrome is a disorder that leads to abnormalities of the voicebox (laryngo-), finger- and toenails (onycho-), and skin (cutaneous). Many of the condition's signs and symptoms are related to the abnormal growth of granulation tissue in different parts of the body. This red, bumpy tissue is normally produced during wound healing and is usually replaced by skin cells as healing continues. However, in people with LOC syndrome, this tissue grows even when there is no major injury. One of the first symptoms in infants with LOC syndrome is a hoarse cry due to ulcers or overgrowth of granulation tissue in the voicebox (the larynx). Excess granulation tissue can also block the airways, leading to life-threatening breathing problems; as a result many affected individuals do not survive past childhood. In LOC syndrome, granulation tissue also grows in the eyes, specifically the conjunctiva, which are the moist tissues that line the eyelids and the white part of the eyes. Affected individuals often have impairment or complete loss of vision due to the tissue overgrowth. Another common feature of LOC syndrome is missing patches of skin (cutaneous erosions). The erosions heal slowly and may become infected. People with LOC syndrome can also have malformed nails and small, abnormal teeth. The hard, white material that forms the protective outer layer of each tooth (enamel) is thin, which contributes to frequent cavities. LOC syndrome is typically considered a subtype of another skin condition called junctional epidermolysis bullosa, which is characterized by fragile skin that blisters easily. While individuals with junctional epidermolysis bullosa can have some of the features of LOC syndrome, they do not usually have overgrowth of granulation tissue in the conjunctiva. LOC syndrome is a rare disorder that primarily affects families of Punjabi background from India and Pakistan, although the condition has also been reported in one family from Iran. LOC syndrome is caused by mutations in the LAMA3 gene, which provides instructions for making one part (subunit) of a protein called laminin 332. This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. The laminin 332 protein plays an important role in strengthening and stabilizing the skin by helping to attach the top layer of skin (the epidermis) to underlying layers. Studies suggest that laminin 332 is also involved in wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The mutations involved in LOC syndrome alter the structure of one version of the alpha subunit of laminin 332 (called alpha-3a). Laminins made with the altered subunit cannot effectively attach the epidermis to underlying layers of skin or regulate wound healing. These abnormalities of laminin 332 cause the cutaneous erosions and overgrowth of granulation tissue that are characteristic of LOC syndrome. The inability of laminin 332 to perform its other functions leads to the nail and tooth abnormalities that occur in this condition. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for laryngo-onycho-cutaneous syndrome ? | These resources address the diagnosis or management of laryngo-onycho-cutaneous syndrome: - Genetic Testing Registry: Laryngoonychocutaneous syndrome These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Adenylosuccinate lyase deficiency is a neurological disorder that causes brain dysfunction (encephalopathy) leading to delayed development of mental and movement abilities (psychomotor delay), autistic behaviors that affect communication and social interaction, and seizures. A characteristic feature that can help with diagnosis of this condition is the presence of chemicals called succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado) in body fluids. Adenylosuccinate lyase deficiency is classified into three forms based on the severity of the signs and symptoms. The most severe is the neonatal form. Signs and symptoms of this form can be detected at or before birth and can include impaired growth during fetal development and a small head size (microcephaly). Affected newborns have severe encephalopathy, which leads to a lack of movement, difficulty feeding, and life-threatening respiratory problems. Some affected babies develop seizures that do not improve with treatment. Because of the severity of the encephalopathy, infants with this form of the condition generally do not survive more than a few weeks after birth. Adenylosuccinate lyase deficiency type I (also known as the severe form) is the most common. The signs and symptoms of this form begin in the first months of life. Affected babies have severe psychomotor delay, weak muscle tone (hypotonia), and microcephaly. Many affected infants develop recurrent seizures that are difficult to treat, and some exhibit autistic behaviors, such as repetitive behaviors and a lack of eye contact. In individuals with adenylosuccinate lyase deficiency type II (also known as the moderate or mild form), development is typically normal for the first few years of life but then slows. Psychomotor delay is considered mild or moderate. Some children with this form of the condition develop seizures and autistic behaviors. Adenylosuccinate lyase deficiency is a rare disorder; fewer than 100 cases have been reported. The condition is most common in the Netherlands and Belgium, but it has been found worldwide. All forms of adenylosuccinate lyase deficiency are caused by mutations in the ADSL gene. This gene provides instructions for making an enzyme called adenylosuccinate lyase, which performs two steps in the process that produces purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). Most of the mutations involved in adenylosuccinate lyase deficiency change single protein building blocks (amino acids) in the adenylosuccinate lyase enzyme, which impairs its function. Reduced function of this enzyme leads to buildup of SAICAR and SAMP, which are converted through a different reaction to succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado). Researchers believe that SAICAr and S-Ado are toxic; damage to brain tissue caused by one or both of these substances likely underlies the neurological problems that occur in adenylosuccinate lyase deficiency. Studies suggest that the amount of SAICAr relative to S-Ado reflects the severity of adenylosuccinate lyase deficiency. Individuals with more SAICAr than S-Ado have more severe encephalopathy and psychomotor delay. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) adenylosuccinate lyase deficiency ? | Adenylosuccinate lyase deficiency is a neurological disorder that causes brain dysfunction (encephalopathy) leading to delayed development of mental and movement abilities (psychomotor delay), autistic behaviors that affect communication and social interaction, and seizures. A characteristic feature that can help with diagnosis of this condition is the presence of chemicals called succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado) in body fluids. Adenylosuccinate lyase deficiency is classified into three forms based on the severity of the signs and symptoms. The most severe is the neonatal form. Signs and symptoms of this form can be detected at or before birth and can include impaired growth during fetal development and a small head size (microcephaly). Affected newborns have severe encephalopathy, which leads to a lack of movement, difficulty feeding, and life-threatening respiratory problems. Some affected babies develop seizures that do not improve with treatment. Because of the severity of the encephalopathy, infants with this form of the condition generally do not survive more than a few weeks after birth. Adenylosuccinate lyase deficiency type I (also known as the severe form) is the most common. The signs and symptoms of this form begin in the first months of life. Affected babies have severe psychomotor delay, weak muscle tone (hypotonia), and microcephaly. Many affected infants develop recurrent seizures that are difficult to treat, and some exhibit autistic behaviors, such as repetitive behaviors and a lack of eye contact. In individuals with adenylosuccinate lyase deficiency type II (also known as the moderate or mild form), development is typically normal for the first few years of life but then slows. Psychomotor delay is considered mild or moderate. Some children with this form of the condition develop seizures and autistic behaviors. |
Adenylosuccinate lyase deficiency is a neurological disorder that causes brain dysfunction (encephalopathy) leading to delayed development of mental and movement abilities (psychomotor delay), autistic behaviors that affect communication and social interaction, and seizures. A characteristic feature that can help with diagnosis of this condition is the presence of chemicals called succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado) in body fluids. Adenylosuccinate lyase deficiency is classified into three forms based on the severity of the signs and symptoms. The most severe is the neonatal form. Signs and symptoms of this form can be detected at or before birth and can include impaired growth during fetal development and a small head size (microcephaly). Affected newborns have severe encephalopathy, which leads to a lack of movement, difficulty feeding, and life-threatening respiratory problems. Some affected babies develop seizures that do not improve with treatment. Because of the severity of the encephalopathy, infants with this form of the condition generally do not survive more than a few weeks after birth. Adenylosuccinate lyase deficiency type I (also known as the severe form) is the most common. The signs and symptoms of this form begin in the first months of life. Affected babies have severe psychomotor delay, weak muscle tone (hypotonia), and microcephaly. Many affected infants develop recurrent seizures that are difficult to treat, and some exhibit autistic behaviors, such as repetitive behaviors and a lack of eye contact. In individuals with adenylosuccinate lyase deficiency type II (also known as the moderate or mild form), development is typically normal for the first few years of life but then slows. Psychomotor delay is considered mild or moderate. Some children with this form of the condition develop seizures and autistic behaviors. Adenylosuccinate lyase deficiency is a rare disorder; fewer than 100 cases have been reported. The condition is most common in the Netherlands and Belgium, but it has been found worldwide. All forms of adenylosuccinate lyase deficiency are caused by mutations in the ADSL gene. This gene provides instructions for making an enzyme called adenylosuccinate lyase, which performs two steps in the process that produces purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). Most of the mutations involved in adenylosuccinate lyase deficiency change single protein building blocks (amino acids) in the adenylosuccinate lyase enzyme, which impairs its function. Reduced function of this enzyme leads to buildup of SAICAR and SAMP, which are converted through a different reaction to succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado). Researchers believe that SAICAr and S-Ado are toxic; damage to brain tissue caused by one or both of these substances likely underlies the neurological problems that occur in adenylosuccinate lyase deficiency. Studies suggest that the amount of SAICAr relative to S-Ado reflects the severity of adenylosuccinate lyase deficiency. Individuals with more SAICAr than S-Ado have more severe encephalopathy and psychomotor delay. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by adenylosuccinate lyase deficiency ? | Adenylosuccinate lyase deficiency is a rare disorder; fewer than 100 cases have been reported. The condition is most common in the Netherlands and Belgium, but it has been found worldwide. |
Adenylosuccinate lyase deficiency is a neurological disorder that causes brain dysfunction (encephalopathy) leading to delayed development of mental and movement abilities (psychomotor delay), autistic behaviors that affect communication and social interaction, and seizures. A characteristic feature that can help with diagnosis of this condition is the presence of chemicals called succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado) in body fluids. Adenylosuccinate lyase deficiency is classified into three forms based on the severity of the signs and symptoms. The most severe is the neonatal form. Signs and symptoms of this form can be detected at or before birth and can include impaired growth during fetal development and a small head size (microcephaly). Affected newborns have severe encephalopathy, which leads to a lack of movement, difficulty feeding, and life-threatening respiratory problems. Some affected babies develop seizures that do not improve with treatment. Because of the severity of the encephalopathy, infants with this form of the condition generally do not survive more than a few weeks after birth. Adenylosuccinate lyase deficiency type I (also known as the severe form) is the most common. The signs and symptoms of this form begin in the first months of life. Affected babies have severe psychomotor delay, weak muscle tone (hypotonia), and microcephaly. Many affected infants develop recurrent seizures that are difficult to treat, and some exhibit autistic behaviors, such as repetitive behaviors and a lack of eye contact. In individuals with adenylosuccinate lyase deficiency type II (also known as the moderate or mild form), development is typically normal for the first few years of life but then slows. Psychomotor delay is considered mild or moderate. Some children with this form of the condition develop seizures and autistic behaviors. Adenylosuccinate lyase deficiency is a rare disorder; fewer than 100 cases have been reported. The condition is most common in the Netherlands and Belgium, but it has been found worldwide. All forms of adenylosuccinate lyase deficiency are caused by mutations in the ADSL gene. This gene provides instructions for making an enzyme called adenylosuccinate lyase, which performs two steps in the process that produces purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). Most of the mutations involved in adenylosuccinate lyase deficiency change single protein building blocks (amino acids) in the adenylosuccinate lyase enzyme, which impairs its function. Reduced function of this enzyme leads to buildup of SAICAR and SAMP, which are converted through a different reaction to succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado). Researchers believe that SAICAr and S-Ado are toxic; damage to brain tissue caused by one or both of these substances likely underlies the neurological problems that occur in adenylosuccinate lyase deficiency. Studies suggest that the amount of SAICAr relative to S-Ado reflects the severity of adenylosuccinate lyase deficiency. Individuals with more SAICAr than S-Ado have more severe encephalopathy and psychomotor delay. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to adenylosuccinate lyase deficiency ? | All forms of adenylosuccinate lyase deficiency are caused by mutations in the ADSL gene. This gene provides instructions for making an enzyme called adenylosuccinate lyase, which performs two steps in the process that produces purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). Most of the mutations involved in adenylosuccinate lyase deficiency change single protein building blocks (amino acids) in the adenylosuccinate lyase enzyme, which impairs its function. Reduced function of this enzyme leads to buildup of SAICAR and SAMP, which are converted through a different reaction to succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado). Researchers believe that SAICAr and S-Ado are toxic; damage to brain tissue caused by one or both of these substances likely underlies the neurological problems that occur in adenylosuccinate lyase deficiency. Studies suggest that the amount of SAICAr relative to S-Ado reflects the severity of adenylosuccinate lyase deficiency. Individuals with more SAICAr than S-Ado have more severe encephalopathy and psychomotor delay. |
Adenylosuccinate lyase deficiency is a neurological disorder that causes brain dysfunction (encephalopathy) leading to delayed development of mental and movement abilities (psychomotor delay), autistic behaviors that affect communication and social interaction, and seizures. A characteristic feature that can help with diagnosis of this condition is the presence of chemicals called succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado) in body fluids. Adenylosuccinate lyase deficiency is classified into three forms based on the severity of the signs and symptoms. The most severe is the neonatal form. Signs and symptoms of this form can be detected at or before birth and can include impaired growth during fetal development and a small head size (microcephaly). Affected newborns have severe encephalopathy, which leads to a lack of movement, difficulty feeding, and life-threatening respiratory problems. Some affected babies develop seizures that do not improve with treatment. Because of the severity of the encephalopathy, infants with this form of the condition generally do not survive more than a few weeks after birth. Adenylosuccinate lyase deficiency type I (also known as the severe form) is the most common. The signs and symptoms of this form begin in the first months of life. Affected babies have severe psychomotor delay, weak muscle tone (hypotonia), and microcephaly. Many affected infants develop recurrent seizures that are difficult to treat, and some exhibit autistic behaviors, such as repetitive behaviors and a lack of eye contact. In individuals with adenylosuccinate lyase deficiency type II (also known as the moderate or mild form), development is typically normal for the first few years of life but then slows. Psychomotor delay is considered mild or moderate. Some children with this form of the condition develop seizures and autistic behaviors. Adenylosuccinate lyase deficiency is a rare disorder; fewer than 100 cases have been reported. The condition is most common in the Netherlands and Belgium, but it has been found worldwide. All forms of adenylosuccinate lyase deficiency are caused by mutations in the ADSL gene. This gene provides instructions for making an enzyme called adenylosuccinate lyase, which performs two steps in the process that produces purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). Most of the mutations involved in adenylosuccinate lyase deficiency change single protein building blocks (amino acids) in the adenylosuccinate lyase enzyme, which impairs its function. Reduced function of this enzyme leads to buildup of SAICAR and SAMP, which are converted through a different reaction to succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado). Researchers believe that SAICAr and S-Ado are toxic; damage to brain tissue caused by one or both of these substances likely underlies the neurological problems that occur in adenylosuccinate lyase deficiency. Studies suggest that the amount of SAICAr relative to S-Ado reflects the severity of adenylosuccinate lyase deficiency. Individuals with more SAICAr than S-Ado have more severe encephalopathy and psychomotor delay. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is adenylosuccinate lyase deficiency inherited ? | This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. |
Adenylosuccinate lyase deficiency is a neurological disorder that causes brain dysfunction (encephalopathy) leading to delayed development of mental and movement abilities (psychomotor delay), autistic behaviors that affect communication and social interaction, and seizures. A characteristic feature that can help with diagnosis of this condition is the presence of chemicals called succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado) in body fluids. Adenylosuccinate lyase deficiency is classified into three forms based on the severity of the signs and symptoms. The most severe is the neonatal form. Signs and symptoms of this form can be detected at or before birth and can include impaired growth during fetal development and a small head size (microcephaly). Affected newborns have severe encephalopathy, which leads to a lack of movement, difficulty feeding, and life-threatening respiratory problems. Some affected babies develop seizures that do not improve with treatment. Because of the severity of the encephalopathy, infants with this form of the condition generally do not survive more than a few weeks after birth. Adenylosuccinate lyase deficiency type I (also known as the severe form) is the most common. The signs and symptoms of this form begin in the first months of life. Affected babies have severe psychomotor delay, weak muscle tone (hypotonia), and microcephaly. Many affected infants develop recurrent seizures that are difficult to treat, and some exhibit autistic behaviors, such as repetitive behaviors and a lack of eye contact. In individuals with adenylosuccinate lyase deficiency type II (also known as the moderate or mild form), development is typically normal for the first few years of life but then slows. Psychomotor delay is considered mild or moderate. Some children with this form of the condition develop seizures and autistic behaviors. Adenylosuccinate lyase deficiency is a rare disorder; fewer than 100 cases have been reported. The condition is most common in the Netherlands and Belgium, but it has been found worldwide. All forms of adenylosuccinate lyase deficiency are caused by mutations in the ADSL gene. This gene provides instructions for making an enzyme called adenylosuccinate lyase, which performs two steps in the process that produces purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). Most of the mutations involved in adenylosuccinate lyase deficiency change single protein building blocks (amino acids) in the adenylosuccinate lyase enzyme, which impairs its function. Reduced function of this enzyme leads to buildup of SAICAR and SAMP, which are converted through a different reaction to succinylaminoimidazole carboxamide riboside (SAICAr) and succinyladenosine (S-Ado). Researchers believe that SAICAr and S-Ado are toxic; damage to brain tissue caused by one or both of these substances likely underlies the neurological problems that occur in adenylosuccinate lyase deficiency. Studies suggest that the amount of SAICAr relative to S-Ado reflects the severity of adenylosuccinate lyase deficiency. Individuals with more SAICAr than S-Ado have more severe encephalopathy and psychomotor delay. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for adenylosuccinate lyase deficiency ? | These resources address the diagnosis or management of adenylosuccinate lyase deficiency: - Genetic Testing Registry: Adenylosuccinate lyase deficiency These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Adolescent idiopathic scoliosis is an abnormal curvature of the spine that appears in late childhood or adolescence. Instead of growing straight, the spine develops a side-to-side curvature, usually in an elongated "S" or "C" shape; the bones of the spine are also slightly twisted or rotated. Adolescent idiopathic scoliosis appears during the adolescent growth spurt, a time when children are growing rapidly. In many cases the abnormal spinal curve is stable, although in some children the curve is progressive (meaning it becomes more severe over time). For unknown reasons, severe and progressive curves occur more frequently in girls than in boys. However, mild spinal curvature is equally common in girls and boys. Mild scoliosis generally does not cause pain, problems with movement, or difficulty breathing. It may only be diagnosed if it is noticed during a regular physical examination or a scoliosis screening at school. The most common signs of the condition include a tilt or unevenness (asymmetry) in the shoulders, hips, or waist, or having one leg that appears longer than the other. A small percentage of affected children develop more severe, pronounced spinal curvature. Scoliosis can occur as a feature of other conditions, including a variety of genetic syndromes. However, adolescent idiopathic scoliosis typically occurs by itself, without signs and symptoms affecting other parts of the body. Adolescent idiopathic scoliosis is the most common spinal abnormality in children. It affects an estimated 2 to 3 percent of children in the U.S. The term "idiopathic" means that the cause of this condition is unknown. Adolescent idiopathic scoliosis probably results from a combination of genetic and environmental factors. Studies suggest that the abnormal spinal curvature may be related to hormonal problems, abnormal bone or muscle growth, nervous system abnormalities, or other factors that have not been identified. Researchers suspect that many genes are involved in adolescent idiopathic scoliosis. Some of these genes likely contribute to causing the disorder, while others play a role in determining the severity of spinal curvature and whether the curve is stable or progressive. Although many genes have been studied, few clear and consistent genetic associations with adolescent idiopathic scoliosis have been identified. Adolescent idiopathic scoliosis can be sporadic, which means it occurs in people without a family history of the condition, or it can cluster in families. The inheritance pattern of adolescent idiopathic scoliosis is unclear because many genetic and environmental factors appear to be involved. However, having a close relative (such as a parent or sibling) with adolescent idiopathic scoliosis increases a child's risk of developing the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) adolescent idiopathic scoliosis ? | Adolescent idiopathic scoliosis is an abnormal curvature of the spine that appears in late childhood or adolescence. Instead of growing straight, the spine develops a side-to-side curvature, usually in an elongated "S" or "C" shape; the bones of the spine are also slightly twisted or rotated. Adolescent idiopathic scoliosis appears during the adolescent growth spurt, a time when children are growing rapidly. In many cases the abnormal spinal curve is stable, although in some children the curve is progressive (meaning it becomes more severe over time). For unknown reasons, severe and progressive curves occur more frequently in girls than in boys. However, mild spinal curvature is equally common in girls and boys. Mild scoliosis generally does not cause pain, problems with movement, or difficulty breathing. It may only be diagnosed if it is noticed during a regular physical examination or a scoliosis screening at school. The most common signs of the condition include a tilt or unevenness (asymmetry) in the shoulders, hips, or waist, or having one leg that appears longer than the other. A small percentage of affected children develop more severe, pronounced spinal curvature. Scoliosis can occur as a feature of other conditions, including a variety of genetic syndromes. However, adolescent idiopathic scoliosis typically occurs by itself, without signs and symptoms affecting other parts of the body. |
Adolescent idiopathic scoliosis is an abnormal curvature of the spine that appears in late childhood or adolescence. Instead of growing straight, the spine develops a side-to-side curvature, usually in an elongated "S" or "C" shape; the bones of the spine are also slightly twisted or rotated. Adolescent idiopathic scoliosis appears during the adolescent growth spurt, a time when children are growing rapidly. In many cases the abnormal spinal curve is stable, although in some children the curve is progressive (meaning it becomes more severe over time). For unknown reasons, severe and progressive curves occur more frequently in girls than in boys. However, mild spinal curvature is equally common in girls and boys. Mild scoliosis generally does not cause pain, problems with movement, or difficulty breathing. It may only be diagnosed if it is noticed during a regular physical examination or a scoliosis screening at school. The most common signs of the condition include a tilt or unevenness (asymmetry) in the shoulders, hips, or waist, or having one leg that appears longer than the other. A small percentage of affected children develop more severe, pronounced spinal curvature. Scoliosis can occur as a feature of other conditions, including a variety of genetic syndromes. However, adolescent idiopathic scoliosis typically occurs by itself, without signs and symptoms affecting other parts of the body. Adolescent idiopathic scoliosis is the most common spinal abnormality in children. It affects an estimated 2 to 3 percent of children in the U.S. The term "idiopathic" means that the cause of this condition is unknown. Adolescent idiopathic scoliosis probably results from a combination of genetic and environmental factors. Studies suggest that the abnormal spinal curvature may be related to hormonal problems, abnormal bone or muscle growth, nervous system abnormalities, or other factors that have not been identified. Researchers suspect that many genes are involved in adolescent idiopathic scoliosis. Some of these genes likely contribute to causing the disorder, while others play a role in determining the severity of spinal curvature and whether the curve is stable or progressive. Although many genes have been studied, few clear and consistent genetic associations with adolescent idiopathic scoliosis have been identified. Adolescent idiopathic scoliosis can be sporadic, which means it occurs in people without a family history of the condition, or it can cluster in families. The inheritance pattern of adolescent idiopathic scoliosis is unclear because many genetic and environmental factors appear to be involved. However, having a close relative (such as a parent or sibling) with adolescent idiopathic scoliosis increases a child's risk of developing the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by adolescent idiopathic scoliosis ? | Adolescent idiopathic scoliosis is the most common spinal abnormality in children. It affects an estimated 2 to 3 percent of children in the U.S. |
Adolescent idiopathic scoliosis is an abnormal curvature of the spine that appears in late childhood or adolescence. Instead of growing straight, the spine develops a side-to-side curvature, usually in an elongated "S" or "C" shape; the bones of the spine are also slightly twisted or rotated. Adolescent idiopathic scoliosis appears during the adolescent growth spurt, a time when children are growing rapidly. In many cases the abnormal spinal curve is stable, although in some children the curve is progressive (meaning it becomes more severe over time). For unknown reasons, severe and progressive curves occur more frequently in girls than in boys. However, mild spinal curvature is equally common in girls and boys. Mild scoliosis generally does not cause pain, problems with movement, or difficulty breathing. It may only be diagnosed if it is noticed during a regular physical examination or a scoliosis screening at school. The most common signs of the condition include a tilt or unevenness (asymmetry) in the shoulders, hips, or waist, or having one leg that appears longer than the other. A small percentage of affected children develop more severe, pronounced spinal curvature. Scoliosis can occur as a feature of other conditions, including a variety of genetic syndromes. However, adolescent idiopathic scoliosis typically occurs by itself, without signs and symptoms affecting other parts of the body. Adolescent idiopathic scoliosis is the most common spinal abnormality in children. It affects an estimated 2 to 3 percent of children in the U.S. The term "idiopathic" means that the cause of this condition is unknown. Adolescent idiopathic scoliosis probably results from a combination of genetic and environmental factors. Studies suggest that the abnormal spinal curvature may be related to hormonal problems, abnormal bone or muscle growth, nervous system abnormalities, or other factors that have not been identified. Researchers suspect that many genes are involved in adolescent idiopathic scoliosis. Some of these genes likely contribute to causing the disorder, while others play a role in determining the severity of spinal curvature and whether the curve is stable or progressive. Although many genes have been studied, few clear and consistent genetic associations with adolescent idiopathic scoliosis have been identified. Adolescent idiopathic scoliosis can be sporadic, which means it occurs in people without a family history of the condition, or it can cluster in families. The inheritance pattern of adolescent idiopathic scoliosis is unclear because many genetic and environmental factors appear to be involved. However, having a close relative (such as a parent or sibling) with adolescent idiopathic scoliosis increases a child's risk of developing the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to adolescent idiopathic scoliosis ? | The term "idiopathic" means that the cause of this condition is unknown. Adolescent idiopathic scoliosis probably results from a combination of genetic and environmental factors. Studies suggest that the abnormal spinal curvature may be related to hormonal problems, abnormal bone or muscle growth, nervous system abnormalities, or other factors that have not been identified. Researchers suspect that many genes are involved in adolescent idiopathic scoliosis. Some of these genes likely contribute to causing the disorder, while others play a role in determining the severity of spinal curvature and whether the curve is stable or progressive. Although many genes have been studied, few clear and consistent genetic associations with adolescent idiopathic scoliosis have been identified. |
