Number of glucocorticoid receptors in lymphocytes and their sensitivity to hormone action .

Number of <protein>glucocorticoid receptors</protein> in <cell_type>lymphocytes</cell_type> and their sensitivity to hormone action .


The study demonstrated a decreased level of glucocorticoid receptors ( GR ) in peripheral blood lymphocytes from hypercholesterolemic subjects , and an elevated level in patients with acute myocardial infarction .

The study demonstrated a decreased level of <protein>glucocorticoid receptors</protein> ( <protein>GR</protein> ) in <cell_type>peripheral blood lymphocytes</cell_type> from hypercholesterolemic subjects , and an elevated level in patients with acute myocardial infarction .


In the lymphocytes with a high GR number , dexamethasone inhibited [ 3H ] -thymidine and [ 3H ] -acetate incorporation into DNA and cholesterol , respectively , in the same manner as in the control cells .

In the <cell_type>lymphocytes</cell_type> with a high <protein>GR</protein> number , dexamethasone inhibited [ 3H ] -thymidine and [ 3H ] -acetate incorporation into DNA and cholesterol , respectively , in the same manner as in the <cell_type>control cells</cell_type> .


On the other hand , a decreased GR number resulted in a less efficient dexamethasone inhibition of the incorporation of labeled compounds .

On the other hand , a decreased <protein>GR</protein> number resulted in a less efficient dexamethasone inhibition of the incorporation of labeled compounds .


These data showed that the sensitivity of lymphocytes to glucocorticoids changed only with a decrease of GR level .

These data showed that the sensitivity of <cell_type>lymphocytes</cell_type> to glucocorticoids changed only with a decrease of <protein>GR</protein> level .


[ 1 , 25-Dihydroxyvitamin D3 receptors in lymphocytes and T- and B-lymphocyte count in patients with glomerulonephritis ]

[ <protein>1 , 25-Dihydroxyvitamin D3 receptors</protein> in <cell_type>lymphocytes</cell_type> and <cell_type>T- and B-lymphocyte</cell_type> count in patients with glomerulonephritis ]


Content of receptors to hormonal form of vitamin D3 , 1.25 ( OH ) 2D3 , constituted 27.3 fmole/mg of protein in lymphocytes of peripheric blood of children with glomerulonephritis .

Content of receptors to hormonal form of vitamin D3 , 1.25 ( OH ) 2D3 , constituted 27.3 fmole/mg of protein in <cell_type>lymphocytes</cell_type> of peripheric blood of children with glomerulonephritis .


In the patients concentration of total and ionized form of Ca2+ was decreased down to 2.04 mmole/L and 1.09 mmole/L , respectively , while an increase in parathormone ( PTH ) by 36 % and a distinct decrease in 25 ( OH ) D concentration ( lower than 1.25 ng/ml ) was found in blood ; content of cAMP was also decreased in lymphocytes by 33 % .


At the same time , total content of T lymphocytes was decreased 1.5-fold in peripheric blood .

At the same time , total content of <cell_type>T lymphocytes</cell_type> was decreased 1.5-fold in peripheric blood .


Treatment with I-hydroxyvitamin D3 ( 1-1.5 mg daily , within 4 weeks ) led to normalization of total and ionized form of Ca2+ and of 25 ( OH ) D , but did not affect the PTH content in blood .


Concentration of the receptors to 1.25 ( OH ) 2D3 was elevated up to 39.7 fmole/mg after I week of the treatment , whereas it was decreased to the initial level 24.8 fmole/mg within 4 weeks ; simultaneous alteration in the cAMP content was observed in lymphocytes .

Concentration of the <protein>receptors</protein> to 1.25 ( OH ) 2D3 was elevated up to 39.7 fmole/mg after I week of the treatment , whereas it was decreased to the initial level 24.8 fmole/mg within 4 weeks ; simultaneous alteration in the cAMP content was observed in <cell_type>lymphocytes</cell_type> .


Treatment with 1- ( OH ) D3 normalized also the T lymphocytes content in peripheric blood .

Treatment with 1- ( OH ) D3 normalized also the <cell_type>T lymphocytes</cell_type> content in peripheric blood .


The data obtained suggest that under conditions of glomerulonephritis only high content of receptors to 1.25 ( OH ) 2D3 in lymphocytes enabled to perform the cell response to the hormone effect .

The data obtained suggest that under conditions of glomerulonephritis only high content of <protein>receptors</protein> to 1.25 ( OH ) 2D3 in <cell_type>lymphocytes</cell_type> enabled to perform the cell response to the hormone effect .


Tumor and serum beta-2-microglobulin expression in women with breast cancer .


To investigate whether the tumor expression of beta-2-microglobulin ( beta 2-M ) could serve as a marker of tumor biologic behavior , the authors studied specimens of breast carcinomas from 60 consecutive female patients .

To investigate whether the <cell_type>tumor</cell_type> expression of <protein>beta-2-microglobulin</protein> ( <protein>beta 2-M</protein> ) could serve as a marker of tumor biologic behavior , the authors studied specimens of <cell_type>breast carcinomas</cell_type> from 60 consecutive female patients .


Presence of beta 2-M was analyzed by immunohistochemistry .

Presence of <protein>beta 2-M</protein> was analyzed by immunohistochemistry .


No significant correlations were found between tumor beta 2-M expression and several histologic attributes such as type , histologic and nuclear grades , mitotic index , necrosis , vascular invasion , and lymphocytic infiltration .

No significant correlations were found between <protein>tumor beta 2-M</protein> expression and several histologic attributes such as type , histologic and nuclear grades , mitotic index , necrosis , vascular invasion , and lymphocytic infiltration .


Likewise , beta 2-M was not associated with markers of disease extension such as TNM , ( UICC , classification of malignant tumors ) staging and axillary lymph node involvement or with estrogen , progesterone , and glucocorticoid receptor levels .

Likewise , <protein>beta 2-M</protein> was not associated with markers of disease extension such as TNM , ( UICC , classification of <cell_type>malignant tumors</cell_type> ) staging and axillary lymph node involvement or with estrogen , progesterone , and glucocorticoid receptor levels .


However , there was a significantly positive association between tumor beta 2-M expression and the degree of lymphocytic infiltration in the tumor tissue .

However , there was a significantly positive association between <protein>tumor beta 2-M</protein> expression and the degree of lymphocytic infiltration in the tumor tissue .


Beta 2-M serum levels were determined by an enzyme-linked immunosorbent assay in samples from 22 of the above women .

<protein>Beta 2-M</protein> serum levels were determined by an enzyme-linked immunosorbent assay in samples from 22 of the above women .


Although some of the highest values had been obtained in women with larger ( T4 ) primary tumors , the authors failed to detect any statistical relationship between beta 2-M expression in the tumor with serum levels or between serum beta 2-M and the above histologic , laboratory , and clinical factors .

Although some of the highest values had been obtained in women with larger ( T4 ) primary tumors , the authors failed to detect any statistical relationship between <protein>beta 2-M</protein> expression in the tumor with serum levels or between <protein>serum beta 2-M</protein> and the above histologic , laboratory , and clinical factors .


[ Preliminary observation of level free-form E receptor levels in serum of normal childbearing-aged and pregnant women ]

[ Preliminary observation of level <protein>free-form E receptor</protein> levels in serum of normal childbearing-aged and pregnant women ]


In 137 cases of childbearing-aged and pregnant women , free form E receptor levels ( sE ) in serum were measured by ELISA .

In 137 cases of childbearing-aged and pregnant women , <protein>free form E receptor</protein> levels ( <protein>sE</protein> ) in serum were measured by ELISA .


The level of sE was significantly decreased during the first trimester , slightly higher in the second trimester , and recovered to normal in the third trimester .

The level of <protein>sE</protein> was significantly decreased during the first trimester , slightly higher in the second trimester , and recovered to normal in the third trimester .


The level remained lower in 29 PIH women but appeared higher in overdue pregnancies as compared with the normal 3rd trimester range .


The results indicate that there is a relationship between a change in T cell function and pregnancy .

The results indicate that there is a relationship between a change in <cell_type>T cell</cell_type> function and pregnancy .


Kappa B-specific DNA binding proteins : role in the regulation of human interleukin-2 gene expression .

<protein>Kappa B-specific DNA binding proteins</protein> : role in the regulation of <dna>human interleukin-2 gene</dna> expression .


Transcriptional activation of the human interleukin-2 ( IL-2 ) gene , like induction of the IL-2 receptor alpha ( IL-2R alpha ) gene and the type 1 human immunodeficiency virus ( HIV-1 ) , is shown to be modulated by a kappa B-like enhancer element .

Transcriptional activation of the <dna>human interleukin-2 ( IL-2 ) gene</dna> , like induction of the <dna>IL-2 receptor alpha ( IL-2R alpha ) gene</dna> and the type 1 human immunodeficiency virus ( HIV-1 ) , is shown to be modulated by a <protein>kappa B-like enhancer element</protein> .


Mutation of a kappa B core sequence identified in the IL-2 promoter ( -206 to -195 ) partially inhibits both mitogen- and HTLV-I Tax-mediated activation of this transcription unit and blocks the specific binding of two inducible cellular factors .

Mutation of a <dna>kappa B core sequence</dna> identified in the <dna>IL-2 promoter</dna> ( -206 to -195 ) partially inhibits both mitogen- and HTLV-I Tax-mediated activation of this <protein>transcription unit</protein> and blocks the specific binding of two <protein>inducible cellular factors</protein> .


These kappa B-specific proteins ( 80 to 90 and 50 to 55 kilodaltons ) similarly interact with the functional kappa B enhancer present in the IL-2R alpha promoter .

These <protein>kappa B-specific proteins</protein> ( 80 to 90 and 50 to 55 kilodaltons ) similarly interact with the functional <protein>kappa B enhancer</protein> present in the <dna>IL-2R alpha promoter</dna> .


These data suggest that these kappa B-specific proteins have a role in the coordinate regulation of this growth factor-growth factor receptor gene system that controls T cell proliferation .

These data suggest that these <protein>kappa B-specific proteins</protein> have a role in the coordinate regulation of this growth factor-growth factor receptor gene system that controls <cell_type>T cell</cell_type> proliferation .


Novel region within the V kappa gene promoter is responsible for tissue and stage-specific expression of immunoglobulin genes in human lymphoid neoplasms .

Novel region within the <dna>V kappa gene promoter</dna> is responsible for tissue and stage-specific expression of <dna>immunoglobulin genes</dna> in <cell_type>human lymphoid neoplasms</cell_type> .


Immunoglobulin gene-specific transacting factors have been shown to play a role in lymphoid tissue-specific expression of immunoglobulin genes .

<protein>Immunoglobulin gene-specific transacting factors</protein> have been shown to play a role in lymphoid tissue-specific expression of <dna>immunoglobulin genes</dna> .


The role of these factors in B-cell differentiation and stage-specific expression of these genes is , however , not fully understood .

The role of these factors in <cell_type>B-cell</cell_type> differentiation and stage-specific expression of these genes is , however , not fully understood .


We have used a model of human lymphoid neoplasia to address this question .


Different fragments of unrearranged human variable region of immunoglobulin kappa gene ( V kappa ) were used for cell-free in vitro transcription and DNA mobility shift assays .

Different fragments of <dna>unrearranged human variable region</dna> of <dna>immunoglobulin kappa gene</dna> ( <dna>V kappa</dna> ) were used for cell-free in vitro transcription and DNA mobility shift assays .


