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700 | More frequent use of the classical Oct2a and Oct2b isoforms was observed in the lipopolysaccharide-stimulated B cells , while a preference for the Oct2ab and Oct2ba isoforms was observed in lipopolysaccharide plus phorbol-di-butyrate-treated cells . | More frequent use of the classical <protein>Oct2a</protein> and <protein>Oct2b</protein> isoforms was observed in the <cell_line>lipopolysaccharide-stimulated B cells</cell_line> , while a preference for the <protein>Oct2ab</protein> and <protein>Oct2ba</protein> isoforms was observed in <cell_line>lipopolysaccharide plus phorbol-di-butyrate-treated cells</cell_line> . |
701 | Positive regulators of the lineage-specific transcription factor GATA-1 in differentiating erythroid cells . | Positive regulators of the lineage-specific <protein>transcription factor</protein> <protein>GATA-1</protein> in <cell_type>differentiating erythroid cells</cell_type> . |
702 | The zinc finger transcription factor GATA-1 is a major regulator of gene expression in erythroid , megakaryocyte , and mast cell lineages . | The <protein>zinc finger transcription factor</protein> <protein>GATA-1</protein> is a major regulator of gene expression in <cell_type>erythroid , megakaryocyte , and mast cell lineages</cell_type> . |
703 | GATA-1 binds to WGATAR consensus motifs in the regulatory regions of virtually all erythroid cell-specific genes . | <protein>GATA-1</protein> binds to <dna>WGATAR consensus motifs</dna> in the <dna>regulatory regions</dna> of virtually all <dna>erythroid cell-specific genes</dna> . |
704 | Analyses with cultured cells and cell-free systems have provided strong evidence that GATA-1 is involved in control of globin gene expression during erythroid differentiation . | Analyses with <cell_line>cultured cells</cell_line> and cell-free systems have provided strong evidence that <protein>GATA-1</protein> is involved in control of <dna>globin gene</dna> expression during erythroid differentiation . |
705 | Targeted mutagenesis of the GATA-1 gene in embryonic stem cells has demonstrated its requirement in normal erythroid development . | Targeted mutagenesis of the <dna>GATA-1 gene</dna> in <cell_type>embryonic stem cells</cell_type> has demonstrated its requirement in normal erythroid development . |
706 | Efficient rescue of the defect requires an intact GATA element in the distal promoter , suggesting autoregulatory control of GATA-1 transcription . | Efficient rescue of the defect requires an intact <dna>GATA element</dna> in the <dna>distal promoter</dna> , suggesting autoregulatory control of <protein>GATA-1</protein> transcription . |
707 | To examine whether GATA-1 expression involves additional regulatory factors or is maintained entirely by an autoregulatory loop , we have used a transient heterokaryon system to test the ability of erythroid factors to activate the GATA-1 gene in nonerythroid nuclei . | To examine whether <protein>GATA-1</protein> expression involves additional <protein>regulatory factors</protein> or is maintained entirely by an autoregulatory loop , we have used a transient heterokaryon system to test the ability of <protein>erythroid factors</protein> to activate the <dna>GATA-1 gene</dna> in nonerythroid nuclei . |
708 | We show here that proerythroblasts and mature erythroid cells contain a diffusible activity ( TAG ) capable of transcriptional activation of GATA-1 and that this activity decreases during the terminal differentiation of erythroid cells . | We show here that <cell_type>proerythroblasts</cell_type> and <cell_type>mature erythroid cells</cell_type> contain a diffusible activity ( TAG ) capable of transcriptional activation of <protein>GATA-1</protein> and that this activity decreases during the terminal differentiation of <cell_type>erythroid cells</cell_type> . |
709 | Nuclei from GATA-1 -mutant embryonic stem cells can still be reprogrammed to express their globin genes in erythroid heterokaryons , indicating that de novo induction of GATA-1 is not required for globin gene activation following cell fusion . | Nuclei from <cell_line>GATA-1 -mutant embryonic stem cells</cell_line> can still be reprogrammed to express their <dna>globin genes</dna> in <cell_type>erythroid heterokaryons</cell_type> , indicating that de novo induction of <protein>GATA-1</protein> is not required for <dna>globin gene</dna> activation following cell fusion . |
710 | Role of HIV-1 Nef expression in activation pathways in CD4 + T cells . | Role of <protein>HIV-1 Nef</protein> expression in activation pathways in <protein>CD4</protein> + T cells . |