Adolescent idiopathic scoliosis is an abnormal curvature of the spine that appears in late childhood or adolescence. Instead of growing straight, the spine develops a side-to-side curvature, usually in an elongated "S" or "C" shape; the bones of the spine are also slightly twisted or rotated. Adolescent idiopathic scoliosis appears during the adolescent growth spurt, a time when children are growing rapidly. In many cases the abnormal spinal curve is stable, although in some children the curve is progressive (meaning it becomes more severe over time). For unknown reasons, severe and progressive curves occur more frequently in girls than in boys. However, mild spinal curvature is equally common in girls and boys. Mild scoliosis generally does not cause pain, problems with movement, or difficulty breathing. It may only be diagnosed if it is noticed during a regular physical examination or a scoliosis screening at school. The most common signs of the condition include a tilt or unevenness (asymmetry) in the shoulders, hips, or waist, or having one leg that appears longer than the other. A small percentage of affected children develop more severe, pronounced spinal curvature. Scoliosis can occur as a feature of other conditions, including a variety of genetic syndromes. However, adolescent idiopathic scoliosis typically occurs by itself, without signs and symptoms affecting other parts of the body. Adolescent idiopathic scoliosis is the most common spinal abnormality in children. It affects an estimated 2 to 3 percent of children in the U.S. The term "idiopathic" means that the cause of this condition is unknown. Adolescent idiopathic scoliosis probably results from a combination of genetic and environmental factors. Studies suggest that the abnormal spinal curvature may be related to hormonal problems, abnormal bone or muscle growth, nervous system abnormalities, or other factors that have not been identified. Researchers suspect that many genes are involved in adolescent idiopathic scoliosis. Some of these genes likely contribute to causing the disorder, while others play a role in determining the severity of spinal curvature and whether the curve is stable or progressive. Although many genes have been studied, few clear and consistent genetic associations with adolescent idiopathic scoliosis have been identified. Adolescent idiopathic scoliosis can be sporadic, which means it occurs in people without a family history of the condition, or it can cluster in families. The inheritance pattern of adolescent idiopathic scoliosis is unclear because many genetic and environmental factors appear to be involved. However, having a close relative (such as a parent or sibling) with adolescent idiopathic scoliosis increases a child's risk of developing the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is adolescent idiopathic scoliosis inherited ? | Adolescent idiopathic scoliosis can be sporadic, which means it occurs in people without a family history of the condition, or it can cluster in families. The inheritance pattern of adolescent idiopathic scoliosis is unclear because many genetic and environmental factors appear to be involved. However, having a close relative (such as a parent or sibling) with adolescent idiopathic scoliosis increases a child's risk of developing the condition. |
Adolescent idiopathic scoliosis is an abnormal curvature of the spine that appears in late childhood or adolescence. Instead of growing straight, the spine develops a side-to-side curvature, usually in an elongated "S" or "C" shape; the bones of the spine are also slightly twisted or rotated. Adolescent idiopathic scoliosis appears during the adolescent growth spurt, a time when children are growing rapidly. In many cases the abnormal spinal curve is stable, although in some children the curve is progressive (meaning it becomes more severe over time). For unknown reasons, severe and progressive curves occur more frequently in girls than in boys. However, mild spinal curvature is equally common in girls and boys. Mild scoliosis generally does not cause pain, problems with movement, or difficulty breathing. It may only be diagnosed if it is noticed during a regular physical examination or a scoliosis screening at school. The most common signs of the condition include a tilt or unevenness (asymmetry) in the shoulders, hips, or waist, or having one leg that appears longer than the other. A small percentage of affected children develop more severe, pronounced spinal curvature. Scoliosis can occur as a feature of other conditions, including a variety of genetic syndromes. However, adolescent idiopathic scoliosis typically occurs by itself, without signs and symptoms affecting other parts of the body. Adolescent idiopathic scoliosis is the most common spinal abnormality in children. It affects an estimated 2 to 3 percent of children in the U.S. The term "idiopathic" means that the cause of this condition is unknown. Adolescent idiopathic scoliosis probably results from a combination of genetic and environmental factors. Studies suggest that the abnormal spinal curvature may be related to hormonal problems, abnormal bone or muscle growth, nervous system abnormalities, or other factors that have not been identified. Researchers suspect that many genes are involved in adolescent idiopathic scoliosis. Some of these genes likely contribute to causing the disorder, while others play a role in determining the severity of spinal curvature and whether the curve is stable or progressive. Although many genes have been studied, few clear and consistent genetic associations with adolescent idiopathic scoliosis have been identified. Adolescent idiopathic scoliosis can be sporadic, which means it occurs in people without a family history of the condition, or it can cluster in families. The inheritance pattern of adolescent idiopathic scoliosis is unclear because many genetic and environmental factors appear to be involved. However, having a close relative (such as a parent or sibling) with adolescent idiopathic scoliosis increases a child's risk of developing the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for adolescent idiopathic scoliosis ? | These resources address the diagnosis or management of adolescent idiopathic scoliosis: - Genetic Testing Registry: Scoliosis, idiopathic 1 - Genetic Testing Registry: Scoliosis, idiopathic 2 - Genetic Testing Registry: Scoliosis, idiopathic 3 - National Scoliosis Foundation: FAQs - Scoliosis Research Society: Find A Specialist - Scoliosis Research Society: For Adolescents These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Fragile X syndrome is a genetic condition that causes a range of developmental problems including learning disabilities and cognitive impairment. Usually, males are more severely affected by this disorder than females. Affected individuals usually have delayed development of speech and language by age 2. Most males with fragile X syndrome have mild to moderate intellectual disability, while about one-third of affected females are intellectually disabled. Children with fragile X syndrome may also have anxiety and hyperactive behavior such as fidgeting or impulsive actions. They may have attention deficit disorder (ADD), which includes an impaired ability to maintain attention and difficulty focusing on specific tasks. About one-third of individuals with fragile X syndrome have features of autism spectrum disorder that affect communication and social interaction. Seizures occur in about 15 percent of males and about 5 percent of females with fragile X syndrome. Most males and about half of females with fragile X syndrome have characteristic physical features that become more apparent with age. These features include a long and narrow face, large ears, a prominent jaw and forehead, unusually flexible fingers, flat feet, and in males, enlarged testicles (macroorchidism) after puberty. Fragile X syndrome occurs in approximately 1 in 4,000 males and 1 in 8,000 females. Mutations in the FMR1 gene cause fragile X syndrome. The FMR1 gene provides instructions for making a protein called FMRP. This protein helps regulate the production of other proteins and plays a role in the development of synapses, which are specialized connections between nerve cells. Synapses are critical for relaying nerve impulses. Nearly all cases of fragile X syndrome are caused by a mutation in which a DNA segment, known as the CGG triplet repeat, is expanded within the FMR1 gene. Normally, this DNA segment is repeated from 5 to about 40 times. In people with fragile X syndrome, however, the CGG segment is repeated more than 200 times. The abnormally expanded CGG segment turns off (silences) the FMR1 gene, which prevents the gene from producing FMRP. Loss or a shortage (deficiency) of this protein disrupts nervous system functions and leads to the signs and symptoms of fragile X syndrome. Males and females with 55 to 200 repeats of the CGG segment are said to have an FMR1 gene premutation. Most people with this premutation are intellectually normal. In some cases, however, individuals with a premutation have lower than normal amounts of FMRP. As a result, they may have mild versions of the physical features seen in fragile X syndrome (such as prominent ears) and may experience emotional problems such as anxiety or depression. Some children with an FMR1 premutation may have learning disabilities or autistic-like behavior. The premutation is also associated with an increased risk of disorders called fragile X-associated primary ovarian insufficiency (FXPOI) and fragile X-associated tremor/ataxia syndrome (FXTAS). Fragile X syndrome is inherited in an X-linked dominant pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. (The Y chromosome is the other sex chromosome.) The inheritance is dominant if one copy of the altered gene in each cell is sufficient to cause the condition. X-linked dominant means that in females (who have two X chromosomes), a mutation in one of the two copies of a gene in each cell is sufficient to cause the disorder. In males (who have only one X chromosome), a mutation in the only copy of a gene in each cell causes the disorder. In most cases, males experience more severe symptoms of the disorder than females. In women, the FMR1 gene premutation on the X chromosome can expand to more than 200 CGG repeats in cells that develop into eggs. This means that women with the premutation have an increased risk of having a child with fragile X syndrome. By contrast, the premutation in men does not expand to more than 200 repeats as it is passed to the next generation. Men pass the premutation only to their daughters. Their sons receive a Y chromosome, which does not include the FMR1 gene. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) fragile X syndrome ? | Fragile X syndrome is a genetic condition that causes a range of developmental problems including learning disabilities and cognitive impairment. Usually, males are more severely affected by this disorder than females. Affected individuals usually have delayed development of speech and language by age 2. Most males with fragile X syndrome have mild to moderate intellectual disability, while about one-third of affected females are intellectually disabled. Children with fragile X syndrome may also have anxiety and hyperactive behavior such as fidgeting or impulsive actions. They may have attention deficit disorder (ADD), which includes an impaired ability to maintain attention and difficulty focusing on specific tasks. About one-third of individuals with fragile X syndrome have features of autism spectrum disorders that affect communication and social interaction. Seizures occur in about 15 percent of males and about 5 percent of females with fragile X syndrome. Most males and about half of females with fragile X syndrome have characteristic physical features that become more apparent with age. These features include a long and narrow face, large ears, a prominent jaw and forehead, unusually flexible fingers, flat feet, and in males, enlarged testicles (macroorchidism) after puberty. |
Fragile X syndrome is a genetic condition that causes a range of developmental problems including learning disabilities and cognitive impairment. Usually, males are more severely affected by this disorder than females. Affected individuals usually have delayed development of speech and language by age 2. Most males with fragile X syndrome have mild to moderate intellectual disability, while about one-third of affected females are intellectually disabled. Children with fragile X syndrome may also have anxiety and hyperactive behavior such as fidgeting or impulsive actions. They may have attention deficit disorder (ADD), which includes an impaired ability to maintain attention and difficulty focusing on specific tasks. About one-third of individuals with fragile X syndrome have features of autism spectrum disorder that affect communication and social interaction. Seizures occur in about 15 percent of males and about 5 percent of females with fragile X syndrome. Most males and about half of females with fragile X syndrome have characteristic physical features that become more apparent with age. These features include a long and narrow face, large ears, a prominent jaw and forehead, unusually flexible fingers, flat feet, and in males, enlarged testicles (macroorchidism) after puberty. Fragile X syndrome occurs in approximately 1 in 4,000 males and 1 in 8,000 females. Mutations in the FMR1 gene cause fragile X syndrome. The FMR1 gene provides instructions for making a protein called FMRP. This protein helps regulate the production of other proteins and plays a role in the development of synapses, which are specialized connections between nerve cells. Synapses are critical for relaying nerve impulses. Nearly all cases of fragile X syndrome are caused by a mutation in which a DNA segment, known as the CGG triplet repeat, is expanded within the FMR1 gene. Normally, this DNA segment is repeated from 5 to about 40 times. In people with fragile X syndrome, however, the CGG segment is repeated more than 200 times. The abnormally expanded CGG segment turns off (silences) the FMR1 gene, which prevents the gene from producing FMRP. Loss or a shortage (deficiency) of this protein disrupts nervous system functions and leads to the signs and symptoms of fragile X syndrome. Males and females with 55 to 200 repeats of the CGG segment are said to have an FMR1 gene premutation. Most people with this premutation are intellectually normal. In some cases, however, individuals with a premutation have lower than normal amounts of FMRP. As a result, they may have mild versions of the physical features seen in fragile X syndrome (such as prominent ears) and may experience emotional problems such as anxiety or depression. Some children with an FMR1 premutation may have learning disabilities or autistic-like behavior. The premutation is also associated with an increased risk of disorders called fragile X-associated primary ovarian insufficiency (FXPOI) and fragile X-associated tremor/ataxia syndrome (FXTAS). Fragile X syndrome is inherited in an X-linked dominant pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. (The Y chromosome is the other sex chromosome.) The inheritance is dominant if one copy of the altered gene in each cell is sufficient to cause the condition. X-linked dominant means that in females (who have two X chromosomes), a mutation in one of the two copies of a gene in each cell is sufficient to cause the disorder. In males (who have only one X chromosome), a mutation in the only copy of a gene in each cell causes the disorder. In most cases, males experience more severe symptoms of the disorder than females. In women, the FMR1 gene premutation on the X chromosome can expand to more than 200 CGG repeats in cells that develop into eggs. This means that women with the premutation have an increased risk of having a child with fragile X syndrome. By contrast, the premutation in men does not expand to more than 200 repeats as it is passed to the next generation. Men pass the premutation only to their daughters. Their sons receive a Y chromosome, which does not include the FMR1 gene. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by fragile X syndrome ? | Fragile X syndrome occurs in approximately 1 in 4,000 males and 1 in 8,000 females. |
Fragile X syndrome is a genetic condition that causes a range of developmental problems including learning disabilities and cognitive impairment. Usually, males are more severely affected by this disorder than females. Affected individuals usually have delayed development of speech and language by age 2. Most males with fragile X syndrome have mild to moderate intellectual disability, while about one-third of affected females are intellectually disabled. Children with fragile X syndrome may also have anxiety and hyperactive behavior such as fidgeting or impulsive actions. They may have attention deficit disorder (ADD), which includes an impaired ability to maintain attention and difficulty focusing on specific tasks. About one-third of individuals with fragile X syndrome have features of autism spectrum disorder that affect communication and social interaction. Seizures occur in about 15 percent of males and about 5 percent of females with fragile X syndrome. Most males and about half of females with fragile X syndrome have characteristic physical features that become more apparent with age. These features include a long and narrow face, large ears, a prominent jaw and forehead, unusually flexible fingers, flat feet, and in males, enlarged testicles (macroorchidism) after puberty. Fragile X syndrome occurs in approximately 1 in 4,000 males and 1 in 8,000 females. Mutations in the FMR1 gene cause fragile X syndrome. The FMR1 gene provides instructions for making a protein called FMRP. This protein helps regulate the production of other proteins and plays a role in the development of synapses, which are specialized connections between nerve cells. Synapses are critical for relaying nerve impulses. Nearly all cases of fragile X syndrome are caused by a mutation in which a DNA segment, known as the CGG triplet repeat, is expanded within the FMR1 gene. Normally, this DNA segment is repeated from 5 to about 40 times. In people with fragile X syndrome, however, the CGG segment is repeated more than 200 times. The abnormally expanded CGG segment turns off (silences) the FMR1 gene, which prevents the gene from producing FMRP. Loss or a shortage (deficiency) of this protein disrupts nervous system functions and leads to the signs and symptoms of fragile X syndrome. Males and females with 55 to 200 repeats of the CGG segment are said to have an FMR1 gene premutation. Most people with this premutation are intellectually normal. In some cases, however, individuals with a premutation have lower than normal amounts of FMRP. As a result, they may have mild versions of the physical features seen in fragile X syndrome (such as prominent ears) and may experience emotional problems such as anxiety or depression. Some children with an FMR1 premutation may have learning disabilities or autistic-like behavior. The premutation is also associated with an increased risk of disorders called fragile X-associated primary ovarian insufficiency (FXPOI) and fragile X-associated tremor/ataxia syndrome (FXTAS). Fragile X syndrome is inherited in an X-linked dominant pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. (The Y chromosome is the other sex chromosome.) The inheritance is dominant if one copy of the altered gene in each cell is sufficient to cause the condition. X-linked dominant means that in females (who have two X chromosomes), a mutation in one of the two copies of a gene in each cell is sufficient to cause the disorder. In males (who have only one X chromosome), a mutation in the only copy of a gene in each cell causes the disorder. In most cases, males experience more severe symptoms of the disorder than females. In women, the FMR1 gene premutation on the X chromosome can expand to more than 200 CGG repeats in cells that develop into eggs. This means that women with the premutation have an increased risk of having a child with fragile X syndrome. By contrast, the premutation in men does not expand to more than 200 repeats as it is passed to the next generation. Men pass the premutation only to their daughters. Their sons receive a Y chromosome, which does not include the FMR1 gene. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to fragile X syndrome ? | Mutations in the FMR1 gene cause fragile X syndrome. The FMR1 gene provides instructions for making a protein called FMRP. This protein helps regulate the production of other proteins and plays a role in the development of synapses, which are specialized connections between nerve cells. Synapses are critical for relaying nerve impulses. Nearly all cases of fragile X syndrome are caused by a mutation in which a DNA segment, known as the CGG triplet repeat, is expanded within the FMR1 gene. Normally, this DNA segment is repeated from 5 to about 40 times. In people with fragile X syndrome, however, the CGG segment is repeated more than 200 times. The abnormally expanded CGG segment turns off (silences) the FMR1 gene, which prevents the gene from producing FMRP. Loss or a shortage (deficiency) of this protein disrupts nervous system functions and leads to the signs and symptoms of fragile X syndrome. Males and females with 55 to 200 repeats of the CGG segment are said to have an FMR1 gene premutation. Most people with a premutation are intellectually normal. In some cases, however, individuals with a premutation have lower than normal amounts of FMRP. As a result, they may have mild versions of the physical features seen in fragile X syndrome (such as prominent ears) and may experience emotional problems such as anxiety or depression. Some children with a premutation may have learning disabilities or autistic-like behavior. The premutation is also associated with an increased risk of disorders called fragile X-associated primary ovarian insufficiency (FXPOI) and fragile X-associated tremor/ataxia syndrome (FXTAS). |
Fragile X syndrome is a genetic condition that causes a range of developmental problems including learning disabilities and cognitive impairment. Usually, males are more severely affected by this disorder than females. Affected individuals usually have delayed development of speech and language by age 2. Most males with fragile X syndrome have mild to moderate intellectual disability, while about one-third of affected females are intellectually disabled. Children with fragile X syndrome may also have anxiety and hyperactive behavior such as fidgeting or impulsive actions. They may have attention deficit disorder (ADD), which includes an impaired ability to maintain attention and difficulty focusing on specific tasks. About one-third of individuals with fragile X syndrome have features of autism spectrum disorder that affect communication and social interaction. Seizures occur in about 15 percent of males and about 5 percent of females with fragile X syndrome. Most males and about half of females with fragile X syndrome have characteristic physical features that become more apparent with age. These features include a long and narrow face, large ears, a prominent jaw and forehead, unusually flexible fingers, flat feet, and in males, enlarged testicles (macroorchidism) after puberty. Fragile X syndrome occurs in approximately 1 in 4,000 males and 1 in 8,000 females. Mutations in the FMR1 gene cause fragile X syndrome. The FMR1 gene provides instructions for making a protein called FMRP. This protein helps regulate the production of other proteins and plays a role in the development of synapses, which are specialized connections between nerve cells. Synapses are critical for relaying nerve impulses. Nearly all cases of fragile X syndrome are caused by a mutation in which a DNA segment, known as the CGG triplet repeat, is expanded within the FMR1 gene. Normally, this DNA segment is repeated from 5 to about 40 times. In people with fragile X syndrome, however, the CGG segment is repeated more than 200 times. The abnormally expanded CGG segment turns off (silences) the FMR1 gene, which prevents the gene from producing FMRP. Loss or a shortage (deficiency) of this protein disrupts nervous system functions and leads to the signs and symptoms of fragile X syndrome. Males and females with 55 to 200 repeats of the CGG segment are said to have an FMR1 gene premutation. Most people with this premutation are intellectually normal. In some cases, however, individuals with a premutation have lower than normal amounts of FMRP. As a result, they may have mild versions of the physical features seen in fragile X syndrome (such as prominent ears) and may experience emotional problems such as anxiety or depression. Some children with an FMR1 premutation may have learning disabilities or autistic-like behavior. The premutation is also associated with an increased risk of disorders called fragile X-associated primary ovarian insufficiency (FXPOI) and fragile X-associated tremor/ataxia syndrome (FXTAS). Fragile X syndrome is inherited in an X-linked dominant pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. (The Y chromosome is the other sex chromosome.) The inheritance is dominant if one copy of the altered gene in each cell is sufficient to cause the condition. X-linked dominant means that in females (who have two X chromosomes), a mutation in one of the two copies of a gene in each cell is sufficient to cause the disorder. In males (who have only one X chromosome), a mutation in the only copy of a gene in each cell causes the disorder. In most cases, males experience more severe symptoms of the disorder than females. In women, the FMR1 gene premutation on the X chromosome can expand to more than 200 CGG repeats in cells that develop into eggs. This means that women with the premutation have an increased risk of having a child with fragile X syndrome. By contrast, the premutation in men does not expand to more than 200 repeats as it is passed to the next generation. Men pass the premutation only to their daughters. Their sons receive a Y chromosome, which does not include the FMR1 gene. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is fragile X syndrome inherited ? | Fragile X syndrome is inherited in an X-linked dominant pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. (The Y chromosome is the other sex chromosome.) The inheritance is dominant if one copy of the altered gene in each cell is sufficient to cause the condition. X-linked dominant means that in females (who have two X chromosomes), a mutation in one of the two copies of a gene in each cell is sufficient to cause the disorder. In males (who have only one X chromosome), a mutation in the only copy of a gene in each cell causes the disorder. In most cases, males experience more severe symptoms of the disorder than females. In women, the FMR1 gene premutation on the X chromosome can expand to more than 200 CGG repeats in cells that develop into eggs. This means that women with the premutation have an increased risk of having a child with fragile X syndrome. By contrast, the premutation in men does not expand to more than 200 repeats as it is passed to the next generation. Men pass the premutation only to their daughters. Their sons receive a Y chromosome, which does not include the FMR1 gene. |
Fragile X syndrome is a genetic condition that causes a range of developmental problems including learning disabilities and cognitive impairment. Usually, males are more severely affected by this disorder than females. Affected individuals usually have delayed development of speech and language by age 2. Most males with fragile X syndrome have mild to moderate intellectual disability, while about one-third of affected females are intellectually disabled. Children with fragile X syndrome may also have anxiety and hyperactive behavior such as fidgeting or impulsive actions. They may have attention deficit disorder (ADD), which includes an impaired ability to maintain attention and difficulty focusing on specific tasks. About one-third of individuals with fragile X syndrome have features of autism spectrum disorder that affect communication and social interaction. Seizures occur in about 15 percent of males and about 5 percent of females with fragile X syndrome. Most males and about half of females with fragile X syndrome have characteristic physical features that become more apparent with age. These features include a long and narrow face, large ears, a prominent jaw and forehead, unusually flexible fingers, flat feet, and in males, enlarged testicles (macroorchidism) after puberty. Fragile X syndrome occurs in approximately 1 in 4,000 males and 1 in 8,000 females. Mutations in the FMR1 gene cause fragile X syndrome. The FMR1 gene provides instructions for making a protein called FMRP. This protein helps regulate the production of other proteins and plays a role in the development of synapses, which are specialized connections between nerve cells. Synapses are critical for relaying nerve impulses. Nearly all cases of fragile X syndrome are caused by a mutation in which a DNA segment, known as the CGG triplet repeat, is expanded within the FMR1 gene. Normally, this DNA segment is repeated from 5 to about 40 times. In people with fragile X syndrome, however, the CGG segment is repeated more than 200 times. The abnormally expanded CGG segment turns off (silences) the FMR1 gene, which prevents the gene from producing FMRP. Loss or a shortage (deficiency) of this protein disrupts nervous system functions and leads to the signs and symptoms of fragile X syndrome. Males and females with 55 to 200 repeats of the CGG segment are said to have an FMR1 gene premutation. Most people with this premutation are intellectually normal. In some cases, however, individuals with a premutation have lower than normal amounts of FMRP. As a result, they may have mild versions of the physical features seen in fragile X syndrome (such as prominent ears) and may experience emotional problems such as anxiety or depression. Some children with an FMR1 premutation may have learning disabilities or autistic-like behavior. The premutation is also associated with an increased risk of disorders called fragile X-associated primary ovarian insufficiency (FXPOI) and fragile X-associated tremor/ataxia syndrome (FXTAS). Fragile X syndrome is inherited in an X-linked dominant pattern. A condition is considered X-linked if the mutated gene that causes the disorder is located on the X chromosome, one of the two sex chromosomes. (The Y chromosome is the other sex chromosome.) The inheritance is dominant if one copy of the altered gene in each cell is sufficient to cause the condition. X-linked dominant means that in females (who have two X chromosomes), a mutation in one of the two copies of a gene in each cell is sufficient to cause the disorder. In males (who have only one X chromosome), a mutation in the only copy of a gene in each cell causes the disorder. In most cases, males experience more severe symptoms of the disorder than females. In women, the FMR1 gene premutation on the X chromosome can expand to more than 200 CGG repeats in cells that develop into eggs. This means that women with the premutation have an increased risk of having a child with fragile X syndrome. By contrast, the premutation in men does not expand to more than 200 repeats as it is passed to the next generation. Men pass the premutation only to their daughters. Their sons receive a Y chromosome, which does not include the FMR1 gene. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for fragile X syndrome ? | These resources address the diagnosis or management of fragile X syndrome: - Gene Review: Gene Review: FMR1-Related Disorders - GeneFacts: Fragile X Syndrome: Diagnosis - GeneFacts: Fragile X Syndrome: Management - Genetic Testing Registry: Fragile X syndrome - MedlinePlus Encyclopedia: Fragile X syndrome These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Or, try one of these pages: If you need help, see our site map or contact us. | What is (are) Langer-Giedion syndrome ? | Langer-Giedion syndrome is a condition that causes bone abnormalities and distinctive facial features. People with this condition have multiple noncancerous (benign) bone tumors called osteochondromas. Multiple osteochondromas may result in pain, limited range of joint movement, and pressure on nerves, blood vessels, the spinal cord, and tissues surrounding the osteochondromas. Affected individuals also have short stature and cone-shaped ends of the long bones (epiphyses). The characteristic appearance of individuals with Langer-Giedion syndrome includes sparse scalp hair, a rounded nose, a long flat area between the nose and the upper lip (philtrum), and a thin upper lip. Some people with this condition have loose skin in childhood, which typically resolves with age. Affected individuals may have some intellectual disability. |