Previously described enhancement of in vitro transcription that was only seen with nuclear extracts derived from B-cell neoplasms corresponding to the late stages of B-cell differentiation was shown to be dependent on the actions of these factor ( s ) on the DNA region within the V kappa gene promoter .

Previously described enhancement of in vitro transcription that was only seen with nuclear extracts derived from <cell_type>B-cell neoplasms</cell_type> corresponding to the late stages of <cell_type>B-cell</cell_type> differentiation was shown to be dependent on the actions of these factor ( s ) on the DNA region within the <dna>V kappa gene promoter</dna> .


This region is located within the 920 bp fragment located 210 bp upstream from the coding region and this fragment represents a possible novel DNA region , which plays a role in the stage- and tissue-specific expression of immunoglobulin genes .

This region is located within the 920 bp fragment located 210 bp upstream from the coding region and this fragment represents a possible novel DNA region , which plays a role in the stage- and tissue-specific expression of <dna>immunoglobulin genes</dna> .


[ Determination of the sensitivity to glucocorticoids in vitro ]

[ Determination of the sensitivity to <protein>glucocorticoids</protein> in vitro ]


A modified method for the determination of glucocorticoid receptors in human lymphocytes is suggested .

A modified method for the determination of <protein>glucocorticoid receptors</protein> in <cell_type>human lymphocytes</cell_type> is suggested .


The principal distinction of the method is standardization by the lymphocyte count in a sample ( 1 mln ) and the labeled hormone concentration .

The principal distinction of the method is standardization by the <cell_type>lymphocyte</cell_type> count in a sample ( 1 mln ) and the labeled <protein>hormone</protein> concentration .


The modification saves time and money , limits the range of the data variations , and makes use of a lesser volume of blood .


Examinations of 70 children aged 4 to 15 suffering from the nephrotic form of glomerulonephritis have made it possible to distinguish two groups of patients : with relatively high values of specific binding X = 6820.1 +/- 530.0 ( n = 30 , p = 0.95 , t = 2.04 ) , this corresponding to a clinical form of hormone -sensitive glomerulonephritis , and with relatively low values of specific binding X = 1815.2 +/- 302.8 ( n = 40 , p = 0.95 , t = 1.96 ) , that corresponds to hormone -resistant glomerulonephritis .

Examinations of 70 children aged 4 to 15 suffering from the nephrotic form of glomerulonephritis have made it possible to distinguish two groups of patients : with relatively high values of specific binding X = 6820.1 +/- 530.0 ( n = 30 , p = 0.95 , t = 2.04 ) , this corresponding to a clinical form of <protein>hormone</protein> -sensitive glomerulonephritis , and with relatively low values of specific binding X = 1815.2 +/- 302.8 ( n = 40 , p = 0.95 , t = 1.96 ) , that corresponds to <protein>hormone</protein> -resistant glomerulonephritis .


Dynamic studies have not shown any statistically significant changes in the specific binding values .


These results permit regarding the specific binding value as a prognostic criterion in the assessment of corticosteroid therapy ; this allows a wide employment of the described method in practical nephrology .

These results permit regarding the specific binding value as a prognostic criterion in the assessment of <protein>corticosteroid</protein> therapy ; this allows a wide employment of the described method in practical nephrology .


Octamer-binding proteins from B or HeLa cells stimulate transcription of the immunoglobulin heavy-chain promoter in vitro .

<protein>Octamer-binding proteins</protein> from <cell_line>B or HeLa cells</cell_line> stimulate transcription of the <dna>immunoglobulin heavy-chain promoter</dna> in vitro .


The B-cell -type specificity of the immunoglobulin ( Ig ) heavy-chain and light-chain promoters is mediated by an octanucleotide ( OCTA ) element , ATGCAAAT , that is also a functional component of other RNA polymerase II promoters , such as snRNA and histone H2B promoters .

The <cell_type>B-cell</cell_type> -type specificity of the <protein>immunoglobulin</protein> ( <protein>Ig</protein> ) heavy-chain and light-chain promoters is mediated by an <dna>octanucleotide ( OCTA ) element</dna> , ATGCAAAT , that is also a functional component of other <dna>RNA polymerase II promoters</dna> , such as snRNA and histone H2B promoters .


Two nuclear proteins that bind specifically and with high affinity to the OCTA element have been identified .

Two <protein>nuclear proteins</protein> that bind specifically and with high affinity to the <dna>OCTA element</dna> have been identified .


NF-A1 is present in a variety of cell types , whereas the presence of NF-A2 is essentially confined to B cells , leading to the hypothesis that NF-A2 activates cell-type-specific transcription of the Ig promoter and NF-A1 mediates the other responses of the OCTA element .

<protein>NF-A1</protein> is present in a variety of cell types , whereas the presence of <protein>NF-A2</protein> is essentially confined to <cell_type>B cells</cell_type> , leading to the hypothesis that <protein>NF-A2</protein> activates cell-type-specific transcription of the <dna>Ig promoter</dna> and <protein>NF-A1</protein> mediates the other responses of the <dna>OCTA element</dna> .


Extracts of the B-cell line , BJA-B , contain high levels of NF-A2 and specifically transcribe Ig promoters .

Extracts of the <cell_line>B-cell line</cell_line> , <cell_line>BJA-B</cell_line> , contain high levels of <protein>NF-A2</protein> and specifically transcribe <dna>Ig promoters</dna> .


In contrast , extracts from HeLa cells transcribed the Ig promoter poorly .

In contrast , extracts from <cell_line>HeLa cells</cell_line> transcribed the <dna>Ig promoter</dna> poorly .


Surprisingly , addition of either affinity-enriched NF-A2 or NF-A1 to either a HeLa extract or a partially purified reaction system specifically stimulates the Ig promoter .

Surprisingly , addition of either affinity-enriched NF-A2 or NF-A1 to either a HeLa extract or a partially purified reaction system specifically stimulates the <dna>Ig promoter</dna> .


This suggests that the constitutive OCTA-binding factor NF-A1 can activate transcription of the Ig promoter and that B-cell -specific transcription of this promoter , at least in vitro , is partially due to a quantitative difference in the amount of OCTA-binding protein .

This suggests that the constitutive <protein>OCTA-binding factor NF-A1</protein> can activate transcription of the <dna>Ig promoter</dna> and that <cell_type>B-cell</cell_type> -specific transcription of this promoter , at least in vitro , is partially due to a quantitative difference in the amount of <protein>OCTA-binding protein</protein> .


Because NF-A1 can stimulate Ig transcription , the inability of this factor to activate in vivo the Ig promoter to the same degree as the snRNA promoters probably reflects a difference in the context of the OCTA element in these two types of promoters .

Because <protein>NF-A1</protein> can stimulate <protein>Ig</protein> transcription , the inability of this factor to activate in vivo the <dna>Ig promoter</dna> to the same degree as the <dna>snRNA promoters</dna> probably reflects a difference in the context of the <dna>OCTA element</dna> in these two types of <dna>promoters</dna> .


Identification of a putative regulator of early T cell activation genes .

Identification of a putative regulator of <dna>early T cell activation genes</dna> .


Molecules involved in the antigen receptor-dependent regulation of early T cell activation genes were investigated with the use of functional sequences of the T cell activation-specific enhancer of interleukin-2 ( IL-2 ) .

Molecules involved in the antigen receptor-dependent regulation of <dna>early T cell activation genes</dna> were investigated with the use of functional sequences of the <protein>T cell activation-specific enhancer</protein> of <protein>interleukin-2</protein> ( <protein>IL-2</protein> ) .


One of these sequences forms a protein complex , NFAT-1 , specifically with nuclear extracts of activated T cells .

One of these sequences forms a protein complex , <protein>NFAT-1</protein> , specifically with nuclear extracts of activated <cell_type>T cells</cell_type> .


This complex appeared 10 to 25 minutes before the activation of the IL-2 gene .

This complex appeared 10 to 25 minutes before the activation of the <dna>IL-2 gene</dna> .


Studies with inhibitors of protein synthesis indicated that the time of synthesis of the activator of the IL-2 gene in Jurkat T cells corresponds to the time of appearance of NFAT-1 .

Studies with inhibitors of protein synthesis indicated that the time of synthesis of the activator of the <dna>IL-2 gene</dna> in <cell_line>Jurkat T cells</cell_line> corresponds to the time of appearance of <protein>NFAT-1</protein> .


NFAT-1 , or a very similar protein , bound functional sequences of the long terminal repeat ( LTR ) of the human immunodeficiency virus type 1 ; the LTR of this virus is known to be stimulated during early T cell activation .

<protein>NFAT-1</protein> , or a very similar protein , bound functional sequences of the <dna>long terminal repeat</dna> ( <dna>LTR</dna> ) of the human immunodeficiency virus type 1 ; the <dna>LTR</dna> of this virus is known to be stimulated during early <cell_type>T cell</cell_type> activation .


The binding site for this complex activated a linked promoter after transfection into antigen receptor-activated T cells but not other cell types .

The <dna>binding site</dna> for this complex activated a linked promoter after transfection into <cell_type>antigen receptor-activated T cells</cell_type> but not other cell types .


These characteristics suggest that NFAT-1 transmits signals initiated at the T cell antigen receptor .

These characteristics suggest that <protein>NFAT-1</protein> transmits signals initiated at the <protein>T cell antigen receptor</protein> .


Characterization of thyroid hormone receptors in human IM-9 lymphocytes .

Characterization of <protein>thyroid hormone receptors</protein> in <cell_line>human IM-9 lymphocytes</cell_line> .


Although putatively identified more than 10 years ago , thyroid hormone receptors in human tissues remain poorly characterized .

Although putatively identified more than 10 years ago , <protein>thyroid hormone receptors</protein> in human tissues remain poorly characterized .


As a first step towards understanding the mechanism of thyroid hormone action in man we have characterized T3 binding sites in nuclei of the human lymphoblastoid line , IM-9 cells .

As a first step towards understanding the mechanism of thyroid hormone action in man we have characterized <protein>T3 binding sites</protein> in nuclei of the <cell_line>human lymphoblastoid line</cell_line> , <cell_line>IM-9 cells</cell_line> .


In whole cell experiments at 37 degrees C , nuclear binding of [ 125I ] T3 was saturable ( Kd 34 +/- 6 pmol/l ) and of finite capacity ( approximately equal to 350 sites/cell ) .

In whole cell experiments at 37 degrees C , nuclear binding of <protein>[ 125I ] T3</protein> was saturable ( Kd 34 +/- 6 pmol/l ) and of finite capacity ( approximately equal to 350 sites/cell ) .


The binding sites were extracted from a nuclear pellet by treatment with 0.4 mol/l KCl and sonication .

The <protein>binding sites</protein> were extracted from a nuclear pellet by treatment with 0.4 mol/l KCl and sonication .


Separation of bound from free [ 125I ] T3 in the extracts was achieved using the calcium phosphate matrix , hydroxyapatite at a concentration of 0.3 ml of a 150 g/l slurry .

Separation of bound from free <protein>[ 125I ] T3</protein> in the extracts was achieved using the calcium phosphate matrix , hydroxyapatite at a concentration of 0.3 ml of a 150 g/l slurry .


Rectilinear Scatchard plots were obtained only when the hydroxyapatite was washed with a buffer containing 0.5 % Triton X-100 .


Under these conditions T3 binding sites in the nuclear extracts were present at a concentration of 22.4 +/- 8.6 fmol/mg protein and showed an affinity of ( Kd , room temperature ) 140 +/- 10 pmol/l .

