Western blot analysis showed that N-acetyl-cysteine reduced the accumulation of the 47-kD mature glycoprotein in LPS-treated cells , a finding consistent with the results of the immunofluorescence studies .

Western blot analysis showed that N-acetyl-cysteine reduced the accumulation of the <protein>47-kD mature glycoprotein</protein> in <cell_line>LPS-treated cells</cell_line> , a finding consistent with the results of the immunofluorescence studies .


Furthermore , these conditions did not result in an accumulation of the less mature forms of TF .

Furthermore , these conditions did not result in an accumulation of the less mature forms of <protein>TF</protein> .


When considered together , these data suggest that antioxidants exert their effects by impairing translation and/or by causing degradation of newly translated protein .

When considered together , these data suggest that antioxidants exert their effects by impairing translation and/or by causing degradation of newly <protein>translated protein</protein> .


The effect of antioxidants on tumor necrosis factor appeared to be species specific , with no effect on LPS-induced tumor necrosis factor in murine cells , but with inhibition in human monocytes .

The effect of antioxidants on <protein>tumor necrosis factor</protein> appeared to be species specific , with no effect on LPS-induced tumor necrosis factor in murine cells , but with inhibition in <cell_type>human monocytes</cell_type> .


The posttranscriptional effect of antioxidants on TF expression data suggests a novel mechanism whereby these agents might modulate monocyte /macrophage activation .

The posttranscriptional effect of antioxidants on <protein>TF</protein> expression data suggests a novel mechanism whereby these agents might modulate <cell_type>monocyte</cell_type> <cell_type>/macrophage</cell_type> activation .


Characterization of the CD48 gene demonstrates a positive element that is specific to Epstein-Barr virus-immortalized B-cell lines and contains an essential NF-kappa B site .

Characterization of the <dna>CD48 gene</dna> demonstrates a positive element that is specific to <cell_type>Epstein-Barr virus-immortalized B-cell lines</cell_type> and contains an essential <dna>NF-kappa B site</dna> .


Epstein-Barr virus ( EBV ) infection of mature , resting B cells drives them to become lymphoblasts expressing high levels of cell surface molecules , such as CD48 , characteristically expressed on normal activated B cells .

Epstein-Barr virus ( EBV ) infection of mature , <cell_type>resting B cells</cell_type> drives them to become lymphoblasts expressing high levels of cell surface molecules , such as <protein>CD48</protein> , characteristically expressed on <cell_type>normal activated B cells</cell_type> .


Here , we report on the identification of an enhancer element in the CD48 gene which reproducibly confers strong transcriptional activity only in EBV-positive B-lymphoblastoid cell lines .

Here , we report on the identification of an <dna>enhancer element</dna> in the <dna>CD48 gene</dna> which reproducibly confers strong transcriptional activity only in <cell_line>EBV-positive B-lymphoblastoid cell lines</cell_line> .


The element is not activated upon infection of established EBV-negative B-cell lines , indicating that EBV fails to drive these cells to a fully lymphoblastoid phenotype .

The element is not activated upon infection of established <cell_line>EBV-negative B-cell lines</cell_line> , indicating that EBV fails to drive these cells to a fully <cell_type>lymphoblastoid phenotype</cell_type> .


An NF-kappa B binding site is an essential component of the element but alone is not sufficient to account for the activity or the specificity of the element .

An <protein>NF-kappa B</protein> binding site is an essential component of the element but alone is not sufficient to account for the activity or the specificity of the element .


We have detected a specific nuclear protein complex that binds to the element and show that NF-kappa B1 ( p50 ) is a part of this complex .

We have detected a specific <protein>nuclear protein complex</protein> that binds to the element and show that <protein>NF-kappa B1</protein> ( <protein>p50</protein> ) is a part of this complex .


The EBV-encoded latent membrane protein 1 is capable of transactivating the isolated CD48 NF-kappa B site but not the intact element , suggesting that the latent membrane protein 1 -driven activation of NF-kappa B/Rel must interact with other regulatory pathways to control expression of cellular genes as EBV drives resting B cells into the cell cycle .

The <protein>EBV-encoded latent membrane protein 1</protein> is capable of transactivating the isolated <protein>CD48</protein> <dna>NF-kappa B site</dna> but not the <dna>intact element</dna> , suggesting that the <protein>latent membrane protein 1</protein> -driven activation of <protein>NF-kappa B/Rel</protein> must interact with other regulatory pathways to control expression of cellular genes as EBV drives <cell_type>resting B cells</cell_type> into the cell cycle .


Thapsigargin induces IL-2 receptor alpha-chain in human peripheral and Jurkat T cells via a protein kinase C -independent mechanism .

Thapsigargin induces <protein>IL-2 receptor alpha-chain</protein> in <cell_type>human peripheral</cell_type> and <cell_line>Jurkat T cells</cell_line> via a <protein>protein kinase C</protein> -independent mechanism .


Thapsigargin ( TG ) , an inhibitor of Ca ( 2+ ) -ATPase , depletes intracellular Ca2+ stores and induces a sustained Ca2+ influx without altering phosphatidyl inositol levels .

Thapsigargin ( TG ) , an inhibitor of <protein>Ca ( 2+ ) -ATPase</protein> , depletes intracellular Ca2+ stores and induces a sustained Ca2+ influx without altering phosphatidyl inositol levels .


TG plus phorbol myristate acetate ( PMA ) but not TG alone induced IL-2 in Jurkat T cells , suggesting that TG had no effect on protein kinase C ( PKC ) .

TG plus phorbol myristate acetate ( PMA ) but not TG alone induced <protein>IL-2</protein> in <cell_line>Jurkat T cells</cell_line> , suggesting that TG had no effect on <protein>protein kinase C</protein> ( <protein>PKC</protein> ) .


However , TG induced increases in IL-2R alpha protein as well as IL-2R alpha mRNA in Jurkat T cells in a dose-dependent manner .

However , TG induced increases in <protein>IL-2R alpha protein</protein> as well as <rna>IL-2R alpha mRNA</rna> in <cell_line>Jurkat T cells</cell_line> in a dose-dependent manner .


A similar increase in IL-2R alpha by TG was also observed in human peripheral T cells .

A similar increase in <protein>IL-2R alpha</protein> by TG was also observed in <cell_type>human peripheral T cells</cell_type> .


Further , like PMA , TG markedly induced NF kappa B in Jurkat T cells .

Further , like PMA , TG markedly induced <protein>NF kappa B</protein> in <cell_line>Jurkat T cells</cell_line> .


However , TG and PMA exhibited a synergistic action on IL-2R alpha expression , suggesting that TG and PMA induce IL-2R alpha through distinct pathways .

However , TG and PMA exhibited a synergistic action on <protein>IL-2R alpha</protein> expression , suggesting that TG and PMA induce <protein>IL-2R alpha</protein> through distinct pathways .


PMA -but not TG-induced IL-2R alpha is inhibited by the PKC inhibitor H7 , whereas TG -but not PMA-induced IL-2R alpha was inhibited by cholera toxin , forskolin and 1 , 9-dideoxy forskolin .

<protein>PMA -but not TG-induced IL-2R alpha</protein> is inhibited by the <protein>PKC</protein> inhibitor H7 , whereas <protein>TG -but not PMA-induced IL-2R alpha</protein> was inhibited by cholera toxin , forskolin and 1 , 9-dideoxy forskolin .


In toto , these results suggest that TG induces IL-2R alpha in human T cells through a PKC -independent pathway .

In toto , these results suggest that TG induces <protein>IL-2R alpha</protein> in <cell_type>human T cells</cell_type> through a <protein>PKC</protein> -independent pathway .


Physiological concentration of estradiol inhibits polymorphonuclear leukocyte chemotaxis via a receptor mediated system .

Physiological concentration of estradiol inhibits <cell_type>polymorphonuclear leukocyte</cell_type> chemotaxis via a receptor mediated system .


Estrogen exhibits a variety of actions , including immuno-modulatory effects , in vivo and in vitro .


The mechanism by which estrogen exerts its anti-inflammatory effect is not yet understood .


We investigated the possible mechanisms of estradiol acting via the polymorphonuclear leukocytes ( PMNs ) , which are important in the immune response .

We investigated the possible mechanisms of estradiol acting via the <cell_type>polymorphonuclear leukocytes</cell_type> ( <cell_type>PMNs</cell_type> ) , which are important in the immune response .


The agent , 17 beta-estradiol , but not 17 alpha-estradiol , significantly reduced PMNs chemotaxis to FMLP in a dose-dependent manner ( control vs estrogen 10 ( -10 ) - ( -6 ) M , P < 0.05 ) .

The agent , 17 beta-estradiol , but not 17 alpha-estradiol , significantly reduced <cell_type>PMNs</cell_type> chemotaxis to FMLP in a dose-dependent manner ( control vs estrogen 10 ( -10 ) - ( -6 ) M , P < 0.05 ) .


Physiological concentrations of estradiol significantly reduced the chemotaxis of PMNs ( 10 ( -10 ) mol ) .

Physiological concentrations of estradiol significantly reduced the chemotaxis of <cell_type>PMNs</cell_type> ( 10 ( -10 ) mol ) .


Pre-incubation with clomiphene or tamoxifen which are estrogen receptor antagonists , eliminated the inhibitory effect of 17 beta-estradiol on the chemotaxis of PMNs , restoring it to the control level .

Pre-incubation with clomiphene or tamoxifen which are estrogen receptor antagonists , eliminated the inhibitory effect of 17 beta-estradiol on the chemotaxis of <cell_type>PMNs</cell_type> , restoring it to the control level .


These observations suggest that 17 beta-estradiol suppressed the chemotaxis of PMNs by a receptor-dependent mechanism .

These observations suggest that 17 beta-estradiol suppressed the chemotaxis of <cell_type>PMNs</cell_type> by a receptor-dependent mechanism .


In addition , the level of estradiol in human plasma , which PMNs were drawn , showed a close , inverse correlation with the PMNs chemotaxis to FMLP ( r = -0.821 p < 0.001 ) .

In addition , the level of estradiol in <cell_type>human plasma</cell_type> , which <cell_type>PMNs</cell_type> were drawn , showed a close , inverse correlation with the <cell_type>PMNs</cell_type> chemotaxis to FMLP ( r = -0.821 p < 0.001 ) .


Estrogen may modify the activity of neutrophils during the normal menstrual cycle , not only during pregnancy , and influence inflammation .

Estrogen may modify the activity of <cell_type>neutrophils</cell_type> during the normal menstrual cycle , not only during pregnancy , and influence inflammation .


Identification of the TCL1 gene involved in T-cell malignancies .

Identification of the <dna>TCL1 gene</dna> involved in <cell_type>T-cell</cell_type> malignancies .


The TCL1 locus on chromosome 14q32.1 is frequently involved in chromosomal translocations and inversions with one of the T-cell receptor loci in human T-cell leukemias and lymphomas .

The <dna>TCL1 locus</dna> on <dna>chromosome 14q32.1</dna> is frequently involved in chromosomal translocations and inversions with one of the <dna>T-cell receptor loci</dna> in human T-cell leukemias and lymphomas .


The chromosome 14 region translocated or rearranged involves approximately 350 kb of DNA at chromosome band 14q32.1 .

The <dna>chromosome 14 region</dna> translocated or rearranged involves approximately 350 kb of DNA at chromosome band 14q32.1 .


Within this region we have identified a gene coding for a 1.3-kb transcript , expressed only in restricted subsets of cells within the lymphoid lineage and expressed at high levels in leukemic cells carrying a t ( 14 ; 14 ) ( q11 ; q32 ) chromosome translocation or a inv ( 14 ) ( q11 ; q32 ) chromosome inversion .