Or, try one of these pages: If you need help, see our site map or contact us. | How many people are affected by Langer-Giedion syndrome ? | Langer-Giedion syndrome is a rare condition; its incidence is unknown. |
Or, try one of these pages: If you need help, see our site map or contact us. | What are the genetic changes related to Langer-Giedion syndrome ? | Langer-Giedion syndrome is caused by the deletion or mutation of at least two genes on chromosome 8. Researchers have determined that the loss of a functional EXT1 gene is responsible for the multiple osteochondromas seen in people with Langer-Giedion syndrome. Loss of a functional TRPS1 gene may cause the other bone and facial abnormalities. The EXT1 gene and the TRPS1 gene are always missing or mutated in affected individuals, but other neighboring genes may also be involved. The loss of additional genes from this region of chromosome 8 likely contributes to the varied features of this condition. Langer-Giedion syndrome is often described as a contiguous gene deletion syndrome because it results from the loss of several neighboring genes. |
Or, try one of these pages: If you need help, see our site map or contact us. | Is Langer-Giedion syndrome inherited ? | Most cases of Langer-Giedion syndrome are not inherited, but occur as random events during the formation of reproductive cells (eggs or sperm) in a parent of an affected individual. These cases occur in people with no history of the disorder in their family. There have been very few instances in which people with Langer-Giedion syndrome have inherited the chromosomal deletion from a parent with the condition. Langer-Giedion syndrome is considered an autosomal dominant condition because one copy of the altered chromosome 8 in each cell is sufficient to cause the disorder. |
Or, try one of these pages: If you need help, see our site map or contact us. | What are the treatments for Langer-Giedion syndrome ? | These resources address the diagnosis or management of Langer-Giedion syndrome: - Genetic Testing Registry: Langer-Giedion syndrome These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Fanconi anemia is a condition that affects many parts of the body. People with this condition may have bone marrow failure, physical abnormalities, organ defects, and an increased risk of certain cancers. The major function of bone marrow is to produce new blood cells. These include red blood cells, which carry oxygen to the body's tissues; white blood cells, which fight infections; and platelets, which are necessary for normal blood clotting. Approximately 90 percent of people with Fanconi anemia have impaired bone marrow function that leads to a decrease in the production of all blood cells (aplastic anemia). Affected individuals experience extreme tiredness (fatigue) due to low numbers of red blood cells (anemia), frequent infections due to low numbers of white blood cells (neutropenia), and clotting problems due to low numbers of platelets (thrombocytopenia). People with Fanconi anemia may also develop myelodysplastic syndrome, a condition in which immature blood cells fail to develop normally. More than half of people with Fanconi anemia have physical abnormalities. These abnormalities can involve irregular skin coloring such as unusually light-colored skin (hypopigmentation) or café-au-lait spots, which are flat patches on the skin that are darker than the surrounding area. Other possible symptoms of Fanconi anemia include malformed thumbs or forearms and other skeletal problems including short stature; malformed or absent kidneys and other defects of the urinary tract; gastrointestinal abnormalities; heart defects; eye abnormalities such as small or abnormally shaped eyes; and malformed ears and hearing loss. People with this condition may have abnormal genitalia or malformations of the reproductive system. As a result, most affected males and about half of affected females cannot have biological children (are infertile). Additional signs and symptoms can include abnormalities of the brain and spinal cord (central nervous system), including increased fluid in the center of the brain (hydrocephalus) or an unusually small head size (microcephaly). Individuals with Fanconi anemia have an increased risk of developing a cancer of blood-forming cells in the bone marrow called acute myeloid leukemia (AML) or tumors of the head, neck, skin, gastrointestinal system, or genital tract. The likelihood of developing one of these cancers in people with Fanconi anemia is between 10 and 30 percent. Fanconi anemia occurs in 1 in 160,000 individuals worldwide. This condition is more common among people of Ashkenazi Jewish descent, the Roma population of Spain, and Black South Africans. Mutations in at least 15 genes can cause Fanconi anemia. Proteins produced from these genes are involved in a cell process known as the FA pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway sends certain proteins to the area of damage, which trigger DNA repair so DNA replication can continue. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. Eight proteins associated with Fanconi anemia group together to form a complex known as the FA core complex. The FA core complex activates two proteins, called FANCD2 and FANCI. The activation of these two proteins brings DNA repair proteins to the area of the ICL so the cross-link can be removed and DNA replication can continue. Eighty to 90 percent of cases of Fanconi anemia are due to mutations in one of three genes, FANCA, FANCC, and FANCG. These genes provide instructions for producing components of the FA core complex. Mutations in any of the many genes associated with the FA core complex will cause the complex to be nonfunctional and disrupt the entire FA pathway. As a result, DNA damage is not repaired efficiently and ICLs build up over time. The ICLs stall DNA replication, ultimately resulting in either abnormal cell death due to an inability make new DNA molecules or uncontrolled cell growth due to a lack of DNA repair processes. Cells that divide quickly, such as bone marrow cells and cells of the developing fetus, are particularly affected. The death of these cells results in the decrease in blood cells and the physical abnormalities characteristic of Fanconi anemia. When the buildup of errors in DNA leads to uncontrolled cell growth, affected individuals can develop acute myeloid leukemia or other cancers. Additional Information from NCBI Gene: Fanconi anemia is most often inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Very rarely, this condition is inherited in an X-linked recessive pattern. The gene associated with X-linked recessive Fanconi anemia is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) Fanconi anemia ? | Fanconi anemia is a condition that affects many parts of the body. People with this condition may have bone marrow failure, physical abnormalities, organ defects, and an increased risk of certain cancers. The major function of bone marrow is to produce new blood cells. These include red blood cells, which carry oxygen to the body's tissues; white blood cells, which fight infections; and platelets, which are necessary for normal blood clotting. Approximately 90 percent of people with Fanconi anemia have impaired bone marrow function that leads to a decrease in the production of all blood cells (aplastic anemia). Affected individuals experience extreme tiredness (fatigue) due to low numbers of red blood cells (anemia), frequent infections due to low numbers of white blood cells (neutropenia), and clotting problems due to low numbers of platelets (thrombocytopenia). People with Fanconi anemia may also develop myelodysplastic syndrome, a condition in which immature blood cells fail to develop normally. More than half of people with Fanconi anemia have physical abnormalities. These abnormalities can involve irregular skin coloring such as unusually light-colored skin (hypopigmentation) or caf-au-lait spots, which are flat patches on the skin that are darker than the surrounding area. Other possible symptoms of Fanconi anemia include malformed thumbs or forearms and other skeletal problems including short stature; malformed or absent kidneys and other defects of the urinary tract; gastrointestinal abnormalities; heart defects; eye abnormalities such as small or abnormally shaped eyes; and malformed ears and hearing loss. People with this condition may have abnormal genitalia or malformations of the reproductive system. As a result, most affected males and about half of affected females cannot have biological children (are infertile). Additional signs and symptoms can include abnormalities of the brain and spinal cord (central nervous system), including increased fluid in the center of the brain (hydrocephalus) or an unusually small head size (microcephaly). Individuals with Fanconi anemia have an increased risk of developing a cancer of blood-forming cells in the bone marrow called acute myeloid leukemia (AML) or tumors of the head, neck, skin, gastrointestinal system, or genital tract. The likelihood of developing one of these cancers in people with Fanconi anemia is between 10 and 30 percent. |
Fanconi anemia is a condition that affects many parts of the body. People with this condition may have bone marrow failure, physical abnormalities, organ defects, and an increased risk of certain cancers. The major function of bone marrow is to produce new blood cells. These include red blood cells, which carry oxygen to the body's tissues; white blood cells, which fight infections; and platelets, which are necessary for normal blood clotting. Approximately 90 percent of people with Fanconi anemia have impaired bone marrow function that leads to a decrease in the production of all blood cells (aplastic anemia). Affected individuals experience extreme tiredness (fatigue) due to low numbers of red blood cells (anemia), frequent infections due to low numbers of white blood cells (neutropenia), and clotting problems due to low numbers of platelets (thrombocytopenia). People with Fanconi anemia may also develop myelodysplastic syndrome, a condition in which immature blood cells fail to develop normally. More than half of people with Fanconi anemia have physical abnormalities. These abnormalities can involve irregular skin coloring such as unusually light-colored skin (hypopigmentation) or café-au-lait spots, which are flat patches on the skin that are darker than the surrounding area. Other possible symptoms of Fanconi anemia include malformed thumbs or forearms and other skeletal problems including short stature; malformed or absent kidneys and other defects of the urinary tract; gastrointestinal abnormalities; heart defects; eye abnormalities such as small or abnormally shaped eyes; and malformed ears and hearing loss. People with this condition may have abnormal genitalia or malformations of the reproductive system. As a result, most affected males and about half of affected females cannot have biological children (are infertile). Additional signs and symptoms can include abnormalities of the brain and spinal cord (central nervous system), including increased fluid in the center of the brain (hydrocephalus) or an unusually small head size (microcephaly). Individuals with Fanconi anemia have an increased risk of developing a cancer of blood-forming cells in the bone marrow called acute myeloid leukemia (AML) or tumors of the head, neck, skin, gastrointestinal system, or genital tract. The likelihood of developing one of these cancers in people with Fanconi anemia is between 10 and 30 percent. Fanconi anemia occurs in 1 in 160,000 individuals worldwide. This condition is more common among people of Ashkenazi Jewish descent, the Roma population of Spain, and Black South Africans. Mutations in at least 15 genes can cause Fanconi anemia. Proteins produced from these genes are involved in a cell process known as the FA pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway sends certain proteins to the area of damage, which trigger DNA repair so DNA replication can continue. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. Eight proteins associated with Fanconi anemia group together to form a complex known as the FA core complex. The FA core complex activates two proteins, called FANCD2 and FANCI. The activation of these two proteins brings DNA repair proteins to the area of the ICL so the cross-link can be removed and DNA replication can continue. Eighty to 90 percent of cases of Fanconi anemia are due to mutations in one of three genes, FANCA, FANCC, and FANCG. These genes provide instructions for producing components of the FA core complex. Mutations in any of the many genes associated with the FA core complex will cause the complex to be nonfunctional and disrupt the entire FA pathway. As a result, DNA damage is not repaired efficiently and ICLs build up over time. The ICLs stall DNA replication, ultimately resulting in either abnormal cell death due to an inability make new DNA molecules or uncontrolled cell growth due to a lack of DNA repair processes. Cells that divide quickly, such as bone marrow cells and cells of the developing fetus, are particularly affected. The death of these cells results in the decrease in blood cells and the physical abnormalities characteristic of Fanconi anemia. When the buildup of errors in DNA leads to uncontrolled cell growth, affected individuals can develop acute myeloid leukemia or other cancers. Additional Information from NCBI Gene: Fanconi anemia is most often inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Very rarely, this condition is inherited in an X-linked recessive pattern. The gene associated with X-linked recessive Fanconi anemia is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by Fanconi anemia ? | Fanconi anemia occurs in 1 in 160,000 individuals worldwide. This condition is more common among people of Ashkenazi Jewish descent, the Roma population of Spain, and black South Africans. |
Fanconi anemia is a condition that affects many parts of the body. People with this condition may have bone marrow failure, physical abnormalities, organ defects, and an increased risk of certain cancers. The major function of bone marrow is to produce new blood cells. These include red blood cells, which carry oxygen to the body's tissues; white blood cells, which fight infections; and platelets, which are necessary for normal blood clotting. Approximately 90 percent of people with Fanconi anemia have impaired bone marrow function that leads to a decrease in the production of all blood cells (aplastic anemia). Affected individuals experience extreme tiredness (fatigue) due to low numbers of red blood cells (anemia), frequent infections due to low numbers of white blood cells (neutropenia), and clotting problems due to low numbers of platelets (thrombocytopenia). People with Fanconi anemia may also develop myelodysplastic syndrome, a condition in which immature blood cells fail to develop normally. More than half of people with Fanconi anemia have physical abnormalities. These abnormalities can involve irregular skin coloring such as unusually light-colored skin (hypopigmentation) or café-au-lait spots, which are flat patches on the skin that are darker than the surrounding area. Other possible symptoms of Fanconi anemia include malformed thumbs or forearms and other skeletal problems including short stature; malformed or absent kidneys and other defects of the urinary tract; gastrointestinal abnormalities; heart defects; eye abnormalities such as small or abnormally shaped eyes; and malformed ears and hearing loss. People with this condition may have abnormal genitalia or malformations of the reproductive system. As a result, most affected males and about half of affected females cannot have biological children (are infertile). Additional signs and symptoms can include abnormalities of the brain and spinal cord (central nervous system), including increased fluid in the center of the brain (hydrocephalus) or an unusually small head size (microcephaly). Individuals with Fanconi anemia have an increased risk of developing a cancer of blood-forming cells in the bone marrow called acute myeloid leukemia (AML) or tumors of the head, neck, skin, gastrointestinal system, or genital tract. The likelihood of developing one of these cancers in people with Fanconi anemia is between 10 and 30 percent. Fanconi anemia occurs in 1 in 160,000 individuals worldwide. This condition is more common among people of Ashkenazi Jewish descent, the Roma population of Spain, and Black South Africans. Mutations in at least 15 genes can cause Fanconi anemia. Proteins produced from these genes are involved in a cell process known as the FA pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway sends certain proteins to the area of damage, which trigger DNA repair so DNA replication can continue. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. Eight proteins associated with Fanconi anemia group together to form a complex known as the FA core complex. The FA core complex activates two proteins, called FANCD2 and FANCI. The activation of these two proteins brings DNA repair proteins to the area of the ICL so the cross-link can be removed and DNA replication can continue. Eighty to 90 percent of cases of Fanconi anemia are due to mutations in one of three genes, FANCA, FANCC, and FANCG. These genes provide instructions for producing components of the FA core complex. Mutations in any of the many genes associated with the FA core complex will cause the complex to be nonfunctional and disrupt the entire FA pathway. As a result, DNA damage is not repaired efficiently and ICLs build up over time. The ICLs stall DNA replication, ultimately resulting in either abnormal cell death due to an inability make new DNA molecules or uncontrolled cell growth due to a lack of DNA repair processes. Cells that divide quickly, such as bone marrow cells and cells of the developing fetus, are particularly affected. The death of these cells results in the decrease in blood cells and the physical abnormalities characteristic of Fanconi anemia. When the buildup of errors in DNA leads to uncontrolled cell growth, affected individuals can develop acute myeloid leukemia or other cancers. Additional Information from NCBI Gene: Fanconi anemia is most often inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Very rarely, this condition is inherited in an X-linked recessive pattern. The gene associated with X-linked recessive Fanconi anemia is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to Fanconi anemia ? | Mutations in at least 15 genes can cause Fanconi anemia. Proteins produced from these genes are involved in a cell process known as the FA pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway sends certain proteins to the area of damage, which trigger DNA repair so DNA replication can continue. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. Eight proteins associated with Fanconi anemia group together to form a complex known as the FA core complex. The FA core complex activates two proteins, called FANCD2 and FANCI. The activation of these two proteins brings DNA repair proteins to the area of the ICL so the cross-link can be removed and DNA replication can continue. Eighty to 90 percent of cases of Fanconi anemia are due to mutations in one of three genes, FANCA, FANCC, and FANCG. These genes provide instructions for producing components of the FA core complex. Mutations in any of the many genes associated with the FA core complex will cause the complex to be nonfunctional and disrupt the entire FA pathway. As a result, DNA damage is not repaired efficiently and ICLs build up over time. The ICLs stall DNA replication, ultimately resulting in either abnormal cell death due to an inability make new DNA molecules or uncontrolled cell growth due to a lack of DNA repair processes. Cells that divide quickly, such as bone marrow cells and cells of the developing fetus, are particularly affected. The death of these cells results in the decrease in blood cells and the physical abnormalities characteristic of Fanconi anemia. When the buildup of errors in DNA leads to uncontrolled cell growth, affected individuals can develop acute myeloid leukemia or other cancers. |
Fanconi anemia is a condition that affects many parts of the body. People with this condition may have bone marrow failure, physical abnormalities, organ defects, and an increased risk of certain cancers. The major function of bone marrow is to produce new blood cells. These include red blood cells, which carry oxygen to the body's tissues; white blood cells, which fight infections; and platelets, which are necessary for normal blood clotting. Approximately 90 percent of people with Fanconi anemia have impaired bone marrow function that leads to a decrease in the production of all blood cells (aplastic anemia). Affected individuals experience extreme tiredness (fatigue) due to low numbers of red blood cells (anemia), frequent infections due to low numbers of white blood cells (neutropenia), and clotting problems due to low numbers of platelets (thrombocytopenia). People with Fanconi anemia may also develop myelodysplastic syndrome, a condition in which immature blood cells fail to develop normally. More than half of people with Fanconi anemia have physical abnormalities. These abnormalities can involve irregular skin coloring such as unusually light-colored skin (hypopigmentation) or café-au-lait spots, which are flat patches on the skin that are darker than the surrounding area. Other possible symptoms of Fanconi anemia include malformed thumbs or forearms and other skeletal problems including short stature; malformed or absent kidneys and other defects of the urinary tract; gastrointestinal abnormalities; heart defects; eye abnormalities such as small or abnormally shaped eyes; and malformed ears and hearing loss. People with this condition may have abnormal genitalia or malformations of the reproductive system. As a result, most affected males and about half of affected females cannot have biological children (are infertile). Additional signs and symptoms can include abnormalities of the brain and spinal cord (central nervous system), including increased fluid in the center of the brain (hydrocephalus) or an unusually small head size (microcephaly). Individuals with Fanconi anemia have an increased risk of developing a cancer of blood-forming cells in the bone marrow called acute myeloid leukemia (AML) or tumors of the head, neck, skin, gastrointestinal system, or genital tract. The likelihood of developing one of these cancers in people with Fanconi anemia is between 10 and 30 percent. Fanconi anemia occurs in 1 in 160,000 individuals worldwide. This condition is more common among people of Ashkenazi Jewish descent, the Roma population of Spain, and Black South Africans. Mutations in at least 15 genes can cause Fanconi anemia. Proteins produced from these genes are involved in a cell process known as the FA pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway sends certain proteins to the area of damage, which trigger DNA repair so DNA replication can continue. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. Eight proteins associated with Fanconi anemia group together to form a complex known as the FA core complex. The FA core complex activates two proteins, called FANCD2 and FANCI. The activation of these two proteins brings DNA repair proteins to the area of the ICL so the cross-link can be removed and DNA replication can continue. Eighty to 90 percent of cases of Fanconi anemia are due to mutations in one of three genes, FANCA, FANCC, and FANCG. These genes provide instructions for producing components of the FA core complex. Mutations in any of the many genes associated with the FA core complex will cause the complex to be nonfunctional and disrupt the entire FA pathway. As a result, DNA damage is not repaired efficiently and ICLs build up over time. The ICLs stall DNA replication, ultimately resulting in either abnormal cell death due to an inability make new DNA molecules or uncontrolled cell growth due to a lack of DNA repair processes. Cells that divide quickly, such as bone marrow cells and cells of the developing fetus, are particularly affected. The death of these cells results in the decrease in blood cells and the physical abnormalities characteristic of Fanconi anemia. When the buildup of errors in DNA leads to uncontrolled cell growth, affected individuals can develop acute myeloid leukemia or other cancers. Additional Information from NCBI Gene: Fanconi anemia is most often inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Very rarely, this condition is inherited in an X-linked recessive pattern. The gene associated with X-linked recessive Fanconi anemia is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is Fanconi anemia inherited ? | Fanconi anemia is most often inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Very rarely, this condition is inherited in an X-linked recessive pattern. The gene associated with X-linked recessive Fanconi anemia is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. |
Fanconi anemia is a condition that affects many parts of the body. People with this condition may have bone marrow failure, physical abnormalities, organ defects, and an increased risk of certain cancers. The major function of bone marrow is to produce new blood cells. These include red blood cells, which carry oxygen to the body's tissues; white blood cells, which fight infections; and platelets, which are necessary for normal blood clotting. Approximately 90 percent of people with Fanconi anemia have impaired bone marrow function that leads to a decrease in the production of all blood cells (aplastic anemia). Affected individuals experience extreme tiredness (fatigue) due to low numbers of red blood cells (anemia), frequent infections due to low numbers of white blood cells (neutropenia), and clotting problems due to low numbers of platelets (thrombocytopenia). People with Fanconi anemia may also develop myelodysplastic syndrome, a condition in which immature blood cells fail to develop normally. More than half of people with Fanconi anemia have physical abnormalities. These abnormalities can involve irregular skin coloring such as unusually light-colored skin (hypopigmentation) or café-au-lait spots, which are flat patches on the skin that are darker than the surrounding area. Other possible symptoms of Fanconi anemia include malformed thumbs or forearms and other skeletal problems including short stature; malformed or absent kidneys and other defects of the urinary tract; gastrointestinal abnormalities; heart defects; eye abnormalities such as small or abnormally shaped eyes; and malformed ears and hearing loss. People with this condition may have abnormal genitalia or malformations of the reproductive system. As a result, most affected males and about half of affected females cannot have biological children (are infertile). Additional signs and symptoms can include abnormalities of the brain and spinal cord (central nervous system), including increased fluid in the center of the brain (hydrocephalus) or an unusually small head size (microcephaly). Individuals with Fanconi anemia have an increased risk of developing a cancer of blood-forming cells in the bone marrow called acute myeloid leukemia (AML) or tumors of the head, neck, skin, gastrointestinal system, or genital tract. The likelihood of developing one of these cancers in people with Fanconi anemia is between 10 and 30 percent. Fanconi anemia occurs in 1 in 160,000 individuals worldwide. This condition is more common among people of Ashkenazi Jewish descent, the Roma population of Spain, and Black South Africans. Mutations in at least 15 genes can cause Fanconi anemia. Proteins produced from these genes are involved in a cell process known as the FA pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway sends certain proteins to the area of damage, which trigger DNA repair so DNA replication can continue. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. Eight proteins associated with Fanconi anemia group together to form a complex known as the FA core complex. The FA core complex activates two proteins, called FANCD2 and FANCI. The activation of these two proteins brings DNA repair proteins to the area of the ICL so the cross-link can be removed and DNA replication can continue. Eighty to 90 percent of cases of Fanconi anemia are due to mutations in one of three genes, FANCA, FANCC, and FANCG. These genes provide instructions for producing components of the FA core complex. Mutations in any of the many genes associated with the FA core complex will cause the complex to be nonfunctional and disrupt the entire FA pathway. As a result, DNA damage is not repaired efficiently and ICLs build up over time. The ICLs stall DNA replication, ultimately resulting in either abnormal cell death due to an inability make new DNA molecules or uncontrolled cell growth due to a lack of DNA repair processes. Cells that divide quickly, such as bone marrow cells and cells of the developing fetus, are particularly affected. The death of these cells results in the decrease in blood cells and the physical abnormalities characteristic of Fanconi anemia. When the buildup of errors in DNA leads to uncontrolled cell growth, affected individuals can develop acute myeloid leukemia or other cancers. Additional Information from NCBI Gene: Fanconi anemia is most often inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Very rarely, this condition is inherited in an X-linked recessive pattern. The gene associated with X-linked recessive Fanconi anemia is located on the X chromosome, which is one of the two sex chromosomes. In males (who have only one X chromosome), one altered copy of the gene in each cell is sufficient to cause the condition. In females (who have two X chromosomes), a mutation would have to occur in both copies of the gene to cause the disorder. Because it is unlikely that females will have two altered copies of this gene, males are affected by X-linked recessive disorders much more frequently than females. A characteristic of X-linked inheritance is that fathers cannot pass X-linked traits to their sons. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for Fanconi anemia ? | These resources address the diagnosis or management of Fanconi anemia: - Cincinnati Children's Hospital: Fanconi Anemia Comprehensive Care Center - Fanconi Anemia Research Fund: Fanconi Anemia Guidelines for Diagnosis and Management - Gene Review: Gene Review: Fanconi Anemia - Genetic Testing Registry: Fanconi anemia - Genetic Testing Registry: Fanconi anemia, complementation group A - Genetic Testing Registry: Fanconi anemia, complementation group B - Genetic Testing Registry: Fanconi anemia, complementation group C - Genetic Testing Registry: Fanconi anemia, complementation group D1 - Genetic Testing Registry: Fanconi anemia, complementation group D2 - Genetic Testing Registry: Fanconi anemia, complementation group E - Genetic Testing Registry: Fanconi anemia, complementation group F - Genetic Testing Registry: Fanconi anemia, complementation group G - Genetic Testing Registry: Fanconi anemia, complementation group I - Genetic Testing Registry: Fanconi anemia, complementation group J - Genetic Testing Registry: Fanconi anemia, complementation group L - Genetic Testing Registry: Fanconi anemia, complementation group M - Genetic Testing Registry: Fanconi anemia, complementation group N - Genetic Testing Registry: Fanconi anemia, complementation group O - Genetic Testing Registry: Fanconi anemia, complementation group P - MedlinePlus Encyclopedia: Fanconi's Anemia - National Cancer Institute: Adult Acute Myeloid Leukemia Treatment PDQ - National Cancer Institute: Myelodysplastic Syndromes Treatment PDQ - National Heart Lung and Blood Institute: How is Fanconi Anemia Treated? - The Rockefeller University: International Fanconi Anemia Registry These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Supravalvular aortic stenosis (SVAS) is a heart defect that develops before birth. This defect is a narrowing (stenosis) of the large blood vessel that carries blood from the heart to the rest of the body (the aorta). The condition is described as supravalvular because the section of the aorta that is narrowed is located just above the valve that connects the aorta with the heart (the aortic valve). Some people with SVAS also have defects in other blood vessels, most commonly stenosis of the artery from the heart to the lungs (the pulmonary artery). An abnormal heart sound during a heartbeat (heart murmur) can often be heard during a chest exam. If SVAS is not treated, the aortic narrowing can lead to shortness of breath, chest pain, and ultimately heart failure. The severity of SVAS varies considerably, even among family members. Some affected individuals die in infancy, while others never experience symptoms of the disorder. SVAS occurs in 1 in 20,000 newborns worldwide. Mutations in the ELN gene cause SVAS. The ELN gene provides instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are slender bundles of proteins that provide strength and flexibility to connective tissue (tissue that supports the body's joints and organs). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix), where they give structural support to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. Elastic fibers make up approximately 50 percent of the aorta, the rest being primarily muscle cells called vascular smooth muscle cells that line the aorta. Together, elastic fibers and vascular smooth muscle cells provide flexibility and resilience to the aorta. Most of the ELN gene mutations that cause SVAS lead to a decrease in the production of tropoelastin. A shortage of tropoelastin reduces the amount of mature elastin protein that is processed and available for forming elastic fibers. As a result, elastic fibers that make up the aorta are thinner than normal. To compensate, the smooth muscle cells that line the aorta increase in number, making the aorta thicker and narrower than usual. A thickened aorta is less flexible and resilient to the stress of constant blood flow and pumping of the heart. Over time, the wall of the aorta can become damaged. Aortic narrowing causes the heart to work harder to pump blood through the aorta, resulting in the signs and symptoms of SVAS. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. However, some people who inherit the altered gene never develop features of SVAS. (This situation is known as reduced penetrance.) In some cases, a person inherits the mutation from one parent who has the mutation. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) supravalvular aortic stenosis ? | Supravalvular aortic stenosis (SVAS) is a heart defect that develops before birth. This defect is a narrowing (stenosis) of the large blood vessel that carries blood from the heart to the rest of the body (the aorta). The condition is described as supravalvular because the section of the aorta that is narrowed is located just above the valve that connects the aorta with the heart (the aortic valve). Some people with SVAS also have defects in other blood vessels, most commonly stenosis of the artery from the heart to the lungs (the pulmonary artery). An abnormal heart sound during a heartbeat (heart murmur) can often be heard during a chest exam. If SVAS is not treated, the aortic narrowing can lead to shortness of breath, chest pain, and ultimately heart failure. The severity of SVAS varies considerably, even among family members. Some affected individuals die in infancy, while others never experience symptoms of the disorder. |