711 | The role of the human immunodeficiency virus ( HIV-1 ) Nef protein in T cell activation pathways was investigated using a Jurkat CD4+ cell line stably transfected with a Nef expression vector . | The role of the <protein>human immunodeficiency virus ( HIV-1 ) Nef protein</protein> in T cell activation pathways was investigated using a <cell_line>Jurkat CD4+ cell line</cell_line> stably transfected with a Nef expression vector . |
712 | Secretion of IL-2 and TNF-alpha , surface expression of IL-2R , and DNA-binding activity of NF-kappa B and AP-1 ( Fos/Jun ) complex in response to phorbol myristate acetate , TNF-alpha , or immobilized antibodies to CD3 were monitored . | Secretion of <protein>IL-2</protein> and <protein>TNF-alpha</protein> , surface expression of <protein>IL-2R</protein> , and DNA-binding activity of <protein>NF-kappa B</protein> and <protein>AP-1 ( Fos/Jun ) complex</protein> in response to phorbol myristate acetate , <protein>TNF-alpha</protein> , or immobilized antibodies to <protein>CD3</protein> were monitored . |
713 | These parameters were not modified by Nef expression in Jurkat cells , whereas stimulation with the same stimuli resulted in partial inhibition of LTR activation in Nef+ Jurkat cells . | These parameters were not modified by <protein>Nef</protein> expression in <cell_line>Jurkat cells</cell_line> , whereas stimulation with the same stimuli resulted in partial inhibition of <dna>LTR</dna> activation in <cell_line>Nef+ Jurkat cells</cell_line> . |
714 | This inhibition was not mediated through Nef phosphorylation on Thr-15 or GTP-binding activity because mutations in critical sites did not alter this inhibition . | This inhibition was not mediated through <protein>Nef</protein> phosphorylation on Thr-15 or GTP-binding activity because mutations in critical sites did not alter this inhibition . |
715 | Analysis of truncated LTRs confirmed that inhibition of LTR activation was not mediated through NF-kappa B -binding activity but through the region containing the negative responding elements ( NREs ) . | Analysis of truncated <dna>LTRs</dna> confirmed that inhibition of <dna>LTR</dna> activation was not mediated through <protein>NF-kappa B</protein> -binding activity but through the region containing the <dna>negative responding elements</dna> ( <dna>NREs</dna> ) . |
716 | These results suggest that Nef downmodulates LTR activation without significantly inhibiting the capacity of T cells to respond to immunological activations . | These results suggest that <protein>Nef</protein> downmodulates <dna>LTR</dna> activation without significantly inhibiting the capacity of <cell_type>T cells</cell_type> to respond to immunological activations . |
717 | Tat-binding protein 7 is a subunit of the 26S protease . | <protein>Tat-binding protein 7</protein> is a subunit of the <protein>26S protease</protein> . |
718 | Subunit 6 ( S6 ) , an integral component of the 26S protease from human erythrocytes , has been studied by SDS-PAGE , peptide mapping and sequence analysis . | <protein>Subunit 6</protein> ( <protein>S6</protein> ) , an integral component of the <protein>26S protease</protein> from <cell_type>human erythrocytes</cell_type> , has been studied by SDS-PAGE , peptide mapping and sequence analysis . |
719 | S6 was cleaved with CNBr and three internal peptides were sequenced . | <protein>S6</protein> was cleaved with <protein>CNBr</protein> and three internal peptides were sequenced . |
720 | A comparison with known proteins in Genbank revealed that all three S6 peptides match the predicted sequence of TBP7 , Tat-binding protein 7 . | A comparison with known proteins in Genbank revealed that all three <protein>S6</protein> peptides match the predicted sequence of <protein>TBP7</protein> , <protein>Tat-binding protein 7</protein> . |
721 | Based on peptide matches covering more than 10 % of the TBP7 sequence , and the fact that the migration of S6 on SDS-PAGE is consistent with the estimated molecular mass for TBP7 , we conclude that subunit 6 of the 26S protease is TBP7 . | Based on peptide matches covering more than 10 % of the <protein>TBP7</protein> sequence , and the fact that the migration of <protein>S6</protein> on SDS-PAGE is consistent with the estimated molecular mass for <protein>TBP7</protein> , we conclude that <protein>subunit 6</protein> of the <protein>26S protease</protein> is <protein>TBP7</protein> . |