Within this region we have identified a gene coding for a <rna>1.3-kb transcript</rna> , expressed only in restricted subsets of cells within the <cell_type>lymphoid lineage</cell_type> and expressed at high levels in <cell_type>leukemic cells</cell_type> carrying a t ( 14 ; 14 ) ( q11 ; q32 ) chromosome translocation or a inv ( 14 ) ( q11 ; q32 ) chromosome inversion .


The cognate cDNA sequence reveals an open reading frame of 342 nt encoding a protein of 14 kDa .

The <dna>cognate cDNA sequence</dna> reveals an <dna>open reading frame</dna> of 342 nt encoding a <protein>protein of 14 kDa</protein> .


The TCL1 gene sequence , which , to our knowledge , shows no sequence homology with other human genes , is preferentially expressed early in T- and B-lymphocyte differentiation .

The <dna>TCL1 gene</dna> sequence , which , to our knowledge , shows no sequence homology with other <dna>human genes</dna> , is preferentially expressed early in <cell_type>T- and B-lymphocyte</cell_type> differentiation .


Identification of a region which directs the monocytic activity of the colony-stimulating factor 1 ( macrophage colony-stimulating factor ) receptor promoter and binds PEBP2/CBF ( AML1 ) .

Identification of a region which directs the monocytic activity of the <dna>colony-stimulating factor 1 ( macrophage colony-stimulating factor ) receptor promoter</dna> and binds <protein>PEBP2/CBF</protein> ( <protein>AML1</protein> ) .


The receptor for the macrophage colony-stimulating factor ( or colony-stimulating factor 1 [ CSF-1 ] ) is expressed from different promoters in monocytic cells and placental trophoblasts .

The receptor for the <protein>macrophage colony-stimulating factor</protein> ( or <protein>colony-stimulating factor 1</protein> [ <protein>CSF-1</protein> ] ) is expressed from different promoters in <cell_type>monocytic cells</cell_type> and <cell_type>placental trophoblasts</cell_type> .


We have demonstrated that the monocyte-specific expression of the CSF-1 receptor is regulated at the level of transcription by a tissue-specific promoter whose activity is stimulated by the monocyte/B-cell-specific transcription factor PU.1 ( D.-E.Zhang , C.J.Hetherington , H.-M.Chen , and D.G.Tenen , Mol.Cell. Biol.14 : 373-381 , 1994 ) .

We have demonstrated that the monocyte-specific expression of the <protein>CSF-1 receptor</protein> is regulated at the level of transcription by a <dna>tissue-specific promoter</dna> whose activity is stimulated by the <protein>monocyte/B-cell-specific transcription factor</protein> <protein>PU.1</protein> ( D.-E.Zhang , C.J.Hetherington , H.-M.Chen , and D.G.Tenen , Mol.Cell. Biol.14 : 373-381 , 1994 ) .


Here we report that the tissue specificity of this promoter is also mediated by sequences in a region II ( bp -88 to - 59 ) , which lies 10 bp upstream from the PU.1-binding site .

Here we report that the tissue specificity of this <dna>promoter</dna> is also mediated by sequences in a <dna>region II</dna> ( bp -88 to - 59 ) , which lies <dna>10 bp upstream</dna> from the <dna>PU.1-binding site</dna> .


When analyzed by DNase footprinting , region II was protected preferentially in monocytic cells .

When analyzed by <protein>DNase</protein> footprinting , <dna>region II</dna> was protected preferentially in <cell_type>monocytic cells</cell_type> .


Electrophoretic mobility shift assays confirmed that region II interacts specifically with nuclear proteins from monocytic cells .

Electrophoretic mobility shift assays confirmed that <dna>region II</dna> interacts specifically with <protein>nuclear proteins</protein> from <cell_type>monocytic cells</cell_type> .


Two gel shift complexes ( Mono A and Mono B ) were formed with separate sequence elements within this region .

Two <protein>gel shift complexes</protein> ( <protein>Mono A</protein> and <protein>Mono B</protein> ) were formed with separate sequence elements within this region .


Competition and supershift experiments indicate that Mono B contains a member of the polyomavirus enhancer-binding protein 2/core-binding factor ( PEBP2/CBF ) family , which includes the AML1 gene product , while Mono A is a distinct complex preferentially expressed in monocytic cells .

Competition and supershift experiments indicate that <protein>Mono B</protein> contains a member of the <protein>polyomavirus enhancer-binding protein 2/core-binding factor ( PEBP2/CBF ) family ,</protein> which includes the AML1 gene product , while <protein>Mono A</protein> is a distinct complex preferentially expressed in <cell_type>monocytic cells</cell_type> .


Promoter constructs with mutations in these sequence elements were no longer expressed specifically in monocytes .

<dna>Promoter constructs</dna> with mutations in these sequence elements were no longer expressed specifically in <cell_type>monocytes</cell_type> .


Furthermore , multimerized region II sequence elements enhanced the activity of a heterologous thymidine kinase promoter in monocytic cells but not other cell types tested .

Furthermore , <dna>multimerized region II sequence elements</dna> enhanced the activity of a heterologous thymidine kinase promoter in <cell_type>monocytic cells</cell_type> but not other cell types tested .


These results indicate that the monocyte/B-cell-specific transcription factor PU.1 and the Mono A and Mono B protein complexes act in concert to regulate monocyte-specific transcription of the CSF-1 receptor .

These results indicate that the <protein>monocyte/B-cell-specific transcription factor</protein> <protein>PU.1</protein> and the <protein>Mono A and Mono B protein complexes</protein> act in concert to regulate monocyte-specific transcription of the <protein>CSF-1 receptor</protein> .


Pyrrolidine dithiocarbamate , a potent inhibitor of nuclear factor kappa B ( NF-kappa B ) activation , prevents apoptosis in human promyelocytic leukemia HL-60 cells and thymocytes .

Pyrrolidine dithiocarbamate , a potent inhibitor of <protein>nuclear factor kappa B</protein> ( <protein>NF-kappa B</protein> ) activation , prevents apoptosis in human <cell_line>promyelocytic leukemia HL-60 cells</cell_line> and <cell_type>thymocytes</cell_type> .


We examined the effect of pyrrolidine dithiocarbamate ( PDTC ) , which potently blocks the activation of nuclear factor kappa B ( NF-kappa B ) , on the induction of apoptosis by a variety of agents .

We examined the effect of pyrrolidine dithiocarbamate ( PDTC ) , which potently blocks the activation of <protein>nuclear factor kappa B</protein> ( <protein>NF-kappa B</protein> ) , on the induction of apoptosis by a variety of agents .


Treatment of a human promyelocytic leukemia cell line , HL-60 , with 10 micrograms/mL etoposide or 2 microM 1-beta-D-arabinofuranosylcytosine induced NF-kappa B activation within 1 hr and subsequently caused apoptosis within 3-4 hr .

Treatment of a <cell_line>human promyelocytic leukemia cell line</cell_line> , <cell_line>HL-60</cell_line> , with 10 micrograms/mL etoposide or 2 microM 1-beta-D-arabinofuranosylcytosine induced <protein>NF-kappa B</protein> activation within 1 hr and subsequently caused apoptosis within 3-4 hr .


The simultaneous addition of 50-500 microM PDTC with these agents blocked NF-kappa B activation and completely abrogated both morphologically apoptotic changes and internucleosomal DNA fragmentation for up to 6 hr .

The simultaneous addition of 50-500 microM PDTC with these agents blocked <protein>NF-kappa B</protein> activation and completely abrogated both morphologically apoptotic changes and internucleosomal DNA fragmentation for up to 6 hr .


However , PDTC failed to inhibit the endonuclease activity contained in the whole cell lysates .

However , PDTC failed to inhibit the <protein>endonuclease</protein> activity contained in the whole cell lysates .


The inhibitory effect of PDTC was also observed in etoposide -and dexamethasone-induced apoptosis in human thymocytes at a concentration of 1-10 microM .

The inhibitory effect of PDTC was also observed in etoposide -and dexamethasone-induced apoptosis in <cell_type>human thymocytes</cell_type> at a concentration of 1-10 microM .


Since PDTC has both antioxidant and metal-ion chelating activities , we tested the effects of N-acetyl-L-cysteine ( NAC ) ( antioxidant ) or o-phenanthroline ( OP ) ( metal-ion chelator ) on the induction of apoptosis .


Pretreatment of HL-60 cells or thymocytes with 100-500 microM OP for 2 hr , but not 10-60 mM NAC , suppressed subsequent occurrence of apoptosis induced by etoposide .

Pretreatment of HL-60 cells or <cell_type>thymocytes</cell_type> with 100-500 microM OP for 2 hr , but not 10-60 mM NAC , suppressed subsequent occurrence of apoptosis induced by etoposide .


These results suggest that the activation of NF-kappa B plays an important role in the apoptotic process of human hematopoietic cells .

These results suggest that the activation of <protein>NF-kappa B</protein> plays an important role in the apoptotic process of <cell_type>human hematopoietic cells</cell_type> .


Overexpression of protein kinase C-zeta stimulates leukemic cell differentiation .

Overexpression of <protein>protein kinase C-zeta</protein> stimulates <cell_type>leukemic cell</cell_type> differentiation .


A function for protein kinase C-zeta ( PKC-zeta ) , a member of the phorbol ester nonresponsive atypical protein kinase C subfamily , in modulating differentiation was examined in the leukemic U937 cell .

A function for <protein>protein kinase C-zeta</protein> ( <protein>PKC-zeta</protein> ) , a member of the phorbol ester nonresponsive atypical <protein>protein kinase C subfamily</protein> , in modulating differentiation was examined in the <cell_line>leukemic U937 cell</cell_line> .


Transfected U937 cells stably overexpressing PKC-zeta displayed a longer doubling time , lower saturation density at confluency , and an increase in adherence to plastic as compared to control cells .

Transfected <cell_line>U937 cells</cell_line> stably overexpressing <protein>PKC-zeta</protein> displayed a longer doubling time , lower saturation density at confluency , and an increase in adherence to plastic as compared to <cell_line>control cells</cell_line> .


PKC-zeta cells expressed a more differentiated phenotype as assessed by changes in morphology , surface antigen expression , and lysosomal enzyme activities and were distinct from parental U937 cells stimulated to differentiate by exposure to phorbol esters .

<cell_line>PKC-zeta cells</cell_line> expressed a more differentiated phenotype as assessed by changes in morphology , surface antigen expression , and <protein>lysosomal enzyme</protein> activities and were distinct from <cell_line>parental U937 cells</cell_line> stimulated to differentiate by exposure to phorbol esters .


In contrast to parental U937 cells , PKC-zeta cells constitutively expressed mRNA transcripts for c-jun and a low mobility AP-1 binding activity .

In contrast to parental <cell_line>U937 cells</cell_line> , <cell_line>PKC-zeta cells</cell_line> constitutively expressed <rna>mRNA transcripts</rna> for <dna>c-jun</dna> and a low mobility <protein>AP-1</protein> binding activity .


Thus , PKC-zeta overexpression stimulates a type of phenotypic differentiation that differs significantly from maturation occurring upon activation of other PKC subfamilies induced by phorbol ester treatment .

Thus , <protein>PKC-zeta</protein> overexpression stimulates a type of phenotypic differentiation that differs significantly from maturation occurring upon activation of other <protein>PKC subfamilies</protein> induced by phorbol ester treatment .


Increased expression of the c-jun protooncogene and an increase in AP-1 binding activity in PKC-zeta cells provides a potential mechanism for explaining the altered differentiation status of this cell .

Increased expression of the <dna>c-jun</dna> protooncogene and an increase in <protein>AP-1</protein> binding activity in <cell_line>PKC-zeta cells</cell_line> provides a potential mechanism for explaining the altered differentiation status of this cell .