Supravalvular aortic stenosis (SVAS) is a heart defect that develops before birth. This defect is a narrowing (stenosis) of the large blood vessel that carries blood from the heart to the rest of the body (the aorta). The condition is described as supravalvular because the section of the aorta that is narrowed is located just above the valve that connects the aorta with the heart (the aortic valve). Some people with SVAS also have defects in other blood vessels, most commonly stenosis of the artery from the heart to the lungs (the pulmonary artery). An abnormal heart sound during a heartbeat (heart murmur) can often be heard during a chest exam. If SVAS is not treated, the aortic narrowing can lead to shortness of breath, chest pain, and ultimately heart failure. The severity of SVAS varies considerably, even among family members. Some affected individuals die in infancy, while others never experience symptoms of the disorder. SVAS occurs in 1 in 20,000 newborns worldwide. Mutations in the ELN gene cause SVAS. The ELN gene provides instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are slender bundles of proteins that provide strength and flexibility to connective tissue (tissue that supports the body's joints and organs). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix), where they give structural support to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. Elastic fibers make up approximately 50 percent of the aorta, the rest being primarily muscle cells called vascular smooth muscle cells that line the aorta. Together, elastic fibers and vascular smooth muscle cells provide flexibility and resilience to the aorta. Most of the ELN gene mutations that cause SVAS lead to a decrease in the production of tropoelastin. A shortage of tropoelastin reduces the amount of mature elastin protein that is processed and available for forming elastic fibers. As a result, elastic fibers that make up the aorta are thinner than normal. To compensate, the smooth muscle cells that line the aorta increase in number, making the aorta thicker and narrower than usual. A thickened aorta is less flexible and resilient to the stress of constant blood flow and pumping of the heart. Over time, the wall of the aorta can become damaged. Aortic narrowing causes the heart to work harder to pump blood through the aorta, resulting in the signs and symptoms of SVAS. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. However, some people who inherit the altered gene never develop features of SVAS. (This situation is known as reduced penetrance.) In some cases, a person inherits the mutation from one parent who has the mutation. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by supravalvular aortic stenosis ? | SVAS occurs in 1 in 20,000 newborns worldwide. |
Supravalvular aortic stenosis (SVAS) is a heart defect that develops before birth. This defect is a narrowing (stenosis) of the large blood vessel that carries blood from the heart to the rest of the body (the aorta). The condition is described as supravalvular because the section of the aorta that is narrowed is located just above the valve that connects the aorta with the heart (the aortic valve). Some people with SVAS also have defects in other blood vessels, most commonly stenosis of the artery from the heart to the lungs (the pulmonary artery). An abnormal heart sound during a heartbeat (heart murmur) can often be heard during a chest exam. If SVAS is not treated, the aortic narrowing can lead to shortness of breath, chest pain, and ultimately heart failure. The severity of SVAS varies considerably, even among family members. Some affected individuals die in infancy, while others never experience symptoms of the disorder. SVAS occurs in 1 in 20,000 newborns worldwide. Mutations in the ELN gene cause SVAS. The ELN gene provides instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are slender bundles of proteins that provide strength and flexibility to connective tissue (tissue that supports the body's joints and organs). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix), where they give structural support to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. Elastic fibers make up approximately 50 percent of the aorta, the rest being primarily muscle cells called vascular smooth muscle cells that line the aorta. Together, elastic fibers and vascular smooth muscle cells provide flexibility and resilience to the aorta. Most of the ELN gene mutations that cause SVAS lead to a decrease in the production of tropoelastin. A shortage of tropoelastin reduces the amount of mature elastin protein that is processed and available for forming elastic fibers. As a result, elastic fibers that make up the aorta are thinner than normal. To compensate, the smooth muscle cells that line the aorta increase in number, making the aorta thicker and narrower than usual. A thickened aorta is less flexible and resilient to the stress of constant blood flow and pumping of the heart. Over time, the wall of the aorta can become damaged. Aortic narrowing causes the heart to work harder to pump blood through the aorta, resulting in the signs and symptoms of SVAS. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. However, some people who inherit the altered gene never develop features of SVAS. (This situation is known as reduced penetrance.) In some cases, a person inherits the mutation from one parent who has the mutation. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to supravalvular aortic stenosis ? | Mutations in the ELN gene cause SVAS. The ELN gene provides instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are slender bundles of proteins that provide strength and flexibility to connective tissue (tissue that supports the body's joints and organs). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix), where they give structural support to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. Elastic fibers make up approximately 50 percent of the aorta, the rest being primarily muscle cells called vascular smooth muscle cells that line the aorta. Together, elastic fibers and vascular smooth muscle cells provide flexibility and resilience to the aorta. Most of the ELN gene mutations that cause SVAS lead to a decrease in the production of tropoelastin. A shortage of tropoelastin reduces the amount of mature elastin protein that is processed and available for forming elastic fibers. As a result, elastic fibers that make up the aorta are thinner than normal. To compensate, the smooth muscle cells that line the aorta increase in number, making the aorta thicker and narrower than usual. A thickened aorta is less flexible and resilient to the stress of constant blood flow and pumping of the heart. Over time, the wall of the aorta can become damaged. Aortic narrowing causes the heart to work harder to pump blood through the aorta, resulting in the signs and symptoms of SVAS. |
Supravalvular aortic stenosis (SVAS) is a heart defect that develops before birth. This defect is a narrowing (stenosis) of the large blood vessel that carries blood from the heart to the rest of the body (the aorta). The condition is described as supravalvular because the section of the aorta that is narrowed is located just above the valve that connects the aorta with the heart (the aortic valve). Some people with SVAS also have defects in other blood vessels, most commonly stenosis of the artery from the heart to the lungs (the pulmonary artery). An abnormal heart sound during a heartbeat (heart murmur) can often be heard during a chest exam. If SVAS is not treated, the aortic narrowing can lead to shortness of breath, chest pain, and ultimately heart failure. The severity of SVAS varies considerably, even among family members. Some affected individuals die in infancy, while others never experience symptoms of the disorder. SVAS occurs in 1 in 20,000 newborns worldwide. Mutations in the ELN gene cause SVAS. The ELN gene provides instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are slender bundles of proteins that provide strength and flexibility to connective tissue (tissue that supports the body's joints and organs). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix), where they give structural support to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. Elastic fibers make up approximately 50 percent of the aorta, the rest being primarily muscle cells called vascular smooth muscle cells that line the aorta. Together, elastic fibers and vascular smooth muscle cells provide flexibility and resilience to the aorta. Most of the ELN gene mutations that cause SVAS lead to a decrease in the production of tropoelastin. A shortage of tropoelastin reduces the amount of mature elastin protein that is processed and available for forming elastic fibers. As a result, elastic fibers that make up the aorta are thinner than normal. To compensate, the smooth muscle cells that line the aorta increase in number, making the aorta thicker and narrower than usual. A thickened aorta is less flexible and resilient to the stress of constant blood flow and pumping of the heart. Over time, the wall of the aorta can become damaged. Aortic narrowing causes the heart to work harder to pump blood through the aorta, resulting in the signs and symptoms of SVAS. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. However, some people who inherit the altered gene never develop features of SVAS. (This situation is known as reduced penetrance.) In some cases, a person inherits the mutation from one parent who has the mutation. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is supravalvular aortic stenosis inherited ? | This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. However, some people who inherit the altered gene never develop features of SVAS. (This situation is known as reduced penetrance.) In some cases, a person inherits the mutation from one parent who has the mutation. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. |
Supravalvular aortic stenosis (SVAS) is a heart defect that develops before birth. This defect is a narrowing (stenosis) of the large blood vessel that carries blood from the heart to the rest of the body (the aorta). The condition is described as supravalvular because the section of the aorta that is narrowed is located just above the valve that connects the aorta with the heart (the aortic valve). Some people with SVAS also have defects in other blood vessels, most commonly stenosis of the artery from the heart to the lungs (the pulmonary artery). An abnormal heart sound during a heartbeat (heart murmur) can often be heard during a chest exam. If SVAS is not treated, the aortic narrowing can lead to shortness of breath, chest pain, and ultimately heart failure. The severity of SVAS varies considerably, even among family members. Some affected individuals die in infancy, while others never experience symptoms of the disorder. SVAS occurs in 1 in 20,000 newborns worldwide. Mutations in the ELN gene cause SVAS. The ELN gene provides instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are slender bundles of proteins that provide strength and flexibility to connective tissue (tissue that supports the body's joints and organs). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix), where they give structural support to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. Elastic fibers make up approximately 50 percent of the aorta, the rest being primarily muscle cells called vascular smooth muscle cells that line the aorta. Together, elastic fibers and vascular smooth muscle cells provide flexibility and resilience to the aorta. Most of the ELN gene mutations that cause SVAS lead to a decrease in the production of tropoelastin. A shortage of tropoelastin reduces the amount of mature elastin protein that is processed and available for forming elastic fibers. As a result, elastic fibers that make up the aorta are thinner than normal. To compensate, the smooth muscle cells that line the aorta increase in number, making the aorta thicker and narrower than usual. A thickened aorta is less flexible and resilient to the stress of constant blood flow and pumping of the heart. Over time, the wall of the aorta can become damaged. Aortic narrowing causes the heart to work harder to pump blood through the aorta, resulting in the signs and symptoms of SVAS. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. However, some people who inherit the altered gene never develop features of SVAS. (This situation is known as reduced penetrance.) In some cases, a person inherits the mutation from one parent who has the mutation. Other cases result from new mutations in the gene and occur in people with no history of the disorder in their family. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for supravalvular aortic stenosis ? | These resources address the diagnosis or management of supravalvular aortic stenosis: - Children's Hospital of Philadelphia - Genetic Testing Registry: Supravalvar aortic stenosis - Monroe Carell Jr. Children's Hospital at Vanderbilt These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Type 1 diabetes is a disorder characterized by abnormally high blood sugar levels. In this form of diabetes, specialized cells in the pancreas called beta cells stop producing insulin. Insulin controls how much glucose (a type of sugar) is passed from the blood into cells for conversion to energy. Lack of insulin results in the inability to use glucose for energy or to control the amount of sugar in the blood. Type 1 diabetes can occur at any age, from early childhood to late adulthood. The first signs and symptoms of the disorder are caused by high blood sugar and may include frequent urination (polyuria), excessive thirst (polydipsia), fatigue, blurred vision, tingling or loss of feeling in the hands and feet, and weight loss. These symptoms may recur during the course of the disorder if blood sugar is not well controlled by insulin replacement therapy. Improper control can also cause blood sugar levels to become too low (hypoglycemia). This may occur when the body's needs change, such as during exercise or if eating is delayed. Hypoglycemia can cause headache, dizziness, hunger, shaking, sweating, weakness, and agitation. Uncontrolled type 1 diabetes can lead to a life-threatening complication called diabetic ketoacidosis. Without insulin, cells cannot take in glucose. A lack of glucose in cells prompts the liver to try to compensate by releasing more glucose into the blood, and blood sugar can become extremely high. The cells, unable to use the glucose in the blood for energy, respond by using fats instead. Breaking down fats to obtain energy produces waste products called ketones, which can build up to toxic levels in people with type 1 diabetes, resulting in diabetic ketoacidosis. Affected individuals may begin breathing rapidly; develop a fruity odor in the breath; and experience nausea, vomiting, facial flushing, stomach pain, and dryness of the mouth (xerostomia). In severe cases, diabetic ketoacidosis can lead to coma and death. Over many years, the chronic high blood sugar associated with diabetes may cause damage to blood vessels and nerves, leading to complications affecting many organs and tissues. The retina, which is the light-sensitive tissue at the back of the eye, can be damaged (diabetic retinopathy), leading to vision loss and eventual blindness. Kidney damage (diabetic nephropathy) may also occur and can lead to kidney failure and end-stage renal disease (ESRD). Pain, tingling, and loss of normal sensation (diabetic neuropathy) often occur, especially in the feet. Impaired circulation and absence of the normal sensations that prompt reaction to injury can result in permanent damage to the feet; in severe cases, the damage can lead to amputation. People with type 1 diabetes are also at increased risk of heart attacks, strokes, and problems with urinary and sexual function. Type 1 diabetes occurs in 10 to 20 per 100,000 people per year in the United States. By age 18, approximately 1 in 300 people in the United States develop type 1 diabetes. The disorder occurs with similar frequencies in Europe, the United Kingdom, Canada, and New Zealand. Type 1 diabetes occurs much less frequently in Asia and South America, with reported incidences as low as 1 in 1 million per year. For unknown reasons, during the past 20 years the worldwide incidence of type 1 diabetes has been increasing by 2 to 5 percent each year. Type 1 diabetes accounts for 5 to 10 percent of cases of diabetes worldwide. Most people with diabetes have type 2 diabetes, in which the body continues to produce insulin but becomes less able to use it. The causes of type 1 diabetes are unknown, although several risk factors have been identified. The risk of developing type 1 diabetes is increased by certain variants of the HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes. These genes provide instructions for making proteins that play a critical role in the immune system. The HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. Type 1 diabetes is generally considered to be an autoimmune disorder. Autoimmune disorders occur when the immune system attacks the body's own tissues and organs. For unknown reasons, in people with type 1 diabetes the immune system damages the insulin-producing beta cells in the pancreas. Damage to these cells impairs insulin production and leads to the signs and symptoms of type 1 diabetes. HLA genes, including HLA-DQA1, HLA-DQB1, and HLA-DRB1, have many variations, and individuals have a certain combination of these variations, called a haplotype. Certain HLA haplotypes are associated with a higher risk of developing type 1 diabetes, with particular combinations of HLA-DQA1, HLA-DQB1, and HLA-DRB1 gene variations resulting in the highest risk. These haplotypes seem to increase the risk of an inappropriate immune response to beta cells. However, these variants are also found in the general population, and only about 5 percent of individuals with the gene variants develop type 1 diabetes. HLA variations account for approximately 40 percent of the genetic risk for the condition. Other HLA variations appear to be protective against the disease. Additional contributors, such as environmental factors and variations in other genes, are also thought to influence the development of this complex disorder. Additional Information from NCBI Gene: A predisposition to develop type 1 diabetes is passed through generations in families, but the inheritance pattern is unknown. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) type 1 diabetes ? | Type 1 diabetes is a disorder characterized by abnormally high blood sugar levels. In this form of diabetes, specialized cells in the pancreas called beta cells stop producing insulin. Insulin controls how much glucose (a type of sugar) is passed from the blood into cells for conversion to energy. Lack of insulin results in the inability to use glucose for energy or to control the amount of sugar in the blood. Type 1 diabetes can occur at any age; however, it usually develops by early adulthood, most often starting in adolescence. The first signs and symptoms of the disorder are caused by high blood sugar and may include frequent urination (polyuria), excessive thirst (polydipsia), fatigue, blurred vision, tingling or loss of feeling in the hands and feet, and weight loss. These symptoms may recur during the course of the disorder if blood sugar is not well controlled by insulin replacement therapy. Improper control can also cause blood sugar levels to become too low (hypoglycemia). This may occur when the body's needs change, such as during exercise or if eating is delayed. Hypoglycemia can cause headache, dizziness, hunger, shaking, sweating, weakness, and agitation. Uncontrolled type 1 diabetes can lead to a life-threatening complication called diabetic ketoacidosis. Without insulin, cells cannot take in glucose. A lack of glucose in cells prompts the liver to try to compensate by releasing more glucose into the blood, and blood sugar can become extremely high. The cells, unable to use the glucose in the blood for energy, respond by using fats instead. Breaking down fats to obtain energy produces waste products called ketones, which can build up to toxic levels in people with type 1 diabetes, resulting in diabetic ketoacidosis. Affected individuals may begin breathing rapidly; develop a fruity odor in the breath; and experience nausea, vomiting, facial flushing, stomach pain, and dryness of the mouth (xerostomia). In severe cases, diabetic ketoacidosis can lead to coma and death. Over many years, the chronic high blood sugar associated with diabetes may cause damage to blood vessels and nerves, leading to complications affecting many organs and tissues. The retina, which is the light-sensitive tissue at the back of the eye, can be damaged (diabetic retinopathy), leading to vision loss and eventual blindness. Kidney damage (diabetic nephropathy) may also occur and can lead to kidney failure and end-stage renal disease (ESRD). Pain, tingling, and loss of normal sensation (diabetic neuropathy) often occur, especially in the feet. Impaired circulation and absence of the normal sensations that prompt reaction to injury can result in permanent damage to the feet; in severe cases, the damage can lead to amputation. People with type 1 diabetes are also at increased risk of heart attacks, strokes, and problems with urinary and sexual function. |
Type 1 diabetes is a disorder characterized by abnormally high blood sugar levels. In this form of diabetes, specialized cells in the pancreas called beta cells stop producing insulin. Insulin controls how much glucose (a type of sugar) is passed from the blood into cells for conversion to energy. Lack of insulin results in the inability to use glucose for energy or to control the amount of sugar in the blood. Type 1 diabetes can occur at any age, from early childhood to late adulthood. The first signs and symptoms of the disorder are caused by high blood sugar and may include frequent urination (polyuria), excessive thirst (polydipsia), fatigue, blurred vision, tingling or loss of feeling in the hands and feet, and weight loss. These symptoms may recur during the course of the disorder if blood sugar is not well controlled by insulin replacement therapy. Improper control can also cause blood sugar levels to become too low (hypoglycemia). This may occur when the body's needs change, such as during exercise or if eating is delayed. Hypoglycemia can cause headache, dizziness, hunger, shaking, sweating, weakness, and agitation. Uncontrolled type 1 diabetes can lead to a life-threatening complication called diabetic ketoacidosis. Without insulin, cells cannot take in glucose. A lack of glucose in cells prompts the liver to try to compensate by releasing more glucose into the blood, and blood sugar can become extremely high. The cells, unable to use the glucose in the blood for energy, respond by using fats instead. Breaking down fats to obtain energy produces waste products called ketones, which can build up to toxic levels in people with type 1 diabetes, resulting in diabetic ketoacidosis. Affected individuals may begin breathing rapidly; develop a fruity odor in the breath; and experience nausea, vomiting, facial flushing, stomach pain, and dryness of the mouth (xerostomia). In severe cases, diabetic ketoacidosis can lead to coma and death. Over many years, the chronic high blood sugar associated with diabetes may cause damage to blood vessels and nerves, leading to complications affecting many organs and tissues. The retina, which is the light-sensitive tissue at the back of the eye, can be damaged (diabetic retinopathy), leading to vision loss and eventual blindness. Kidney damage (diabetic nephropathy) may also occur and can lead to kidney failure and end-stage renal disease (ESRD). Pain, tingling, and loss of normal sensation (diabetic neuropathy) often occur, especially in the feet. Impaired circulation and absence of the normal sensations that prompt reaction to injury can result in permanent damage to the feet; in severe cases, the damage can lead to amputation. People with type 1 diabetes are also at increased risk of heart attacks, strokes, and problems with urinary and sexual function. Type 1 diabetes occurs in 10 to 20 per 100,000 people per year in the United States. By age 18, approximately 1 in 300 people in the United States develop type 1 diabetes. The disorder occurs with similar frequencies in Europe, the United Kingdom, Canada, and New Zealand. Type 1 diabetes occurs much less frequently in Asia and South America, with reported incidences as low as 1 in 1 million per year. For unknown reasons, during the past 20 years the worldwide incidence of type 1 diabetes has been increasing by 2 to 5 percent each year. Type 1 diabetes accounts for 5 to 10 percent of cases of diabetes worldwide. Most people with diabetes have type 2 diabetes, in which the body continues to produce insulin but becomes less able to use it. The causes of type 1 diabetes are unknown, although several risk factors have been identified. The risk of developing type 1 diabetes is increased by certain variants of the HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes. These genes provide instructions for making proteins that play a critical role in the immune system. The HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. Type 1 diabetes is generally considered to be an autoimmune disorder. Autoimmune disorders occur when the immune system attacks the body's own tissues and organs. For unknown reasons, in people with type 1 diabetes the immune system damages the insulin-producing beta cells in the pancreas. Damage to these cells impairs insulin production and leads to the signs and symptoms of type 1 diabetes. HLA genes, including HLA-DQA1, HLA-DQB1, and HLA-DRB1, have many variations, and individuals have a certain combination of these variations, called a haplotype. Certain HLA haplotypes are associated with a higher risk of developing type 1 diabetes, with particular combinations of HLA-DQA1, HLA-DQB1, and HLA-DRB1 gene variations resulting in the highest risk. These haplotypes seem to increase the risk of an inappropriate immune response to beta cells. However, these variants are also found in the general population, and only about 5 percent of individuals with the gene variants develop type 1 diabetes. HLA variations account for approximately 40 percent of the genetic risk for the condition. Other HLA variations appear to be protective against the disease. Additional contributors, such as environmental factors and variations in other genes, are also thought to influence the development of this complex disorder. Additional Information from NCBI Gene: A predisposition to develop type 1 diabetes is passed through generations in families, but the inheritance pattern is unknown. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by type 1 diabetes ? | Type 1 diabetes occurs in 10 to 20 per 100,000 people per year in the United States. By age 18, approximately 1 in 300 people in the United States develop type 1 diabetes. The disorder occurs with similar frequencies in Europe, the United Kingdom, Canada, and New Zealand. Type 1 diabetes occurs much less frequently in Asia and South America, with reported incidences as low as 1 in 1 million per year. For unknown reasons, during the past 20 years the worldwide incidence of type 1 diabetes has been increasing by 2 to 5 percent each year. Type 1 diabetes accounts for 5 to 10 percent of cases of diabetes worldwide. Most people with diabetes have type 2 diabetes, in which the body continues to produce insulin but becomes less able to use it. |