Under these conditions <protein>T3 binding sites</protein> in the nuclear extracts were present at a concentration of 22.4 +/- 8.6 fmol/mg protein and showed an affinity of ( Kd , room temperature ) 140 +/- 10 pmol/l .


The same assay system was used to determine the hierarchy of affinities for a range of natural and synthetic analogues .


Calling T3 100 , the order of potencies observed was : Triac , 500 ; 3 , 5-diiodo-3'-isopropylthyronine , 89 ; T4 , 32 ; 3 , 5-dimethyl-3'isopropylthyronine 2 ; 3 , 5-T2 , 0.7 , rT3 , 0.4 ; 3'5'-T2 , less than 0.01 .


These results suggest that the T3 binding sites present in human IM-9 lymphocyte nuclei and extracts thereof are thyroid hormone receptors .

These results suggest that the <protein>T3 binding sites</protein> present in <cell_line>human IM-9 lymphocyte</cell_line> nuclei and extracts thereof are <protein>thyroid hormone receptors</protein> .


These cells may be a useful tool to increase our understanding of human T3 receptors

These cells may be a useful tool to increase our understanding of <protein>human T3 receptors</protein>


Definition of T-cell specific DNA-binding factors that interact with a 3'-silencer in the CD4+ T-cell gene Rpt-1 .

Definition of <protein>T-cell specific DNA-binding factors</protein> that interact with a <dna>3'-silencer</dna> in the <dna>CD4+ T-cell gene Rpt-1</dna> .


Analysis of the region 3 ' to the CD4+ T-cell gene Rpt-1 ( encoding regulatory protein T-lymphocyte 1 ) led to the definition of a silencer element that inhibits heterologous gene expression in certain CD4+ T-cell lines but not in B-cell or non-lymphoid cell lines .

Analysis of the region 3 ' to the <dna>CD4+ T-cell gene Rpt-1</dna> ( encoding regulatory protein <protein>T-lymphocyte 1</protein> ) led to the definition of a <dna>silencer element</dna> that inhibits <dna>heterologous gene</dna> expression in certain <cell_type>CD4+ T-cell lines</cell_type> but not in <cell_type>B-cell</cell_type> or <cell_type>non-lymphoid cell lines</cell_type> .


Functional silencer activity in vivo was associated with the presence of a specific silencer-DNA-protein complex in electrophoretic mobility shift assays with T-cell extracts .

Functional <dna>silencer</dna> activity in vivo was associated with the presence of a specific <protein>silencer-DNA-protein complex</protein> in electrophoretic mobility shift assays with <cell_type>T-cell</cell_type> extracts .


Formation of this complex was selectively inhibited by the region in HIV-1 containing a silencer element .

Formation of this complex was selectively inhibited by the region in <dna>HIV-1</dna> containing a <dna>silencer element</dna> .


We discuss the possibility that DNA-binding factors may coregulate HIV-1 and Rpt-1 gene expression through a common transcriptional silencer element .

We discuss the possibility that <protein>DNA-binding factors</protein> may coregulate HIV-1 and Rpt-1 gene expression through a common <dna>transcriptional silencer element</dna> .


Congenital immunodeficiencies associated with absence of HLA class II antigens on lymphocytes result from distinct mutations in trans-acting factors .

Congenital immunodeficiencies associated with absence of <protein>HLA class II antigens</protein> on <cell_type>lymphocytes</cell_type> result from distinct mutations in <protein>trans-acting factors</protein> .


Coordinate regulation of HLA class II gene expression during development and coinduction of class II genes by soluble factors suggests that common trans-acting factor ( s ) control expression of these genes .

Coordinate regulation of <dna>HLA class II gene</dna> expression during development and coinduction of <dna>class II genes</dna> by <protein>soluble factors</protein> suggests that common <protein>trans-acting factor</protein> ( s ) control expression of these genes .


In B-lymphoblastoid cell lines derived from two independent class II-deficient bare lymphocyte syndrome patients , we observed a drastic decrease in transcription rates of the class II genes .

In <cell_type>B-lymphoblastoid cell lines</cell_type> derived from two independent class II-deficient bare lymphocyte syndrome patients , we observed a drastic decrease in transcription rates of the <dna>class II genes</dna> .


When these cell lines are fused , class II genes are reexpressed , indicating that immunodeficiencies in bare lymphocyte syndrome patients are the result of two distinct mutations .

When these cell lines are fused , <dna>class II genes</dna> are reexpressed , indicating that immunodeficiencies in bare lymphocyte syndrome patients are the result of two distinct mutations .


Further studies show that genes governing the expression of class II antigens fall into at least three complementation groups ; two of these were previously unidentified in mutant cell lines generated in vitro .

Further studies show that genes governing the expression of <protein>class II antigens</protein> fall into at least three complementation groups ; two of these were previously unidentified in <cell_line>mutant cell lines</cell_line> generated in vitro .


In addition , we report the identification of two discrete complexes , NFX1.1 and NFX1.2 , that bind to the DRA X consensus element .

In addition , we report the identification of two discrete complexes , <protein>NFX1.1</protein> and <protein>NFX1.2</protein> , that bind to the <dna>DRA X consensus element</dna> .


Though the mutation in at least one mutant line generated in vitro ( RJ2.2.5 ) affects products functioning via interaction with the X box , clear alterations in either NFX1.1 or NFX1.2 are not found in any of the mutant cell lines .

Though the mutation in at least one <cell_line>mutant line</cell_line> generated in vitro ( <cell_line>RJ2.2.5</cell_line> ) affects products functioning via interaction with the <dna>X box</dna> , clear alterations in either <protein>NFX1.1</protein> or <protein>NFX1.2</protein> are not found in any of the <cell_line>mutant cell lines</cell_line> .


In vivo responsiveness to glucocorticoid correlated with glucocorticoid receptor content in peripheral blood leukocytes in normal humans .

In vivo responsiveness to glucocorticoid correlated with <protein>glucocorticoid receptor</protein> content in <cell_type>peripheral blood leukocytes</cell_type> in normal humans .


Dexamethasone loading tests ( 0.1 mg dexamethasone/kg , iv ) were performed in 18 normal males to evaluate the individual responsiveness to glucocorticoid .


There were inter-individual differences in increase in peripheral blood polymorphonuclear leukocyte count , decrease in peripheral blood lymphocyte count , and increase in plasma free fatty acids levels after dexamethasone injection .

There were inter-individual differences in increase in <cell_type>peripheral blood polymorphonuclear leukocyte</cell_type> count , decrease in <cell_type>peripheral blood lymphocyte</cell_type> count , and increase in plasma free fatty acids levels after dexamethasone injection .


In addition , there was a significant correlation between the maximum increase in polymorphonuclear leukocytes and the maximum decrease in lymphocytes ( r = 0.7514 , p less than 0.0003 ) .

In addition , there was a significant correlation between the maximum increase in <cell_type>polymorphonuclear leukocytes</cell_type> and the maximum decrease in <cell_type>lymphocytes</cell_type> ( r = 0.7514 , p less than 0.0003 ) .


Simultaneous measurements of glucocorticoid receptor content by whole-cell assay revealed that glucocorticoid receptor content in polymorphonuclear leukocytes linearly correlated with that in the corresponding lymphocytes ( r = 0.9482 , p less than 0.0001 ) .

Simultaneous measurements of <protein>glucocorticoid receptor</protein> content by whole-cell assay revealed that <protein>glucocorticoid receptor</protein> content in <cell_type>polymorphonuclear leukocytes</cell_type> linearly correlated with that in the corresponding <cell_type>lymphocytes</cell_type> ( r = 0.9482 , p less than 0.0001 ) .


There were also significant correlations between the maximum increase in polymorphonuclear leukocytes and glucocorticoid receptor content in polymorphonuclear leukocytes ( r = 0.7239 , p less than 0.0007 ) , and between the maximum decrease in lymphocytes and glucocorticoid receptor content in lymphocytes ( r = 0.7703 , p less than 0.0002 ) .

There were also significant correlations between the maximum increase in <cell_type>polymorphonuclear leukocytes</cell_type> and <protein>glucocorticoid receptor</protein> content in <cell_type>polymorphonuclear leukocytes</cell_type> ( r = 0.7239 , p less than 0.0007 ) , and between the maximum decrease in <cell_type>lymphocytes</cell_type> and <protein>glucocorticoid receptor</protein> content in <cell_type>lymphocytes</cell_type> ( r = 0.7703 , p less than 0.0002 ) .


These results suggest that individual differences are preserved both in glucocorticoid responsiveness and in glucocorticoid receptor content in peripheral blood leukocytes in normal humans .

These results suggest that individual differences are preserved both in glucocorticoid responsiveness and in <protein>glucocorticoid receptor</protein> content in <cell_type>peripheral blood leukocytes</cell_type> in normal humans .


Estradiol receptors in the cytosol of peripheral blood mononuclear cells in hepatitis B virus carriers treated with interferon-alpha .

Estradiol receptors in the cytosol of <cell_type>peripheral blood mononuclear cells</cell_type> in hepatitis B virus carriers treated with <protein>interferon-alpha</protein> .


Estradiol receptors in the cytosol of peripheral blood mononuclear cells and the effects of interferon-alpha ( IFN-alpha ) on estradiol receptors were studied in asymptomatic hepatitis B virus ( HBV ) carriers , patients with chronic hepatitis B and normal controls .

<protein>Estradiol receptors</protein> in the cytosol of <cell_type>peripheral blood mononuclear cells</cell_type> and the effects of <protein>interferon-alpha</protein> ( <protein>IFN-alpha</protein> ) on <protein>estradiol receptors</protein> were studied in asymptomatic hepatitis B virus ( HBV ) carriers , patients with chronic hepatitis B and normal controls .


The level of estradiol receptors in the cytosol of mononuclear cells was significantly lower in asymptomatic HBV carriers and patients with chronic hepatitis B , compared to normal controls .

The level of <protein>estradiol receptors</protein> in the cytosol of <cell_type>mononuclear cells</cell_type> was significantly lower in asymptomatic HBV carriers and patients with chronic hepatitis B , compared to normal controls .


This low level of cytosol estradiol receptors in patients with chronic hepatitis B was increased by the administration of IFN-alpha .

This low level of cytosol <protein>estradiol receptors</protein> in patients with chronic hepatitis B was increased by the administration of <protein>IFN-alpha</protein> .


In addition , when peripheral blood mononuclear cells from patients with chronic hepatitis B were incubated with IFN-alpha in vitro , the level of cytosol estradiol receptors also increased by increasing the concentration of IFN-alpha .

In addition , when <cell_type>peripheral blood mononuclear cells</cell_type> from patients with chronic hepatitis B were incubated with <protein>IFN-alpha</protein> in vitro , the level of cytosol <protein>estradiol receptors</protein> also increased by increasing the concentration of <protein>IFN-alpha</protein> .


We previously reported that the response of mononuclear cells to estrogen is impaired in HBV carriers , and our present results suggested that this may be due to the low level of estradiol receptors in the cytosol of mononuclear cells .

We previously reported that the response of <cell_type>mononuclear cells</cell_type> to estrogen is impaired in HBV carriers , and our present results suggested that this may be due to the low level of <protein>estradiol receptors</protein> in the cytosol of <cell_type>mononuclear cells</cell_type> .


Association of increased lytic effector cell function with high estrogen receptor levels in tumor-bearing patients with breast cancer .

Association of increased lytic effector cell function with high <protein>estrogen receptor</protein> levels in tumor-bearing patients with breast cancer .