722 | Hypoxia causes the activation of nuclear factor kappa B through the phosphorylation of I kappa B alpha on tyrosine residues . | Hypoxia causes the activation of <protein>nuclear factor kappa B</protein> through the phosphorylation of <protein>I kappa B alpha</protein> on tyrosine residues . |
723 | The response of mammalian cells to stress is controlled by transcriptional regulatory proteins such as nuclear factor kappa B ( NF-kappa B ) to induce a wide variety of early response genes . | The response of <cell_type>mammalian cells</cell_type> to stress is controlled by <protein>transcriptional regulatory proteins</protein> such as <protein>nuclear factor kappa B</protein> ( <protein>NF-kappa B</protein> ) to induce a wide variety of <dna>early response genes</dna> . |
724 | In this report , we show that exposure of cells to hypoxia ( 0.02 % O2 ) results in I kappa B alpha degradation , increased NF-kappa B DNA binding activity , and transactivation of a reporter gene construct containing two NF-kappa B DNA binding sites . | In this report , we show that exposure of cells to hypoxia ( 0.02 % O2 ) results in <protein>I kappa B alpha</protein> degradation , increased <protein>NF-kappa B</protein> DNA binding activity , and transactivation of a <dna>reporter gene construct</dna> containing two <dna>NF-kappa B DNA binding sites</dna> . |
725 | Pretreatment of cells with protein tyrosine kinase inhibitors and the dominant negative allele of c-Raf-1 ( Raf 301 ) inhibited I kappa B alpha degradation , NF-kappa B binding , and transactivation of kappa B reporter constructs by hypoxia . | Pretreatment of cells with protein <protein>tyrosine kinase</protein> inhibitors and the <dna>dominant negative allele</dna> of <dna>c-Raf-1</dna> ( <protein>Raf 301</protein> ) inhibited <protein>I kappa B alpha</protein> degradation , <protein>NF-kappa B</protein> binding , and transactivation of <dna>kappa B reporter constructs</dna> by hypoxia . |
726 | To demonstrate a direct link between changes in the phosphorylation pattern of I kappa B alpha with NF-kappa B activation , we immunoprecipitated I kappa B alpha after varying times of hypoxic exposure and found that its tyrosine phosphorylation status increased during hypoxic exposure . | To demonstrate a direct link between changes in the phosphorylation pattern of <protein>I kappa B alpha</protein> with <protein>NF-kappa B</protein> activation , we immunoprecipitated <protein>I kappa B alpha</protein> after varying times of hypoxic exposure and found that its tyrosine phosphorylation status increased during hypoxic exposure . |
727 | Inhibition of the transfer of tyrosine phosphoryl groups onto I kappa B alpha prevented I kappa B alpha degradation and NF-kappa B binding . | Inhibition of the transfer of tyrosine phosphoryl groups onto <protein>I kappa B alpha</protein> prevented <protein>I kappa B alpha</protein> degradation and <protein>NF-kappa B</protein> binding . |
728 | In comparison to other activators of NF-kappa B such as phorbol myristate acetate or tumor necrosis factor , we did not detect changes in the tyrosine phosphorylation status of I kappa B alpha following treatment with either of these agents . | In comparison to other activators of <protein>NF-kappa B</protein> such as phorbol myristate acetate or <protein>tumor necrosis factor</protein> , we did not detect changes in the tyrosine phosphorylation status of <protein>I kappa B alpha</protein> following treatment with either of these agents . |
729 | These results suggest that tyrosine phosphorylation of I kappa B alpha during hypoxia is an important proximal step which precedes its dissociation and degradation from NF-kappa B . | These results suggest that tyrosine phosphorylation of <protein>I kappa B alpha</protein> during hypoxia is an important proximal step which precedes its dissociation and degradation from <protein>NF-kappa B</protein> . |
730 | Overproduction of NFKB2 ( lyt-10 ) and c-Rel : a mechanism for HTLV-I Tax -mediated trans-activation via the NF-kappa B signalling pathway . | Overproduction of <protein>NFKB2</protein> ( <protein>lyt-10</protein> ) and <protein>c-Rel</protein> : a mechanism for <protein>HTLV-I Tax</protein> -mediated trans-activation via the <protein>NF-kappa B</protein> signalling pathway . |
731 | Molecular , biochemical and epidemiological evidence implicate HTLV-I as an etiologic agent of adult T cell leukemia ( ATL ) . | Molecular , biochemical and epidemiological evidence implicate HTLV-I as an etiologic agent of adult T cell leukemia ( ATL ) . |