Type 1 diabetes is a disorder characterized by abnormally high blood sugar levels. In this form of diabetes, specialized cells in the pancreas called beta cells stop producing insulin. Insulin controls how much glucose (a type of sugar) is passed from the blood into cells for conversion to energy. Lack of insulin results in the inability to use glucose for energy or to control the amount of sugar in the blood. Type 1 diabetes can occur at any age, from early childhood to late adulthood. The first signs and symptoms of the disorder are caused by high blood sugar and may include frequent urination (polyuria), excessive thirst (polydipsia), fatigue, blurred vision, tingling or loss of feeling in the hands and feet, and weight loss. These symptoms may recur during the course of the disorder if blood sugar is not well controlled by insulin replacement therapy. Improper control can also cause blood sugar levels to become too low (hypoglycemia). This may occur when the body's needs change, such as during exercise or if eating is delayed. Hypoglycemia can cause headache, dizziness, hunger, shaking, sweating, weakness, and agitation. Uncontrolled type 1 diabetes can lead to a life-threatening complication called diabetic ketoacidosis. Without insulin, cells cannot take in glucose. A lack of glucose in cells prompts the liver to try to compensate by releasing more glucose into the blood, and blood sugar can become extremely high. The cells, unable to use the glucose in the blood for energy, respond by using fats instead. Breaking down fats to obtain energy produces waste products called ketones, which can build up to toxic levels in people with type 1 diabetes, resulting in diabetic ketoacidosis. Affected individuals may begin breathing rapidly; develop a fruity odor in the breath; and experience nausea, vomiting, facial flushing, stomach pain, and dryness of the mouth (xerostomia). In severe cases, diabetic ketoacidosis can lead to coma and death. Over many years, the chronic high blood sugar associated with diabetes may cause damage to blood vessels and nerves, leading to complications affecting many organs and tissues. The retina, which is the light-sensitive tissue at the back of the eye, can be damaged (diabetic retinopathy), leading to vision loss and eventual blindness. Kidney damage (diabetic nephropathy) may also occur and can lead to kidney failure and end-stage renal disease (ESRD). Pain, tingling, and loss of normal sensation (diabetic neuropathy) often occur, especially in the feet. Impaired circulation and absence of the normal sensations that prompt reaction to injury can result in permanent damage to the feet; in severe cases, the damage can lead to amputation. People with type 1 diabetes are also at increased risk of heart attacks, strokes, and problems with urinary and sexual function. Type 1 diabetes occurs in 10 to 20 per 100,000 people per year in the United States. By age 18, approximately 1 in 300 people in the United States develop type 1 diabetes. The disorder occurs with similar frequencies in Europe, the United Kingdom, Canada, and New Zealand. Type 1 diabetes occurs much less frequently in Asia and South America, with reported incidences as low as 1 in 1 million per year. For unknown reasons, during the past 20 years the worldwide incidence of type 1 diabetes has been increasing by 2 to 5 percent each year. Type 1 diabetes accounts for 5 to 10 percent of cases of diabetes worldwide. Most people with diabetes have type 2 diabetes, in which the body continues to produce insulin but becomes less able to use it. The causes of type 1 diabetes are unknown, although several risk factors have been identified. The risk of developing type 1 diabetes is increased by certain variants of the HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes. These genes provide instructions for making proteins that play a critical role in the immune system. The HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. Type 1 diabetes is generally considered to be an autoimmune disorder. Autoimmune disorders occur when the immune system attacks the body's own tissues and organs. For unknown reasons, in people with type 1 diabetes the immune system damages the insulin-producing beta cells in the pancreas. Damage to these cells impairs insulin production and leads to the signs and symptoms of type 1 diabetes. HLA genes, including HLA-DQA1, HLA-DQB1, and HLA-DRB1, have many variations, and individuals have a certain combination of these variations, called a haplotype. Certain HLA haplotypes are associated with a higher risk of developing type 1 diabetes, with particular combinations of HLA-DQA1, HLA-DQB1, and HLA-DRB1 gene variations resulting in the highest risk. These haplotypes seem to increase the risk of an inappropriate immune response to beta cells. However, these variants are also found in the general population, and only about 5 percent of individuals with the gene variants develop type 1 diabetes. HLA variations account for approximately 40 percent of the genetic risk for the condition. Other HLA variations appear to be protective against the disease. Additional contributors, such as environmental factors and variations in other genes, are also thought to influence the development of this complex disorder. Additional Information from NCBI Gene: A predisposition to develop type 1 diabetes is passed through generations in families, but the inheritance pattern is unknown. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to type 1 diabetes ? | The causes of type 1 diabetes are unknown, although several risk factors have been identified. The risk of developing type 1 diabetes is increased by certain variants of the HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes. These genes provide instructions for making proteins that play a critical role in the immune system. The HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. Type 1 diabetes is generally considered to be an autoimmune disorder. Autoimmune disorders occur when the immune system attacks the body's own tissues and organs. For unknown reasons, in people with type 1 diabetes the immune system damages the insulin-producing beta cells in the pancreas. Damage to these cells impairs insulin production and leads to the signs and symptoms of type 1 diabetes. HLA genes, including HLA-DQA1, HLA-DQB1, and HLA-DRB1, have many variations, and individuals have a certain combination of these variations, called a haplotype. Certain HLA haplotypes are associated with a higher risk of developing type 1 diabetes, with particular combinations of HLA-DQA1, HLA-DQB1, and HLA-DRB1 gene variations resulting in the highest risk. These haplotypes seem to increase the risk of an inappropriate immune response to beta cells. However, these variants are also found in the general population, and only about 5 percent of individuals with the gene variants develop type 1 diabetes. HLA variations account for approximately 40 percent of the genetic risk for the condition. Other HLA variations appear to be protective against the disease. Additional contributors, such as environmental factors and variations in other genes, are also thought to influence the development of this complex disorder. |
Type 1 diabetes is a disorder characterized by abnormally high blood sugar levels. In this form of diabetes, specialized cells in the pancreas called beta cells stop producing insulin. Insulin controls how much glucose (a type of sugar) is passed from the blood into cells for conversion to energy. Lack of insulin results in the inability to use glucose for energy or to control the amount of sugar in the blood. Type 1 diabetes can occur at any age, from early childhood to late adulthood. The first signs and symptoms of the disorder are caused by high blood sugar and may include frequent urination (polyuria), excessive thirst (polydipsia), fatigue, blurred vision, tingling or loss of feeling in the hands and feet, and weight loss. These symptoms may recur during the course of the disorder if blood sugar is not well controlled by insulin replacement therapy. Improper control can also cause blood sugar levels to become too low (hypoglycemia). This may occur when the body's needs change, such as during exercise or if eating is delayed. Hypoglycemia can cause headache, dizziness, hunger, shaking, sweating, weakness, and agitation. Uncontrolled type 1 diabetes can lead to a life-threatening complication called diabetic ketoacidosis. Without insulin, cells cannot take in glucose. A lack of glucose in cells prompts the liver to try to compensate by releasing more glucose into the blood, and blood sugar can become extremely high. The cells, unable to use the glucose in the blood for energy, respond by using fats instead. Breaking down fats to obtain energy produces waste products called ketones, which can build up to toxic levels in people with type 1 diabetes, resulting in diabetic ketoacidosis. Affected individuals may begin breathing rapidly; develop a fruity odor in the breath; and experience nausea, vomiting, facial flushing, stomach pain, and dryness of the mouth (xerostomia). In severe cases, diabetic ketoacidosis can lead to coma and death. Over many years, the chronic high blood sugar associated with diabetes may cause damage to blood vessels and nerves, leading to complications affecting many organs and tissues. The retina, which is the light-sensitive tissue at the back of the eye, can be damaged (diabetic retinopathy), leading to vision loss and eventual blindness. Kidney damage (diabetic nephropathy) may also occur and can lead to kidney failure and end-stage renal disease (ESRD). Pain, tingling, and loss of normal sensation (diabetic neuropathy) often occur, especially in the feet. Impaired circulation and absence of the normal sensations that prompt reaction to injury can result in permanent damage to the feet; in severe cases, the damage can lead to amputation. People with type 1 diabetes are also at increased risk of heart attacks, strokes, and problems with urinary and sexual function. Type 1 diabetes occurs in 10 to 20 per 100,000 people per year in the United States. By age 18, approximately 1 in 300 people in the United States develop type 1 diabetes. The disorder occurs with similar frequencies in Europe, the United Kingdom, Canada, and New Zealand. Type 1 diabetes occurs much less frequently in Asia and South America, with reported incidences as low as 1 in 1 million per year. For unknown reasons, during the past 20 years the worldwide incidence of type 1 diabetes has been increasing by 2 to 5 percent each year. Type 1 diabetes accounts for 5 to 10 percent of cases of diabetes worldwide. Most people with diabetes have type 2 diabetes, in which the body continues to produce insulin but becomes less able to use it. The causes of type 1 diabetes are unknown, although several risk factors have been identified. The risk of developing type 1 diabetes is increased by certain variants of the HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes. These genes provide instructions for making proteins that play a critical role in the immune system. The HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. Type 1 diabetes is generally considered to be an autoimmune disorder. Autoimmune disorders occur when the immune system attacks the body's own tissues and organs. For unknown reasons, in people with type 1 diabetes the immune system damages the insulin-producing beta cells in the pancreas. Damage to these cells impairs insulin production and leads to the signs and symptoms of type 1 diabetes. HLA genes, including HLA-DQA1, HLA-DQB1, and HLA-DRB1, have many variations, and individuals have a certain combination of these variations, called a haplotype. Certain HLA haplotypes are associated with a higher risk of developing type 1 diabetes, with particular combinations of HLA-DQA1, HLA-DQB1, and HLA-DRB1 gene variations resulting in the highest risk. These haplotypes seem to increase the risk of an inappropriate immune response to beta cells. However, these variants are also found in the general population, and only about 5 percent of individuals with the gene variants develop type 1 diabetes. HLA variations account for approximately 40 percent of the genetic risk for the condition. Other HLA variations appear to be protective against the disease. Additional contributors, such as environmental factors and variations in other genes, are also thought to influence the development of this complex disorder. Additional Information from NCBI Gene: A predisposition to develop type 1 diabetes is passed through generations in families, but the inheritance pattern is unknown. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is type 1 diabetes inherited ? | A predisposition to develop type 1 diabetes is passed through generations in families, but the inheritance pattern is unknown. |
Type 1 diabetes is a disorder characterized by abnormally high blood sugar levels. In this form of diabetes, specialized cells in the pancreas called beta cells stop producing insulin. Insulin controls how much glucose (a type of sugar) is passed from the blood into cells for conversion to energy. Lack of insulin results in the inability to use glucose for energy or to control the amount of sugar in the blood. Type 1 diabetes can occur at any age, from early childhood to late adulthood. The first signs and symptoms of the disorder are caused by high blood sugar and may include frequent urination (polyuria), excessive thirst (polydipsia), fatigue, blurred vision, tingling or loss of feeling in the hands and feet, and weight loss. These symptoms may recur during the course of the disorder if blood sugar is not well controlled by insulin replacement therapy. Improper control can also cause blood sugar levels to become too low (hypoglycemia). This may occur when the body's needs change, such as during exercise or if eating is delayed. Hypoglycemia can cause headache, dizziness, hunger, shaking, sweating, weakness, and agitation. Uncontrolled type 1 diabetes can lead to a life-threatening complication called diabetic ketoacidosis. Without insulin, cells cannot take in glucose. A lack of glucose in cells prompts the liver to try to compensate by releasing more glucose into the blood, and blood sugar can become extremely high. The cells, unable to use the glucose in the blood for energy, respond by using fats instead. Breaking down fats to obtain energy produces waste products called ketones, which can build up to toxic levels in people with type 1 diabetes, resulting in diabetic ketoacidosis. Affected individuals may begin breathing rapidly; develop a fruity odor in the breath; and experience nausea, vomiting, facial flushing, stomach pain, and dryness of the mouth (xerostomia). In severe cases, diabetic ketoacidosis can lead to coma and death. Over many years, the chronic high blood sugar associated with diabetes may cause damage to blood vessels and nerves, leading to complications affecting many organs and tissues. The retina, which is the light-sensitive tissue at the back of the eye, can be damaged (diabetic retinopathy), leading to vision loss and eventual blindness. Kidney damage (diabetic nephropathy) may also occur and can lead to kidney failure and end-stage renal disease (ESRD). Pain, tingling, and loss of normal sensation (diabetic neuropathy) often occur, especially in the feet. Impaired circulation and absence of the normal sensations that prompt reaction to injury can result in permanent damage to the feet; in severe cases, the damage can lead to amputation. People with type 1 diabetes are also at increased risk of heart attacks, strokes, and problems with urinary and sexual function. Type 1 diabetes occurs in 10 to 20 per 100,000 people per year in the United States. By age 18, approximately 1 in 300 people in the United States develop type 1 diabetes. The disorder occurs with similar frequencies in Europe, the United Kingdom, Canada, and New Zealand. Type 1 diabetes occurs much less frequently in Asia and South America, with reported incidences as low as 1 in 1 million per year. For unknown reasons, during the past 20 years the worldwide incidence of type 1 diabetes has been increasing by 2 to 5 percent each year. Type 1 diabetes accounts for 5 to 10 percent of cases of diabetes worldwide. Most people with diabetes have type 2 diabetes, in which the body continues to produce insulin but becomes less able to use it. The causes of type 1 diabetes are unknown, although several risk factors have been identified. The risk of developing type 1 diabetes is increased by certain variants of the HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes. These genes provide instructions for making proteins that play a critical role in the immune system. The HLA-DQA1, HLA-DQB1, and HLA-DRB1 genes belong to a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. Type 1 diabetes is generally considered to be an autoimmune disorder. Autoimmune disorders occur when the immune system attacks the body's own tissues and organs. For unknown reasons, in people with type 1 diabetes the immune system damages the insulin-producing beta cells in the pancreas. Damage to these cells impairs insulin production and leads to the signs and symptoms of type 1 diabetes. HLA genes, including HLA-DQA1, HLA-DQB1, and HLA-DRB1, have many variations, and individuals have a certain combination of these variations, called a haplotype. Certain HLA haplotypes are associated with a higher risk of developing type 1 diabetes, with particular combinations of HLA-DQA1, HLA-DQB1, and HLA-DRB1 gene variations resulting in the highest risk. These haplotypes seem to increase the risk of an inappropriate immune response to beta cells. However, these variants are also found in the general population, and only about 5 percent of individuals with the gene variants develop type 1 diabetes. HLA variations account for approximately 40 percent of the genetic risk for the condition. Other HLA variations appear to be protective against the disease. Additional contributors, such as environmental factors and variations in other genes, are also thought to influence the development of this complex disorder. Additional Information from NCBI Gene: A predisposition to develop type 1 diabetes is passed through generations in families, but the inheritance pattern is unknown. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for type 1 diabetes ? | These resources address the diagnosis or management of type 1 diabetes: - Food and Drug Administration: Blood Glucose Measuring Devices - Food and Drug Administration: Insulin - Genetic Testing Registry: Diabetes mellitus type 1 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 10 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 11 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 12 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 13 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 15 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 17 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 18 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 19 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 2 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 20 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 21 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 22 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 23 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 24 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 3 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 4 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 5 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 6 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 7 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, 8 - Genetic Testing Registry: Diabetes mellitus, insulin-dependent, X-linked, susceptibility to - MedlinePlus Encyclopedia: Anti-Insulin Antibody Test - MedlinePlus Encyclopedia: Home Blood Sugar Testing - MedlinePlus Health Topic: Islet Cell Transplantation - MedlinePlus Health Topic: Pancreas Transplantation - Type 1 Diabetes in Adults: National Clinical Guideline for Diagnosis and Management in Primary and Secondary Care (2004) - Type 1 Diabetes: Diagnosis and Management of Type 1 Diabetes in Children and Young People (2004) These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Alexander disease is a rare disorder of the nervous system. It is one of a group of disorders, called leukodystrophies, that involve the destruction of myelin. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. If myelin is not properly maintained, the transmission of nerve impulses could be disrupted. As myelin deteriorates in leukodystrophies such as Alexander disease, nervous system functions are impaired. Most cases of Alexander disease begin before age 2 and are described as the infantile form. Signs and symptoms of the infantile form typically include an enlarged brain and head size (megalencephaly), seizures, stiffness in the arms and/or legs (spasticity), intellectual disability, and developmental delay. Less frequently, onset occurs later in childhood (the juvenile form) or in adulthood. Common problems in juvenile and adult forms of Alexander disease include speech abnormalities, swallowing difficulties, seizures, and poor coordination (ataxia). Rarely, a neonatal form of Alexander disease occurs within the first month of life and is associated with severe intellectual disability and developmental delay, a buildup of fluid in the brain (hydrocephalus), and seizures. Alexander disease is also characterized by abnormal protein deposits known as Rosenthal fibers. These deposits are found in specialized cells called astroglial cells, which support and nourish other cells in the brain and spinal cord (central nervous system). The prevalence of Alexander disease is unknown. About 500 cases have been reported since the disorder was first described in 1949. Mutations in the GFAP gene cause Alexander disease. The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein. Several molecules of this protein bind together to form intermediate filaments, which provide support and strength to cells. Mutations in the GFAP gene lead to the production of a structurally altered glial fibrillary acidic protein. The altered protein is thought to impair the formation of normal intermediate filaments. As a result, the abnormal glial fibrillary acidic protein likely accumulates in astroglial cells, leading to the formation of Rosenthal fibers, which impair cell function. It is not well understood how impaired astroglial cells contribute to the abnormal formation or maintenance of myelin, leading to the signs and symptoms of Alexander disease. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Most cases result from new mutations in the gene. These cases occur in people with no history of the disorder in their family. Rarely, an affected person inherits the mutation from one affected parent. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) Alexander disease ? | Alexander disease is a rare disorder of the nervous system. It is one of a group of disorders, called leukodystrophies, that involve the destruction of myelin. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. If myelin is not properly maintained, the transmission of nerve impulses could be disrupted. As myelin deteriorates in leukodystrophies such as Alexander disease, nervous system functions are impaired. Most cases of Alexander disease begin before age 2 and are described as the infantile form. Signs and symptoms of the infantile form typically include an enlarged brain and head size (megalencephaly), seizures, stiffness in the arms and/or legs (spasticity), intellectual disability, and developmental delay. Less frequently, onset occurs later in childhood (the juvenile form) or in adulthood. Common problems in juvenile and adult forms of Alexander disease include speech abnormalities, swallowing difficulties, seizures, and poor coordination (ataxia). Rarely, a neonatal form of Alexander disease occurs within the first month of life and is associated with severe intellectual disability and developmental delay, a buildup of fluid in the brain (hydrocephalus), and seizures. Alexander disease is also characterized by abnormal protein deposits known as Rosenthal fibers. These deposits are found in specialized cells called astroglial cells, which support and nourish other cells in the brain and spinal cord (central nervous system). |
Alexander disease is a rare disorder of the nervous system. It is one of a group of disorders, called leukodystrophies, that involve the destruction of myelin. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. If myelin is not properly maintained, the transmission of nerve impulses could be disrupted. As myelin deteriorates in leukodystrophies such as Alexander disease, nervous system functions are impaired. Most cases of Alexander disease begin before age 2 and are described as the infantile form. Signs and symptoms of the infantile form typically include an enlarged brain and head size (megalencephaly), seizures, stiffness in the arms and/or legs (spasticity), intellectual disability, and developmental delay. Less frequently, onset occurs later in childhood (the juvenile form) or in adulthood. Common problems in juvenile and adult forms of Alexander disease include speech abnormalities, swallowing difficulties, seizures, and poor coordination (ataxia). Rarely, a neonatal form of Alexander disease occurs within the first month of life and is associated with severe intellectual disability and developmental delay, a buildup of fluid in the brain (hydrocephalus), and seizures. Alexander disease is also characterized by abnormal protein deposits known as Rosenthal fibers. These deposits are found in specialized cells called astroglial cells, which support and nourish other cells in the brain and spinal cord (central nervous system). The prevalence of Alexander disease is unknown. About 500 cases have been reported since the disorder was first described in 1949. Mutations in the GFAP gene cause Alexander disease. The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein. Several molecules of this protein bind together to form intermediate filaments, which provide support and strength to cells. Mutations in the GFAP gene lead to the production of a structurally altered glial fibrillary acidic protein. The altered protein is thought to impair the formation of normal intermediate filaments. As a result, the abnormal glial fibrillary acidic protein likely accumulates in astroglial cells, leading to the formation of Rosenthal fibers, which impair cell function. It is not well understood how impaired astroglial cells contribute to the abnormal formation or maintenance of myelin, leading to the signs and symptoms of Alexander disease. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Most cases result from new mutations in the gene. These cases occur in people with no history of the disorder in their family. Rarely, an affected person inherits the mutation from one affected parent. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by Alexander disease ? | The prevalence of Alexander disease is unknown. About 500 cases have been reported since the disorder was first described in 1949. |
Alexander disease is a rare disorder of the nervous system. It is one of a group of disorders, called leukodystrophies, that involve the destruction of myelin. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. If myelin is not properly maintained, the transmission of nerve impulses could be disrupted. As myelin deteriorates in leukodystrophies such as Alexander disease, nervous system functions are impaired. Most cases of Alexander disease begin before age 2 and are described as the infantile form. Signs and symptoms of the infantile form typically include an enlarged brain and head size (megalencephaly), seizures, stiffness in the arms and/or legs (spasticity), intellectual disability, and developmental delay. Less frequently, onset occurs later in childhood (the juvenile form) or in adulthood. Common problems in juvenile and adult forms of Alexander disease include speech abnormalities, swallowing difficulties, seizures, and poor coordination (ataxia). Rarely, a neonatal form of Alexander disease occurs within the first month of life and is associated with severe intellectual disability and developmental delay, a buildup of fluid in the brain (hydrocephalus), and seizures. Alexander disease is also characterized by abnormal protein deposits known as Rosenthal fibers. These deposits are found in specialized cells called astroglial cells, which support and nourish other cells in the brain and spinal cord (central nervous system). The prevalence of Alexander disease is unknown. About 500 cases have been reported since the disorder was first described in 1949. Mutations in the GFAP gene cause Alexander disease. The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein. Several molecules of this protein bind together to form intermediate filaments, which provide support and strength to cells. Mutations in the GFAP gene lead to the production of a structurally altered glial fibrillary acidic protein. The altered protein is thought to impair the formation of normal intermediate filaments. As a result, the abnormal glial fibrillary acidic protein likely accumulates in astroglial cells, leading to the formation of Rosenthal fibers, which impair cell function. It is not well understood how impaired astroglial cells contribute to the abnormal formation or maintenance of myelin, leading to the signs and symptoms of Alexander disease. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Most cases result from new mutations in the gene. These cases occur in people with no history of the disorder in their family. Rarely, an affected person inherits the mutation from one affected parent. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to Alexander disease ? | Mutations in the GFAP gene cause Alexander disease. The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein. Several molecules of this protein bind together to form intermediate filaments, which provide support and strength to cells. Mutations in the GFAP gene lead to the production of a structurally altered glial fibrillary acidic protein. The altered protein is thought to impair the formation of normal intermediate filaments. As a result, the abnormal glial fibrillary acidic protein likely accumulates in astroglial cells, leading to the formation of Rosenthal fibers, which impair cell function. It is not well understood how impaired astroglial cells contribute to the abnormal formation or maintenance of myelin, leading to the signs and symptoms of Alexander disease. |
Alexander disease is a rare disorder of the nervous system. It is one of a group of disorders, called leukodystrophies, that involve the destruction of myelin. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. If myelin is not properly maintained, the transmission of nerve impulses could be disrupted. As myelin deteriorates in leukodystrophies such as Alexander disease, nervous system functions are impaired. Most cases of Alexander disease begin before age 2 and are described as the infantile form. Signs and symptoms of the infantile form typically include an enlarged brain and head size (megalencephaly), seizures, stiffness in the arms and/or legs (spasticity), intellectual disability, and developmental delay. Less frequently, onset occurs later in childhood (the juvenile form) or in adulthood. Common problems in juvenile and adult forms of Alexander disease include speech abnormalities, swallowing difficulties, seizures, and poor coordination (ataxia). Rarely, a neonatal form of Alexander disease occurs within the first month of life and is associated with severe intellectual disability and developmental delay, a buildup of fluid in the brain (hydrocephalus), and seizures. Alexander disease is also characterized by abnormal protein deposits known as Rosenthal fibers. These deposits are found in specialized cells called astroglial cells, which support and nourish other cells in the brain and spinal cord (central nervous system). The prevalence of Alexander disease is unknown. About 500 cases have been reported since the disorder was first described in 1949. Mutations in the GFAP gene cause Alexander disease. The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein. Several molecules of this protein bind together to form intermediate filaments, which provide support and strength to cells. Mutations in the GFAP gene lead to the production of a structurally altered glial fibrillary acidic protein. The altered protein is thought to impair the formation of normal intermediate filaments. As a result, the abnormal glial fibrillary acidic protein likely accumulates in astroglial cells, leading to the formation of Rosenthal fibers, which impair cell function. It is not well understood how impaired astroglial cells contribute to the abnormal formation or maintenance of myelin, leading to the signs and symptoms of Alexander disease. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Most cases result from new mutations in the gene. These cases occur in people with no history of the disorder in their family. Rarely, an affected person inherits the mutation from one affected parent. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is Alexander disease inherited ? | This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Most cases result from new mutations in the gene. These cases occur in people with no history of the disorder in their family. Rarely, an affected person inherits the mutation from one affected parent. |