Tumor-bearing patients with breast cancer were assayed for their natural killer ( NK ) cell activity and for the function of activated cytotoxic T-cells , as assessed by lectin-dependent cellular cytotoxicity ( LDCC ) .

Tumor-bearing patients with breast cancer were assayed for their <cell_type>natural killer ( NK ) cell</cell_type> activity and for the function of activated <cell_type>cytotoxic T-cells</cell_type> , as assessed by lectin-dependent cellular cytotoxicity ( LDCC ) .


Tumor-bearing patients with breast cancer had a significant increase in NK activity and in LDCC , as compared with healthy control individuals .

Tumor-bearing patients with breast cancer had a significant increase in <cell_type>NK</cell_type> activity and in LDCC , as compared with healthy control individuals .


Although the enhanced NK cell activity and LDCC were closely associated with high levels ( greater than 31 fmol/mg ) of estrogen receptor ( ER ) content in the primary tumor , no other clinical or histologic correlation between the increase in either parameter of cytotoxic effector cell function could be found .

Although the enhanced <cell_type>NK cell</cell_type> activity and LDCC were closely associated with high levels ( greater than 31 fmol/mg ) of <protein>estrogen receptor</protein> ( <protein>ER</protein> ) content in the primary tumor , no other clinical or histologic correlation between the increase in either parameter of <cell_type>cytotoxic effector cell</cell_type> function could be found .


Thus , ER levels greater than 31 fmol/mg might be associated with increased cytotoxic effector cell function in tumor-bearing patients with breast cancer .

Thus , <protein>ER</protein> levels greater than 31 fmol/mg might be associated with increased <cell_type>cytotoxic effector cell</cell_type> function in tumor-bearing patients with breast cancer .


Properties of glucocorticoid receptors in Epstein-Barr virus-transformed lymphocytes from patients with familial cortisol resistance .

Properties of <protein>glucocorticoid receptors</protein> in <cell_line>Epstein-Barr virus-transformed lymphocytes</cell_line> from patients with familial cortisol resistance .


In a previous report of two patients with familial glucocorticoid resistance due to reduced numbers of glucocorticoid receptors ( GR ) , we have shown decreased numbers of GR in peripheral mononuclear cells and cultured fibroblasts but normal affinity of GR in both patients .

In a previous report of two patients with familial glucocorticoid resistance due to reduced numbers of <protein>glucocorticoid receptors</protein> ( <protein>GR</protein> ) , we have shown decreased numbers of <protein>GR</protein> in <cell_type>peripheral mononuclear cells</cell_type> and <cell_line>cultured fibroblasts</cell_line> but normal affinity of <protein>GR</protein> in both patients .


In this study , peripheral lymphocytes from these patients , one patient 's son and daughter , and normal subjects were transformed with Epstein-Barr virus .

In this study , <cell_type>peripheral lymphocytes</cell_type> from these patients , one patient 's son and daughter , and normal subjects were transformed with Epstein-Barr virus .


Reduced numbers and normal affinity of GR were found in the Epstein-Barr virus-transformed lymphocytes from both patients while the son and daughter had normal numbers and affinity of GR .

Reduced numbers and normal affinity of <protein>GR</protein> were found in the <cell_line>Epstein-Barr virus-transformed lymphocytes</cell_line> from both patients while the son and daughter had normal numbers and affinity of <protein>GR</protein> .


The thermal stability of GR and thermal activation of cytosolic receptors in both patients were found to be normal .

The thermal stability of <protein>GR</protein> and thermal activation of <protein>cytosolic receptors</protein> in both patients were found to be normal .


Although the percentages of nuclear bound GR were similar in both patients and normal controls , the absolute amounts of nuclear bound GR of the patients were about one-half that of normal controls .

Although the percentages of nuclear bound <protein>GR</protein> were similar in both patients and normal controls , the absolute amounts of nuclear bound <protein>GR</protein> of the patients were about one-half that of normal controls .


These abnormal properties of GR ( reduced numbers of GR ) were preserved in the transformed cells from the patients .

These abnormal properties of <protein>GR</protein> ( reduced numbers of <protein>GR</protein> ) were preserved in the <cell_line>transformed cells</cell_line> from the patients .


Octamer transcription factors 1 and 2 each bind to two different functional elements in the immunoglobulin heavy-chain promoter .

Octamer transcription factors 1 and 2 each bind to two different <dna>functional elements</dna> in the <dna>immunoglobulin heavy-chain promoter</dna> .


Immunoglobulin heavy-chain genes contain two conserved sequence elements 5 ' to the site of transcription initiation : the octamer ATGCAAAT and the heptamer CTCATGA .

<dna>Immunoglobulin heavy-chain genes</dna> contain two <dna>conserved sequence elements</dna> 5 ' to the site of transcription initiation : the octamer ATGCAAAT and the heptamer CTCATGA .


Both of these elements are required for normal cell-specific promoter function .

Both of these elements are required for <dna>normal cell-specific promoter</dna> function .


The present study demonstrates that both the ubiquitous and lymphoid-cell-specific octamer transcription factors ( OTF-1 and OTF-2 , respectively ) interact specifically with each of the two conserved sequence elements , forming either homo- or heterodimeric complexes .

The present study demonstrates that both the <protein>ubiquitous and lymphoid-cell-specific octamer transcription factors</protein> ( <protein>OTF-1</protein> and <protein>OTF-2</protein> , respectively ) interact specifically with each of the two <dna>conserved sequence elements</dna> , forming either <protein>homo- or heterodimeric complexes</protein> .


This was surprising , since the heptamer and octamer sequence motifs bear no obvious similarity to each other .


Binding of either factor to the octamer element occurred independently .

Binding of either factor to the <dna>octamer element</dna> occurred independently .


However , OTF interaction with the heptamer sequence appeared to require the presence of an intact octamer motif and occurred with a spacing of either 2 or 14 base pairs between the two elements , suggesting coordinate binding resulting from protein-protein interactions .

However , <protein>OTF</protein> interaction with the <dna>heptamer sequence</dna> appeared to require the presence of an intact octamer motif and occurred with a spacing of either <dna>2 or 14 base pairs</dna> between the two elements , suggesting coordinate binding resulting from protein-protein interactions .


The degeneracy in sequences recognized by the OTFs may be important in widening the range over which gene expression can be modulated and in establishing cell type specificity .

The degeneracy in sequences recognized by the <protein>OTFs</protein> may be important in widening the range over which gene expression can be modulated and in establishing cell type specificity .


Identification of a novel lymphoid specific octamer binding protein ( OTF-2B ) by proteolytic clipping bandshift assay ( PCBA ) .

Identification of a novel <protein>lymphoid specific octamer binding protein</protein> ( <protein>OTF-2B</protein> ) by proteolytic clipping bandshift assay ( PCBA ) .


The octamer sequence ATGCAAAT is found in the promoters of immunoglobulin ( Ig ) heavy and light chain genes and in the heavy chain enhancer and is a major determinant of the cell type specific expression of Ig genes in B cells .

The octamer sequence ATGCAAAT is found in the promoters of <dna>immunoglobulin ( Ig ) heavy and light chain genes</dna> and in the <dna>heavy chain enhancer</dna> and is a major determinant of the cell type specific expression of <dna>Ig genes</dna> in <cell_type>B cells</cell_type> .


An apparent paradox is that the same sequence serves as an upstream promoter or enhancer element in a variety of housekeeping genes such as the histone H2B and U snRNA genes .

An apparent paradox is that the same sequence serves as an <dna>upstream promoter or enhancer element</dna> in a variety of <dna>housekeeping genes</dna> such as the <dna>histone H2B and U snRNA genes</dna> .


The differential usage of this regulatory sequence motif is thought to be mediated by different species of octamer binding proteins .

The differential usage of this regulatory sequence motif is thought to be mediated by different species of <protein>octamer binding proteins</protein> .


One species of 100 kd , designated OTF-1 , is present in all cell types and may exert its activating function only when it can interact with additional adjacent transcription factors .

One species of 100 kd , designated <protein>OTF-1</protein> , is present in all cell types and may exert its activating function only when it can interact with additional adjacent <protein>transcription factors</protein> .


The lymphoid cell specific octamer binding protein of 60 kd ( OTF-2A ) specifically stimulates Ig promoters which consist essentially of a TATA-box and an octamer sequence upstream of it .

The <protein>lymphoid cell specific octamer binding protein</protein> of 60 kd ( <protein>OTF-2A</protein> ) specifically stimulates <dna>Ig promoters</dna> which consist essentially of a <dna>TATA-box</dna> and an <dna>octamer sequence</dna> upstream of it .


Here we present evidence for yet another B cell specific octamer binding protein of 75 kd ( OTF-2B ) .

Here we present evidence for yet another <protein>B cell specific octamer binding protein</protein> of 75 kd ( <protein>OTF-2B</protein> ) .


From several findings , including the absence of OTF-2B ( but not OTF-2A ) from a lymphocyte line that can not respond to the IgH enhancer , we propose a role of the novel octamer factor in the long range activation by the IgH enhancer .

From several findings , including the absence of <protein>OTF-2B</protein> ( but not <protein>OTF-2A</protein> ) from a <cell_line>lymphocyte line</cell_line> that can not respond to the <dna>IgH enhancer</dna> , we propose a role of the <protein>novel octamer factor</protein> in the long range activation by the <dna>IgH enhancer</dna> .


We have used the proteolytic clipping bandshift assay ( PCBA ) technique to distinguish the three different forms found in B cells .

We have used the proteolytic clipping bandshift assay ( PCBA ) technique to distinguish the three different forms found in <cell_type>B cells</cell_type> .


This analysis indicates that the 75 kd-species OTF-2B is closely related to the 60 kd species OTF-2A .

This analysis indicates that the 75 kd-species <protein>OTF-2B</protein> is closely related to the <protein>60 kd species OTF-2A</protein> .


Inhibition of interleukin 2 -induced proliferation of cloned murine T cells by glucocorticoids .

Inhibition of <protein>interleukin 2</protein> -induced proliferation of <cell_line>cloned murine T cells</cell_line> by glucocorticoids .


Possible involvement of an inhibitory protein .

Possible involvement of an <protein>inhibitory protein</protein> .


The ability of glucocorticoids to inhibit interleukin 2 ( IL 2 ) -induced T cell proliferation in two cytotoxic T cell ( CTL ) clones has been studied .

The ability of glucocorticoids to inhibit <protein>interleukin 2</protein> ( <protein>IL 2</protein> ) -induced <cell_type>T cell</cell_type> proliferation in two <cell_line>cytotoxic T cell ( CTL ) clones</cell_line> has been studied .


A complete inhibition of DNA synthesis by dexamethasone ( Dx ) could be observed when IL 2-depleted cultures of CTL were either incubated for 6 h with the hormone prior to the addition of IL 2 or treated simultaneously with Dx and a low concentration of IL 2 .

A complete inhibition of DNA synthesis by dexamethasone ( Dx ) could be observed when <cell_line>IL 2-depleted cultures</cell_line> of <cell_line>CTL</cell_line> were either incubated for 6 h with the <protein>hormone</protein> prior to the addition of <protein>IL 2</protein> or treated simultaneously with Dx and a low concentration of <protein>IL 2</protein> .


No significant reduction in the number and affinity of IL 2 receptors was seen after 6 h incubation with Dx .

No significant reduction in the number and affinity of <protein>IL 2 receptors</protein> was seen after 6 h incubation with Dx .


The order of potency observed with the different steroids indicated that this inhibitory effect was mediated through binding to a specific glucocorticoid receptor .