732 | The Tax protein of HTLV-I , a positive transcriptional activator of HTLV-I gene expression , is a viral oncogene that also increases transcription of cellular genes including GM-CSF , IL-2R alpha and IL-2 . | The <protein>Tax protein</protein> of HTLV-I , a <protein>positive transcriptional activator</protein> of HTLV-I gene expression , is a viral oncogene that also increases transcription of <dna>cellular genes</dna> including <protein>GM-CSF</protein> , <protein>IL-2R alpha</protein> and <protein>IL-2</protein> . |
733 | One of the cellular targets of the trans-activating effects of Tax is the NF-kappa B/Rel family of transcription factors , pleiotropic regulators of immunoregulatory , cytokine and viral gene expression . | One of the cellular targets of the trans-activating effects of Tax is the <protein>NF-kappa B/Rel family</protein> of <protein>transcription factors</protein> , <protein>pleiotropic regulators</protein> of immunoregulatory , cytokine and viral gene expression . |
734 | In this report , we demonstrate that NFKB2 ( lyt-10 ) and c-Rel are overexpressed in HTLV-I infected and Tax-expressing cells and , together , account for the majority of the constitutive NF-kappa B binding activity in these cells before and after PMA stimulation . | In this report , we demonstrate that <protein>NFKB2</protein> ( <protein>lyt-10</protein> ) and <protein>c-Rel</protein> are overexpressed in HTLV-I infected and <cell_type>Tax-expressing cells</cell_type> and , together , account for the majority of the constitutive <protein>NF-kappa B</protein> binding activity in these cells before and after PMA stimulation . |
735 | Most importantly , we show a Tax -dependent correlation between expression of NFKB2 ( p100 ) and processing to the DNA binding NFKB2 ( p52 ) form , induction of c-Rel , and trans-activation of NF-kappa B -mediated gene expression . | Most importantly , we show a <protein>Tax</protein> -dependent correlation between expression of <protein>NFKB2</protein> ( <protein>p100</protein> ) and processing to the DNA binding <protein>NFKB2</protein> ( <protein>p52</protein> ) form , induction of <protein>c-Rel</protein> , and trans-activation of <protein>NF-kappa B</protein> -mediated gene expression . |
736 | Furthermore , the NFKB2 precursor is physically associated with c-Rel and with Tax in HTLV-I infected cells . | Furthermore , the <protein>NFKB2</protein> precursor is physically associated with <protein>c-Rel</protein> and with <protein>Tax</protein> in <cell_type>HTLV-I infected cells</cell_type> . |
737 | We propose that NFKB2 synthesis and processing allows continuous nuclear expression of an otherwise cytoplasmic protein and , in conjunction with overexpression of c-Rel , NFKB2 alters the NF-kappa B signalling pathway and contributes to leukemic transformation of T cells by HTLV-I . | We propose that <protein>NFKB2</protein> synthesis and processing allows continuous nuclear expression of an otherwise <protein>cytoplasmic protein</protein> and , in conjunction with overexpression of <protein>c-Rel</protein> , <protein>NFKB2</protein> alters the <protein>NF-kappa B</protein> signalling pathway and contributes to leukemic transformation of <cell_type>T cells</cell_type> by HTLV-I . |
738 | Retinoic acid downmodulates erythroid differentiation and GATA1 expression in purified adult-progenitor culture . | Retinoic acid downmodulates erythroid differentiation and <protein>GATA1</protein> expression in <cell_line>purified adult-progenitor culture</cell_line> . |
739 | All-trans retinoic acid ( RA ) is an important morphogen in vertebrate development , a normal constituent in human adult blood and is also involved in the control of cell growth and differentiation in acute promyelocytic leukemia . | All-trans retinoic acid ( RA ) is an important morphogen in vertebrate development , a normal constituent in human adult blood and is also involved in the control of cell growth and differentiation in acute promyelocytic leukemia . |
740 | We have examined the effects of RA on normal hematopoiesis by using early hematopoietic progenitor cells ( HPC ) stringently purified from adult peripheral blood . | We have examined the effects of RA on normal hematopoiesis by using early <cell_type>hematopoietic progenitor cells</cell_type> ( <cell_type>HPC</cell_type> ) stringently purified from adult peripheral blood . |