Alexander disease is a rare disorder of the nervous system. It is one of a group of disorders, called leukodystrophies, that involve the destruction of myelin. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. If myelin is not properly maintained, the transmission of nerve impulses could be disrupted. As myelin deteriorates in leukodystrophies such as Alexander disease, nervous system functions are impaired. Most cases of Alexander disease begin before age 2 and are described as the infantile form. Signs and symptoms of the infantile form typically include an enlarged brain and head size (megalencephaly), seizures, stiffness in the arms and/or legs (spasticity), intellectual disability, and developmental delay. Less frequently, onset occurs later in childhood (the juvenile form) or in adulthood. Common problems in juvenile and adult forms of Alexander disease include speech abnormalities, swallowing difficulties, seizures, and poor coordination (ataxia). Rarely, a neonatal form of Alexander disease occurs within the first month of life and is associated with severe intellectual disability and developmental delay, a buildup of fluid in the brain (hydrocephalus), and seizures. Alexander disease is also characterized by abnormal protein deposits known as Rosenthal fibers. These deposits are found in specialized cells called astroglial cells, which support and nourish other cells in the brain and spinal cord (central nervous system). The prevalence of Alexander disease is unknown. About 500 cases have been reported since the disorder was first described in 1949. Mutations in the GFAP gene cause Alexander disease. The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein. Several molecules of this protein bind together to form intermediate filaments, which provide support and strength to cells. Mutations in the GFAP gene lead to the production of a structurally altered glial fibrillary acidic protein. The altered protein is thought to impair the formation of normal intermediate filaments. As a result, the abnormal glial fibrillary acidic protein likely accumulates in astroglial cells, leading to the formation of Rosenthal fibers, which impair cell function. It is not well understood how impaired astroglial cells contribute to the abnormal formation or maintenance of myelin, leading to the signs and symptoms of Alexander disease. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. Most cases result from new mutations in the gene. These cases occur in people with no history of the disorder in their family. Rarely, an affected person inherits the mutation from one affected parent. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for Alexander disease ? | These resources address the diagnosis or management of Alexander disease: - Gene Review: Gene Review: Alexander Disease - Genetic Testing Registry: Alexander's disease - MedlinePlus Encyclopedia: Myelin These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Ataxia neuropathy spectrum is part of a group of conditions called the POLG-related disorders. The conditions in this group feature a range of similar signs and symptoms involving muscle-, nerve-, and brain-related functions. Ataxia neuropathy spectrum now includes the conditions previously called mitochondrial recessive ataxia syndrome (MIRAS) and sensory ataxia neuropathy dysarthria and ophthalmoplegia (SANDO). As the name implies, people with ataxia neuropathy spectrum typically have problems with coordination and balance (ataxia) and disturbances in nerve function (neuropathy). The neuropathy can be classified as sensory, motor, or a combination of the two (mixed). Sensory neuropathy causes numbness, tingling, or pain in the arms and legs, and motor neuropathy refers to disturbance in the nerves used for muscle movement. Most people with ataxia neuropathy spectrum also have severe brain dysfunction (encephalopathy) and seizures. Some affected individuals have weakness of the external muscles of the eye (ophthalmoplegia), which leads to drooping eyelids (ptosis). Other signs and symptoms can include involuntary muscle twitches (myoclonus), liver disease, depression, migraine headaches, or blindness. The prevalence of ataxia neuropathy spectrum is unknown. Ataxia neuropathy spectrum is caused by mutations in the POLG gene or, rarely, the TWNK gene. The POLG gene provides instructions for making one part, the alpha subunit, of a protein called polymerase gamma (pol γ). The TWNK gene provides instructions for making a protein called Twinkle. Pol γ and Twinkle function in mitochondria, which are structures within cells that use oxygen to convert the energy from food into a form cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol γ and Twinkle are both integral to the process of DNA replication by which new copies of mtDNA are produced. Mutated pol γ or mutated Twinkle reduce mtDNA replication. Although the mechanisms are unknown, mutations in the POLG gene often result in fewer copies of mtDNA (mtDNA depletion), and mutations in the TWNK gene often result in deletions of large regions of mtDNA (mtDNA deletion). MtDNA depletion or deletion occurs most commonly in muscle, brain, or liver cells. MtDNA depletion causes a decrease in cellular energy, which could account for the signs and symptoms of ataxia neuropathy spectrum. It is unclear what role mtDNA deletions play in the signs and symptoms of the condition. Ataxia neuropathy spectrum can have different inheritance patterns depending on the associated gene. Mutations in the POLG gene cause a form of the condition that is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Mutations in the TWNK gene cause a form of the condition that is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) ataxia neuropathy spectrum ? | Ataxia neuropathy spectrum is part of a group of conditions called the POLG-related disorders. The conditions in this group feature a range of similar signs and symptoms involving muscle-, nerve-, and brain-related functions. Ataxia neuropathy spectrum now includes the conditions previously called mitochondrial recessive ataxia syndrome (MIRAS) and sensory ataxia neuropathy dysarthria and ophthalmoplegia (SANDO). As the name implies, people with ataxia neuropathy spectrum typically have problems with coordination and balance (ataxia) and disturbances in nerve function (neuropathy). The neuropathy can be classified as sensory, motor, or a combination of the two (mixed). Sensory neuropathy causes numbness, tingling, or pain in the arms and legs, and motor neuropathy refers to disturbance in the nerves used for muscle movement. Most people with ataxia neuropathy spectrum also have severe brain dysfunction (encephalopathy) and seizures. Some affected individuals have weakness of the external muscles of the eye (ophthalmoplegia), which leads to drooping eyelids (ptosis). Other signs and symptoms can include involuntary muscle twitches (myoclonus), liver disease, depression, migraine headaches, or blindness. |
Ataxia neuropathy spectrum is part of a group of conditions called the POLG-related disorders. The conditions in this group feature a range of similar signs and symptoms involving muscle-, nerve-, and brain-related functions. Ataxia neuropathy spectrum now includes the conditions previously called mitochondrial recessive ataxia syndrome (MIRAS) and sensory ataxia neuropathy dysarthria and ophthalmoplegia (SANDO). As the name implies, people with ataxia neuropathy spectrum typically have problems with coordination and balance (ataxia) and disturbances in nerve function (neuropathy). The neuropathy can be classified as sensory, motor, or a combination of the two (mixed). Sensory neuropathy causes numbness, tingling, or pain in the arms and legs, and motor neuropathy refers to disturbance in the nerves used for muscle movement. Most people with ataxia neuropathy spectrum also have severe brain dysfunction (encephalopathy) and seizures. Some affected individuals have weakness of the external muscles of the eye (ophthalmoplegia), which leads to drooping eyelids (ptosis). Other signs and symptoms can include involuntary muscle twitches (myoclonus), liver disease, depression, migraine headaches, or blindness. The prevalence of ataxia neuropathy spectrum is unknown. Ataxia neuropathy spectrum is caused by mutations in the POLG gene or, rarely, the TWNK gene. The POLG gene provides instructions for making one part, the alpha subunit, of a protein called polymerase gamma (pol γ). The TWNK gene provides instructions for making a protein called Twinkle. Pol γ and Twinkle function in mitochondria, which are structures within cells that use oxygen to convert the energy from food into a form cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol γ and Twinkle are both integral to the process of DNA replication by which new copies of mtDNA are produced. Mutated pol γ or mutated Twinkle reduce mtDNA replication. Although the mechanisms are unknown, mutations in the POLG gene often result in fewer copies of mtDNA (mtDNA depletion), and mutations in the TWNK gene often result in deletions of large regions of mtDNA (mtDNA deletion). MtDNA depletion or deletion occurs most commonly in muscle, brain, or liver cells. MtDNA depletion causes a decrease in cellular energy, which could account for the signs and symptoms of ataxia neuropathy spectrum. It is unclear what role mtDNA deletions play in the signs and symptoms of the condition. Ataxia neuropathy spectrum can have different inheritance patterns depending on the associated gene. Mutations in the POLG gene cause a form of the condition that is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Mutations in the TWNK gene cause a form of the condition that is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by ataxia neuropathy spectrum ? | The prevalence of ataxia neuropathy spectrum is unknown. |
Ataxia neuropathy spectrum is part of a group of conditions called the POLG-related disorders. The conditions in this group feature a range of similar signs and symptoms involving muscle-, nerve-, and brain-related functions. Ataxia neuropathy spectrum now includes the conditions previously called mitochondrial recessive ataxia syndrome (MIRAS) and sensory ataxia neuropathy dysarthria and ophthalmoplegia (SANDO). As the name implies, people with ataxia neuropathy spectrum typically have problems with coordination and balance (ataxia) and disturbances in nerve function (neuropathy). The neuropathy can be classified as sensory, motor, or a combination of the two (mixed). Sensory neuropathy causes numbness, tingling, or pain in the arms and legs, and motor neuropathy refers to disturbance in the nerves used for muscle movement. Most people with ataxia neuropathy spectrum also have severe brain dysfunction (encephalopathy) and seizures. Some affected individuals have weakness of the external muscles of the eye (ophthalmoplegia), which leads to drooping eyelids (ptosis). Other signs and symptoms can include involuntary muscle twitches (myoclonus), liver disease, depression, migraine headaches, or blindness. The prevalence of ataxia neuropathy spectrum is unknown. Ataxia neuropathy spectrum is caused by mutations in the POLG gene or, rarely, the TWNK gene. The POLG gene provides instructions for making one part, the alpha subunit, of a protein called polymerase gamma (pol γ). The TWNK gene provides instructions for making a protein called Twinkle. Pol γ and Twinkle function in mitochondria, which are structures within cells that use oxygen to convert the energy from food into a form cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol γ and Twinkle are both integral to the process of DNA replication by which new copies of mtDNA are produced. Mutated pol γ or mutated Twinkle reduce mtDNA replication. Although the mechanisms are unknown, mutations in the POLG gene often result in fewer copies of mtDNA (mtDNA depletion), and mutations in the TWNK gene often result in deletions of large regions of mtDNA (mtDNA deletion). MtDNA depletion or deletion occurs most commonly in muscle, brain, or liver cells. MtDNA depletion causes a decrease in cellular energy, which could account for the signs and symptoms of ataxia neuropathy spectrum. It is unclear what role mtDNA deletions play in the signs and symptoms of the condition. Ataxia neuropathy spectrum can have different inheritance patterns depending on the associated gene. Mutations in the POLG gene cause a form of the condition that is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Mutations in the TWNK gene cause a form of the condition that is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to ataxia neuropathy spectrum ? | Ataxia neuropathy spectrum is caused by mutations in the POLG gene or, rarely, the C10orf2 gene. The POLG gene provides instructions for making one part, the alpha subunit, of a protein called polymerase gamma (pol ). The C10orf2 gene provides instructions for making a protein called Twinkle. Pol and Twinkle function in mitochondria, which are structures within cells that use oxygen to convert the energy from food into a form cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol and Twinkle are both integral to the process of DNA replication by which new copies of mtDNA are produced. Mutated pol or mutated Twinkle reduce mtDNA replication. Although the mechanisms are unknown, mutations in the POLG gene often result in fewer copies of mtDNA (mtDNA depletion), and mutations in the C10orf2 gene often result in deletions of large regions of mtDNA (mtDNA deletion). MtDNA depletion or deletion occurs most commonly in muscle, brain, or liver cells. MtDNA depletion causes a decrease in cellular energy, which could account for the signs and symptoms of ataxia neuropathy spectrum. It is unclear what role mtDNA deletions play in the signs and symptoms of the condition. |
Ataxia neuropathy spectrum is part of a group of conditions called the POLG-related disorders. The conditions in this group feature a range of similar signs and symptoms involving muscle-, nerve-, and brain-related functions. Ataxia neuropathy spectrum now includes the conditions previously called mitochondrial recessive ataxia syndrome (MIRAS) and sensory ataxia neuropathy dysarthria and ophthalmoplegia (SANDO). As the name implies, people with ataxia neuropathy spectrum typically have problems with coordination and balance (ataxia) and disturbances in nerve function (neuropathy). The neuropathy can be classified as sensory, motor, or a combination of the two (mixed). Sensory neuropathy causes numbness, tingling, or pain in the arms and legs, and motor neuropathy refers to disturbance in the nerves used for muscle movement. Most people with ataxia neuropathy spectrum also have severe brain dysfunction (encephalopathy) and seizures. Some affected individuals have weakness of the external muscles of the eye (ophthalmoplegia), which leads to drooping eyelids (ptosis). Other signs and symptoms can include involuntary muscle twitches (myoclonus), liver disease, depression, migraine headaches, or blindness. The prevalence of ataxia neuropathy spectrum is unknown. Ataxia neuropathy spectrum is caused by mutations in the POLG gene or, rarely, the TWNK gene. The POLG gene provides instructions for making one part, the alpha subunit, of a protein called polymerase gamma (pol γ). The TWNK gene provides instructions for making a protein called Twinkle. Pol γ and Twinkle function in mitochondria, which are structures within cells that use oxygen to convert the energy from food into a form cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol γ and Twinkle are both integral to the process of DNA replication by which new copies of mtDNA are produced. Mutated pol γ or mutated Twinkle reduce mtDNA replication. Although the mechanisms are unknown, mutations in the POLG gene often result in fewer copies of mtDNA (mtDNA depletion), and mutations in the TWNK gene often result in deletions of large regions of mtDNA (mtDNA deletion). MtDNA depletion or deletion occurs most commonly in muscle, brain, or liver cells. MtDNA depletion causes a decrease in cellular energy, which could account for the signs and symptoms of ataxia neuropathy spectrum. It is unclear what role mtDNA deletions play in the signs and symptoms of the condition. Ataxia neuropathy spectrum can have different inheritance patterns depending on the associated gene. Mutations in the POLG gene cause a form of the condition that is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Mutations in the TWNK gene cause a form of the condition that is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is ataxia neuropathy spectrum inherited ? | Ataxia neuropathy spectrum can have different inheritance patterns depending on the associated gene. Mutations in the POLG gene cause a form of the condition that is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Mutations in the C10orf2 gene cause a form of the condition that is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. |
Ataxia neuropathy spectrum is part of a group of conditions called the POLG-related disorders. The conditions in this group feature a range of similar signs and symptoms involving muscle-, nerve-, and brain-related functions. Ataxia neuropathy spectrum now includes the conditions previously called mitochondrial recessive ataxia syndrome (MIRAS) and sensory ataxia neuropathy dysarthria and ophthalmoplegia (SANDO). As the name implies, people with ataxia neuropathy spectrum typically have problems with coordination and balance (ataxia) and disturbances in nerve function (neuropathy). The neuropathy can be classified as sensory, motor, or a combination of the two (mixed). Sensory neuropathy causes numbness, tingling, or pain in the arms and legs, and motor neuropathy refers to disturbance in the nerves used for muscle movement. Most people with ataxia neuropathy spectrum also have severe brain dysfunction (encephalopathy) and seizures. Some affected individuals have weakness of the external muscles of the eye (ophthalmoplegia), which leads to drooping eyelids (ptosis). Other signs and symptoms can include involuntary muscle twitches (myoclonus), liver disease, depression, migraine headaches, or blindness. The prevalence of ataxia neuropathy spectrum is unknown. Ataxia neuropathy spectrum is caused by mutations in the POLG gene or, rarely, the TWNK gene. The POLG gene provides instructions for making one part, the alpha subunit, of a protein called polymerase gamma (pol γ). The TWNK gene provides instructions for making a protein called Twinkle. Pol γ and Twinkle function in mitochondria, which are structures within cells that use oxygen to convert the energy from food into a form cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol γ and Twinkle are both integral to the process of DNA replication by which new copies of mtDNA are produced. Mutated pol γ or mutated Twinkle reduce mtDNA replication. Although the mechanisms are unknown, mutations in the POLG gene often result in fewer copies of mtDNA (mtDNA depletion), and mutations in the TWNK gene often result in deletions of large regions of mtDNA (mtDNA deletion). MtDNA depletion or deletion occurs most commonly in muscle, brain, or liver cells. MtDNA depletion causes a decrease in cellular energy, which could account for the signs and symptoms of ataxia neuropathy spectrum. It is unclear what role mtDNA deletions play in the signs and symptoms of the condition. Ataxia neuropathy spectrum can have different inheritance patterns depending on the associated gene. Mutations in the POLG gene cause a form of the condition that is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. Mutations in the TWNK gene cause a form of the condition that is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for ataxia neuropathy spectrum ? | These resources address the diagnosis or management of ataxia neuropathy spectrum: - Gene Review: Gene Review: POLG-Related Disorders - Genetic Testing Registry: Sensory ataxic neuropathy, dysarthria, and ophthalmoparesis - National Ataxia Foundation: Gene Testing for Hereditary Ataxia - United Mitochondrial Disease Foundation: Diagnosis of Mitochondrial Disease These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Task-specific focal dystonia is a movement disorder that interferes with the performance of particular tasks, such as writing, playing a musical instrument, or participating in a sport. Dystonias are a group of movement problems characterized by involuntary, sustained muscle contractions, tremors, and other uncontrolled movements. The term "focal" refers to a type of dystonia that affects a single part of the body, such as the hand or jaw. Researchers have described several forms of task-specific focal dystonia. The most common is writer's cramp, in which muscle cramps or spasms in the hand, wrist, or forearm interfere with holding a pen or pencil. Writer's cramp begins in the hand used for writing (the dominant hand) and is usually limited to that task, but with time it can spread to the other hand and affect other fine-motor activities such as shaving or typing. Musician's dystonia is a form of task-specific focal dystonia characterized by muscle cramps and spasms that occur while playing a musical instrument. This condition can affect amateur or professional musicians, and the location of the dystonia depends on the instrument. Some musicians (such as piano, guitar, and violin players) develop focal hand dystonia, which causes loss of fine-motor control in the hand and wrist muscles. This condition reduces finger coordination, speed, and endurance while playing. Musicians who play woodwind or brass instruments can develop what is known as embouchure dystonia. This condition causes muscle cramps or spasms involving the lips, tongue, or jaw, which prevents normal positioning of the mouth around the instrument's mouthpiece. Musician's dystonia often occurs only when playing a particular instrument. However, over time focal hand dystonia may impair other activities, and embouchure dystonia can worsen to affect eating and speech. Task-specific focal dystonia can affect people who play sports and engage in other occupations involving repetitive, highly practiced movements. For example, some golfers experience involuntary jerking of the wrists during putting, a condition known informally as "the yips." Cramps and spasms of the hand and arm muscles can also affect tennis players, billiards players, dart throwers, and other athletes. Additionally, task-specific dystonia has been reported in tailors, shoemakers, hair stylists, and people who frequently type or use a computer mouse. The abnormal movements associated with task-specific focal dystonia are usually painless, although they can cause anxiety when they interfere with musical performance and other activities. Severe cases can cause professional disability. Task-specific focal dystonia affects an estimated 7 to 69 per million people in the general population. Musician's dystonia that is severe enough to impact performance occurs in about 1 percent of musicians. The causes of task-specific focal dystonia are unknown, although the disorder likely results from a combination of genetic and environmental factors. Certain genetic changes probably increase the likelihood of developing this condition, and environmental factors may trigger the onset of symptoms in people who are at risk. It is possible that the different forms of task-specific focal dystonia have different underlying causes. Having a family history of dystonia, particularly focal dystonia, is one of the only established risk factors for task-specific focal dystonia. Studies suggest that previous injury, changes in practice routine, and exposure to anti-psychotic drugs (which can cause other types of dystonia) are not major risk factors. Nor does the condition appear to be a form of performance anxiety. Task-specific focal dystonia may be associated with dysfunction in areas of the brain that regulate movement. In particular, researchers have found that at least some cases of the condition are related to malfunction of the basal ganglia, which are structures deep within the brain that help start and control movement. Although genetic factors are almost certainly involved in task-specific focal dystonia, no genes have been clearly associated with the condition. Researchers have looked for mutations in several genes known to be involved in other forms of dystonia, but these genetic changes do not appear to be a major cause of task-specific focal dystonia. Researchers are working to determine which genetic factors are related to this disorder. Most cases of task-specific focal dystonia are sporadic, which means they occur in people with no history of the condition in their family. However, at least 10 percent of affected individuals have a family history of focal dystonia. (For example, writer's cramp and musician's dystonia have been reported to occur in the same family.) The dystonia often appears to have an autosomal dominant pattern of inheritance, based on the observation that some affected people have a parent with the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) task-specific focal dystonia ? | Task-specific focal dystonia is a movement disorder that interferes with the performance of particular tasks, such as writing, playing a musical instrument, or participating in a sport. Dystonias are a group of movement problems characterized by involuntary, sustained muscle contractions, tremors, and other uncontrolled movements. The term "focal" refers to a type of dystonia that affects a single part of the body, such as the hand or jaw. Researchers have described several forms of task-specific focal dystonia. The most common is writer's cramp, in which muscle cramps or spasms in the hand, wrist, or forearm interfere with holding a pen or pencil. Writer's cramp begins in the hand used for writing (the dominant hand) and is usually limited to that task, but with time it can spread to the other hand and affect other fine-motor activities such as shaving or typing. Musician's dystonia is a form of task-specific focal dystonia characterized by muscle cramps and spasms that occur while playing a musical instrument. This condition can affect amateur or professional musicians, and the location of the dystonia depends on the instrument. Some musicians (such as piano, guitar, and violin players) develop focal hand dystonia, which causes loss of fine-motor control in the hand and wrist muscles. This condition reduces finger coordination, speed, and endurance while playing. Musicians who play woodwind or brass instruments can develop what is known as embouchure dystonia. This condition causes muscle cramps or spasms involving the lips, tongue, or jaw, which prevents normal positioning of the mouth around the instrument's mouthpiece. Musician's dystonia often occurs only when playing a particular instrument. However, over time focal hand dystonia may impair other activities, and embouchure dystonia can worsen to affect eating and speech. Task-specific focal dystonia can affect people who play sports and engage in other occupations involving repetitive, highly practiced movements. For example, some golfers experience involuntary jerking of the wrists during putting, a condition known informally as "the yips." Cramps and spasms of the hand and arm muscles can also affect tennis players, billiards players, dart throwers, and other athletes. Additionally, task-specific dystonia has been reported in tailors, shoemakers, hair stylists, and people who frequently type or use a computer mouse. The abnormal movements associated with task-specific focal dystonia are usually painless, although they can cause anxiety when they interfere with musical performance and other activities. Severe cases can cause professional disability. |
Task-specific focal dystonia is a movement disorder that interferes with the performance of particular tasks, such as writing, playing a musical instrument, or participating in a sport. Dystonias are a group of movement problems characterized by involuntary, sustained muscle contractions, tremors, and other uncontrolled movements. The term "focal" refers to a type of dystonia that affects a single part of the body, such as the hand or jaw. Researchers have described several forms of task-specific focal dystonia. The most common is writer's cramp, in which muscle cramps or spasms in the hand, wrist, or forearm interfere with holding a pen or pencil. Writer's cramp begins in the hand used for writing (the dominant hand) and is usually limited to that task, but with time it can spread to the other hand and affect other fine-motor activities such as shaving or typing. Musician's dystonia is a form of task-specific focal dystonia characterized by muscle cramps and spasms that occur while playing a musical instrument. This condition can affect amateur or professional musicians, and the location of the dystonia depends on the instrument. Some musicians (such as piano, guitar, and violin players) develop focal hand dystonia, which causes loss of fine-motor control in the hand and wrist muscles. This condition reduces finger coordination, speed, and endurance while playing. Musicians who play woodwind or brass instruments can develop what is known as embouchure dystonia. This condition causes muscle cramps or spasms involving the lips, tongue, or jaw, which prevents normal positioning of the mouth around the instrument's mouthpiece. Musician's dystonia often occurs only when playing a particular instrument. However, over time focal hand dystonia may impair other activities, and embouchure dystonia can worsen to affect eating and speech. Task-specific focal dystonia can affect people who play sports and engage in other occupations involving repetitive, highly practiced movements. For example, some golfers experience involuntary jerking of the wrists during putting, a condition known informally as "the yips." Cramps and spasms of the hand and arm muscles can also affect tennis players, billiards players, dart throwers, and other athletes. Additionally, task-specific dystonia has been reported in tailors, shoemakers, hair stylists, and people who frequently type or use a computer mouse. The abnormal movements associated with task-specific focal dystonia are usually painless, although they can cause anxiety when they interfere with musical performance and other activities. Severe cases can cause professional disability. Task-specific focal dystonia affects an estimated 7 to 69 per million people in the general population. Musician's dystonia that is severe enough to impact performance occurs in about 1 percent of musicians. The causes of task-specific focal dystonia are unknown, although the disorder likely results from a combination of genetic and environmental factors. Certain genetic changes probably increase the likelihood of developing this condition, and environmental factors may trigger the onset of symptoms in people who are at risk. It is possible that the different forms of task-specific focal dystonia have different underlying causes. Having a family history of dystonia, particularly focal dystonia, is one of the only established risk factors for task-specific focal dystonia. Studies suggest that previous injury, changes in practice routine, and exposure to anti-psychotic drugs (which can cause other types of dystonia) are not major risk factors. Nor does the condition appear to be a form of performance anxiety. Task-specific focal dystonia may be associated with dysfunction in areas of the brain that regulate movement. In particular, researchers have found that at least some cases of the condition are related to malfunction of the basal ganglia, which are structures deep within the brain that help start and control movement. Although genetic factors are almost certainly involved in task-specific focal dystonia, no genes have been clearly associated with the condition. Researchers have looked for mutations in several genes known to be involved in other forms of dystonia, but these genetic changes do not appear to be a major cause of task-specific focal dystonia. Researchers are working to determine which genetic factors are related to this disorder. Most cases of task-specific focal dystonia are sporadic, which means they occur in people with no history of the condition in their family. However, at least 10 percent of affected individuals have a family history of focal dystonia. (For example, writer's cramp and musician's dystonia have been reported to occur in the same family.) The dystonia often appears to have an autosomal dominant pattern of inheritance, based on the observation that some affected people have a parent with the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by task-specific focal dystonia ? | Task-specific focal dystonia affects an estimated 7 to 69 per million people in the general population. Musician's dystonia that is severe enough to impact performance occurs in about 1 percent of musicians. |