The order of potency observed with the different steroids indicated that this inhibitory effect was mediated through binding to a specific <protein>glucocorticoid receptor</protein> .


The action of these hormones possibly involves the synthesis of an inhibitory protein ( s ) , since the presence of cycloheximide during the incubation with Dx prevented the inhibition of DNA synthesis .

The action of these <protein>hormones</protein> possibly involves the synthesis of an <protein>inhibitory protein</protein> ( s ) , since the presence of cycloheximide during the incubation with Dx prevented the inhibition of DNA synthesis .


Furthermore , supernatant from Dx-treated CTL contained a nondialyzable factor which inhibited DNA synthesis and cell growth of CTL clones induced by IL 2 .

Furthermore , supernatant from Dx-treated <cell_line>CTL</cell_line> contained a nondialyzable factor which inhibited DNA synthesis and cell growth of <cell_line>CTL clones</cell_line> induced by <protein>IL 2</protein> .


Blocking of IL 2 synthesis and IL 2 receptor formation have been proposed as one of the major mechanisms of glucocorticoid-induced immunosuppression .

Blocking of <protein>IL 2</protein> synthesis and <protein>IL 2 receptor</protein> formation have been proposed as one of the major mechanisms of glucocorticoid-induced immunosuppression .


Our results indicate that these hormones may also affect T cell proliferation by inhibiting IL 2 activity .

Our results indicate that these <protein>hormones</protein> may also affect <cell_type>T cell</cell_type> proliferation by inhibiting <protein>IL 2</protein> activity .


Identification and purification of a human immunoglobulin-enhancer-binding protein ( NF-kappa B ) that activates transcription from a human immunodeficiency virus type 1 promoter in vitro .

Identification and purification of a <protein>human immunoglobulin-enhancer-binding protein</protein> ( <protein>NF-kappa B</protein> ) that activates transcription from a <dna>human immunodeficiency virus type 1 promoter</dna> in vitro .


The enhancer-binding factor NF-kappa B , which is found only in cells that transcribe immunoglobulin light chain genes , has been purified from nuclear extracts of Namalwa cells ( human Burkitt lymphoma cells ) by sequence-specific DNA affinity chromatography .

The <protein>enhancer-binding factor NF-kappa B</protein> , which is found only in cells that transcribe <dna>immunoglobulin light chain genes</dna> , has been purified from nuclear extracts of <cell_line>Namalwa cells</cell_line> ( <cell_line>human Burkitt lymphoma cells</cell_line> ) by sequence-specific DNA affinity chromatography .


The purified NF-kappa B has been identified as a 51-kDa polypeptide by UV-crosslinking analysis .

The purified <protein>NF-kappa B</protein> has been identified as a <protein>51-kDa polypeptide</protein> by UV-crosslinking analysis .


`` Footprint '' and methylation-interference analyses have shown that purified NF-kappa B has a binding activity specific for the kappa light chain enhancer sequence .

`` Footprint '' and methylation-interference analyses have shown that purified <protein>NF-kappa B</protein> has a binding activity specific for the <dna>kappa light chain enhancer sequence</dna> .


The purified factor activated in vitro transcription of the human immunodeficiency virus type I promoter by binding to an upstream NF-kappa B-binding site

The purified factor activated in vitro transcription of the <dna>human immunodeficiency virus type I promoter</dna> by binding to an <dna>upstream NF-kappa B-binding site</dna>


Lymphocyte glucocorticoid receptor binding in depression : normal values following recovery .

<cell_type>Lymphocyte</cell_type> <protein>glucocorticoid receptor</protein> binding in depression : normal values following recovery .


The number of glucocorticoid receptor sites in lymphocytes and plasma cortisol concentrations were measured in 20 patients who had recovered from major depressive disorder and 20 healthy control subjects .

The number of <protein>glucocorticoid receptor</protein> sites in <cell_type>lymphocytes</cell_type> and plasma cortisol concentrations were measured in 20 patients who had recovered from major depressive disorder and 20 healthy control subjects .


The number of glucocorticoid receptor sites in lymphocytes from the recovered depressed group was not significantly different from that of the control group .

The number of <protein>glucocorticoid receptor</protein> sites in <cell_type>lymphocytes</cell_type> from the recovered depressed group was not significantly different from that of the control group .


Although the mean plasma cortisol concentration in recovered depressives was higher than in control subjects , the difference only just reached significance .


This study shows that the reduction in glucocorticoid receptor numbers which occurs during acute depressive illness does not persist on recovery and is , therefore , state-dependent .

This study shows that the reduction in <protein>glucocorticoid receptor</protein> numbers which occurs during acute depressive illness does not persist on recovery and is , therefore , state-dependent .


Identification and purification of a human lymphoid-specific octamer-binding protein ( OTF-2 ) that activates transcription of an immunoglobulin promoter in vitro .

Identification and purification of a <protein>human lymphoid-specific octamer-binding protein</protein> ( <protein>OTF-2</protein> ) that activates transcription of an <dna>immunoglobulin promoter</dna> in vitro .


The octamer sequence 5'-ATGCAAAT , in either orientation , serves as an upstream element in a variety of promoters and also occurs as a modular enhancer element .

The octamer sequence 5'-ATGCAAAT , in either orientation , serves as an <dna>upstream element</dna> in a variety of <dna>promoters</dna> and also occurs as a <dna>modular enhancer element</dna> .


It is of particular interest in immunoglobulin genes since it is found in the upstream regions of all heavy and light chain promoters and in the heavy chain enhancer , both of which are known to be necessary for cell-specific expression .

It is of particular interest in <dna>immunoglobulin genes</dna> since it is found in the <dna>upstream regions</dna> of all <dna>heavy and light chain promoters</dna> and in the <dna>heavy chain enhancer</dna> , both of which are known to be necessary for cell-specific expression .


We report here the chromatographic separation of ubiquitous and B cell-specific octamer-binding proteins .

We report here the chromatographic separation of <protein>ubiquitous and B cell-specific octamer-binding proteins</protein> .


The B cell factor was purified to homogeneity using affinity chromatography and consists of three peptides of 62 , 61 , and 58.5 +/- 1.5 kd .

The <protein>B cell factor</protein> was purified to homogeneity using affinity chromatography and consists of three peptides of 62 , 61 , and 58.5 +/- 1.5 kd .


Each of the polypeptides was renatured after SDS-PAGE and shown to bind to the octamer sequence .


The specific DNA binding activity of the pure B cell-specific factor was indistinguishable from that of the affinity-purified ubiquitous factor .

The specific DNA binding activity of the pure <protein>B cell-specific factor</protein> was indistinguishable from that of the <protein>affinity-purified ubiquitous factor</protein> .


This B cell-specific octamer-binding factor , in pure form , activated transcription from a kappa light chain promoter in vitro , thus demonstrating that it is indeed a B cell-specific transcription factor for this gene .

This <protein>B cell-specific octamer-binding factor</protein> , in pure form , activated transcription from a <dna>kappa light chain promoter</dna> in vitro , thus demonstrating that it is indeed a <protein>B cell-specific transcription factor</protein> for this gene .


In addition to the ubiquitous and B cell-specific octamer-binding factors , we identified several additional proteins , one of which is B cell -specific , that interact with the kappa promoter .

In addition to the <protein>ubiquitous and B cell-specific octamer-binding factors</protein> , we identified several additional proteins , one of which is <cell_type>B cell</cell_type> -specific , that interact with the <dna>kappa promoter</dna> .


Decreased deoxyribonucleic acid binding of glucocorticoid-receptor complex in cultured skin fibroblasts from a patient with the glucocorticoid resistance syndrome .

Decreased deoxyribonucleic acid binding of <protein>glucocorticoid-receptor complex</protein> in cultured <cell_line>skin fibroblasts</cell_line> from a patient with the glucocorticoid resistance syndrome .


A patient with the syndrome of glucocorticoid resistance was studied .


A 27-yr-old woman initially was diagnosed as having Cushing 's disease , based on the findings of high plasma ACTH and serum cortisol levels , increased urinary cortisol secretion , resistance to adrenal suppression with dexamethasone , and bilateral adrenal hyperplasia by computed tomography and scintigraphy of the adrenal glands .


However , she had no signs or symptoms of Cushing 's syndrome .


During a 5-yr follow-up , no clinical abnormalities developed , although hypercortisolism persisted .


End-organ resistance to cortisol was suspected .


To explain the end-organ resistance to cortisol , the glucocorticoid receptors ( GR ) in peripheral mononuclear leukocytes and cultured skin fibroblasts from a forearm skin biopsy were characterized and compared with the results of similar studies in normal subjects .

To explain the end-organ resistance to cortisol , the <protein>glucocorticoid receptors</protein> ( <protein>GR</protein> ) in <cell_type>peripheral mononuclear leukocytes</cell_type> and <cell_line>cultured skin fibroblasts</cell_line> from a forearm skin biopsy were characterized and compared with the results of similar studies in normal subjects .


The patient 's GR in whole cell assays had an increased dissociation constant ( Kd ) .

The patient 's <protein>GR</protein> in whole cell assays had an increased dissociation constant ( Kd ) .


In the cytosol of cultured skin fibroblasts from the patient , there was also decreased binding capacity .

In the cytosol of <cell_line>cultured skin fibroblasts</cell_line> from the patient , there was also decreased binding capacity .


The thermal stability and the sedimentation coefficient in a sucrose density gradient of the receptors in the cytosol of cultured skin fibroblasts from the patient and normal subjects were similar .

The thermal stability and the sedimentation coefficient in a sucrose density gradient of the receptors in the cytosol of <cell_line>cultured skin fibroblasts</cell_line> from the patient and normal subjects were similar .


GR complex activation , analyzed by DEAE-cellulose chromatography , was decreased in the patient .

<cell_line>GR complex activation</cell_line> , analyzed by <cell_line>DEAE-cellulose chromatography</cell_line> , was decreased in the patient .


DNA binding of the GR complex after temperature-induced activation was lower in the patient than in normal subjects .

<dna>DNA</dna> binding of the <protein>GR complex</protein> after temperature-induced activation was lower in the patient than in normal subjects .


Nuclear translocation of GR complexes from the patient was also slightly decreased .

Nuclear translocation of <protein>GR complexes</protein> from the patient was also slightly decreased .


These results suggest that the patient 's glucocorticoid resistance was due to a decrease in the affinity of the receptor for glucocorticoids and a decrease in the binding of the GR complex to DNA .

These results suggest that the patient 's glucocorticoid resistance was due to a decrease in the affinity of the receptor for glucocorticoids and a decrease in the binding of the <protein>GR complex</protein> to <dna>DNA</dna> .


Granulocyte-macrophage colony-stimulating factor .

<protein>Granulocyte-macrophage colony-stimulating factor</protein> .


Sensitive and receptor-mediated regulation by 1 , 25-dihydroxyvitamin D3 in normal human peripheral blood lymphocytes .

Sensitive and receptor-mediated regulation by 1 , 25-dihydroxyvitamin D3 in normal <cell_type>human peripheral blood lymphocytes</cell_type> .


We show that 1 , 25-dihydroxyvitamin D3 ( 1 , 25 [ OH ] 2D3 ) , the most hormonally active metabolite of vitamin D3 , modulates sensitively and specifically both the protein and messenger RNA accumulation of the multilineage growth factor granulocyte-macrophage colony-stimulating factor ( GM-CSF ) .