A family of serine proteases expressed exclusively in myelo- monocytic cells specifically processes the nuclear factor-kappa B subunit p65 in vitro and may impair human immunodeficiency virus replication in these cells .

A family of <protein>serine proteases</protein> expressed exclusively in myelo- <cell_type>monocytic cells</cell_type> specifically processes the <protein>nuclear factor-kappa B subunit p65</protein> in vitro and may impair human immunodeficiency virus replication in these cells .


Two groups of U937 promonocytic cells were obtained by limiting dilution cloning which differed strikingly in their ability to support human immunodeficiency virus 1 ( HIV-1 ) replication .

Two groups of <cell_line>U937 promonocytic cells</cell_line> were obtained by limiting dilution cloning which differed strikingly in their ability to support human immunodeficiency virus 1 ( HIV-1 ) replication .


`` Plus '' clones replicated the virus efficiently , whereas `` minus '' clones did not .

<cell_line>`` Plus '' clones</cell_line> replicated the virus efficiently , whereas <cell_line>`` minus '' clones</cell_line> did not .


We examined these clones for differences in nuclear factor ( NF ) -kappa B activity which might account for the observed phenomenon .

We examined these clones for differences in <protein>nuclear factor ( NF ) -kappa B</protein> activity which might account for the observed phenomenon .


Stimulation of plus clones liberated the classical p50-p65 complex from cytoplasmic pools , whereas minus clones produced an apparently novel , faster-migrating complex , as judged by electrophoretic mobility shift assays .

Stimulation of <cell_line>plus clones</cell_line> liberated the classical <protein>p50-p65 complex</protein> from cytoplasmic pools , whereas <cell_line>minus clones</cell_line> produced an apparently novel , <protein>faster-migrating complex</protein> , as judged by electrophoretic mobility shift assays .


It is surprising that the faster-migrating complex was composed also of p50 and p65 .

It is surprising that the <protein>faster-migrating complex</protein> was composed also of <protein>p50</protein> and <protein>p65</protein> .


However , the p65 subunit was COOH-terminally truncated , as shown by immunoprecipitation .

However , the <protein>p65 subunit</protein> was COOH-terminally truncated , as shown by immunoprecipitation .


The truncation resulted from limited proteolysis of p65 during cellular extraction which released particular lysosomal serine proteases , such as elastase , cathepsin G , and proteinase 3 .

The truncation resulted from limited proteolysis of <protein>p65</protein> during cellular extraction which released particular <protein>lysosomal serine proteases</protein> , such as <protein>elastase</protein> , <protein>cathepsin G</protein> , and <protein>proteinase 3</protein> .


These specific proteases are coordinately expressed and were present exclusively in the minus U937 clones , but not in the plus clones , as demonstrated in the case of cathepsin G .

These specific proteases are coordinately expressed and were present exclusively in the <cell_line>minus U937 clones</cell_line> , but not in the <cell_line>plus clones</cell_line> , as demonstrated in the case of <protein>cathepsin G</protein> .


In addition , these proteases were detected in certain subclones of THP-1 and HL-60 cells and in primary monocytes , in each case correlating with the truncated from of p65 .

In addition , these proteases were detected in certain subclones of <cell_line>THP-1</cell_line> and <cell_line>HL-60 cells</cell_line> and in primary <cell_type>monocytes</cell_type> , in each case correlating with the truncated from of <protein>p65</protein> .


We demonstrate in vitro cleavage of p65 by purified elastase and cathepsin G .

We demonstrate in vitro cleavage of <protein>p65</protein> by purified <protein>elastase</protein> and <protein>cathepsin G</protein> .


It is possible that particular serine proteases may have inhibiting effects on the replication of HIV-1 in myelo-monocytic cells .

It is possible that particular <protein>serine proteases</protein> may have inhibiting effects on the replication of HIV-1 in <cell_line>myelo-monocytic cells</cell_line> .


The data also demonstrate that special precautions must be taken when making extracts from myelo-monocytic cells .

The data also demonstrate that special precautions must be taken when making extracts from <cell_line>myelo-monocytic cells</cell_line> .


A germline TaqI restriction fragment length polymorphism in the progesterone receptor gene in ovarian carcinoma [ see comments ]

A <dna>germline TaqI restriction fragment length polymorphism</dna> in the <dna>progesterone receptor gene</dna> in ovarian carcinoma [ see comments ]


Clinical outcome in ovarian carcinoma is predicted by progesterone receptor status , indicating an endocrine aspect to this disease .

Clinical outcome in ovarian carcinoma is predicted by <protein>progesterone receptor</protein> status , indicating an endocrine aspect to this disease .


Peripheral leucocyte genomic DNAs were obtained from 41 patients with primary ovarian carcinoma and 83 controls from Ireland , as well as from 26 primary ovarian carcinoma patients and 101 controls in Germany .

<dna>Peripheral leucocyte genomic DNAs</dna> were obtained from 41 patients with primary ovarian carcinoma and 83 controls from Ireland , as well as from 26 primary ovarian carcinoma patients and 101 controls in Germany .


Southern analysis using a human progesterone receptor ( hPR ) cDNA probe identified a germline TaqI restriction fragment length polymorphism ( RFLP ) defined by two alleles : T1 , represented by a 2.7 kb fragment ; and T2 , represented by a 1.9 kb fragment and characterised by an additional TaqI restriction site with respect to T1 .

Southern analysis using a <dna>human progesterone receptor ( hPR ) cDNA probe</dna> identified a <dna>germline TaqI restriction fragment length polymorphism</dna> ( <dna>RFLP</dna> ) defined by two alleles : <dna>T1</dna> , represented by a <dna>2.7 kb fragment</dna> ; and <dna>T2</dna> , represented by a <dna>1.9 kb fragment</dna> and characterised by an additional <dna>TaqI restriction site</dna> with respect to <dna>T1</dna> .


An over-representation of T2 in ovarian cancer patients compared with controls in the pooled Irish/German population ( P < 0.025 ) was observed .

An over-representation of <dna>T2</dna> in ovarian cancer patients compared with controls in the pooled Irish/German population ( P < 0.025 ) was observed .


A difference ( P < 0.02 ) in the distribution of the RFLP genotypes between Irish and German control populations was also observed .

A difference ( P < 0.02 ) in the distribution of the <dna>RFLP</dna> genotypes between Irish and German control populations was also observed .


The allele distributions could not be shown to differ significantly from Hardy-Weinberg distribution in any subgroup .


Using hPR cDNA region-specific probes , the extra TaqI restriction site was mapped to intron G of the hPR gene .

Using <dna>hPR cDNA region-specific probes</dna> , the extra TaqI restriction site was mapped to <dna>intron G</dna> of the <dna>hPR gene</dna> .


OBF-1 , a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins .

<protein>OBF-1</protein> , a <protein>novel B cell-specific coactivator</protein> that stimulates <dna>immunoglobulin promoter</dna> activity through association with <protein>octamer-binding proteins</protein> .


Recent biochemical and genetic studies indicate that in addition to the octamer-binding proteins Oct-1 and Oct-2 , other B cell components are required for lymphoid-restricted , octamer site-mediated immunoglobulin gene promoter activity .

Recent biochemical and genetic studies indicate that in addition to the <protein>octamer-binding proteins</protein> <protein>Oct-1</protein> and <protein>Oct-2</protein> , other <protein>B cell components</protein> are required for lymphoid-restricted , octamer site-mediated <dna>immunoglobulin gene promoter</dna> activity .


Using a genetic screen in yeast , we have isolated B cell-derived cDNAs encoding Oct-binding factor 1 ( OBF-1 ) , a novel protein that specifically associates with Oct-1 and Oct-2 .

Using a genetic screen in yeast , we have isolated <dna>B cell-derived cDNAs</dna> encoding <protein>Oct-binding factor 1</protein> ( <protein>OBF-1</protein> ) , a novel protein that specifically associates with <protein>Oct-1</protein> and <protein>Oct-2</protein> .


Biochemical studies demonstrate that OBF-1 has no intrinsic DNA-binding activity and recognizes the POU domains of Oct-1 and Oct-2 , but not those of Oct-4 and Oct-6 .

Biochemical studies demonstrate that <protein>OBF-1</protein> has no intrinsic DNA-binding activity and recognizes the <protein>POU domains</protein> of <protein>Oct-1</protein> and <protein>Oct-2</protein> , but not those of <protein>Oct-4</protein> and <protein>Oct-6</protein> .


The OBF-1 mRNA is expressed in a highly cell-specific manner , being most abundant in B cells and essentially absent in most of the other cells or tissues tested .

The <rna>OBF-1 mRNA</rna> is expressed in a highly cell-specific manner , being most abundant in <cell_type>B cells</cell_type> and essentially absent in most of the other cells or tissues tested .


Furthermore , expression of OBF-1 in HeLa cells selectively stimulates the activity of a natural immunoglobulin promoter in an octamer site -dependent manner .

Furthermore , expression of <protein>OBF-1</protein> in <cell_line>HeLa cells</cell_line> selectively stimulates the activity of a natural <dna>immunoglobulin promoter</dna> in an <dna>octamer site</dna> -dependent manner .


Thus , OBF-1 has all the properties expected for a B cell-specific transcriptional coactivator protein .

Thus , <protein>OBF-1</protein> has all the properties expected for a <protein>B cell-specific transcriptional coactivator protein</protein> .


Modulation of transcription factor NF kappa B activity by intracellular glutathione levels and by variations of the extracellular cysteine supply .

Modulation of <protein>transcription factor NF kappa B</protein> activity by intracellular glutathione levels and by variations of the extracellular cysteine supply .


HIV-infected individuals and SIV-infected rhesus macaques have , on the average , decreased plasma cysteine and cystine concentrations and decreased intracellular glutathione levels .


We now show that a depletion of intracellular glutathione in a human T cell line ( Molt-4 ) inhibits the activation and nuclear translocation of the transcription factor NF kappa B , whereas incubation with increasing extracellular concentrations of cysteine inhibits the DNA-binding and transactivating activity of NF kappa B .

We now show that a depletion of intracellular glutathione in a <cell_line>human T cell line</cell_line> ( <cell_line>Molt-4</cell_line> ) inhibits the activation and nuclear translocation of the <protein>transcription factor NF kappa B</protein> , whereas incubation with increasing extracellular concentrations of cysteine inhibits the DNA-binding and transactivating activity of <protein>NF kappa B</protein> .


Because inhibition of DNA-binding activity is associated with increasing intracellular glutathione disulfide levels and GSSG can be shown to inhibit the DNA-binding activity directly in cell-free systems , our studies suggest that GSSG is a physiologically relevant inhibitor in intact cells also .

Because inhibition of DNA-binding activity is associated with increasing intracellular glutathione disulfide levels and <protein>GSSG</protein> can be shown to inhibit the DNA-binding activity directly in cell-free systems , our studies suggest that <protein>GSSG</protein> is a physiologically relevant inhibitor in <cell_type>intact cells</cell_type> also .


NF kappa B controls many immunologically important genes , so our studies suggest that the immune system may be sensitive not only against a cysteine and glutathione deficiency but also against an excess of cysteine .

<protein>NF kappa B</protein> controls many <dna>immunologically important genes</dna> , so our studies suggest that the immune system may be sensitive not only against a cysteine and glutathione deficiency but also against an excess of cysteine .


Two distinct signalling pathways are involved in the control of the biphasic junB transcription induced by interleukin-6 in the B cell hybridoma 7TD1 .

Two distinct signalling pathways are involved in the control of the biphasic <dna>junB</dna> transcription induced by <protein>interleukin-6</protein> in the <cell_line>B cell hybridoma 7TD1</cell_line> .


We have measured the level of junB mRNA in the B hybridoma cell line 7TD1 , under interleukin-6 ( IL-6 ) stimulation .