Task-specific focal dystonia is a movement disorder that interferes with the performance of particular tasks, such as writing, playing a musical instrument, or participating in a sport. Dystonias are a group of movement problems characterized by involuntary, sustained muscle contractions, tremors, and other uncontrolled movements. The term "focal" refers to a type of dystonia that affects a single part of the body, such as the hand or jaw. Researchers have described several forms of task-specific focal dystonia. The most common is writer's cramp, in which muscle cramps or spasms in the hand, wrist, or forearm interfere with holding a pen or pencil. Writer's cramp begins in the hand used for writing (the dominant hand) and is usually limited to that task, but with time it can spread to the other hand and affect other fine-motor activities such as shaving or typing. Musician's dystonia is a form of task-specific focal dystonia characterized by muscle cramps and spasms that occur while playing a musical instrument. This condition can affect amateur or professional musicians, and the location of the dystonia depends on the instrument. Some musicians (such as piano, guitar, and violin players) develop focal hand dystonia, which causes loss of fine-motor control in the hand and wrist muscles. This condition reduces finger coordination, speed, and endurance while playing. Musicians who play woodwind or brass instruments can develop what is known as embouchure dystonia. This condition causes muscle cramps or spasms involving the lips, tongue, or jaw, which prevents normal positioning of the mouth around the instrument's mouthpiece. Musician's dystonia often occurs only when playing a particular instrument. However, over time focal hand dystonia may impair other activities, and embouchure dystonia can worsen to affect eating and speech. Task-specific focal dystonia can affect people who play sports and engage in other occupations involving repetitive, highly practiced movements. For example, some golfers experience involuntary jerking of the wrists during putting, a condition known informally as "the yips." Cramps and spasms of the hand and arm muscles can also affect tennis players, billiards players, dart throwers, and other athletes. Additionally, task-specific dystonia has been reported in tailors, shoemakers, hair stylists, and people who frequently type or use a computer mouse. The abnormal movements associated with task-specific focal dystonia are usually painless, although they can cause anxiety when they interfere with musical performance and other activities. Severe cases can cause professional disability. Task-specific focal dystonia affects an estimated 7 to 69 per million people in the general population. Musician's dystonia that is severe enough to impact performance occurs in about 1 percent of musicians. The causes of task-specific focal dystonia are unknown, although the disorder likely results from a combination of genetic and environmental factors. Certain genetic changes probably increase the likelihood of developing this condition, and environmental factors may trigger the onset of symptoms in people who are at risk. It is possible that the different forms of task-specific focal dystonia have different underlying causes. Having a family history of dystonia, particularly focal dystonia, is one of the only established risk factors for task-specific focal dystonia. Studies suggest that previous injury, changes in practice routine, and exposure to anti-psychotic drugs (which can cause other types of dystonia) are not major risk factors. Nor does the condition appear to be a form of performance anxiety. Task-specific focal dystonia may be associated with dysfunction in areas of the brain that regulate movement. In particular, researchers have found that at least some cases of the condition are related to malfunction of the basal ganglia, which are structures deep within the brain that help start and control movement. Although genetic factors are almost certainly involved in task-specific focal dystonia, no genes have been clearly associated with the condition. Researchers have looked for mutations in several genes known to be involved in other forms of dystonia, but these genetic changes do not appear to be a major cause of task-specific focal dystonia. Researchers are working to determine which genetic factors are related to this disorder. Most cases of task-specific focal dystonia are sporadic, which means they occur in people with no history of the condition in their family. However, at least 10 percent of affected individuals have a family history of focal dystonia. (For example, writer's cramp and musician's dystonia have been reported to occur in the same family.) The dystonia often appears to have an autosomal dominant pattern of inheritance, based on the observation that some affected people have a parent with the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to task-specific focal dystonia ? | The causes of task-specific focal dystonia are unknown, although the disorder likely results from a combination of genetic and environmental factors. Certain genetic changes probably increase the likelihood of developing this condition, and environmental factors may trigger the onset of symptoms in people who are at risk. It is possible that the different forms of task-specific focal dystonia have different underlying causes. Having a family history of dystonia, particularly focal dystonia, is one of the only established risk factors for task-specific focal dystonia. Studies suggest that previous injury, changes in practice routine, and exposure to anti-psychotic drugs (which can cause other types of dystonia) are not major risk factors. Nor does the condition appear to be a form of performance anxiety. Task-specific focal dystonia may be associated with dysfunction in areas of the brain that regulate movement. In particular, researchers have found that at least some cases of the condition are related to malfunction of the basal ganglia, which are structures deep within the brain that help start and control movement. Although genetic factors are almost certainly involved in task-specific focal dystonia, no genes have been clearly associated with the condition. Researchers have looked for mutations in several genes known to be involved in other forms of dystonia, but these genetic changes do not appear to be a major cause of task-specific focal dystonia. Researchers are working to determine which genetic factors are related to this disorder. |
Task-specific focal dystonia is a movement disorder that interferes with the performance of particular tasks, such as writing, playing a musical instrument, or participating in a sport. Dystonias are a group of movement problems characterized by involuntary, sustained muscle contractions, tremors, and other uncontrolled movements. The term "focal" refers to a type of dystonia that affects a single part of the body, such as the hand or jaw. Researchers have described several forms of task-specific focal dystonia. The most common is writer's cramp, in which muscle cramps or spasms in the hand, wrist, or forearm interfere with holding a pen or pencil. Writer's cramp begins in the hand used for writing (the dominant hand) and is usually limited to that task, but with time it can spread to the other hand and affect other fine-motor activities such as shaving or typing. Musician's dystonia is a form of task-specific focal dystonia characterized by muscle cramps and spasms that occur while playing a musical instrument. This condition can affect amateur or professional musicians, and the location of the dystonia depends on the instrument. Some musicians (such as piano, guitar, and violin players) develop focal hand dystonia, which causes loss of fine-motor control in the hand and wrist muscles. This condition reduces finger coordination, speed, and endurance while playing. Musicians who play woodwind or brass instruments can develop what is known as embouchure dystonia. This condition causes muscle cramps or spasms involving the lips, tongue, or jaw, which prevents normal positioning of the mouth around the instrument's mouthpiece. Musician's dystonia often occurs only when playing a particular instrument. However, over time focal hand dystonia may impair other activities, and embouchure dystonia can worsen to affect eating and speech. Task-specific focal dystonia can affect people who play sports and engage in other occupations involving repetitive, highly practiced movements. For example, some golfers experience involuntary jerking of the wrists during putting, a condition known informally as "the yips." Cramps and spasms of the hand and arm muscles can also affect tennis players, billiards players, dart throwers, and other athletes. Additionally, task-specific dystonia has been reported in tailors, shoemakers, hair stylists, and people who frequently type or use a computer mouse. The abnormal movements associated with task-specific focal dystonia are usually painless, although they can cause anxiety when they interfere with musical performance and other activities. Severe cases can cause professional disability. Task-specific focal dystonia affects an estimated 7 to 69 per million people in the general population. Musician's dystonia that is severe enough to impact performance occurs in about 1 percent of musicians. The causes of task-specific focal dystonia are unknown, although the disorder likely results from a combination of genetic and environmental factors. Certain genetic changes probably increase the likelihood of developing this condition, and environmental factors may trigger the onset of symptoms in people who are at risk. It is possible that the different forms of task-specific focal dystonia have different underlying causes. Having a family history of dystonia, particularly focal dystonia, is one of the only established risk factors for task-specific focal dystonia. Studies suggest that previous injury, changes in practice routine, and exposure to anti-psychotic drugs (which can cause other types of dystonia) are not major risk factors. Nor does the condition appear to be a form of performance anxiety. Task-specific focal dystonia may be associated with dysfunction in areas of the brain that regulate movement. In particular, researchers have found that at least some cases of the condition are related to malfunction of the basal ganglia, which are structures deep within the brain that help start and control movement. Although genetic factors are almost certainly involved in task-specific focal dystonia, no genes have been clearly associated with the condition. Researchers have looked for mutations in several genes known to be involved in other forms of dystonia, but these genetic changes do not appear to be a major cause of task-specific focal dystonia. Researchers are working to determine which genetic factors are related to this disorder. Most cases of task-specific focal dystonia are sporadic, which means they occur in people with no history of the condition in their family. However, at least 10 percent of affected individuals have a family history of focal dystonia. (For example, writer's cramp and musician's dystonia have been reported to occur in the same family.) The dystonia often appears to have an autosomal dominant pattern of inheritance, based on the observation that some affected people have a parent with the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is task-specific focal dystonia inherited ? | Most cases of task-specific focal dystonia are sporadic, which means they occur in people with no history of the condition in their family. However, at least 10 percent of affected individuals have a family history of focal dystonia. (For example, writer's cramp and musician's dystonia have been reported to occur in the same family.) The dystonia often appears to have an autosomal dominant pattern of inheritance, based on the observation that some affected people have a parent with the condition. |
Task-specific focal dystonia is a movement disorder that interferes with the performance of particular tasks, such as writing, playing a musical instrument, or participating in a sport. Dystonias are a group of movement problems characterized by involuntary, sustained muscle contractions, tremors, and other uncontrolled movements. The term "focal" refers to a type of dystonia that affects a single part of the body, such as the hand or jaw. Researchers have described several forms of task-specific focal dystonia. The most common is writer's cramp, in which muscle cramps or spasms in the hand, wrist, or forearm interfere with holding a pen or pencil. Writer's cramp begins in the hand used for writing (the dominant hand) and is usually limited to that task, but with time it can spread to the other hand and affect other fine-motor activities such as shaving or typing. Musician's dystonia is a form of task-specific focal dystonia characterized by muscle cramps and spasms that occur while playing a musical instrument. This condition can affect amateur or professional musicians, and the location of the dystonia depends on the instrument. Some musicians (such as piano, guitar, and violin players) develop focal hand dystonia, which causes loss of fine-motor control in the hand and wrist muscles. This condition reduces finger coordination, speed, and endurance while playing. Musicians who play woodwind or brass instruments can develop what is known as embouchure dystonia. This condition causes muscle cramps or spasms involving the lips, tongue, or jaw, which prevents normal positioning of the mouth around the instrument's mouthpiece. Musician's dystonia often occurs only when playing a particular instrument. However, over time focal hand dystonia may impair other activities, and embouchure dystonia can worsen to affect eating and speech. Task-specific focal dystonia can affect people who play sports and engage in other occupations involving repetitive, highly practiced movements. For example, some golfers experience involuntary jerking of the wrists during putting, a condition known informally as "the yips." Cramps and spasms of the hand and arm muscles can also affect tennis players, billiards players, dart throwers, and other athletes. Additionally, task-specific dystonia has been reported in tailors, shoemakers, hair stylists, and people who frequently type or use a computer mouse. The abnormal movements associated with task-specific focal dystonia are usually painless, although they can cause anxiety when they interfere with musical performance and other activities. Severe cases can cause professional disability. Task-specific focal dystonia affects an estimated 7 to 69 per million people in the general population. Musician's dystonia that is severe enough to impact performance occurs in about 1 percent of musicians. The causes of task-specific focal dystonia are unknown, although the disorder likely results from a combination of genetic and environmental factors. Certain genetic changes probably increase the likelihood of developing this condition, and environmental factors may trigger the onset of symptoms in people who are at risk. It is possible that the different forms of task-specific focal dystonia have different underlying causes. Having a family history of dystonia, particularly focal dystonia, is one of the only established risk factors for task-specific focal dystonia. Studies suggest that previous injury, changes in practice routine, and exposure to anti-psychotic drugs (which can cause other types of dystonia) are not major risk factors. Nor does the condition appear to be a form of performance anxiety. Task-specific focal dystonia may be associated with dysfunction in areas of the brain that regulate movement. In particular, researchers have found that at least some cases of the condition are related to malfunction of the basal ganglia, which are structures deep within the brain that help start and control movement. Although genetic factors are almost certainly involved in task-specific focal dystonia, no genes have been clearly associated with the condition. Researchers have looked for mutations in several genes known to be involved in other forms of dystonia, but these genetic changes do not appear to be a major cause of task-specific focal dystonia. Researchers are working to determine which genetic factors are related to this disorder. Most cases of task-specific focal dystonia are sporadic, which means they occur in people with no history of the condition in their family. However, at least 10 percent of affected individuals have a family history of focal dystonia. (For example, writer's cramp and musician's dystonia have been reported to occur in the same family.) The dystonia often appears to have an autosomal dominant pattern of inheritance, based on the observation that some affected people have a parent with the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for task-specific focal dystonia ? | These resources address the diagnosis or management of task-specific focal dystonia: - Dystonia Medical Research Foundation: How Is Dystonia Diagnosed? - Dystonia Medical Research Foundation: Treatments - Gene Review: Gene Review: Dystonia Overview - Genetic Testing Registry: Focal dystonia - Merck Manual Home Health Handbook: Dystonias These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Bladder cancer is a disease in which certain cells in the bladder become abnormal and multiply uncontrollably to form a tumor. The bladder is a muscular organ in the lower abdomen that stores urine until it can be removed (excreted) from the body. Bladder cancer may cause blood in the urine, pain during urination, frequent urination, the feeling of needing to urinate without being able to, or lower back pain. Many of these signs and symptoms are nonspecific, which means they may occur in multiple disorders. People who have one or more of these nonspecific health problems often do not have bladder cancer, but have another condition such as an infection. Bladder cancer develops when tumors form in the tissue that lines the bladder. There are several types of bladder cancer, categorized by the type of cell in the tissue that becomes cancerous. The most common type is transitional cell carcinoma (also known as urothelial carcinoma); others include squamous cell carcinoma and adenocarcinoma. If the tumor spreads  (metastasizes) beyond the lining of the bladder into nearby tissues or organs, it is known as invasive bladder cancer. In the United States, bladder cancer is the fourth most common type of cancer in men. Bladder cancer occurs four times more often in men than in women, with about 60,000 men and 18,000 women diagnosed with the condition each year. Cancers occur when genetic mutations build up in critical genes, specifically those that control cell growth and division (proliferation) or the repair of damaged DNA. These changes allow cells to grow and divide uncontrollably to form a tumor. In nearly all cases of bladder cancer, these genetic changes are acquired during a person's lifetime and are present only in certain cells in the bladder. These changes, which are called somatic mutations, are not inherited. Somatic mutations in many different genes have been found in bladder cancer cells. It is unclear whether genetic changes that are inherited and present in all of the body's cells (germline mutations) play a significant role in causing bladder cancer. Somatic mutations in the FGFR3, PIK3CA, KDM6A, and TP53 genes are common in bladder cancers. Each of these genes plays a critical role in regulating gene activity and cell growth, ensuring cells do not grow and divide too rapidly or uncontrollably. It is likely that mutations in these genes disrupt normal gene regulation, contributing to the uncontrolled cell growth that can lead to tumor formation in bladder cancer. Mutations in many other genes have been found to be associated with bladder cancer; each of these additional genes is associated with a small percentage of cases. Most of these genes are also involved in regulating the normal activity of genes and the growth of cells. Additionally, deletions of part or all of chromosome 9 are commonly found in bladder cancer. Research shows that several genes that control cell growth and division are located on chromosome 9. It is likely that a loss of one or more of these genes plays a role in the early development and progression of bladder cancer. Researchers have identified many lifestyle and environmental factors that expose individuals to cancer-causing compounds (carcinogens), which increase the rate at which somatic mutations occur, contributing to a person's risk of developing bladder cancer. The greatest risk factor is long-term tobacco smoking. It is estimated that half of people with bladder cancer have a history of tobacco smoking. Other environmental risk factors include chronic bladder inflammation, exposure to certain industrial chemicals, certain herbal medicines common in Asia, a parasitic infection called schistosomiasis, and long-term use of urinary catheters. Additional Information from NCBI Gene: Bladder cancer is typically not inherited. It is usually associated with somatic mutations that occur in certain cells in the bladder during a person's lifetime. In rare families, the risk of bladder cancer is inherited. In these cases, the cancer risk follows an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to increase a person's chance of developing the disease. It is important to note that people inherit an increased risk of cancer, not the disease itself. Not all people who inherit mutations in these genes will develop bladder cancer. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) bladder cancer ? | Bladder cancer is a disease in which certain cells in the bladder become abnormal and multiply without control or order. The bladder is a hollow, muscular organ in the lower abdomen that stores urine until it is ready to be excreted from the body. The most common type of bladder cancer begins in cells lining the inside of the bladder and is called transitional cell carcinoma (TCC). Bladder cancer may cause blood in the urine, pain during urination, frequent urination, or the feeling that one needs to urinate without results. These signs and symptoms are not specific to bladder cancer, however. They also can be caused by noncancerous conditions such as infections. |
Bladder cancer is a disease in which certain cells in the bladder become abnormal and multiply uncontrollably to form a tumor. The bladder is a muscular organ in the lower abdomen that stores urine until it can be removed (excreted) from the body. Bladder cancer may cause blood in the urine, pain during urination, frequent urination, the feeling of needing to urinate without being able to, or lower back pain. Many of these signs and symptoms are nonspecific, which means they may occur in multiple disorders. People who have one or more of these nonspecific health problems often do not have bladder cancer, but have another condition such as an infection. Bladder cancer develops when tumors form in the tissue that lines the bladder. There are several types of bladder cancer, categorized by the type of cell in the tissue that becomes cancerous. The most common type is transitional cell carcinoma (also known as urothelial carcinoma); others include squamous cell carcinoma and adenocarcinoma. If the tumor spreads  (metastasizes) beyond the lining of the bladder into nearby tissues or organs, it is known as invasive bladder cancer. In the United States, bladder cancer is the fourth most common type of cancer in men. Bladder cancer occurs four times more often in men than in women, with about 60,000 men and 18,000 women diagnosed with the condition each year. Cancers occur when genetic mutations build up in critical genes, specifically those that control cell growth and division (proliferation) or the repair of damaged DNA. These changes allow cells to grow and divide uncontrollably to form a tumor. In nearly all cases of bladder cancer, these genetic changes are acquired during a person's lifetime and are present only in certain cells in the bladder. These changes, which are called somatic mutations, are not inherited. Somatic mutations in many different genes have been found in bladder cancer cells. It is unclear whether genetic changes that are inherited and present in all of the body's cells (germline mutations) play a significant role in causing bladder cancer. Somatic mutations in the FGFR3, PIK3CA, KDM6A, and TP53 genes are common in bladder cancers. Each of these genes plays a critical role in regulating gene activity and cell growth, ensuring cells do not grow and divide too rapidly or uncontrollably. It is likely that mutations in these genes disrupt normal gene regulation, contributing to the uncontrolled cell growth that can lead to tumor formation in bladder cancer. Mutations in many other genes have been found to be associated with bladder cancer; each of these additional genes is associated with a small percentage of cases. Most of these genes are also involved in regulating the normal activity of genes and the growth of cells. Additionally, deletions of part or all of chromosome 9 are commonly found in bladder cancer. Research shows that several genes that control cell growth and division are located on chromosome 9. It is likely that a loss of one or more of these genes plays a role in the early development and progression of bladder cancer. Researchers have identified many lifestyle and environmental factors that expose individuals to cancer-causing compounds (carcinogens), which increase the rate at which somatic mutations occur, contributing to a person's risk of developing bladder cancer. The greatest risk factor is long-term tobacco smoking. It is estimated that half of people with bladder cancer have a history of tobacco smoking. Other environmental risk factors include chronic bladder inflammation, exposure to certain industrial chemicals, certain herbal medicines common in Asia, a parasitic infection called schistosomiasis, and long-term use of urinary catheters. Additional Information from NCBI Gene: Bladder cancer is typically not inherited. It is usually associated with somatic mutations that occur in certain cells in the bladder during a person's lifetime. In rare families, the risk of bladder cancer is inherited. In these cases, the cancer risk follows an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to increase a person's chance of developing the disease. It is important to note that people inherit an increased risk of cancer, not the disease itself. Not all people who inherit mutations in these genes will develop bladder cancer. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by bladder cancer ? | In the United States, bladder cancer is the fourth most common type of cancer in men and the ninth most common cancer in women. About 45,000 men and 17,000 women are diagnosed with bladder cancer each year. |
Bladder cancer is a disease in which certain cells in the bladder become abnormal and multiply uncontrollably to form a tumor. The bladder is a muscular organ in the lower abdomen that stores urine until it can be removed (excreted) from the body. Bladder cancer may cause blood in the urine, pain during urination, frequent urination, the feeling of needing to urinate without being able to, or lower back pain. Many of these signs and symptoms are nonspecific, which means they may occur in multiple disorders. People who have one or more of these nonspecific health problems often do not have bladder cancer, but have another condition such as an infection. Bladder cancer develops when tumors form in the tissue that lines the bladder. There are several types of bladder cancer, categorized by the type of cell in the tissue that becomes cancerous. The most common type is transitional cell carcinoma (also known as urothelial carcinoma); others include squamous cell carcinoma and adenocarcinoma. If the tumor spreads  (metastasizes) beyond the lining of the bladder into nearby tissues or organs, it is known as invasive bladder cancer. In the United States, bladder cancer is the fourth most common type of cancer in men. Bladder cancer occurs four times more often in men than in women, with about 60,000 men and 18,000 women diagnosed with the condition each year. Cancers occur when genetic mutations build up in critical genes, specifically those that control cell growth and division (proliferation) or the repair of damaged DNA. These changes allow cells to grow and divide uncontrollably to form a tumor. In nearly all cases of bladder cancer, these genetic changes are acquired during a person's lifetime and are present only in certain cells in the bladder. These changes, which are called somatic mutations, are not inherited. Somatic mutations in many different genes have been found in bladder cancer cells. It is unclear whether genetic changes that are inherited and present in all of the body's cells (germline mutations) play a significant role in causing bladder cancer. Somatic mutations in the FGFR3, PIK3CA, KDM6A, and TP53 genes are common in bladder cancers. Each of these genes plays a critical role in regulating gene activity and cell growth, ensuring cells do not grow and divide too rapidly or uncontrollably. It is likely that mutations in these genes disrupt normal gene regulation, contributing to the uncontrolled cell growth that can lead to tumor formation in bladder cancer. Mutations in many other genes have been found to be associated with bladder cancer; each of these additional genes is associated with a small percentage of cases. Most of these genes are also involved in regulating the normal activity of genes and the growth of cells. Additionally, deletions of part or all of chromosome 9 are commonly found in bladder cancer. Research shows that several genes that control cell growth and division are located on chromosome 9. It is likely that a loss of one or more of these genes plays a role in the early development and progression of bladder cancer. Researchers have identified many lifestyle and environmental factors that expose individuals to cancer-causing compounds (carcinogens), which increase the rate at which somatic mutations occur, contributing to a person's risk of developing bladder cancer. The greatest risk factor is long-term tobacco smoking. It is estimated that half of people with bladder cancer have a history of tobacco smoking. Other environmental risk factors include chronic bladder inflammation, exposure to certain industrial chemicals, certain herbal medicines common in Asia, a parasitic infection called schistosomiasis, and long-term use of urinary catheters. Additional Information from NCBI Gene: Bladder cancer is typically not inherited. It is usually associated with somatic mutations that occur in certain cells in the bladder during a person's lifetime. In rare families, the risk of bladder cancer is inherited. In these cases, the cancer risk follows an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to increase a person's chance of developing the disease. It is important to note that people inherit an increased risk of cancer, not the disease itself. Not all people who inherit mutations in these genes will develop bladder cancer. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to bladder cancer ? | As with most cancers, the exact causes of bladder cancer are not known; however, many risk factors are associated with this disease. Many of the major risk factors are environmental, such as smoking and exposure to certain industrial chemicals. Studies suggest that chronic bladder inflammation, a parasitic infection called schistosomiasis, and some medications used to treat cancer are other environmental risk factors associated with bladder cancer. Genetic factors are also likely to play an important role in determining bladder cancer risk. Researchers have studied the effects of mutations in several genes, including FGFR3, RB1, HRAS, TP53, and TSC1, on the formation and growth of bladder tumors. Each of these genes plays a critical role in regulating cell division by preventing cells from dividing too rapidly or in an uncontrolled way. Alterations in these genes may help explain why some bladder cancers grow and spread more rapidly than others. Deletions of part or all of chromosome 9 are common events in bladder tumors. Researchers believe that several genes that control cell growth and division are probably located on chromosome 9. They are working to determine whether a loss of these genes plays a role in the development and progression of bladder cancer. Most of the genetic changes associated with bladder cancer develop in bladder tissue during a person's lifetime, rather than being inherited from a parent. Some people, however, appear to inherit a reduced ability to break down certain chemicals, which makes them more sensitive to the cancer-causing effects of tobacco smoke and industrial chemicals. |