We show that 1 , 25-dihydroxyvitamin D3 ( 1 , 25 [ OH ] 2D3 ) , the most hormonally active metabolite of vitamin D3 , modulates sensitively and specifically both the protein and <rna>messenger RNA</rna> accumulation of the <protein>multilineage growth factor</protein> <protein>granulocyte-macrophage colony-stimulating factor</protein> ( <protein>GM-CSF</protein> ) .


The regulation of GM-CSF expression is seen in both normal human mitogen-activated T lymphocytes and T lymphocytes from a line ( S-LB1 ) transformed with human T cell lymphotropic virus 1 ( HTLV-1 ) .

The regulation of <protein>GM-CSF</protein> expression is seen in both <cell_type>normal human mitogen-activated T lymphocytes</cell_type> and <cell_line>T lymphocytes from a line ( S-LB1 ) transformed with human T cell lymphotropic virus 1</cell_line> ( HTLV-1 ) .


In contrast , cells from a HTLV-1 transformed T lymphocyte line ( Ab-VDR ) established from a patient with vitamin D-resistant rickets type II with undetectable 1 , 25 ( OH ) 2D3 cellular receptors are resistant to the action of 1 , 25 ( OH ) 2D3 .

In contrast , cells from a <cell_line>HTLV-1 transformed T lymphocyte line</cell_line> ( <cell_line>Ab-VDR</cell_line> ) established from a patient with vitamin D-resistant rickets type II with undetectable <protein>1 , 25 ( OH ) 2D3 cellular receptors</protein> are resistant to the action of 1 , 25 ( OH ) 2D3 .


Inhibition of GM-CSF expression by 1 , 25 ( OH ) 2D3 can occur independently of interleukin 2 regulation and is probably mediated through cellular 1 , 25 ( OH ) 2D3 receptors .

Inhibition of <protein>GM-CSF</protein> expression by 1 , 25 ( OH ) 2D3 can occur independently of <protein>interleukin 2</protein> regulation and is probably mediated through <protein>cellular 1 , 25 ( OH ) 2D3 receptors</protein> .


We conclude that 1 , 25 ( OH ) 2D3 may be important in the physiology of hematopoiesis .


Altered interaction between triiodothyronine and its nuclear receptors in absence of cortisol : a proposed mechanism for increased thyrotropin secretion in corticosteroid deficiency states .

Altered interaction between triiodothyronine and its <protein>nuclear receptors</protein> in absence of cortisol : a proposed mechanism for increased thyrotropin secretion in corticosteroid deficiency states .


Thyroid hormones occasionally appear less effective when administered alone to patients with panhypopituitarism , and manifestations suggestive of hypothyroidism have been reported in patients suffering from untreated Addison 's disease .


In the latter condition , thyrotropin secretion is increased : this occurs already after as little as 2 days of temporary withdrawal of therapy with substitution doses of corticosteroids while circulating levels of thyroid hormones remain within normal limits .


Therefore , a possible role of cortisol in interaction between triiodothyronine and its nuclear receptors was examined at the level of circulating lymphocytes obtained from patients with primary or secondary adrenocortical failure .

Therefore , a possible role of cortisol in interaction between triiodothyronine and its <protein>nuclear receptors</protein> was examined at the level of circulating lymphocytes obtained from patients with primary or secondary adrenocortical failure .


The affinity of these receptors was found to be decreased , by more than 50 % on average , in the absence of cortisol treatments .


This change was promptly corrected upon resumption of therapy .


The number of binding sites was not significantly modified .


The influence of cortisol on thyroid hormone receptors discussed here might account for the clinical observations mentioned above .

The influence of cortisol on <protein>thyroid hormone receptors</protein> discussed here might account for the clinical observations mentioned above .


Inhibition by cortisol of human natural killer ( NK ) cell activity .

Inhibition by cortisol of <cell_type>human natural killer ( NK ) cell</cell_type> activity .


The effects of cortisol on the natural killer ( NK ) activity of human peripheral blood mononuclear ( PBM ) cells were studied in vitro using a direct 4-h 51Cr-release assay and K 562 cell line as a target .

The effects of cortisol on the <cell_type>natural killer</cell_type> ( NK ) activity of <cell_type>human peripheral blood mononuclear ( PBM ) cells</cell_type> were studied in vitro using a direct 4-h 51Cr-release assay and <cell_line>K 562 cell line</cell_line> as a target .


Preincubation for 20 h of PBM cells drawn from healthy donors with 1 X 10 ( -8 ) to 1 X 10 ( -5 ) M cortisol resulted in a significant decrease of NK cell activity .

Preincubation for 20 h of <cell_type>PBM cells</cell_type> drawn from healthy donors with 1 X 10 ( -8 ) to 1 X 10 ( -5 ) M cortisol resulted in a significant decrease of <cell_type>NK cell</cell_type> activity .


The magnitude of the suppression was directly related to the steroid concentration and inversely related to the number of effector cells .

The magnitude of the suppression was directly related to the steroid concentration and inversely related to the number of <cell_type>effector cells</cell_type> .


Cortisol was able to minimize the enhancement of NK cytotoxicity obtainable in the presence of immune interferon ( IFN-gamma ) .


A significantly higher suppression was achieved after sequential exposure of PBM cells to cortisol and equimolar levels of prostaglandin E2 ( PgE2 ) .

A significantly higher suppression was achieved after sequential exposure of <cell_type>PBM cells</cell_type> to cortisol and equimolar levels of prostaglandin E2 ( PgE2 ) .


The concomitant incubation with theophylline and isobutyl-methylxanthine failed to enhance the cortisol-induced suppression , whereas PgE2-dependent inhibition significantly increased after exposure of PBM cells to methyl-xanthines .

The concomitant incubation with theophylline and isobutyl-methylxanthine failed to enhance the cortisol-induced suppression , whereas PgE2-dependent inhibition significantly increased after exposure of <cell_type>PBM cells</cell_type> to methyl-xanthines .


The inhibitory effect of cortisol was partially or totally prevented by the concomitant incubation with equimolar amounts of 11-deoxycortisol and RU 486 but not of progesterone .


Treatment of NK effectors with a monoclonal anti-human corticosteroid-binding globulin ( CBG ) antibody produced an enhancement of the spontaneous NK activity and a partial suppression of cortisol-mediated effects .

Treatment of <cell_type>NK effectors</cell_type> with a <protein>monoclonal anti-human corticosteroid-binding globulin ( CBG ) antibody</protein> produced an enhancement of the spontaneous <cell_type>NK</cell_type> activity and a partial suppression of cortisol-mediated effects .


Our results suggest that endogenous glucocorticoids play a role in the regulation of NK cell-mediated cytotoxicity .


Since the effect of cortisol was additive to that of PgE2 and was not changed by phosphodiesterase inhibitors , it is conceivable that the hormone acts at a level different from the adenylate cyclase - phosphodiesterase system .

Since the effect of cortisol was additive to that of PgE2 and was not changed by <protein>phosphodiesterase</protein> inhibitors , it is conceivable that the hormone acts at a level different from the <protein>adenylate cyclase</protein> - <protein>phosphodiesterase</protein> system .


Data obtained with the use of antiglucocorticoids and the anti-CBG antibody are compatible with a role both of high-affinity glucocorticoid receptors and of CBG in mediating cortisol action on the human NK cell activity .

Data obtained with the use of antiglucocorticoids and the <protein>anti-CBG antibody</protein> are compatible with a role both of high-affinity <protein>glucocorticoid receptors</protein> and of <protein>CBG</protein> in mediating cortisol action on the <cell_type>human NK cell</cell_type> activity .


Interaction of cell-type-specific nuclear proteins with immunoglobulin VH promoter region sequences .

Interaction of <protein>cell-type-specific nuclear proteins</protein> with <dna>immunoglobulin VH promoter region sequences</dna> .


All human and murine immunoglobulin heavy chain variable region ( VH ) genes contain the sequence ATGCAAAT approximately 70 nucleotides 5 ' from the site of transcription initiation .

All <dna>human and murine immunoglobulin heavy chain variable region ( VH ) genes</dna> contain the sequence ATGCAAAT approximately 70 nucleotides 5 ' from the site of transcription initiation .


This octanucleotide , in reverse orientation , is also found in all light chain variable region ( VL ) genes , and in the immunoglobulin heavy chain transcriptional enhancer .

This octanucleotide , in reverse orientation , is also found in all <dna>light chain variable region ( VL ) genes</dna> , and in the <dna>immunoglobulin heavy chain transcriptional enhancer</dna> .


Transfection studies have established that this octamer is involved in the lymphoid-specific transcription of immunoglobulin genes .

Transfection studies have established that this octamer is involved in the lymphoid-specific transcription of <dna>immunoglobulin genes</dna> .


Octamer-containing fragments have been reported to bind a factor present in nuclear extracts of human cell lines ; however , identical binding activity was detected in both B lymphoid and non-lymphoid cells .

<dna>Octamer-containing fragments</dna> have been reported to bind a factor present in nuclear extracts of <cell_line>human cell lines</cell_line> ; however , identical binding activity was detected in both <cell_line>B lymphoid and non-lymphoid cells</cell_line> .


Here we establish that nuclear extracts from distinct cell types differ in their ability to interact with octamer-containing fragments .

Here we establish that nuclear extracts from distinct cell types differ in their ability to interact with <dna>octamer-containing fragments</dna> .


We have also detected a DNA-protein interaction that may be involved in the cell-type specificity of immunoglobulin expression , and we have determined that a sequence upstream of the octamer participates in an interaction with a nuclear protein ( s ) .

We have also detected a DNA-protein interaction that may be involved in the cell-type specificity of <protein>immunoglobulin</protein> expression , and we have determined that a sequence upstream of the octamer participates in an interaction with a <protein>nuclear protein</protein> ( s ) .


Preferential transcription of HTLV-I LTR in cell-free extracts of human T cells producing HTLV-I viral proteins .

Preferential transcription of <dna>HTLV-I LTR</dna> in cell-free extracts of <cell_type>human T cells</cell_type> producing <protein>HTLV-I viral proteins</protein> .


The promoters of the adenovirus 2 major late gene , the mouse beta-globin gene , the mouse immunoglobulin VH gene and the LTR of the human T-lymphotropic retrovirus type I were tested for their transcription activities in cell-free extracts of four cell lines ; HeLa , CESS ( Epstein-Barr virus-transformed human B cell line ) , MT-1 ( HTLV-I-infected human T cell line without viral protein synthesis ) , and MT-2 ( HTLV-I-infected human T cell line producing viral proteins ) .

The <dna>promoters</dna> of the <dna>adenovirus 2 major late gene</dna> , the <dna>mouse beta-globin gene</dna> , the <dna>mouse immunoglobulin VH gene</dna> and the <dna>LTR</dna> of the human T-lymphotropic retrovirus type I were tested for their transcription activities in cell-free extracts of four cell lines ; <cell_line>HeLa</cell_line> , <cell_line>CESS</cell_line> ( <cell_line>Epstein-Barr virus-transformed human B cell line</cell_line> ) , <cell_line>MT-1</cell_line> ( <cell_line>HTLV-I-infected human T cell line</cell_line> without viral protein synthesis ) , and <cell_line>MT-2</cell_line> ( <cell_line>HTLV-I-infected human T cell line</cell_line> producing <protein>viral proteins</protein> ) .


LTR was preferentially transcribed in the extracts of MT-2 although the other three genes were transcribed with relatively constant efficiencies in different extracts .

<dna>LTR</dna> was preferentially transcribed in the extracts of <cell_line>MT-2</cell_line> although the other three genes were transcribed with relatively constant efficiencies in different extracts .