741 | In clonogenetic fetal calf serum-supplemented ( FCS+ ) or -nonsupplemented ( FCS- ) culture treated with saturating levels of interleukin-3 ( IL-3 ) granulocyte-macrophage colony-stimulating factor ( GM-CSF ) and erythropoietin ( Ep ) ( combined with c-kit ligand in FCS ( - ) -culture conditions ) , RA induces a dramatic dose-dependent shift from erythroid to granulomonocytic colony formation , the latter colonies being essentially represented by granulocytic clones . | In <cell_line>clonogenetic fetal calf serum-supplemented ( FCS+ ) or -nonsupplemented ( FCS- ) culture</cell_line> treated with saturating levels of <protein>interleukin-3</protein> ( <protein>IL-3</protein> ) <protein>granulocyte-macrophage colony-stimulating factor</protein> ( <protein>GM-CSF</protein> ) and <protein>erythropoietin</protein> ( <protein>Ep</protein> ) ( combined with <protein>c-kit</protein> ligand in FCS ( - ) -culture conditions ) , RA induces a dramatic dose-dependent shift from erythroid to granulomonocytic colony formation , the latter colonies being essentially represented by <cell_line>granulocytic clones</cell_line> . |
742 | This shift is apparently not caused by a recruitment phenomenon , because in FCS+ culture , the total number of colonies is not significantly modified by RA addition . | This shift is apparently not caused by a recruitment phenomenon , because in <cell_line>FCS+ culture</cell_line> , the total number of colonies is not significantly modified by RA addition . |
743 | In FCS- liquid-suspension culture supplemented with saturating Ep level and low-dose IL-3/GM-CSF , adult HPC undergo unilineage erythropoietic differentiation : Here again , treatment with high-dose RA induces a shift from the erythroid to granulocytic differentiation pathway . | In <cell_line>FCS- liquid-suspension culture</cell_line> supplemented with saturating <protein>Ep</protein> level and <protein>low-dose IL-3/GM-CSF</protein> , adult <cell_type>HPC</cell_type> undergo unilineage erythropoietic differentiation : Here again , treatment with high-dose RA induces a shift from the erythroid to granulocytic differentiation pathway . |
744 | Studies on RA time-response or pulse treatment in semisolid or liquid culture show that early RA addition is most effective , thus indicating that early but not late HPC are sensitive to its action . | Studies on RA time-response or pulse treatment in semisolid or liquid culture show that early RA addition is most effective , thus indicating that early but not late <cell_type>HPC</cell_type> are sensitive to its action . |
745 | We then analyzed the expression of the master GATA1 gene , which encodes a finger transcription factor required for normal erythroid development ; addition of RA to HPC stimulated into unilineage erythropoietic differentiation in liquid culture caused a virtually complete inhibition of GATA1 mRNA induction . | We then analyzed the expression of the <dna>master GATA1 gene</dna> , which encodes a <protein>finger transcription factor</protein> required for normal erythroid development ; addition of RA to <cell_type>HPC</cell_type> stimulated into unilineage erythropoietic differentiation in liquid culture caused a virtually complete inhibition of <rna>GATA1 mRNA</rna> induction . |
746 | These results indicate that RA directly inhibits the erythroid differentiation program at the level of early adult HPC , and may lead to a shift from the erythroid to granulocytic differentiation pathway . | These results indicate that RA directly inhibits the erythroid differentiation program at the level of early adult <cell_type>HPC</cell_type> , and may lead to a shift from the erythroid to granulocytic differentiation pathway . |
747 | This phenomenon is correlated with inhibition of GATA1 induction in the early stages of erythropoietic differentiation . | This phenomenon is correlated with inhibition of <protein>GATA1</protein> induction in the early stages of erythropoietic differentiation . |
748 | Induction of phosphatidylinositol turnover and EGR-1 mRNA expression by crosslinking of surface IgM and IgD in the human B cell line B104 . | Induction of phosphatidylinositol turnover and <rna>EGR-1 mRNA</rna> expression by crosslinking of surface <protein>IgM</protein> and <protein>IgD</protein> in the <cell_line>human B cell line B104</cell_line> . |
749 | We have previously shown that a human B lymphoma cell line , B104 , expressed surface IgM ( sIgM ) and surface IgD ( sIgD ) , and that crosslinking of sIgM and sIgD by anti-IgM antibody ( Ab ) and anti-IgD Ab , respectively , induced Ca2+ influx to almost the same degree , whereas only sIgM -crosslinking caused B104 cell death . | We have previously shown that a <cell_line>human B lymphoma cell line , B104</cell_line> , expressed <protein>surface IgM</protein> ( <protein>sIgM</protein> ) and <protein>surface IgD</protein> ( <protein>sIgD</protein> ) , and that crosslinking of <protein>sIgM</protein> and <protein>sIgD</protein> by <protein>anti-IgM antibody ( Ab )</protein> and <protein>anti-IgD Ab</protein> , respectively , induced Ca2+ influx to almost the same degree , whereas only <protein>sIgM</protein> -crosslinking caused <cell_line>B104 cell</cell_line> death . |