We have measured the level of <rna>junB mRNA</rna> in the <cell_line>B hybridoma cell line 7TD1</cell_line> , under <protein>interleukin-6</protein> ( <protein>IL-6</protein> ) stimulation .


IL-6 increases junB mRNA in a biphasic fashion .

<protein>IL-6</protein> increases <rna>junB mRNA</rna> in a biphasic fashion .


The first early-induced peak was transient and likely corresponds to the well documented typical junB mRNA , stimulated in response to numerous growth factors , including IL-6 .

The first early-induced peak was transient and likely corresponds to the well documented typical <rna>junB mRNA</rna> , stimulated in response to numerous <protein>growth factors</protein> , including <protein>IL-6</protein> .


At variance , the second peak which has never been reported previously , lasted several hours .


As a consequence of its effect on junB mRNA , IL-6 stimulated , in a biphasic fashion , the nuclear accumulation of the JunB protein .

As a consequence of its effect on <rna>junB mRNA</rna> , <protein>IL-6</protein> stimulated , in a biphasic fashion , the nuclear accumulation of the <protein>JunB protein</protein> .


In this study , we demonstrated that IL-6 regulation occurred exclusively at the transcriptional level and that the bimodal increase of junB mRNA and JunB protein can be accounted for by a biphasic stimulation of junB transcription .

In this study , we demonstrated that <protein>IL-6</protein> regulation occurred exclusively at the transcriptional level and that the bimodal increase of <rna>junB mRNA</rna> and <protein>JunB protein</protein> can be accounted for by a biphasic stimulation of <dna>junB</dna> transcription .


Furthermore , our data point to two major differences between the mechanism of control of the early and the late IL-6 -induced junB transcription waves .

Furthermore , our data point to two major differences between the mechanism of control of the early and the late <protein>IL-6</protein> -induced <dna>junB</dna> transcription waves .


First , cycloheximide strongly potentiated the transcription of the second wave , whereas it failed to affect the early-induced burst .


Second , tyrphostin , a tyrosine kinase inhibitor , impaired the expression of the first but not the second junB mRNA peak .

Second , tyrphostin , a tyrosine kinase inhibitor , impaired the expression of the first but not the second <rna>junB mRNA</rna> peak .


Conversely , genistein , another tyrosine kinase inhibitor , totally abolished the expression of the second peak of junB mRNA whereas it did not affect the expression of the first peak .

Conversely , genistein , another tyrosine kinase inhibitor , totally abolished the expression of the second peak of <rna>junB mRNA</rna> whereas it did not affect the expression of the first peak .


Altogether these data indicate that , in 7TD1 cells , IL-6 controls junB transcription in a biphasic fashion by means of two separate transduction pathways .

Altogether these data indicate that , in <cell_line>7TD1 cells</cell_line> , <protein>IL-6</protein> controls <dna>junB</dna> transcription in a biphasic fashion by means of two separate transduction pathways .


A newly established megakaryoblastic/erythroid cell line that differentiates to red cells in the presence of erythropoietin and produces platelet-like particles .

A newly established <cell_line>megakaryoblastic/erythroid cell line</cell_line> that differentiates to <cell_type>red cells</cell_type> in the presence of <protein>erythropoietin</protein> and produces <cell_type>platelet-like particles</cell_type> .


In August , 1992 , we established a leukemic cell line ( NS-Meg ) from a patient in megakaryoblastic transformation of Philadelphia chromosome-positive chronic myeloid leukemia .

In August , 1992 , we established a <cell_line>leukemic cell line</cell_line> ( <cell_line>NS-Meg</cell_line> ) from a patient in megakaryoblastic transformation of Philadelphia chromosome-positive chronic myeloid leukemia .


The NS-Meg cells were positive for alpha-naphthyl acetate esterase and periodic acid-Schiff ( PAS ) staining and for surface CD4 , CD7 , CD13 , CD34 , CD41a , and glycophorin A antigens .

The <cell_line>NS-Meg cells</cell_line> were positive for <protein>alpha-naphthyl acetate esterase</protein> and periodic acid-Schiff ( PAS ) staining and for surface <protein>CD4</protein> , <protein>CD7</protein> , <protein>CD13</protein> , <protein>CD34</protein> , <protein>CD41a</protein> , and <protein>glycophorin A antigens</protein> .


Ultrastructurally , the cells had alpha-granules , demarcation membranes , and platelet peroxidase activity .

Ultrastructurally , the cells had alpha-granules , demarcation membranes , and <protein>platelet peroxidase</protein> activity .


The NS-Meg cells spontaneously produced platelet-like particles which contained alpha-granules , mitochondria and dense bodies , strongly suggesting platelet production .

The <cell_line>NS-Meg cells</cell_line> spontaneously produced <cell_type>platelet-like particles</cell_type> which contained alpha-granules , mitochondria and dense bodies , strongly suggesting platelet production .


Erythropoietin ( Epo ) , granulocyte/macrophage colony stimulating factor ( GM-CSF ) , and interleukin 3 ( IL-3 ) promoted the growth of NS-Meg cells .

<protein>Erythropoietin</protein> ( <protein>Epo</protein> ) , <protein>granulocyte/macrophage colony stimulating factor</protein> ( <protein>GM-CSF</protein> ) , and <protein>interleukin 3</protein> ( <protein>IL-3</protein> ) promoted the growth of <cell_line>NS-Meg cells</cell_line> .


Phorbol-12-myristate-13-acetate increased the expression of both CD41a and CD61 antigens .

Phorbol-12-myristate-13-acetate increased the expression of both <protein>CD41a</protein> and CD61 antigens .


Ten-day exposure to Epo induced mature erythroblasts and red cells .

Ten-day exposure to <protein>Epo</protein> induced <cell_type>mature erythroblasts</cell_type> and <cell_type>red cells</cell_type> .


These benzidine-positive cells were positive for hemoglobin F staining .

These <cell_line>benzidine-positive cells</cell_line> were positive for <protein>hemoglobin</protein> F staining .


Untreated NS-Meg cells expressed mRNA for the Epo receptor ( EpoR ) , for GATA-1 , and for alpha 1 , alpha 2 and gamma globin genes .

Untreated <cell_line>NS-Meg cells</cell_line> expressed <rna>mRNA</rna> for the <protein>Epo receptor</protein> ( <protein>EpoR</protein> ) , for <protein>GATA-1</protein> , and for <dna>alpha 1 , alpha 2 and gamma globin genes</dna> .


These results indicate that NS-Meg cells undergo terminal differentiation of both megakaryocytic and erythroid lineages .

These results indicate that <cell_line>NS-Meg cells</cell_line> undergo terminal differentiation of both <cell_type>megakaryocytic and erythroid lineages</cell_type> .


This cell line should be a very useful tool for the investigation of both megakaryocytic and erythroid maturation .

This <cell_line>cell line</cell_line> should be a very useful tool for the investigation of both megakaryocytic and erythroid maturation .


Differential regulation of proto-oncogenes c-jun and c-fos in T lymphocytes activated through CD28 .

Differential regulation of <dna>proto-oncogenes</dna> <dna>c-jun</dna> and <dna>c-fos</dna> in <cell_type>T lymphocytes</cell_type> activated through <protein>CD28</protein> .


The T cell surface molecule CD28 binds to ligands on accessory cells and APCs , playing an important costimulatory role in the response of T cells to Ags .

The <protein>T cell surface molecule</protein> <protein>CD28</protein> binds to ligands on <cell_type>accessory cells</cell_type> and <cell_type>APCs</cell_type> , playing an important costimulatory role in the response of <cell_type>T cells</cell_type> to <protein>Ags</protein> .


Our knowledge of the intracellular signaling pathways coupled to this receptor is incomplete .


In addition to activation of phospholipase C gamma 1 , ligation of this receptor also seems to activate a calcium-independent , CD28 -specific pathway .

In addition to activation of <protein>phospholipase C gamma 1</protein> , ligation of this receptor also seems to activate a calcium-independent , <protein>CD28</protein> -specific pathway .


In this paper , we report that cross-linking of CD28 ( but not CD2 , CD5 , LFA-1 , or CD7 ) leads to an elevation of c-jun mRNA , with only minimal activation of c-fos expression .

In this paper , we report that cross-linking of <protein>CD28</protein> ( but not <protein>CD2</protein> , <protein>CD5</protein> , <protein>LFA-1</protein> , or <protein>CD7</protein> ) leads to an elevation of <rna>c-jun mRNA</rna> , with only minimal activation of <dna>c-fos</dna> expression .


CD28 -dependent induction of c-jun expression requires protein tyrosine kinase activity , but does not depend on activation of a phorbol ester-responsive protein kinase C or elevation of cytosolic calcium .

<protein>CD28</protein> -dependent induction of <dna>c-jun</dna> expression requires <protein>protein tyrosine kinase</protein> activity , but does not depend on activation of a <protein>phorbol ester-responsive protein kinase C</protein> or elevation of cytosolic calcium .


Furthermore , CD28 -dependent elevation of c-jun mRNA does not appear to be mediated at the level of mRNA stability .

Furthermore , <protein>CD28</protein> -dependent elevation of <rna>c-jun mRNA</rna> does not appear to be mediated at the level of mRNA stability .


A mechanism is suggested whereby expression of c-jun and junB , in the absence of members of the fos family , can prevent inappropriate activation of T cells caused by ligation of CD28 in the absence of a specific antigenic stimulus .

A mechanism is suggested whereby expression of <dna>c-jun</dna> and <dna>junB</dna> , in the absence of members of the <dna>fos family</dna> , can prevent inappropriate activation of <cell_type>T cells</cell_type> caused by ligation of <protein>CD28</protein> in the absence of a specific antigenic stimulus .


Enhanced responsiveness to nuclear factor kappa B contributes to the unique phenotype of simian immunodeficiency virus variant SIVsmmPBj14 .

Enhanced responsiveness to <protein>nuclear factor kappa B</protein> contributes to the unique phenotype of simian immunodeficiency virus variant SIVsmmPBj14 .


Infection with a variant of simian immunodeficiency virus , SIVsmmPBj14 , leads to severe acute disease in macaques .


This study was designed to investigate the functional significance of previously described mutations in the viral long terminal repeat ( LTR ) and to elucidate their contribution to the unique phenotype of SIVsmmPBj14 .

This study was designed to investigate the functional significance of previously described mutations in the <dna>viral long terminal repeat</dna> ( <dna>LTR</dna> ) and to elucidate their contribution to the unique phenotype of SIVsmmPBj14 .


LTR -directed transcription was measured by using luciferase reporter constructs that were transiently transfected into cultured cells .

<dna>LTR</dna> -directed transcription was measured by using <dna>luciferase reporter constructs</dna> that were transiently transfected into <cell_line>cultured cells</cell_line> .


In a wide range of cell types , the basal transcriptional activity of the LTR from SIVsmmPBj14 was found to be 2- to 4.5-fold higher than that of an LTR from a non-acutely pathogenic strain .

In a wide range of cell types , the basal transcriptional activity of the <dna>LTR</dna> from SIVsmmPBj14 was found to be 2- to 4.5-fold higher than that of an <dna>LTR</dna> from a non-acutely pathogenic strain .


These LTRs differ by five point mutations and a 22-bp duplication in SIVsmmPBj14 , which includes a nuclear factor kappa B ( NF kappa B ) site .

These <dna>LTRs</dna> differ by five point mutations and a <dna>22-bp duplication</dna> in SIVsmmPBj14 , which includes a <dna>nuclear factor kappa B ( NF kappa B ) site</dna> .


Transcriptional differences between these LTRs were further enhanced by two- to threefold upon treatment of cells with phorbol ester or tumor necrosis factor alpha or by cotransfection with plasmids expressing NF kappa B subunits .