The results agree well with the previous in vivo studies on the promoter activity of HTLV-I LTR .

The results agree well with the previous in vivo studies on the promoter activity of <dna>HTLV-I LTR</dna> .


Mixing of HeLa and MT-2 extracts revealed the presence of a LTR-specific stimulating activity in MT-2 extracts .


A nuclear factor that binds to a conserved sequence motif in transcriptional control elements of immunoglobulin genes .

A <protein>nuclear factor</protein> that binds to a conserved sequence motif in <dna>transcriptional control elements</dna> of <dna>immunoglobulin genes</dna> .


Trans-acting factors that mediate B-cell specific transcription of immunoglobulin genes have been postulated based on an analysis of the expression of exogenously introduced immunoglobulin gene recombinants in lymphoid and non-lymphoid cells .

<protein>Trans-acting factors</protein> that mediate B-cell specific transcription of <dna>immunoglobulin genes</dna> have been postulated based on an analysis of the expression of exogenously introduced <dna>immunoglobulin gene recombinants</dna> in <cell_type>lymphoid and non-lymphoid cells</cell_type> .


Two B-cell-specific , cis-acting transcriptional regulatory elements have been identified .

Two B-cell-specific , <dna>cis-acting transcriptional regulatory elements</dna> have been identified .


One element is located in the intron between the variable ( V ) and constant ( C ) regions of both heavy and kappa light-chain genes and acts as a transcriptional enhancer .

One element is located in the intron between the variable ( V ) and constant ( C ) regions of both <dna>heavy and kappa light-chain genes</dna> and acts as a transcriptional enhancer .


The second element is found upstream of both heavy and kappa light-chain gene promoters .

The second <dna>element</dna> is found upstream of both <dna>heavy and kappa light-chain gene promoters</dna> .


This element directs lymphoid-specific transcription even in the presence of viral enhancers .

This element directs lymphoid-specific transcription even in the presence of <dna>viral enhancers</dna> .


We have sought nuclear factors that might bind specifically to these two regulatory elements by application of a modified gel electrophoresis DNA binding assay .

We have sought nuclear factors that might bind specifically to these two <dna>regulatory elements</dna> by application of a modified gel electrophoresis DNA binding assay .


We report here the identification of a human B-cell nuclear factor ( IgNF-A ) that binds to DNA sequences in the upstream regions of both the mouse heavy and kappa light-chain gene promoters and also to the mouse heavy-chain gene enhancer .

We report here the identification of a <protein>human B-cell nuclear factor</protein> ( <protein>IgNF-A</protein> ) that binds to <dna>DNA sequences</dna> in the <dna>upstream regions</dna> of both the <dna>mouse heavy and kappa light-chain gene promoters</dna> and also to the <dna>mouse heavy-chain gene enhancer</dna> .


This sequence-specific binding is probably mediated by a highly conserved sequence motif , ATTTGCAT , present in all three transcriptional elements .

This sequence-specific binding is probably mediated by a highly conserved sequence motif , ATTTGCAT , present in all three <dna>transcriptional elements</dna> .


Interestingly , a factor showing similar binding specificity to IgNF-A is also present in human HeLa cells .

Interestingly , a factor showing similar binding specificity to <dna>IgNF-A</dna> is also present in <cell_line>human HeLa cells</cell_line> .


The new world primates as animal models of glucocorticoid resistance .


Many New World primate species have greatly increased plasma cortisol concentrations , decreased plasma cortisol binding globulin capacity and affinity , marked resistance of the hypothalamic-pituitary-adrenal axis to suppression by dexamethasone , and no biological evidence of glucocorticoid excess .


These primates also have high levels of circulating progesterone , estrogen , mineralocorticoid , androgen and vitamin D .


The glucocorticoid target tissues that have been examined ( circulating mononuclear lymphocytes and cultured skin fibroblasts ) have normal concentrations of glucocorticoid receptors with decreased affinity for dexamethasone .

The glucocorticoid target tissues that have been examined ( <cell_type>circulating mononuclear lymphocytes</cell_type> and <cell_line>cultured skin fibroblasts</cell_line> ) have normal concentrations of <protein>glucocorticoid receptors</protein> with decreased affinity for dexamethasone .


Transformation of B-lymphocytes with the Epstein-Barr virus leads to glucocorticoid receptor induction that is less than that observed with cells from Old World primates .

Transformation of <cell_type>B-lymphocytes</cell_type> with the Epstein-Barr virus leads to <protein>glucocorticoid receptor</protein> induction that is less than that observed with cells from Old World primates .


The receptor in these cells has a low affinity for dexamethasone .


The low affinity leads to an increased loss of specific bound ligand during thermal activation .


Meroreceptor generation is normal .


The molecular weight of the receptor , determined by SDS-PAGE , is similar to that of Old World primates ( approximately 92 , 000 ) and the activation pattern per se , examined in vitro by heating cytosol and performing phosphocellulose chromatography , appears similar to that of human controls .


The ratios of nuclear to cytosolic hormone-receptor-complexes and of cytosolic activated to unactivated receptor complexes in intact cells are similar to Old World primates .

The ratios of nuclear to <protein>cytosolic hormone-receptor-complexes</protein> and of cytosolic activated to <protein>unactivated receptor complexes</protein> in intact cells are similar to Old World primates .


Results from mixing studies do not support the hypothesis that a binding inhibitor ( s ) or a deficient cytosolic positive modifier ( s ) of binding underlies the findings in these primates .


The New World primates , unlike men with the syndrome of primary cortisol resistance , have compensated for their condition with intra-adrenal and mineralocorticoid receptor adaptations .


Thus , unlike Old World primates , cortisol in New World primates has only weak sodium-retaining potency because the aldosterone receptor has a low affinity for cortisol .

Thus , unlike Old World primates , cortisol in New World primates has only weak sodium-retaining potency because the <protein>aldosterone receptor</protein> has a low affinity for cortisol .


The common element that would explain the apparent resistance to six steroid hormones in New World primates


Acetylation and modulation of erythroid Kruppel-like factor ( EKLF ) activity by interaction with histone acetyltransferases .

Acetylation and modulation of <protein>erythroid Kruppel-like factor</protein> ( <protein>EKLF</protein> ) activity by interaction with <protein>histone acetyltransferases</protein> .


Erythroid Kruppel-like factor ( EKLF ) is a red cell-specific transcriptional activator that is crucial for consolidating the switch to high levels of adult beta-globin expression during erythroid ontogeny .

<protein>Erythroid Kruppel-like factor</protein> ( <protein>EKLF</protein> ) is a <protein>red cell-specific transcriptional activator</protein> that is crucial for consolidating the switch to high levels of adult beta-globin expression during erythroid ontogeny .


EKLF is required for integrity of the chromatin structure at the beta-like globin locus , and it interacts with a positive-acting factor in vivo .

<protein>EKLF</protein> is required for integrity of the chromatin structure at the <dna>beta-like globin locus</dna> , and it interacts with a <protein>positive-acting factor</protein> in vivo .


We find that EKLF is an acetylated transcription factor , and that it interacts in vivo with CBP , p300 , and P/CAF .

We find that <protein>EKLF</protein> is an <protein>acetylated transcription factor</protein> , and that it interacts in vivo with <protein>CBP</protein> , <protein>p300</protein> , and <protein>P/CAF</protein> .


However , its interactions with these histone acetyltransferases are not equivalent , as CBP and p300 , but not P/CAF , utilize EKLF as a substrate for in vitro acetylation within its trans-activation region .

However , its interactions with these <protein>histone acetyltransferases</protein> are not equivalent , as <protein>CBP</protein> and <protein>p300</protein> , but not <protein>P/CAF</protein> , utilize <protein>EKLF</protein> as a substrate for in vitro acetylation within its trans-activation region .


The functional effects of these interactions are that CBP and p300 , but not P/CAF , enhance EKLF 's transcriptional activation of the beta-globin promoter in erythroid cells .

The functional effects of these interactions are that <protein>CBP</protein> and <protein>p300</protein> , but not <protein>P/CAF</protein> , enhance <protein>EKLF</protein> 's transcriptional activation of the <dna>beta-globin promoter</dna> in <cell_type>erythroid cells</cell_type> .


These results establish EKLF as a tissue-specific transcription factor that undergoes post-translational acetylation and suggest a mechanism by which EKLF is able to alter chromatin structure and induce beta-globin expression within the beta-like globin cluster .

These results establish <protein>EKLF</protein> as a <protein>tissue-specific transcription factor</protein> that undergoes post-translational acetylation and suggest a mechanism by which <protein>EKLF</protein> is able to alter chromatin structure and induce beta-globin expression within the <dna>beta-like globin cluster</dna> .


Recognition of herpes simplex virus type 2 tegument proteins by CD4 T cells infiltrating human genital herpes lesions .

Recognition of <protein>herpes simplex virus type 2 tegument proteins</protein> by <cell_type>CD4 T cells</cell_type> infiltrating human genital herpes lesions .


The local cellular immune response to herpes simplex virus ( HSV ) is important in the control of recurrent HSV infection .


The antiviral functions of infiltrating CD4-bearing T cells may include cytotoxicity , inhibition of viral growth , lymphokine secretion , and support of humoral and CD8 responses .

The antiviral functions of <cell_type>infiltrating CD4-bearing T cells</cell_type> may include cytotoxicity , inhibition of viral growth , lymphokine secretion , and support of humoral and CD8 responses .


The antigens recognized by many HSV-specific CD4 T cells localizing to genital HSV-2 lesions are unknown .

The antigens recognized by many <cell_type>HSV-specific CD4 T cells</cell_type> localizing to genital HSV-2 lesions are unknown .


T cells recognizing antigens encoded within map units 0.67 to 0.73 of HSV DNA are frequently recovered from herpetic lesions .

<cell_type>T cells</cell_type> recognizing antigens encoded within map units 0.67 to 0.73 of <dna>HSV DNA</dna> are frequently recovered from herpetic lesions .


Expression cloning with this region of DNA now shows that tegument protein VP22 and the viral dUTPase , encoded by genes UL49 and UL50 , respectively , are T-cell antigens .

Expression cloning with this region of DNA now shows that <protein>tegument protein</protein> <protein>VP22</protein> and the <protein>viral dUTPase</protein> , encoded by <dna>genes UL49 and UL50</dna> , respectively , are <protein>T-cell antigens</protein> .


Separate epitopes in VP22 were defined for T-cell clones from each of three patients .

Separate <protein>epitopes</protein> in <protein>VP22</protein> were defined for <cell_line>T-cell clones</cell_line> from each of three patients .


Reactivity with the tegument protein encoded by UL21 was identified for an additional patient .

Reactivity with the <protein>tegument protein</protein> encoded by <dna>UL21</dna> was identified for an additional patient .


Three new epitopes were identified in VP16 , a tegument protein associated with VP22 .

Three new epitopes were identified in <protein>VP16</protein> , a <protein>tegument protein</protein> associated with <protein>VP22</protein> .


Some tegument-specific CD4 T-cell clones exhibited cytotoxic activity against HSV-infected cells .

Some <cell_line>tegument-specific CD4 T-cell clones</cell_line> exhibited cytotoxic activity against <cell_type>HSV-infected cells</cell_type> .


These results suggest that herpes simplex tegument proteins are processed for antigen presentation in vivo and are possible candidate compounds for herpes simplex vaccines .

These results suggest that <protein>herpes simplex tegument proteins</protein> are processed for antigen presentation in vivo and are possible candidate compounds for herpes simplex vaccines .


Fibrinogen activates NF-kappa B transcription factors in mononuclear phagocytes .