750 | Here , we investigated the accumulation of cyclic AMP ( cAMP ) , the hydrolysis of inositol phosphates , protein kinase C ( PKC ) activity and the induction of Egr-1 and c-fos mRNA expression by sIgM- and sIgD-crosslinking to examine differences in the signals mediated through sIgM and sIgD in B104 cells . | Here , we investigated the accumulation of cyclic AMP ( cAMP ) , the hydrolysis of inositol phosphates , <protein>protein kinase C</protein> ( <protein>PKC</protein> ) activity and the induction of Egr-1 and c-fos mRNA expression by sIgM- and sIgD-crosslinking to examine differences in the signals mediated through <protein>sIgM</protein> and <protein>sIgD</protein> in <cell_line>B104 cells</cell_line> . |
751 | Both sIgM- and sIgD-crosslinking with antibodies induced elevation of cAMP levels , phosphatidylinositol turnover , PKC activation and expression of Egr-1 and c-fos mRNA , although sIgM -crosslinking was more effective than sIgD -crosslinking , presumably due to the higher expression of sIgM than of sIgD . | Both sIgM- and sIgD-crosslinking with antibodies induced elevation of cAMP levels , phosphatidylinositol turnover , <protein>PKC</protein> activation and expression of <rna>Egr-1 and c-fos mRNA</rna> , although <protein>sIgM</protein> -crosslinking was more effective than <protein>sIgD</protein> -crosslinking , presumably due to the higher expression of <protein>sIgM</protein> than of <protein>sIgD</protein> . |
752 | Egr-1 mRNA expression induced by sIgM- and sIgD-crosslinking was inhibited by H7 , erbstatin and genistein , but not by HA1004 . | <rna>Egr-1 mRNA</rna> expression induced by sIgM- and sIgD-crosslinking was inhibited by <protein>H7</protein> , erbstatin and genistein , but not by HA1004 . |
753 | Erbstatin and genistein inhibited the sIg-crosslinking-induced Egr-1 mRNA expression in a dose-dependent manner parallel to that observed in the inhibition of sIg-crosslinking-induced protein tyrosine phosphorylation . | Erbstatin and genistein inhibited the sIg-crosslinking-induced <rna>Egr-1 mRNA</rna> expression in a dose-dependent manner parallel to that observed in the inhibition of sIg-crosslinking-induced protein tyrosine phosphorylation . |
754 | Phorbol myristate acetate induced Egr-1 mRNA expression but forskolin and dibutyryl cyclic AMP did not . | Phorbol myristate acetate induced <rna>Egr-1 mRNA</rna> expression but forskolin and dibutyryl cyclic AMP did not . |
755 | These findings suggest that the Egr-1 mRNA activating signals through sIgM and sIgD are protein tyrosine kinase- and PKC-dependent , but protein kinase A -independent . | These findings suggest that the <rna>Egr-1 mRNA</rna> activating signals through <protein>sIgM</protein> and <protein>sIgD</protein> are protein tyrosine kinase- and PKC-dependent , but <protein>protein kinase A</protein> -independent . |
756 | Cyclosporin A ( CsA ) and FK506 rescued B104 cells from death induced by anti-IgM Ab , but did not affect the expression of Egr-1 and c-fos mRNA , showing that CsA and FK506 affect signal transducers differently from or downstream to these molecules . | Cyclosporin A ( CsA ) and FK506 rescued <cell_line>B104 cells</cell_line> from death induced by <protein>anti-IgM Ab</protein> , but did not affect the expression of <protein>Egr-1</protein> and <rna>c-fos mRNA</rna> , showing that CsA and FK506 affect signal transducers differently from or downstream to these molecules . |
757 | The difference in signals transduced through sIgM and sIgD in B104 cells is discussed . | The difference in signals transduced through <protein>sIgM</protein> and <protein>sIgD</protein> in <cell_line>B104 cells</cell_line> is discussed . |
758 | Direct exposure to 2 , 3 , 7 , 8-tetrachlorodibenzo-p-dioxin ( TCDD ) increases infectivity of human erythrocytes to a malarial parasite . | Direct exposure to 2 , 3 , 7 , 8-tetrachlorodibenzo-p-dioxin ( TCDD ) increases infectivity of <cell_type>human erythrocytes</cell_type> to a malarial parasite . |