Transcriptional differences between these <dna>LTRs</dna> were further enhanced by two- to threefold upon treatment of cells with phorbol ester or <protein>tumor necrosis factor alpha</protein> or by cotransfection with <dna>plasmids</dna> expressing <protein>NF kappa B</protein> subunits .


Mutagenesis studies , and the use of a reporter construct containing an enhancerless promoter , indicate that these transcriptional effects are due principally to the 22-bp sequence duplication and the NF kappa B site contained within it .

Mutagenesis studies , and the use of a reporter construct containing an enhancerless promoter , indicate that these transcriptional effects are due principally to the <dna>22-bp sequence duplication</dna> and the <dna>NF kappa B site</dna> contained within it .


Finally , infectious virus stocks that were isogenic except for the LTR were generated .

Finally , infectious virus stocks that were isogenic except for the <dna>LTR</dna> were generated .


The LTR from SIVsmmPBj14 was found to confer an increase in the kinetics of virus replication in cultured cells .

The <dna>LTR</dna> from SIVsmmPBj14 was found to confer an increase in the kinetics of virus replication in <cell_line>cultured cells</cell_line> .


Inclusion of this LTR in recombinant SIVs also resulted in a two- to threefold rise in the extent of cellular proliferation that was induced in quiescent simian peripheral blood mononuclear cells .

Inclusion of this <dna>LTR</dna> in recombinant SIVs also resulted in a two- to threefold rise in the extent of cellular proliferation that was induced in <cell_line>quiescent simian peripheral blood mononuclear cells</cell_line> .


These studies are consistent with the hypothesis that LTR mutations assist SIVsmmPBj14 in responding efficiently to cellular stimulation and allow it to replicate to high titers during the acute phase of viral infection .

These studies are consistent with the hypothesis that <dna>LTR</dna> mutations assist SIVsmmPBj14 in responding efficiently to cellular stimulation and allow it to replicate to high titers during the acute phase of viral infection .


Constitutive nuclear NF-kappa B in cells of the monocyte lineage .

Constitutive <protein>nuclear NF-kappa B</protein> in cells of the monocyte lineage .


In monocytes , the nuclear factor NF-kappa B has been invoked as an important transcription factor in the expression of cytokine genes , of cell-surface receptors and in the expression of human immunodeficiency virus .

In <cell_type>monocytes</cell_type> , the <protein>nuclear factor NF-kappa B</protein> has been invoked as an important <protein>transcription factor</protein> in the expression of <dna>cytokine genes</dna> , of <protein>cell-surface receptors</protein> and in the expression of human immunodeficiency virus .


In such cells , DNA binding activity of NF-kappa B can be detected without intentional stimulation .

In such cells , DNA binding activity of <protein>NF-kappa B</protein> can be detected without intentional stimulation .


In our studies , cells of the human monocytic line Mono Mac 6 , cultured in medium containing fetal-calf serum and low levels of lipopolysaccharide ( LPS ) , also exhibit such 'constitutive ' NF-kappa B , as demonstrated by mobility-shift analysis of nuclear extracts .

In our studies , cells of the <cell_line>human monocytic line</cell_line> <cell_line>Mono Mac 6</cell_line> , cultured in medium containing fetal-calf serum and low levels of lipopolysaccharide ( LPS ) , also exhibit such 'constitutive ' <protein>NF-kappa B</protein> , as demonstrated by mobility-shift analysis of nuclear extracts .


This nuclear NF-kappa B was still present when contaminant LPS was removed by ultrafiltration and when serum was omitted .

This <protein>nuclear NF-kappa B</protein> was still present when contaminant LPS was removed by ultrafiltration and when serum was omitted .


Protein-DNA complexes of constitutive NF-kappa B are similar in mobility to the LPS-induced NF-kappa B and both are recognized by an antibody specific to the p50 subunit of NF-kappa B .

Protein-DNA complexes of constitutive <protein>NF-kappa B</protein> are similar in mobility to the <protein>LPS-induced NF-kappa B</protein> and both are recognized by an antibody specific to the <protein>p50 subunit</protein> of <protein>NF-kappa B</protein> .


By contrast , treatment of cells with pyrrolidine dithiocarbamate ( PDTC ) will only block LPS-induced NF-kappa B , but not the constitutive binding protein .

By contrast , treatment of cells with pyrrolidine dithiocarbamate ( PDTC ) will only block <protein>LPS-induced NF-kappa B</protein> , but not the <protein>constitutive binding protein</protein> .


Using LPS-free and serum-free conditions , constitutive NF-kappa B can be detected in different cell lines of the monocytic lineage ( HL60 , U937 , THP-1 , Mono Mac 1 and Mono Mac 6 ) , but not in Molt 4 T cells or K562 stem cells .

Using LPS-free and serum-free conditions , constitutive <protein>NF-kappa B</protein> can be detected in different <cell_line>cell lines</cell_line> of the <cell_type>monocytic lineage</cell_type> ( <cell_line>HL60</cell_line> , <cell_line>U937</cell_line> , <cell_line>THP-1</cell_line> , <cell_line>Mono Mac 1</cell_line> and <cell_line>Mono Mac 6</cell_line> ) , but not in <cell_line>Molt 4 T cells</cell_line> or <cell_line>K562 stem cells</cell_line> .


When ordered according to stage of maturation , the amount of constitutive NF-kappa B was not increased in more mature cell lines .

When ordered according to stage of maturation , the amount of constitutive <protein>NF-kappa B</protein> was not increased in more <cell_line>mature cell lines</cell_line> .


Furthermore , when inducing differentiation in Mono Mac 6 cells , with vitamin D3 , no change in constitutive or inducible NF-kappa B can be detected .

Furthermore , when inducing differentiation in <cell_line>Mono Mac 6 cells</cell_line> , with vitamin D3 , no change in constitutive or inducible <protein>NF-kappa B</protein> can be detected .


Analysis of primary cells revealed substantial constitutive NF-kappa B -binding activity in blood monocytes , pleural macrophages and alveolar macrophages .

Analysis of primary cells revealed substantial constitutive <protein>NF-kappa B</protein> -binding activity in <cell_type>blood monocytes</cell_type> , <cell_type>pleural macrophages</cell_type> and <cell_type>alveolar macrophages</cell_type> .


The constitutive NF-kappa B appears to be functionally active , since a low level of tumour necrosis factor ( TNF ) transcript is detectable in monocytes , and this level can be increased by blocking transcript degradation using cycloheximide .

The constitutive <protein>NF-kappa B</protein> appears to be functionally active , since a low level of <rna>tumour necrosis factor ( TNF ) transcript</rna> is detectable in <cell_type>monocytes</cell_type> , and this level can be increased by blocking transcript degradation using cycloheximide .


The level of constitutive NF-kappa B in these cells is variable and is frequently found to be lower in the more mature macrophages .

The level of constitutive <protein>NF-kappa B</protein> in these cells is variable and is frequently found to be lower in the more <cell_type>mature macrophages</cell_type> .


Constitutive NF-kappa B was not maintained by autocrine action of cytokines TNF , interleukin 6 , interleukin 10 , granulocyte-macrophage colony-stimulating factor or macrophage colony-stimulating factor , since neutralizing antibodies did not reduce constitutive DNA-binding activity .

Constitutive <protein>NF-kappa B</protein> was not maintained by autocrine action of <protein>cytokines</protein> <protein>TNF</protein> , <protein>interleukin 6</protein> , <protein>interleukin</protein> 10 , <protein>granulocyte-macrophage colony-stimulating factor</protein> or <protein>macrophage colony-stimulating factor</protein> , since neutralizing antibodies did not reduce constitutive DNA-binding activity .


Furthermore , blockade of prostaglandin or leukotriene biosynthesis did not affect constitutive NF-kappa B .

Furthermore , blockade of prostaglandin or leukotriene biosynthesis did not affect constitutive <protein>NF-kappa B</protein> .


( ABSTRACT TRUNCATED AT 400 WORDS )


Steel factor affects SCL expression during normal erythroid differentiation .

<protein>Steel factor</protein> affects <protein>SCL</protein> expression during normal erythroid differentiation .


Steel factor is one of the growth factors that controls the proliferation and differentiation of hematopoietic cells and SCL , also known as Tcl-5 or Tal-1 , is a transcription factor involved in erythropoiesis .

<protein>Steel factor</protein> is one of the <protein>growth factors</protein> that controls the proliferation and differentiation of <cell_type>hematopoietic cells</cell_type> and <protein>SCL</protein> , also known as <protein>Tcl-5</protein> or <protein>Tal-1</protein> , is a <protein>transcription factor</protein> involved in erythropoiesis .


In this report , we studied the role of SCL in the proliferation of human peripheral blood burst-forming unit-erythroid ( BFU-E ) and the effects of Steel factor on SCL expression in proliferating erythroid cells .

In this report , we studied the role of SCL in the proliferation of <cell_type>human peripheral blood burst-forming unit-erythroid</cell_type> ( <cell_type>BFU-E</cell_type> ) and the effects of <protein>Steel factor</protein> on <protein>SCL</protein> expression in <cell_type>proliferating erythroid cells</cell_type> .


BFU-E-derived colonies increase progressively in size , as determined by cell number , from day 7 to day 14 of culture , with the greatest increase in colony size ( 10-fold expansion ) occurring between day 7 and day 10 .

<cell_line>BFU-E-derived colonies</cell_line> increase progressively in size , as determined by cell number , from day 7 to day 14 of culture , with the greatest increase in colony size ( 10-fold expansion ) occurring between day 7 and day 10 .


SCL protein levels in BFU-E-derived cells were highest in day 7 cells and decreased progressively from day 7 to day 14 of culture , suggesting an association of SCL with erythroid proliferation .

<protein>SCL protein</protein> levels in <cell_line>BFU-E-derived cells</cell_line> were highest in day 7 cells and decreased progressively from day 7 to day 14 of culture , suggesting an association of <protein>SCL</protein> with erythroid proliferation .


In contrast , SCL mRNA levels did not decrease significantly between day 7 and day 14 cells , suggesting that posttranscriptional mechanisms are largely responsible for the decrease in SCL protein observed .

In contrast , <rna>SCL mRNA</rna> levels did not decrease significantly between day 7 and day 14 cells , suggesting that posttranscriptional mechanisms are largely responsible for the decrease in <protein>SCL protein</protein> observed .


The role of SCL in Steel factor -induced erythroid proliferation was then examined .

The role of <protein>SCL</protein> in <protein>Steel factor</protein> -induced erythroid proliferation was then examined .


In BFU-E-derived colonies cultured with Steel factor , colony size was significantly increased compared to control .

In <cell_line>BFU-E-derived colonies</cell_line> cultured with <protein>Steel factor</protein> , colony size was significantly increased compared to control .


In day 7 and day 10 erythroid precursors cultured with Steel factor , SCL protein was increased significantly compared to control .

In day 7 and day 10 <cell_type>erythroid precursors</cell_type> cultured with <protein>Steel factor</protein> , <protein>SCL protein</protein> was increased significantly compared to control .


The increase in SCL protein levels in early erythroid precursors stimulated with Steel factor suggests one mechanism through which Steel factor may enhance normal erythroid proliferation .

The increase in <protein>SCL</protein> protein levels in early <cell_type>erythroid precursors</cell_type> stimulated with <protein>Steel factor</protein> suggests one mechanism through which <protein>Steel factor</protein> may enhance normal erythroid proliferation .


SCL mRNA levels assessed by Northern blot in day 7 cells did not increase significantly in response to Steel factor stimulation , suggesting that posttranscriptional mechanisms may also be important in the increase in SCL protein observed in response to Steel .