<protein>Fibrinogen</protein> activates <protein>NF-kappa B transcription factors</protein> in <cell_type>mononuclear phagocytes</cell_type> .


Adhesion to extracellular matrices is known to modulate leukocyte activation , although the mechanisms are not fully understood .


Mononuclear phagocytes are exposed to fibrinous provisional matrix throughout migration into inflammatory foci , so this study was undertaken to determine whether fibrinogen triggers activation of NF-kappa B transcription factors .

<cell_type>Mononuclear phagocytes</cell_type> are exposed to fibrinous provisional matrix throughout migration into inflammatory foci , so this study was undertaken to determine whether fibrinogen triggers activation of <protein>NF-kappa B transcription factors</protein> .


U937 cells differentiated with PMA in nonadherent culture were shown to express two fibrinogen-binding integrins , predominately CD11b/CD18 , and to a lesser extent , CD11c/CD18 .

<cell_line>U937 cells</cell_line> differentiated with PMA in <cell_line>nonadherent culture</cell_line> were shown to express two <protein>fibrinogen-binding integrins</protein> , predominately <protein>CD11b/CD18</protein> , and to a lesser extent , <protein>CD11c/CD18</protein> .


Cells stimulated with fibrinogen ( 10-100 microg/ml ) /Mn2+ ( 50 microM ) for 2 h were examined by electrophoretic mobility shift assay .

Cells stimulated with <protein>fibrinogen</protein> ( 10-100 microg/ml ) /Mn2+ ( 50 microM ) for 2 h were examined by electrophoretic mobility shift assay .


NF-kappa B activation , minimal in unstimulated cells , was substantially up-regulated by fibrinogen .

<protein>NF-kappa B</protein> activation , minimal in <cell_type>unstimulated cells</cell_type> , was substantially up-regulated by <protein>fibrinogen</protein> .


Fibrinogen also caused activation of AP-1 , but not SP1 or cAMP response element-binding protein ( CREB ) factors .

<protein>Fibrinogen</protein> also caused activation of <protein>AP-1</protein> , but not <protein>SP1</protein> or <protein>cAMP response element-binding protein ( CREB ) factors</protein> .


Blocking mAbs against CD18 and CD11b abrogated fibrinogen -induced NF-kappa B activation .

Blocking <protein>mAbs</protein> against <protein>CD18</protein> and <protein>CD11b</protein> abrogated <protein>fibrinogen</protein> -induced <protein>NF-kappa B</protein> activation .


To determine the effects on transcriptional regulation , U937 cells were transfected with a plasmid containing the HIV-1 enhancer ( bearing two NF-kappa B sites ) coupled to a chloramphenicol acetyltransferase ( CAT ) reporter .

To determine the effects on transcriptional regulation , <cell_line>U937 cells</cell_line> were transfected with a plasmid containing the <dna>HIV-1 enhancer</dna> ( bearing two <dna>NF-kappa B sites</dna> ) coupled to a <dna>chloramphenicol acetyltransferase ( CAT ) reporter</dna> .


Cells were subsequently stimulated with 1 ) PMA for 24 h , inducing CAT activity by 2.6-fold , 2 ) fibrinogen /Mn2+ for 2 h , inducing CAT activity by 3.2-fold , or 3 ) costimulation with fibrinogen and PMA , inducing 5.7-fold the CAT activity induced by PMA alone .

Cells were subsequently stimulated with 1 ) PMA for 24 h , inducing CAT activity by 2.6-fold , 2 ) <protein>fibrinogen</protein> /Mn2+ for 2 h , inducing CAT activity by 3.2-fold , or 3 ) costimulation with <protein>fibrinogen</protein> and PMA , inducing 5.7-fold the CAT activity induced by PMA alone .


We conclude that contact with fibrinogen-derived proteins may contribute to mononuclear phagocyte activation by signaling through CD11b/CD18 , resulting in selective activation of transcriptional regulatory factors , including NF-kappa B .

We conclude that contact with <protein>fibrinogen-derived proteins</protein> may contribute to mononuclear phagocyte activation by signaling through <protein>CD11b/CD18</protein> , resulting in selective activation of <protein>transcriptional regulatory factors</protein> , including <protein>NF-kappa B</protein> .


Peripheral blood T cells and monocytes and B cell lines derived from patients with lupus express estrogen receptor transcripts similar to those of normal cells .

<cell_type>Peripheral blood T cells and monocytes</cell_type> and <cell_line>B cell lines</cell_line> derived from patients with lupus express estrogen receptor transcripts similar to those of <cell_type>normal cells</cell_type> .


OBJECTIVE : To identify and characterize estrogen receptor ( ER ) transcripts expressed in immune cells of patients with systemic lupus erythematosus ( SLE ) and healthy donors .

OBJECTIVE : To identify and characterize <rna>estrogen receptor ( ER ) transcripts</rna> expressed in <cell_type>immune cells</cell_type> of patients with systemic lupus erythematosus ( SLE ) and healthy donors .


METHODS : Peripheral blood monocytes and T cells were prepared from patients with SLE ( n = 6 ) and healthy donors ( n = 8 ) .

METHODS : <cell_type>Peripheral blood monocytes and T cells</cell_type> were prepared from patients with SLE ( n = 6 ) and healthy donors ( n = 8 ) .


T cells were separated into CD4 and CD8 .

<cell_type>T cells</cell_type> were separated into <cell_type>CD4</cell_type> and <cell_type>CD8</cell_type> .


Some monocytes and T cells were stimulated with estradiol , PMA , and ionomycin .

Some <cell_type>monocytes</cell_type> and <cell_type>T cells</cell_type> were stimulated with estradiol , PMA , and ionomycin .


Epstein-Barr virus-transformed B cell lines ( n = 7 ) and B cell hybridomas ( n = 2 ) established from patients with SLE and a healthy individual were used as a B cell source .

Epstein-Barr virus-transformed <cell_line>B cell lines</cell_line> ( n = 7 ) and <cell_line>B cell hybridomas</cell_line> ( n = 2 ) established from patients with SLE and a healthy individual were used as a B cell source .


These cells were examined for ER mRNA by reverse transcription nested polymerase chain reaction .

These cells were examined for <rna>ER mRNA</rna> by reverse transcription nested polymerase chain reaction .


Amplified cDNA were sequenced by standard methods .

Amplified <dna>cDNA</dna> were sequenced by standard methods .


RESULTS : In all cells tested , ER mRNA was expressed without prior in vitro stimulation .

RESULTS : In all cells tested , <rna>ER mRNA</rna> was expressed without prior in vitro stimulation .


Partial sequences from exons 1-8 were nearly identical to the published sequence of the human ER mRNA .

Partial sequences from <dna>exons 1-8</dna> were nearly identical to the published sequence of the <rna>human ER mRNA</rna> .


There were no notable differences in the ER transcripts between patients and healthy controls .

There were no notable differences in the <rna>ER transcripts</rna> between patients and healthy controls .


Variant receptor transcripts lacking exon 5 or exon 7 , which encodes the hormone binding domain , were identified in the majority of the cells .

Variant receptor transcripts lacking <dna>exon 5</dna> or <dna>exon 7</dna> , which encodes the <protein>hormone binding domain</protein> , were identified in the majority of the cells .


Precise deletion of the exons suggests that they are alternatively spliced transcripts .


Whether the detected transcripts are translated into functional receptor proteins remains to be determined .

Whether the detected transcripts are translated into <protein>functional receptor proteins</protein> remains to be determined .


In vitro stimulation did not affect ER mRNA expression .

In vitro stimulation did not affect <rna>ER mRNA</rna> expression .


The presence of variants did not correlate with disease activity or medication .


CONCLUSION : Monocytes , T cells , and B cells in patients express transcripts of the normal wild type ER and the hormone binding domain variants in vivo .

CONCLUSION : <cell_type>Monocytes</cell_type> , <cell_type>T cells</cell_type> , and <cell_type>B cells</cell_type> in patients express transcripts of the normal <protein>wild type ER</protein> and the <protein>hormone binding domain variants</protein> in vivo .


DNA damaging agents induce expression of Fas ligand and subsequent apoptosis in T lymphocytes via the activation of NF-kappa B and AP-1 .

DNA damaging agents induce expression of <protein>Fas ligand</protein> and subsequent apoptosis in <cell_type>T lymphocytes</cell_type> via the activation of <protein>NF-kappa B</protein> and <protein>AP-1</protein> .


Apoptosis induced by DNA damage and other stresses can proceed via expression of Fas ligand ( FasL ) and ligation of its receptor , Fas ( CD95 ) .

Apoptosis induced by DNA damage and other stresses can proceed via expression of <protein>Fas ligand</protein> ( <protein>FasL</protein> ) and ligation of its receptor , Fas ( CD95 ) .


We report that activation of the two transcription factors NF-kappa B and AP-1 is crucially involved in FasL expression induced by etoposide , teniposide , and UV irradiation .

We report that activation of the two <protein>transcription factors NF-kappa B and AP-1</protein> is crucially involved in <protein>FasL</protein> expression induced by etoposide , teniposide , and UV irradiation .


A nondegradable mutant of I kappa B blocked both FasL expression and apoptosis induced by DNA damage but not Fas ligation .

A <protein>nondegradable mutant</protein> of <protein>I kappa B</protein> blocked both <protein>FasL</protein> expression and apoptosis induced by DNA damage but not Fas ligation .


These stimuli also induced the stress-activated kinase pathway ( SAPK/JNK ) , which was required for the maximal induction of apoptosis .


A 1.2 kb FasL promoter responded to DNA damage , as well as coexpression with p65 Rel or Fos/Jun .

A 1.2 kb <dna>FasL promoter</dna> responded to DNA damage , as well as coexpression with <protein>p65 Rel</protein> or <protein>Fos/Jun</protein> .


Mutations in the relevant NF-kappa B and AP-1 binding sites eliminated these responses .

Mutations in the relevant <dna>NF-kappa B and AP-1 binding sites</dna> eliminated these responses .


Thus , activation of NF-kappa B and AP-1 contributes to stress-induced apoptosis via the expression of FasL .

Thus , activation of <protein>NF-kappa B</protein> and <protein>AP-1</protein> contributes to stress-induced apoptosis via the expression of <protein>FasL</protein> .


A small , nonpeptidyl mimic of granulocyte-colony-stimulating factor [ see commetns ]

A small , nonpeptidyl mimic of <protein>granulocyte-colony-stimulating factor</protein> [ see commetns ]


A nonpeptidyl small molecule SB 247464 , capable of activating granulocyte-colony-stimulating factor ( G-CSF ) signal transduction pathways , was identified in a high-throughput assay in cultured cells .

A nonpeptidyl small molecule SB 247464 , capable of activating <protein>granulocyte-colony-stimulating factor</protein> ( <protein>G-CSF</protein> ) signal transduction pathways , was identified in a high-throughput assay in <cell_type>cultured cells</cell_type> .


Like G-CSF , SB 247464 induced tyrosine phosphorylation of multiple signaling proteins and stimulated primary murine bone marrow cells to form granulocytic colonies in vitro .

Like <protein>G-CSF</protein> , SB 247464 induced tyrosine phosphorylation of <protein>multiple signaling proteins</protein> and stimulated <cell_type>primary murine bone marrow cells</cell_type> to form <cell_type>granulocytic colonies</cell_type> in vitro .


It also elevated peripheral blood neutrophil counts in mice .

It also elevated <cell_type>peripheral blood neutrophil</cell_type> counts in mice .