759 | Direct exposure to 10 nM 2 , 3 , 7 , 8-TCDD caused a 75 % increase and a 2-fold increase in the infectivity of isolated human erythrocytes to P. falciparum after 48 hours when the parasites were in an unsynchronized or synchronized state of growth , respectively . | Direct exposure to 10 nM 2 , 3 , 7 , 8-TCDD caused a 75 % increase and a 2-fold increase in the infectivity of isolated <cell_type>human erythrocytes</cell_type> to P. falciparum after 48 hours when the parasites were in an unsynchronized or synchronized state of growth , respectively . |
760 | Treatment of human erythrocytes with 10 microM sodium orthovanadate ( NaOV ) , an inhibitor of plasma membrane Ca-ATPase and phosphotyrosine phosphatase , decreased parasitemia by 30 % . | Treatment of <cell_type>human erythrocytes</cell_type> with 10 microM sodium orthovanadate ( NaOV ) , an inhibitor of <protein>plasma membrane Ca-ATPase</protein> and <protein>phosphotyrosine phosphatase</protein> , decreased parasitemia by 30 % . |
761 | Co-treatment of RBCs with TCDD and NaOV completely blocked the TCDD-induced increase in parasitemia . | Co-treatment of <cell_type>RBCs</cell_type> with TCDD and NaOV completely blocked the TCDD-induced increase in parasitemia . |
762 | Because erythrocytes are anucleated , these results are discussed as evidence for biochemical changes by TCDD without requiring the activation of gene products . | Because <cell_type>erythrocytes</cell_type> are anucleated , these results are discussed as evidence for biochemical changes by TCDD without requiring the activation of <protein>gene products</protein> . |
763 | Evidence for a trans-acting activator function regulating the expression of the human CD5 antigen . | Evidence for a <protein>trans-acting activator</protein> function regulating the expression of the <protein>human CD5 antigen</protein> . |
764 | Interspecies somatic cell hybrids were generated by fusing the mouse T-lymphoma cell line , BW5147 , with normal human T lymphocytes at different stages of differentiation . | Interspecies <cell_line>somatic cell hybrids</cell_line> were generated by fusing the <cell_line>mouse T-lymphoma cell line</cell_line> , <cell_line>BW5147</cell_line> , with <cell_type>normal human T lymphocytes</cell_type> at different stages of differentiation . |
765 | Thymocytes , activated peripheral T lymphocytes , or an activated T-cell clone were used as human partners , respectively , in three independent fusions . | <cell_type>Thymocytes</cell_type> , <cell_type>activated peripheral T lymphocytes</cell_type> , or an <cell_line>activated T-cell clone</cell_line> were used as human partners , respectively , in three independent fusions . |
766 | Irrespective of the human cell partner used for fusion , a certain number of hybrids lost CD5 surface expression over a period of time in culture . | Irrespective of the human cell partner used for fusion , a certain number of <cell_line>hybrids</cell_line> lost <protein>CD5</protein> surface expression over a period of time in culture . |
767 | Analysis at the phenotype and genetic level showed that lack of CD5 expression was due neither to segregation of human autosome 11 , on which the CD5 gene has been mapped , nor to deletion of the CD5 structural gene . | Analysis at the phenotype and genetic level showed that lack of <protein>CD5</protein> expression was due neither to segregation of <dna>human autosome 11</dna> , on which the <dna>CD5 gene</dna> has been mapped , nor to deletion of the <dna>CD5 structural gene</dna> . |
768 | Furthermore , loss of CD5 surface expression correlated with the absence of specific mRNA . | Furthermore , loss of <protein>CD5</protein> surface expression correlated with the absence of specific <rna>mRNA</rna> . |
769 | Since these hybrids preferentially segregate human chromosomes , these results indicate the existence of a non-syntenic trans-active locus , or loci , positively controlling the expression of the human CD5 gene . | Since these hybrids preferentially segregate human chromosomes , these results indicate the existence of a <dna>non-syntenic trans-active locus</dna> , or loci , positively controlling the expression of the <dna>human CD5 gene</dna> . |
770 | Induction of the CD11b gene during activation of the monocytic cell line U937 requires a novel nuclear factor MS-2 [ published erratum appears in J Immunol 1999 Jul 15 ; 163 ( 2 ) : 1091 ] | Induction of the <dna>CD11b gene</dna> during activation of the <cell_line>monocytic cell line U937</cell_line> requires a novel <protein>nuclear factor</protein> <protein>MS-2</protein> [ published erratum appears in J Immunol 1999 Jul 15 ; 163 ( 2 ) : 1091 ] |