<rna>SCL mRNA</rna> levels assessed by Northern blot in day 7 cells did not increase significantly in response to <protein>Steel factor</protein> stimulation , suggesting that posttranscriptional mechanisms may also be important in the increase in <protein>SCL protein</protein> observed in response to <protein>Steel</protein> .


C/EBP beta regulation of the tumor necrosis factor alpha gene .

<protein>C/EBP beta</protein> regulation of the <dna>tumor necrosis factor alpha gene</dna> .


Activated macrophages contribute to chronic inflammation by the secretion of cytokines and proteinases .

<cell_type>Activated macrophages</cell_type> contribute to chronic inflammation by the secretion of <protein>cytokines</protein> and <protein>proteinases</protein> .


Tumor necrosis factor alpha ( TNF alpha ) is particularly important in this process because of its ability to regulate other inflammatory mediators in an autocrine and paracrine fashion .

<protein>Tumor necrosis factor alpha</protein> ( <protein>TNF alpha</protein> ) is particularly important in this process because of its ability to regulate other inflammatory mediators in an autocrine and paracrine fashion .


The mechanism ( s ) responsible for the cell type-specific regulation of TNF alpha is not known .

The mechanism ( s ) responsible for the cell type-specific regulation of <protein>TNF alpha</protein> is not known .


We present data to show that the expression of TNF alpha is regulated by the transcription factor C/EBP beta ( NF-IL6 ) .

We present data to show that the expression of <protein>TNF alpha</protein> is regulated by the <protein>transcription factor</protein> <protein>C/EBP beta</protein> ( <protein>NF-IL6</protein> ) .


C/EBP beta activated the TNF alpha gene promoter in cotransfection assays and bound to it at a site which failed to bind the closely related protein C/EBP alpha .

<protein>C/EBP beta</protein> activated the <dna>TNF alpha gene promoter</dna> in cotransfection assays and bound to it at a site which failed to bind the closely related protein <protein>C/EBP alpha</protein> .


Finally , a dominant-negative version of C/EBP beta blocked TNF alpha promoter activation in myeloid cells .

Finally , a dominant-negative version of <protein>C/EBP beta</protein> blocked <dna>TNF alpha promoter</dna> activation in <cell_type>myeloid cells</cell_type> .


Our results implicate C/EBP beta as an important regulator of TNF alpha by myelomonocytic cells .

Our results implicate <protein>C/EBP beta</protein> as an important regulator of <protein>TNF alpha</protein> by <cell_type>myelomonocytic cells</cell_type> .


Calcium/calmodulin-dependent protein kinase II downregulates both calcineurin and protein kinase C-mediated pathways for cytokine gene transcription in human T cells .

<protein>Calcium/calmodulin-dependent protein kinase II</protein> downregulates both calcineurin and protein kinase C-mediated pathways for <dna>cytokine gene</dna> transcription in <cell_type>human T cells</cell_type> .


Engagement of the T cell receptor for antigen activates phospholipase C resulting in an increase in intracellular free calcium concentration ( [ Ca2+ ] i ) and activation of protein kinase C ( PKC ) .

Engagement of the <protein>T cell receptor</protein> for antigen activates <protein>phospholipase C</protein> resulting in an increase in intracellular free calcium concentration ( [ Ca2+ ] i ) and activation of <protein>protein kinase C</protein> ( <protein>PKC</protein> ) .


Increased [ Ca2+ ] i activates Ca2+/calmodulin-dependent kinases including the multifunctional Ca2+/calmodulin-dependent protein kinase II ( CaM-K II ) , as well as calcineurin , a type 2B protein phosphatase .

Increased [ Ca2+ ] i activates <protein>Ca2+/calmodulin-dependent kinases</protein> including the multifunctional <protein>Ca2+/calmodulin-dependent protein kinase II</protein> ( <protein>CaM-K II</protein> ) , as well as <protein>calcineurin</protein> , a <protein>type 2B protein phosphatase</protein> .


Recent studies have identified calcineurin as a key enzyme for interleukin ( IL ) -2 and IL-4 promoter activation .

Recent studies have identified <protein>calcineurin</protein> as a key enzyme for interleukin ( IL ) -2 and IL-4 promoter activation .


However , the role of CaM-K II remains unknown .

However , the role of <protein>CaM-K II</protein> remains unknown .


We have used mutants of these kinases and phosphatases ( gamma B*CaM-K and delta CaM-AI , respectively ) to explore their relative role in cytokine gene transcription and their interactions with PKC -dependent signaling systems .

We have used mutants of these <protein>kinases</protein> and <protein>phosphatases</protein> ( <protein>gamma B*CaM-K</protein> and <protein>delta CaM-AI</protein> , respectively ) to explore their relative role in <dna>cytokine gene</dna> transcription and their interactions with <protein>PKC</protein> -dependent signaling systems .


gamma B*CaM-K and delta CaM-AI , known to exhibit constitutive Ca ( 2+ ) -independent activity , were cotransfected ( alone or in combination ) in Jurkat T cells with a plasmid containing the intact IL-2 promoter driving the expression of the chloramphenicol acetyltransferase reporter gene .

<protein>gamma B*CaM-K</protein> and <protein>delta CaM-AI</protein> , known to exhibit constitutive Ca ( 2+ ) -independent activity , were cotransfected ( alone or in combination ) in <cell_line>Jurkat T cells</cell_line> with a plasmid containing the intact <dna>IL-2 promoter</dna> driving the expression of the <dna>chloramphenicol acetyltransferase reporter gene</dna> .


Cotransfection of gamma B*CaM-K with the IL-2 promoter construct downregulated its transcription in response to stimulation with ionomycin and phorbol myristate acetate ( PMA ) .

Cotransfection of <protein>gamma B*CaM-K</protein> with the <dna>IL-2 promoter construct</dna> downregulated its transcription in response to stimulation with ionomycin and phorbol myristate acetate ( PMA ) .


The inhibitory effect of CaM-K II on IL-2 promoter was associated with decreased transcription of its AP-1 and NF-AT transactivating pathways .

The inhibitory effect of <protein>CaM-K II</protein> on <dna>IL-2 promoter</dna> was associated with decreased transcription of its AP-1 and NF-AT transactivating pathways .


Under the same conditions , delta CaM-AI superinduced IL-2 promoter activity ( approximately twofold increase ) .

Under the same conditions , <protein>delta CaM-AI</protein> superinduced <dna>IL-2 promoter</dna> activity ( approximately twofold increase ) .


When both mutants were used in combination , gamma B*CaM-K inhibited the induction of the IL-2 promoter by delta CaM-AI .

When both mutants were used in combination , <protein>gamma B*CaM-K</protein> inhibited the induction of the <dna>IL-2 promoter</dna> by <protein>delta CaM-AI</protein> .


Similar results were obtained when a construct containing the IL-4 promoter also was used .

Similar results were obtained when a construct containing the <dna>IL-4 promoter</dna> also was used .


gamma B*CaM-K also downregulated the activation of AP-1 in response to transfection with a constitutively active mutant of PKC or stimulation with PMA .

<protein>gamma B*CaM-K</protein> also downregulated the activation of <protein>AP-1</protein> in response to transfection with a constitutively active mutant of <protein>PKC</protein> or stimulation with PMA .


These results suggest that CaM-K II may exert negative influences on cytokine gene transcription in human T cells , and provide preliminary evidence for negative cross-talk with the calcineurin- and PKC- dependent signaling systems .

These results suggest that <protein>CaM-K II</protein> may exert negative influences on <dna>cytokine gene</dna> transcription in <cell_type>human T cells</cell_type> , and provide preliminary evidence for negative cross-talk with the calcineurin- and PKC- dependent signaling systems .


Induction of ICAM-1 and LFA-3 by Tax1 of human T-cell leukemia virus type 1 and mechanism of down-regulation of ICAM-1 or LFA-1 in adult-T-cell-leukemia cell lines .

Induction of <protein>ICAM-1</protein> and <protein>LFA-3</protein> by <protein>Tax1</protein> of human T-cell leukemia virus type 1 and mechanism of down-regulation of <protein>ICAM-1</protein> or <protein>LFA-1</protein> in <cell_line>adult-T-cell-leukemia cell lines</cell_line> .


The present study was undertaken to determine the role of HTLV-I TaxI in the up-regulation of ICAM-I and LFA-3 in human T cells transformed with HTLV-I and the mechanism of down-regulation of ICAM-I and LFA-I in ATL-derived cell lines .

The present study was undertaken to determine the role of <protein>HTLV-I TaxI</protein> in the up-regulation of <protein>ICAM-I</protein> and <protein>LFA-3</protein> in <cell_type>human T cells</cell_type> transformed with HTLV-I and the mechanism of down-regulation of <protein>ICAM-I</protein> and <protein>LFA-I</protein> in <cell_line>ATL-derived cell lines</cell_line> .


Induction of TaxI in a human T-cell line Jurkat carrying the TaxI gene under the metallothionein promoter led to increases in mRNA and surface expression of ICAM-I .

Induction of <protein>TaxI</protein> in a <cell_line>human T-cell line Jurkat</cell_line> carrying the <dna>TaxI gene</dna> under the <dna>metallothionein promoter</dna> led to increases in <rna>mRNA</rna> and surface expression of <protein>ICAM-I</protein> .


The response of LFA-3 to TaxI induction was , on the other hand , relatively slow and weak , and might be indirect .

The response of <protein>LFA-3</protein> to <protein>TaxI</protein> induction was , on the other hand , relatively slow and weak , and might be indirect .


Transactivation of the ICAM-I promoter by TaxI was further shown by co-transfection of a CAT reporter construct with the ICAM-I promoter and a plasmid expressing TaxI .

Transactivation of the <dna>ICAM-I promoter</dna> by <protein>TaxI</protein> was further shown by co-transfection of a <dna>CAT reporter construct</dna> with the <dna>ICAM-I promoter</dna> and a <dna>plasmid</dna> expressing <protein>TaxI</protein> .


The mechanism of down-regulation of ICAM-I or LFA-I in 4 ATL cell lines was next examined .

The mechanism of down-regulation of <protein>ICAM-I</protein> or <protein>LFA-I</protein> in <cell_line>4 ATL cell lines</cell_line> was next examined .


ICAM-I mRNA was quite low in MT-I , but no genomic changes were found .

<rna>ICAM-I mRNA</rna> was quite low in <cell_line>MT-I</cell_line> , but no genomic changes were found .


The CAT reporter with the ICAM-I promoter was inactive in MT-I .

The <dna>CAT reporter</dna> with the <dna>ICAM-I promoter</dna> was inactive in <cell_line>MT-I</cell_line> .


Finally , combined treatment of MT-I with 5-azacytidine and IFN-gamma induced re-expression of ICAM-I .

Finally , combined treatment of <cell_line>MT-I</cell_line> with 5-azacytidine and <protein>IFN-gamma</protein> induced re-expression of <protein>ICAM-I</protein> .


Collectively , ( a ) transcriptional factor ( s ) necessary for expression of ICAM-I gene may be repressed in MT-I through DNA methylation .

Collectively , ( a ) <protein>transcriptional factor</protein> ( s ) necessary for expression of <dna>ICAM-I gene</dna> may be repressed in <cell_line>MT-I</cell_line> through DNA methylation .


Three other ATL cell lines ( TL-OmI , H582 , HuT102 ) were found to have little mRNA for the LFA-I beta chain ( CD18 ) .

Three other <cell_line>ATL cell lines</cell_line> ( <cell_line>TL-OmI</cell_line> , <cell_line>H582</cell_line> , <cell_line>HuT102</cell_line> ) were found to have little <rna>mRNA</rna> for the <protein>LFA-I beta chain</protein> ( <protein>CD18</protein> ) .


H582 and HuT102 were also negative for the LFA-I alpha chain ( CDIIa ) mRNA .