Bladder cancer is a disease in which certain cells in the bladder become abnormal and multiply uncontrollably to form a tumor. The bladder is a muscular organ in the lower abdomen that stores urine until it can be removed (excreted) from the body. Bladder cancer may cause blood in the urine, pain during urination, frequent urination, the feeling of needing to urinate without being able to, or lower back pain. Many of these signs and symptoms are nonspecific, which means they may occur in multiple disorders. People who have one or more of these nonspecific health problems often do not have bladder cancer, but have another condition such as an infection. Bladder cancer develops when tumors form in the tissue that lines the bladder. There are several types of bladder cancer, categorized by the type of cell in the tissue that becomes cancerous. The most common type is transitional cell carcinoma (also known as urothelial carcinoma); others include squamous cell carcinoma and adenocarcinoma. If the tumor spreads  (metastasizes) beyond the lining of the bladder into nearby tissues or organs, it is known as invasive bladder cancer. In the United States, bladder cancer is the fourth most common type of cancer in men. Bladder cancer occurs four times more often in men than in women, with about 60,000 men and 18,000 women diagnosed with the condition each year. Cancers occur when genetic mutations build up in critical genes, specifically those that control cell growth and division (proliferation) or the repair of damaged DNA. These changes allow cells to grow and divide uncontrollably to form a tumor. In nearly all cases of bladder cancer, these genetic changes are acquired during a person's lifetime and are present only in certain cells in the bladder. These changes, which are called somatic mutations, are not inherited. Somatic mutations in many different genes have been found in bladder cancer cells. It is unclear whether genetic changes that are inherited and present in all of the body's cells (germline mutations) play a significant role in causing bladder cancer. Somatic mutations in the FGFR3, PIK3CA, KDM6A, and TP53 genes are common in bladder cancers. Each of these genes plays a critical role in regulating gene activity and cell growth, ensuring cells do not grow and divide too rapidly or uncontrollably. It is likely that mutations in these genes disrupt normal gene regulation, contributing to the uncontrolled cell growth that can lead to tumor formation in bladder cancer. Mutations in many other genes have been found to be associated with bladder cancer; each of these additional genes is associated with a small percentage of cases. Most of these genes are also involved in regulating the normal activity of genes and the growth of cells. Additionally, deletions of part or all of chromosome 9 are commonly found in bladder cancer. Research shows that several genes that control cell growth and division are located on chromosome 9. It is likely that a loss of one or more of these genes plays a role in the early development and progression of bladder cancer. Researchers have identified many lifestyle and environmental factors that expose individuals to cancer-causing compounds (carcinogens), which increase the rate at which somatic mutations occur, contributing to a person's risk of developing bladder cancer. The greatest risk factor is long-term tobacco smoking. It is estimated that half of people with bladder cancer have a history of tobacco smoking. Other environmental risk factors include chronic bladder inflammation, exposure to certain industrial chemicals, certain herbal medicines common in Asia, a parasitic infection called schistosomiasis, and long-term use of urinary catheters. Additional Information from NCBI Gene: Bladder cancer is typically not inherited. It is usually associated with somatic mutations that occur in certain cells in the bladder during a person's lifetime. In rare families, the risk of bladder cancer is inherited. In these cases, the cancer risk follows an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to increase a person's chance of developing the disease. It is important to note that people inherit an increased risk of cancer, not the disease itself. Not all people who inherit mutations in these genes will develop bladder cancer. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is bladder cancer inherited ? | Bladder cancer is typically not inherited. Most often, tumors result from genetic mutations that occur in bladder cells during a person's lifetime. These noninherited genetic changes are called somatic mutations. |
Bladder cancer is a disease in which certain cells in the bladder become abnormal and multiply uncontrollably to form a tumor. The bladder is a muscular organ in the lower abdomen that stores urine until it can be removed (excreted) from the body. Bladder cancer may cause blood in the urine, pain during urination, frequent urination, the feeling of needing to urinate without being able to, or lower back pain. Many of these signs and symptoms are nonspecific, which means they may occur in multiple disorders. People who have one or more of these nonspecific health problems often do not have bladder cancer, but have another condition such as an infection. Bladder cancer develops when tumors form in the tissue that lines the bladder. There are several types of bladder cancer, categorized by the type of cell in the tissue that becomes cancerous. The most common type is transitional cell carcinoma (also known as urothelial carcinoma); others include squamous cell carcinoma and adenocarcinoma. If the tumor spreads  (metastasizes) beyond the lining of the bladder into nearby tissues or organs, it is known as invasive bladder cancer. In the United States, bladder cancer is the fourth most common type of cancer in men. Bladder cancer occurs four times more often in men than in women, with about 60,000 men and 18,000 women diagnosed with the condition each year. Cancers occur when genetic mutations build up in critical genes, specifically those that control cell growth and division (proliferation) or the repair of damaged DNA. These changes allow cells to grow and divide uncontrollably to form a tumor. In nearly all cases of bladder cancer, these genetic changes are acquired during a person's lifetime and are present only in certain cells in the bladder. These changes, which are called somatic mutations, are not inherited. Somatic mutations in many different genes have been found in bladder cancer cells. It is unclear whether genetic changes that are inherited and present in all of the body's cells (germline mutations) play a significant role in causing bladder cancer. Somatic mutations in the FGFR3, PIK3CA, KDM6A, and TP53 genes are common in bladder cancers. Each of these genes plays a critical role in regulating gene activity and cell growth, ensuring cells do not grow and divide too rapidly or uncontrollably. It is likely that mutations in these genes disrupt normal gene regulation, contributing to the uncontrolled cell growth that can lead to tumor formation in bladder cancer. Mutations in many other genes have been found to be associated with bladder cancer; each of these additional genes is associated with a small percentage of cases. Most of these genes are also involved in regulating the normal activity of genes and the growth of cells. Additionally, deletions of part or all of chromosome 9 are commonly found in bladder cancer. Research shows that several genes that control cell growth and division are located on chromosome 9. It is likely that a loss of one or more of these genes plays a role in the early development and progression of bladder cancer. Researchers have identified many lifestyle and environmental factors that expose individuals to cancer-causing compounds (carcinogens), which increase the rate at which somatic mutations occur, contributing to a person's risk of developing bladder cancer. The greatest risk factor is long-term tobacco smoking. It is estimated that half of people with bladder cancer have a history of tobacco smoking. Other environmental risk factors include chronic bladder inflammation, exposure to certain industrial chemicals, certain herbal medicines common in Asia, a parasitic infection called schistosomiasis, and long-term use of urinary catheters. Additional Information from NCBI Gene: Bladder cancer is typically not inherited. It is usually associated with somatic mutations that occur in certain cells in the bladder during a person's lifetime. In rare families, the risk of bladder cancer is inherited. In these cases, the cancer risk follows an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to increase a person's chance of developing the disease. It is important to note that people inherit an increased risk of cancer, not the disease itself. Not all people who inherit mutations in these genes will develop bladder cancer. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for bladder cancer ? | These resources address the diagnosis or management of bladder cancer: - Genetic Testing Registry: Malignant tumor of urinary bladder - MedlinePlus Encyclopedia: Bladder Cancer These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
UV-sensitive syndrome is a condition that is characterized by sensitivity to the ultraviolet (UV) rays in sunlight. Even a small amount of sun exposure can cause a sunburn in affected individuals. In addition, these individuals can have freckles, dryness, or changes in coloring (pigmentation) on sun-exposed areas of skin after repeated exposure. Some people with UV-sensitive syndrome have small clusters of enlarged blood vessels just under the skin (telangiectasia), usually on the cheeks and nose. Although UV exposure can cause skin cancers, people with UV-sensitive syndrome do not have an increased risk of developing these forms of cancer compared with the general population. UV-sensitive syndrome appears to be a rare condition; only a small number of affected individuals have been reported in the scientific literature. However, this condition may be underdiagnosed. UV-sensitive syndrome can result from mutations in the ERCC6 gene (also known as the CSB gene), the ERCC8 gene (also known as the CSA gene), or the UVSSA gene. These genes provide instructions for making proteins that are involved in repairing damaged DNA. DNA can be damaged by UV rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. Cells are usually able to fix DNA damage before it causes problems. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death. Cells have several mechanisms to correct DNA damage. The CSB, CSA, and UVSSA proteins are involved in one mechanism that repairs damaged DNA within active genes (those genes undergoing gene transcription, the first step in protein production). When DNA in active genes is damaged, the enzyme that carries out gene transcription (RNA polymerase) gets stuck, and the process stalls. Researchers think that the CSB, CSA, and UVSSA proteins help remove RNA polymerase from the damaged site, so the DNA can be repaired. Mutations in the ERCC6, ERCC8, or UVSSA genes lead to the production of an abnormal protein or the loss of the protein. If any of these proteins is not functioning normally, skin cells cannot repair DNA damage caused by UV rays, and transcription of damaged genes is blocked. However, it is unclear exactly how abnormalities in these proteins cause the signs and symptoms of UV-sensitive syndrome. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) UV-sensitive syndrome ? | UV-sensitive syndrome is a condition that is characterized by sensitivity to the ultraviolet (UV) rays in sunlight. Even a small amount of sun exposure can cause a sunburn in affected individuals. In addition, these individuals can have freckles, dryness, or changes in coloring (pigmentation) on sun-exposed areas of skin after repeated exposure. Some people with UV-sensitive syndrome have small clusters of enlarged blood vessels just under the skin (telangiectasia), usually on the cheeks and nose. Although UV exposure can cause skin cancers, people with UV-sensitive syndrome do not have an increased risk of developing these forms of cancer compared with the general population. |
UV-sensitive syndrome is a condition that is characterized by sensitivity to the ultraviolet (UV) rays in sunlight. Even a small amount of sun exposure can cause a sunburn in affected individuals. In addition, these individuals can have freckles, dryness, or changes in coloring (pigmentation) on sun-exposed areas of skin after repeated exposure. Some people with UV-sensitive syndrome have small clusters of enlarged blood vessels just under the skin (telangiectasia), usually on the cheeks and nose. Although UV exposure can cause skin cancers, people with UV-sensitive syndrome do not have an increased risk of developing these forms of cancer compared with the general population. UV-sensitive syndrome appears to be a rare condition; only a small number of affected individuals have been reported in the scientific literature. However, this condition may be underdiagnosed. UV-sensitive syndrome can result from mutations in the ERCC6 gene (also known as the CSB gene), the ERCC8 gene (also known as the CSA gene), or the UVSSA gene. These genes provide instructions for making proteins that are involved in repairing damaged DNA. DNA can be damaged by UV rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. Cells are usually able to fix DNA damage before it causes problems. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death. Cells have several mechanisms to correct DNA damage. The CSB, CSA, and UVSSA proteins are involved in one mechanism that repairs damaged DNA within active genes (those genes undergoing gene transcription, the first step in protein production). When DNA in active genes is damaged, the enzyme that carries out gene transcription (RNA polymerase) gets stuck, and the process stalls. Researchers think that the CSB, CSA, and UVSSA proteins help remove RNA polymerase from the damaged site, so the DNA can be repaired. Mutations in the ERCC6, ERCC8, or UVSSA genes lead to the production of an abnormal protein or the loss of the protein. If any of these proteins is not functioning normally, skin cells cannot repair DNA damage caused by UV rays, and transcription of damaged genes is blocked. However, it is unclear exactly how abnormalities in these proteins cause the signs and symptoms of UV-sensitive syndrome. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by UV-sensitive syndrome ? | UV-sensitive syndrome appears to be a rare condition; only a small number of affected individuals have been reported in the scientific literature. However, this condition may be underdiagnosed. |
UV-sensitive syndrome is a condition that is characterized by sensitivity to the ultraviolet (UV) rays in sunlight. Even a small amount of sun exposure can cause a sunburn in affected individuals. In addition, these individuals can have freckles, dryness, or changes in coloring (pigmentation) on sun-exposed areas of skin after repeated exposure. Some people with UV-sensitive syndrome have small clusters of enlarged blood vessels just under the skin (telangiectasia), usually on the cheeks and nose. Although UV exposure can cause skin cancers, people with UV-sensitive syndrome do not have an increased risk of developing these forms of cancer compared with the general population. UV-sensitive syndrome appears to be a rare condition; only a small number of affected individuals have been reported in the scientific literature. However, this condition may be underdiagnosed. UV-sensitive syndrome can result from mutations in the ERCC6 gene (also known as the CSB gene), the ERCC8 gene (also known as the CSA gene), or the UVSSA gene. These genes provide instructions for making proteins that are involved in repairing damaged DNA. DNA can be damaged by UV rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. Cells are usually able to fix DNA damage before it causes problems. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death. Cells have several mechanisms to correct DNA damage. The CSB, CSA, and UVSSA proteins are involved in one mechanism that repairs damaged DNA within active genes (those genes undergoing gene transcription, the first step in protein production). When DNA in active genes is damaged, the enzyme that carries out gene transcription (RNA polymerase) gets stuck, and the process stalls. Researchers think that the CSB, CSA, and UVSSA proteins help remove RNA polymerase from the damaged site, so the DNA can be repaired. Mutations in the ERCC6, ERCC8, or UVSSA genes lead to the production of an abnormal protein or the loss of the protein. If any of these proteins is not functioning normally, skin cells cannot repair DNA damage caused by UV rays, and transcription of damaged genes is blocked. However, it is unclear exactly how abnormalities in these proteins cause the signs and symptoms of UV-sensitive syndrome. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the genetic changes related to UV-sensitive syndrome ? | UV-sensitive syndrome can result from mutations in the ERCC6 gene (also known as the CSB gene), the ERCC8 gene (also known as the CSA gene), or the UVSSA gene. These genes provide instructions for making proteins that are involved in repairing damaged DNA. DNA can be damaged by UV rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. Cells are usually able to fix DNA damage before it causes problems. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death. Cells have several mechanisms to correct DNA damage. The CSB, CSA, and UVSSA proteins are involved in one mechanism that repairs damaged DNA within active genes (those genes undergoing gene transcription, the first step in protein production). When DNA in active genes is damaged, the enzyme that carries out gene transcription (RNA polymerase) gets stuck, and the process stalls. Researchers think that the CSB, CSA, and UVSSA proteins help remove RNA polymerase from the damaged site, so the DNA can be repaired. Mutations in the ERCC6, ERCC8, or UVSSA genes lead to the production of an abnormal protein or the loss of the protein. If any of these proteins is not functioning normally, skin cells cannot repair DNA damage caused by UV rays, and transcription of damaged genes is blocked. However, it is unclear exactly how abnormalities in these proteins cause the signs and symptoms of UV-sensitive syndrome. |
UV-sensitive syndrome is a condition that is characterized by sensitivity to the ultraviolet (UV) rays in sunlight. Even a small amount of sun exposure can cause a sunburn in affected individuals. In addition, these individuals can have freckles, dryness, or changes in coloring (pigmentation) on sun-exposed areas of skin after repeated exposure. Some people with UV-sensitive syndrome have small clusters of enlarged blood vessels just under the skin (telangiectasia), usually on the cheeks and nose. Although UV exposure can cause skin cancers, people with UV-sensitive syndrome do not have an increased risk of developing these forms of cancer compared with the general population. UV-sensitive syndrome appears to be a rare condition; only a small number of affected individuals have been reported in the scientific literature. However, this condition may be underdiagnosed. UV-sensitive syndrome can result from mutations in the ERCC6 gene (also known as the CSB gene), the ERCC8 gene (also known as the CSA gene), or the UVSSA gene. These genes provide instructions for making proteins that are involved in repairing damaged DNA. DNA can be damaged by UV rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. Cells are usually able to fix DNA damage before it causes problems. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death. Cells have several mechanisms to correct DNA damage. The CSB, CSA, and UVSSA proteins are involved in one mechanism that repairs damaged DNA within active genes (those genes undergoing gene transcription, the first step in protein production). When DNA in active genes is damaged, the enzyme that carries out gene transcription (RNA polymerase) gets stuck, and the process stalls. Researchers think that the CSB, CSA, and UVSSA proteins help remove RNA polymerase from the damaged site, so the DNA can be repaired. Mutations in the ERCC6, ERCC8, or UVSSA genes lead to the production of an abnormal protein or the loss of the protein. If any of these proteins is not functioning normally, skin cells cannot repair DNA damage caused by UV rays, and transcription of damaged genes is blocked. However, it is unclear exactly how abnormalities in these proteins cause the signs and symptoms of UV-sensitive syndrome. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | Is UV-sensitive syndrome inherited ? | This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. |
UV-sensitive syndrome is a condition that is characterized by sensitivity to the ultraviolet (UV) rays in sunlight. Even a small amount of sun exposure can cause a sunburn in affected individuals. In addition, these individuals can have freckles, dryness, or changes in coloring (pigmentation) on sun-exposed areas of skin after repeated exposure. Some people with UV-sensitive syndrome have small clusters of enlarged blood vessels just under the skin (telangiectasia), usually on the cheeks and nose. Although UV exposure can cause skin cancers, people with UV-sensitive syndrome do not have an increased risk of developing these forms of cancer compared with the general population. UV-sensitive syndrome appears to be a rare condition; only a small number of affected individuals have been reported in the scientific literature. However, this condition may be underdiagnosed. UV-sensitive syndrome can result from mutations in the ERCC6 gene (also known as the CSB gene), the ERCC8 gene (also known as the CSA gene), or the UVSSA gene. These genes provide instructions for making proteins that are involved in repairing damaged DNA. DNA can be damaged by UV rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. Cells are usually able to fix DNA damage before it causes problems. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death. Cells have several mechanisms to correct DNA damage. The CSB, CSA, and UVSSA proteins are involved in one mechanism that repairs damaged DNA within active genes (those genes undergoing gene transcription, the first step in protein production). When DNA in active genes is damaged, the enzyme that carries out gene transcription (RNA polymerase) gets stuck, and the process stalls. Researchers think that the CSB, CSA, and UVSSA proteins help remove RNA polymerase from the damaged site, so the DNA can be repaired. Mutations in the ERCC6, ERCC8, or UVSSA genes lead to the production of an abnormal protein or the loss of the protein. If any of these proteins is not functioning normally, skin cells cannot repair DNA damage caused by UV rays, and transcription of damaged genes is blocked. However, it is unclear exactly how abnormalities in these proteins cause the signs and symptoms of UV-sensitive syndrome. This condition is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What are the treatments for UV-sensitive syndrome ? | These resources address the diagnosis or management of UV-sensitive syndrome: - Genetic Testing Registry: UV-sensitive syndrome - Genetic Testing Registry: UV-sensitive syndrome 2 - Genetic Testing Registry: UV-sensitive syndrome 3 - Merck Manual Home Health Edition: Sunburn - World Health Organization: Sun Protection These resources from MedlinePlus offer information about the diagnosis and management of various health conditions: - Diagnostic Tests - Drug Therapy - Surgery and Rehabilitation - Genetic Counseling - Palliative Care |
Hyperferritinemia-cataract syndrome is a disorder characterized by an excess of an iron storage protein called ferritin in the blood (hyperferritinemia) and tissues of the body. A buildup of this protein begins early in life, leading to clouding of the lenses of the eyes (cataracts). In affected individuals, cataracts usually develop in infancy, rather than after age 60 as typically occurs in the general population. Cataracts that are not removed surgically cause progressive dimming and blurriness of vision because the clouded lenses reduce and distort incoming light. Although the hyperferritinemia in this disorder does not usually cause any health problems other than cataracts, the elevated ferritin levels in the blood can be mistaken for a sign of certain liver disorders. These conditions result in excess iron in the body and may be treated by blood-drawing. However, individuals with hyperferritinemia-cataract syndrome do not have an excess of iron, and with repeated blood draws will develop reduced iron levels leading to a low number of red blood cells (anemia). Therefore, correct diagnosis of hyperferritinemia-cataract syndrome is important to avoid unnecessary treatments or invasive test procedures such as liver biopsies. Hyperferritinemia-cataract syndrome has been estimated to occur in 1 in 200,000 individuals. Hyperferritinemia-cataract syndrome is caused by mutations in the FTL gene. This gene provides instructions for making the ferritin light chain, which is one part (subunit) of the protein ferritin. Ferritin is made up of 24 subunits formed into a hollow spherical molecule. The 24 subunits consist of varying numbers of the ferritin light chain and another subunit called the ferritin heavy chain, which is produced from another gene. The proportion of the two subunits varies in different tissues. Ferritin stores and releases iron in cells. Each ferritin molecule can hold as many as 4,500 iron atoms inside its spherical structure. This storage capacity allows ferritin to regulate the amount of iron in cells and tissues. The mutations that cause hyperferritinemia-cataract syndrome are found in a segment of the gene called the iron responsive element (IRE). The IRE normally can attach (bind) to a protein called the iron regulatory protein (IRP). When this binding occurs, the activity (expression) of the FTL gene is stopped to prevent too much ferritin light chain from being produced. This normally occurs when iron levels are low, because under those circumstances less ferritin is needed to store the iron. Mutations in the IRE segment of the FTL gene prevent it from binding with IRP, interfering with the mechanism by which ferritin production is matched to iron levels and resulting in excess ferritin being formed. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | What is (are) hyperferritinemia-cataract syndrome ? | Hyperferritinemia-cataract syndrome is a disorder characterized by an excess of an iron storage protein called ferritin in the blood (hyperferritinemia) and tissues of the body. A buildup of this protein begins early in life, leading to clouding of the lenses of the eyes (cataracts). In affected individuals, cataracts usually develop in infancy, rather than after age 60 as typically occurs in the general population. Cataracts that are not removed surgically cause progressive dimming and blurriness of vision because the clouded lenses reduce and distort incoming light. Although the hyperferritinemia in this disorder does not usually cause any health problems other than cataracts, the elevated ferritin levels in the blood can be mistaken for a sign of certain liver disorders. These conditions result in excess iron in the body and may be treated by blood-drawing. However, individuals with hyperferritinemia-cataract syndrome do not have an excess of iron, and with repeated blood draws will develop reduced iron levels leading to a low number of red blood cells (anemia). Therefore, correct diagnosis of hyperferritinemia-cataract syndrome is important to avoid unnecessary treatments or invasive test procedures such as liver biopsies. |
Hyperferritinemia-cataract syndrome is a disorder characterized by an excess of an iron storage protein called ferritin in the blood (hyperferritinemia) and tissues of the body. A buildup of this protein begins early in life, leading to clouding of the lenses of the eyes (cataracts). In affected individuals, cataracts usually develop in infancy, rather than after age 60 as typically occurs in the general population. Cataracts that are not removed surgically cause progressive dimming and blurriness of vision because the clouded lenses reduce and distort incoming light. Although the hyperferritinemia in this disorder does not usually cause any health problems other than cataracts, the elevated ferritin levels in the blood can be mistaken for a sign of certain liver disorders. These conditions result in excess iron in the body and may be treated by blood-drawing. However, individuals with hyperferritinemia-cataract syndrome do not have an excess of iron, and with repeated blood draws will develop reduced iron levels leading to a low number of red blood cells (anemia). Therefore, correct diagnosis of hyperferritinemia-cataract syndrome is important to avoid unnecessary treatments or invasive test procedures such as liver biopsies. Hyperferritinemia-cataract syndrome has been estimated to occur in 1 in 200,000 individuals. Hyperferritinemia-cataract syndrome is caused by mutations in the FTL gene. This gene provides instructions for making the ferritin light chain, which is one part (subunit) of the protein ferritin. Ferritin is made up of 24 subunits formed into a hollow spherical molecule. The 24 subunits consist of varying numbers of the ferritin light chain and another subunit called the ferritin heavy chain, which is produced from another gene. The proportion of the two subunits varies in different tissues. Ferritin stores and releases iron in cells. Each ferritin molecule can hold as many as 4,500 iron atoms inside its spherical structure. This storage capacity allows ferritin to regulate the amount of iron in cells and tissues. The mutations that cause hyperferritinemia-cataract syndrome are found in a segment of the gene called the iron responsive element (IRE). The IRE normally can attach (bind) to a protein called the iron regulatory protein (IRP). When this binding occurs, the activity (expression) of the FTL gene is stopped to prevent too much ferritin light chain from being produced. This normally occurs when iron levels are low, because under those circumstances less ferritin is needed to store the iron. Mutations in the IRE segment of the FTL gene prevent it from binding with IRP, interfering with the mechanism by which ferritin production is matched to iron levels and resulting in excess ferritin being formed. This condition is inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health. | How many people are affected by hyperferritinemia-cataract syndrome ? | Hyperferritinemia-cataract syndrome has been estimated to occur in 1 in 200,000 individuals. |
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