<cell_line>H582</cell_line> and <cell_line>HuT102</cell_line> were also negative for the <rna>LFA-I alpha chain ( CDIIa ) mRNA</rna> .


No genomic changes were found , and a CAT reporter gene with the CD18 promoter was inactive in the 3 of them , again suggesting lack of ( a ) transcriptional factor ( s ) necessary for CD18 expression .

No genomic changes were found , and a <dna>CAT reporter gene</dna> with the <dna>CD18 promoter</dna> was inactive in the 3 of them , again suggesting lack of ( a ) <protein>transcriptional factor</protein> ( s ) necessary for <protein>CD18</protein> expression .


Infection with Theileria annulata induces expression of matrix metalloproteinase 9 and transcription factor AP-1 in bovine leucocytes .

Infection with Theileria annulata induces expression of <protein>matrix metalloproteinase 9</protein> and <protein>transcription factor</protein> <protein>AP-1</protein> in <cell_type>bovine leucocytes</cell_type> .


Theileria annulata infects bovine leucocytes and results in their reversible transformation such that they become immortalised and metastatic .

Theileria annulata infects <cell_type>bovine leucocytes</cell_type> and results in their reversible transformation such that they become immortalised and metastatic .


The present study describes parasite-induced changes in host cell gene expression which have a direct bearing on this transformation process .

The present study describes parasite-induced changes in <dna>host cell gene</dna> expression which have a direct bearing on this transformation process .


T. annulata-infected leucocytes produce a number of novel metalloproteinase activities .

<cell_type>T. annulata-infected leucocytes</cell_type> produce a number of novel <protein>metalloproteinase</protein> activities .


One of these , previously called B1 , is a 97-kDa protein which is secreted in large amounts and has been purified from protein-free , conditioned medium .

One of these , previously called <protein>B1</protein> , is a <protein>97-kDa protein</protein> which is secreted in large amounts and has been purified from protein-free , conditioned medium .


An antiserum to this enzyme was used to isolate a cDNA clone .

An antiserum to this enzyme was used to isolate a <dna>cDNA clone</dna> .


The predicted protein sequence of B1 is 81 % identical to human matrix metalloproteinase 9 ( MMP9 ) , demonstrating that it is the bovine homologue of this enzyme .

The predicted protein sequence of <protein>B1</protein> is 81 % identical to human <protein>matrix metalloproteinase 9</protein> ( <protein>MMP9</protein> ) , demonstrating that it is the bovine homologue of this enzyme .


RNAase protection assays demonstrated that the MMP9 activity , unique to infected cells , is due to increased MMP9 mRNA levels .

<protein>RNAase</protein> protection assays demonstrated that the <protein>MMP9</protein> activity , unique to <cell_type>infected cells</cell_type> , is due to increased <protein>MMP9</protein> mRNA levels .


We also assayed the levels of transcription factor AP-1 and demonstrated that it was constitutively present in increased amounts in Theileria-infected cells .

We also assayed the levels of <protein>transcription factor</protein> <protein>AP-1</protein> and demonstrated that it was constitutively present in increased amounts in <cell_type>Theileria-infected cells</cell_type> .


In addition we assayed the level of mRNA encoding c-Fos , a common component of AP-1 and observed that it was indeed up-regulated in infected cells .

In addition we assayed the level of <rna>mRNA</rna> encoding <protein>c-Fos</protein> , a common component of <protein>AP-1</protein> and observed that it was indeed up-regulated in <cell_type>infected cells</cell_type> .


Since AP-1 is implicated in the control of the cell cycle , and MMP9 can confer metastatic properties , these results are of considerable significance with respect to the transformed phenotype induced by Theileria infection .

Since <protein>AP-1</protein> is implicated in the control of the cell cycle , and <protein>MMP9</protein> can confer metastatic properties , these results are of considerable significance with respect to the transformed phenotype induced by Theileria infection .


B-cell proliferation and induction of early G1-regulating proteins by Epstein-Barr virus mutants conditional for EBNA2 .

<cell_type>B-cell</cell_type> proliferation and induction of early <protein>G1-regulating proteins</protein> by Epstein-Barr virus mutants conditional for <protein>EBNA2</protein> .


Infection of primary B-lymphocytes by Epstein-Barr virus ( EBV ) leads to growth transformation of these B-cells in vitro .

Infection of <cell_type>primary B-lymphocytes</cell_type> by Epstein-Barr virus ( EBV ) leads to growth transformation of these <cell_type>B-cells</cell_type> in vitro .


EBV nuclear antigen 2 ( EBNA2 ) , one of the first genes expressed after EBV infection of B-cells , is a transcriptional activator of viral and cellular genes and is essential for the transforming potential of the virus .

EBV nuclear antigen 2 ( <protein>EBNA2</protein> ) , one of the first genes expressed after EBV infection of <cell_type>B-cells</cell_type> , is a transcriptional activator of <dna>viral and cellular genes</dna> and is essential for the transforming potential of the virus .


We generated conditional EBV mutants by expressing EBNA2 as chimeric fusion protein with the hormone binding domain of the estrogen receptor on the genetic background of the virus .

We generated conditional EBV mutants by expressing <protein>EBNA2</protein> as <protein>chimeric fusion protein</protein> with the hormone binding domain of the <protein>estrogen receptor</protein> on the genetic background of the virus .


Growth transformation of primary normal B-cells by mutant virus resulted in estrogen-dependent lymphoblastoid cell lines expressing the chimeric EBNA2 protein .

Growth transformation of <cell_type>primary normal B-cells</cell_type> by mutant virus resulted in <cell_line>estrogen-dependent lymphoblastoid cell lines</cell_line> expressing the chimeric <protein>EBNA2 protein</protein> .


In the absence of estrogen about half of the cells enter a quiescent non-proliferative state whereas the others die by apoptosis .


EBNA2 is thus required not only for initiation but also for maintenance of transformation .

<protein>EBNA2</protein> is thus required not only for initiation but also for maintenance of transformation .


Growth arrest occurred at G1 and G2 stages of the cell cycle , indicating that functional EBNA2 is required at different restriction points of the cell cycle .

Growth arrest occurred at G1 and G2 stages of the cell cycle , indicating that functional <protein>EBNA2</protein> is required at different restriction points of the cell cycle .


Growth arrest is reversible for G1/G0 cells as indicated by the sequential accumulation and modification of cell cycle regulating proteins .

Growth arrest is reversible for <cell_type>G1/G0 cells</cell_type> as indicated by the sequential accumulation and modification of <protein>cell cycle regulating proteins</protein> .


EBV induces the same cell cycle regulating proteins as polyclonal stimuli in primary B-cells .

EBV induces the same cell cycle regulating proteins as polyclonal stimuli in primary <cell_type>B-cells</cell_type> .


These data suggest that EBV is using a common pathway for B-cell activation bypassing the requirement for antigen , T-cell signals and growth factors .

These data suggest that EBV is using a common pathway for B-cell activation bypassing the requirement for antigen , T-cell signals and <protein>growth factors</protein> .


IL-1 receptor and TCR signals synergize to activate NF-kappa B -mediated gene transcription .

<protein>IL-1 receptor</protein> and <protein>TCR</protein> signals synergize to activate <protein>NF-kappa B</protein> -mediated gene transcription .


Previous studies have demonstrated that IL-1 receptor ( IL-1R ) - and TCR -initiated signals can interact synergistically to increase the rate of transcription of several lymphokine and lymphokine receptor genes during the competence phase of the activation program in T helper lymphocytes .

Previous studies have demonstrated that <protein>IL-1 receptor</protein> ( <protein>IL-1R</protein> ) - and <protein>TCR</protein> -initiated signals can interact synergistically to increase the rate of transcription of several <dna>lymphokine and lymphokine receptor genes</dna> during the competence phase of the activation program in <cell_type>T helper lymphocytes</cell_type> .


In this report we describe how signals initiated through the type I IL-1R interact with signals from the antigen receptor to synergistically augment the transactivating properties of NF-kappa B .

In this report we describe how signals initiated through the <protein>type I IL-1R</protein> interact with signals from the antigen receptor to synergistically augment the transactivating properties of <protein>NF-kappa B</protein> .


The synergistic antigen receptor initiated signals are mediated through protein kinase C because they can be mimicked by the phorbol ester , 12-O-tetradecanoylphorbol-13-acetate , but not with calcium ionophores ; and are staurosporine sensitive but cyclosporine resistant .

The synergistic <protein>antigen receptor</protein> initiated signals are mediated through <protein>protein kinase C</protein> because they can be mimicked by the phorbol ester , 12-O-tetradecanoylphorbol-13-acetate , but not with calcium ionophores ; and are staurosporine sensitive but cyclosporine resistant .


Gel shift analyses demonstrate that NF-kappa B nuclear translocation is stimulated primarily by IL-1 rather than by antigen receptor signals .

Gel shift analyses demonstrate that <protein>NF-kappa B</protein> nuclear translocation is stimulated primarily by <protein>IL-1</protein> rather than by <protein>antigen receptor</protein> signals .


Western blot and phosphorylation analyses demonstrate that the synergistic effect on NF-kappa B functional activity is independent of I kappa B alpha ( MAD3 ) - NF-kappa B dissociation in the cytosol and is not associated with I kappa B nuclear translocation .

Western blot and phosphorylation analyses demonstrate that the synergistic effect on <protein>NF-kappa B</protein> functional activity is independent of <protein>I kappa B alpha</protein> ( <protein>MAD3</protein> ) - <protein>NF-kappa B</protein> dissociation in the cytosol and is not associated with <protein>I kappa B</protein> nuclear translocation .


The IL-1 -induced NF-kappa B DNA nuclear localization is transient and can be prolonged either by an antigen receptor-initiated signal or by inhibiting protein synthesis .

The <protein>IL-1</protein> -induced <protein>NF-kappa B</protein> DNA nuclear localization is transient and can be prolonged either by an antigen receptor-initiated signal or by inhibiting protein synthesis .


These results suggest that IL-1 induces both NF-kappa B nuclear translocation and the synthesis of a protein ( s ) responsible for terminating NF-kappa B -DNA interaction in the nucleus .

These results suggest that <protein>IL-1</protein> induces both <protein>NF-kappa B</protein> nuclear translocation and the synthesis of a protein ( s ) responsible for terminating <protein>NF-kappa B</protein> -DNA interaction in the nucleus .


Antigen receptor signals prolong NF-kappa B -DNA interaction , probably by functionally antagonizing the IL-1 -induced synthesis of a protein ( s ) responsible for the transient NF-kappa B -DNA interaction and consequently synergistically enhance IL-1 -induced NF-kappa B -dependent gene transcription .

Antigen receptor signals prolong <protein>NF-kappa B</protein> -DNA interaction , probably by functionally antagonizing the <protein>IL-1</protein> -induced synthesis of a protein ( s ) responsible for the transient <protein>NF-kappa B</protein> -DNA interaction and consequently synergistically enhance <protein>IL-1</protein> -induced <protein>NF-kappa B</protein> -dependent gene transcription .


Identification of the promoter region of chicken anemia virus ( CAV ) containing a novel enhancer-like element .

Identification of the <dna>promoter region</dna> of chicken anemia virus ( CAV ) containing a novel <dna>enhancer-like element</dna> .


The single promoter region in the cloned genome [ Noteborn et al. , J. Virol. 65 ( 1991 ) 3131-3139 ] of chicken anemia virus ( CAV ) in chicken T-cells was analysed via CAT assays .

The single <dna>promoter region</dna> in the cloned genome [ Noteborn et al. , J. Virol. 65 ( 1991 ) 3131-3139 ] of chicken anemia virus ( CAV ) in <cell_type>chicken T-cells</cell_type> was analysed via <protein>CAT</protein> assays .


A unique region containing four or five near-perfect direct repeats ( DR ) of 21 bp with one 12-bp insert was proven to be the main transcription-activation element , with enhancer-like characteristics .

A unique region containing four or five near-perfect direct repeats ( DR ) of 21 bp with one <dna>12-bp insert</dna> was proven to be the main <dna>transcription-activation element</dna> , with enhancer-like characteristics .


PCR studies revealed that CAV isolates from across the world all contained this promoter sequence .

PCR studies revealed that CAV isolates from across the world all contained this <dna>promoter sequence</dna> .


Electrophoretic mobility-shift assays ( EMSA ) showed that individual DR units , as well as the 12-bp insert , can bind to nuclear factors of chicken T-cells .

Electrophoretic mobility-shift assays ( EMSA ) showed that <dna>individual DR units</dna> , as well as the <dna>12-bp insert</dna> , can bind to <protein>nuclear factors</protein> of <cell_type>chicken T-cells</cell_type> .


Competition assays revealed that the DR units bound to factors other than the 12-bp insert .

Competition assays revealed that the <dna>DR units</dna> bound to factors other than the <dna>12-bp insert</dna> .


A synthetic oligodeoxyribonucleotide containing an SP1-box ( 5'-GGGCGG ) could compete with factors binding to the 12-bp insert .

A synthetic oligodeoxyribonucleotide containing an <dna>SP1-box</dna> ( 5'-GGGCGG ) could compete with factors binding to the <dna>12-bp insert</dna> .


Purified human SP1 was shown to have very strong affinity for the 12-bp insert .

Purified <protein>human SP1</protein> was shown to have very strong affinity for the <dna>12-bp insert</dna> .


Functional Myc-Max heterodimer is required for activation-induced apoptosis in T cell hybridomas .

Functional <protein>Myc-Max heterodimer</protein> is required for activation-induced apoptosis in <cell_line>T cell hybridomas</cell_line> .


T cell hybridomas respond to activation signals by undergoing apoptotic cell death , and this is likely to represent comparable events related to tolerance induction in immature and mature T cells in vivo .

<cell_line>T cell hybridomas</cell_line> respond to activation signals by undergoing apoptotic cell death , and this is likely to represent comparable events related to tolerance induction in <cell_type>immature and mature T cells</cell_type> in vivo .


Previous studies using antisense oligonucleotides implicated the c-Myc protein in the phenomenon of activation-induced apoptosis .

Previous studies using antisense oligonucleotides implicated the <protein>c-Myc protein</protein> in the phenomenon of activation-induced apoptosis .


This role for c-Myc in apoptosis is now confirmed in studies using a dominant negative form of its heterodimeric binding partner , Max , which we show here inhibits activation-induced apoptosis .

This role for <protein>c-Myc</protein> in apoptosis is now confirmed in studies using a dominant negative form of its heterodimeric binding partner , <protein>Max</protein> , which we show here inhibits activation-induced apoptosis .


Further , coexpression of a reciprocally mutant Myc protein capable of forming functional heterodimers with the mutant Max can compensate for the dominant negative activity and restore activation-induced apoptosis .

Further , coexpression of a <protein>reciprocally mutant Myc protein</protein> capable of forming functional <protein>heterodimers</protein> with the mutant <protein>Max</protein> can compensate for the dominant negative activity and restore activation-induced apoptosis .


These results imply that Myc promotes activation-induced apoptosis by obligatory heterodimerization with Max , and therefore , by regulating gene transcription .

These results imply that <protein>Myc</protein> promotes activation-induced apoptosis by obligatory heterodimerization with <protein>Max</protein> , and therefore , by regulating gene transcription .


Epstein-Barr virus SM protein .

<protein>Epstein-Barr virus SM protein</protein> .


The protein products of the Epstein-Barr virus ( EBV ) BMLF1 open reading frame have been characterized in the early productive cycle in B95-8 and Akata cells .

The protein products of the Epstein-Barr virus ( EBV ) BMLF1 open reading frame have been characterized in the early productive cycle in <cell_line>B95-8</cell_line> and <cell_line>Akata cells</cell_line> .


The SM protein derived from the spliced RNA joining BSLF2 to BMLF1 is much the most abundant protein .

The <protein>SM protein</protein> derived from the spliced RNA joining <protein>BSLF2</protein> to <protein>BMLF1</protein> is much the most abundant protein .


SM is a phosphoprotein in EBV -infected cells and can be phosphorylated in vitro with casein kinase II ( CKII ) .

<protein>SM</protein> is a <protein>phosphoprotein</protein> in EBV <cell_type>-infected cells</cell_type> and can be phosphorylated in vitro with <protein>casein kinase II</protein> ( <protein>CKII</protein> ) .


Computer analysis of the SM protein sequence showed a C terminal section of SM to be related to genome positional homologues of four other herpesviruses and revealed consensus CKII sites near the N termini of the EBV SM protein , the herpes simplex virus ( HSV ) ICP27 protein and the herpesvirus saimiri ( HVS ) open reading frame 57 protein .

Computer analysis of the <protein>SM protein</protein> sequence showed a <protein>C terminal section</protein> of <protein>SM</protein> to be related to <protein>genome positional homologues</protein> of four other herpesviruses and revealed <protein>consensus CKII sites</protein> near the <protein>N termini</protein> of the <protein>EBV SM protein</protein> , the <protein>herpes simplex virus ( HSV ) ICP27 protein</protein> and the <protein>herpesvirus saimiri ( HVS ) open reading frame 57 protein</protein> .


Site-directed mutagenesis of the consensus CKII site in EBV SM greatly reduced the in vitro phosphorylation of SM by CKII .

Site-directed mutagenesis of the <dna>consensus CKII site</dna> in EBV SM greatly reduced the in vitro phosphorylation of <protein>SM</protein> by <protein>CKII</protein> .


The mechanism of transactivation by BMLF1 proteins has been controversial but SM was shown to transactivate gene expression from a CAT reporter construct by increasing the amount of cytoplasmic CAT mRNA .

The mechanism of transactivation by <protein>BMLF1 proteins</protein> has been controversial but <protein>SM</protein> was shown to transactivate gene expression from a <dna>CAT reporter construct</dna> by increasing the amount of <rna>cytoplasmic CAT mRNA</rna> .


Mutagenesis of the CKII site in SM made no difference to the transactivation in this transient transfection assay .

Mutagenesis of the <protein>CKII</protein> site in <protein>SM</protein> made no difference to the transactivation in this transient transfection assay .


Inducible binding to the c-fos serum response element during T cell activation is regulated by a phosphotyrosine-containing protein .

Inducible binding to the c-fos serum response element during T cell activation is regulated by a <protein>phosphotyrosine-containing protein</protein> .


The proto-oncogene c-fos is an immediate-early gene , and one of the first genes transcribed after stimulation of most cells with a variety of ligands .

The <dna>proto-oncogene c-fos</dna> is an <dna>immediate-early gene</dna> , and one of the first genes transcribed after stimulation of most cells with a variety of ligands .


Fos expression may be a pivotal event in converting ligand-receptor interactions at the membrane into functional modulation of cell phenotype .


The serum response element ( SRE ) in the c-fos regulatory region participates in induction of transcription by various growth factors and by phorbol esters and subsequent squelching of transcription .

The <dna>serum response element</dna> ( <dna>SRE</dna> ) in the <dna>c-fos regulatory region</dna> participates in induction of transcription by various <protein>growth factors</protein> and by phorbol esters and subsequent squelching of transcription .


We show that an inducible protein complex ( Band A ) binds to SRE DNA within 10 min after mitogenic stimulation of human PBL-T , and becomes nondetectable by 60 min .

We show that an inducible <protein>protein complex</protein> ( <protein>Band A</protein> ) binds to <dna>SRE DNA</dna> within 10 min after mitogenic stimulation of <cell_line>human PBL-T</cell_line> , and becomes nondetectable by 60 min .


Band A contains the serum response factor plus additional factor ( s ) .

<protein>Band A</protein> contains the <protein>serum response factor</protein> plus additional factor ( s ) .


A protein that is phosphorylated on a tyrosine residue in resting PBL-T suppresses binding of a component of Band A to the SRE motif .

A protein that is phosphorylated on a tyrosine residue in <cell_line>resting PBL-T</cell_line> suppresses binding of a component of <protein>Band A</protein> to the <dna>SRE motif</dna> .


Upon stimulation of the cells , this protein no longer prevents binding of DNA by Band A , and suppression of binding is restored within 30 min .

Upon stimulation of the cells , this protein no longer prevents binding of DNA by <protein>Band A</protein> , and suppression of binding is restored within 30 min .


The phosphorylated tyrosine residue itself is important for the protein-protein interaction .


In vivo modification of major histocompatibility complex class II DRA promoter occupancy mediated by the AIR-1 trans-activator .

In vivo modification of <dna>major histocompatibility complex class II DRA promoter</dna> occupancy mediated by the <protein>AIR-1 trans-activator</protein> .


RJ 2.2.5 is a human B cell mutant derived from the Burkitt lymphoma Raji cell which is defective in the AIR-1 locus function .

<cell_line>RJ 2.2.5</cell_line> is a <cell_line>human B cell mutant</cell_line> derived from the <cell_line>Burkitt lymphoma Raji cell</cell_line> which is defective in the AIR-1 locus function .


This locus encodes a transcriptional trans-activator required for the constitutive expression of major histocompatibility complex ( MHC ) class II genes .

This locus encodes a transcriptional trans-activator required for the constitutive expression of <dna>major histocompatibility complex ( MHC ) class II genes</dna> .


Here we show , by in vivo DNase I footprinting , that the AIR-1 locus defect correlates with changes in the DRA promoter occupancy .

Here we show , by in vivo <protein>DNase I</protein> footprinting , that the <dna>AIR-1 locus defect</dna> correlates with changes in the <dna>DRA promoter</dna> occupancy .


Interestingly , reexpression of human MHC class II genes in RJ 2.2.5 x mouse spleen cell hybrids is associated with partial reversion of DRA promoter occupancy to the Raji pattern .

Interestingly , reexpression of <dna>human MHC class II genes</dna> in <cell_line>RJ 2.2.5 x mouse spleen cell hybrids</cell_line> is associated with partial reversion of <dna>DRA promoter</dna> occupancy to the Raji pattern .


DRA promoter occupancy in other class II-negative B cell lines , derived from patients with bare lymphocyte syndrome , is drastically different from the one observed in RJ 2.2.5 and Raji cells .

<dna>DRA promoter</dna> occupancy in other <cell_line>class II-negative B cell lines</cell_line> , derived from patients with bare lymphocyte syndrome , is drastically different from the one observed in <cell_line>RJ 2.2.5</cell_line> and <cell_line>Raji cells</cell_line> .


Moreover , the use of the DNase I as an in vivo footprinting agent reveals that the patients ' cell lines do not display a completely `` bare promoter `` as previously reported using dimethyl sulfate as the footprinting agent .

Moreover , the use of the <protein>DNase I</protein> as an in vivo footprinting agent reveals that the <cell_line>patients ' cell lines</cell_line> do not display a completely `` <dna>bare promoter</dna> `` as previously reported using dimethyl sulfate as the footprinting agent .


Thus , the use of DNase I allowed us , for the first time , to correlate the AIR-1 locus defect with class II promoter occupancy alterations and distinguish these alterations from the ones observed in phenotypically similar but genetically distinct MHC class II-negative cells .

Thus , the use of <protein>DNase I</protein> allowed us , for the first time , to correlate the <dna>AIR-1 locus defect</dna> with <dna>class II promoter</dna> occupancy alterations and distinguish these alterations from the ones observed in phenotypically similar but genetically distinct <cell_line>MHC class II-negative cells</cell_line> .