771 | The differentiation of myeloid precursors into mature myelomonocytic cells is characterized by the induction of the gene encoding the beta2 integrin CD11b . | The differentiation of <cell_type>myeloid precursors</cell_type> into mature <cell_type>myelomonocytic cells</cell_type> is characterized by the induction of the gene encoding the <protein>beta2 integrin</protein> <protein>CD11b</protein> . |
772 | The transcription factors Sp1 and PU.1 prime the CD11b promoter , but the nature of the factors responsible for its inducible expression are unknown . | The <protein>transcription factors</protein> <protein>Sp1</protein> and <protein>PU.1 prime</protein> the <dna>CD11b promoter</dna> , but the nature of the factors responsible for its inducible expression are unknown . |
773 | In addition to the CD11b gene , the homologous genes encoding CD11a and CD11c also exhibit inducible expression during myeloid differentiation . | In addition to the <dna>CD11b gene</dna> , the homologous genes encoding <protein>CD11a</protein> and <protein>CD11c</protein> also exhibit inducible expression during myeloid differentiation . |
774 | Therefore , we compared the nucleotide sequences of the CD11a , CD11b , and CD11c gene promoters to identify common elements that might contribute to inducible expression . | Therefore , we compared the <dna>nucleotide sequences</dna> of the <dna>CD11a , CD11b , and CD11c gene promoters</dna> to identify common elements that might contribute to inducible expression . |
775 | This analysis identified one such element repeated four times within the CD11b promoter . | This analysis identified one such element repeated four times within the <dna>CD11b promoter</dna> . |
776 | Mutation of these elements indicated that two , MS-2beta and MS-2gamma , are critical to the induction of the CD11b gene during differentiation of the pro-monocytic cell line U937 . | Mutation of these elements indicated that two , <protein>MS-2beta</protein> and <protein>MS-2gamma</protein> , are critical to the induction of the <dna>CD11b gene</dna> during differentiation of the <cell_line>pro-monocytic cell line U937</cell_line> . |
777 | Electrophoretic mobility shift assays indicate that MS-2beta and MS-2gamma interact with nuclear factors that are induced during U937 differentiation . | Electrophoretic mobility shift assays indicate that <protein>MS-2beta</protein> and <protein>MS-2gamma</protein> interact with <protein>nuclear factors</protein> that are induced during <cell_line>U937</cell_line> differentiation . |
778 | These factors are detected at the time the CD11b promoter is activated . | These factors are detected at the time the <dna>CD11b promoter</dna> is activated . |
779 | The molecular mass of these factors is approximately 28 kDa , and their DNA binding characteristics are indistinguishable from those of the novel nuclear factor MS-2 . | The molecular mass of these factors is approximately 28 kDa , and their DNA binding characteristics are indistinguishable from those of the novel <protein>nuclear factor</protein> <protein>MS-2</protein> . |
780 | Taken together , our data indicate that MS-2 mediates induction of the CD11b gene as cells of the monocytic lineage mature . | Taken together , our data indicate that <protein>MS-2</protein> mediates induction of the <dna>CD11b gene</dna> as cells of the monocytic lineage mature . |
781 | The presence of multiple potential binding sites for MS-2 in the promoter regions of a wide range of genes expressed in mature myeloid cells suggests this factor plays a general role in myeloid differentiation . | The presence of multiple potential binding sites for <protein>MS-2</protein> in the promoter regions of a wide range of genes expressed in <cell_type>mature myeloid cells</cell_type> suggests this factor plays a general role in myeloid differentiation . |
782 | Acetylsalicylic acid and sodium salicylate inhibit LPS-induced NF-kappa B/c-Rel nuclear translocation , and synthesis of tissue factor ( TF ) and tumor necrosis factor alfa ( TNF-alpha ) in human monocytes . | Acetylsalicylic acid and sodium salicylate inhibit LPS-induced <protein>NF-kappa B/c-Rel</protein> nuclear translocation , and synthesis of <protein>tissue factor</protein> ( <protein>TF</protein> ) and <protein>tumor necrosis factor alfa</protein> ( <protein>TNF-alpha</protein> ) in <cell_type>human monocytes</cell_type> . |
783 | We have investigated the effects of acetylsalicylic acid and sodium salicylate on the LPS-induced synthesis of the pro-coagulant protein tissue factor ( TF ) and the pro-inflammatory protein tumor necrosis factor-alpha ( TNF-alpha ) , as well as the prostaglandin PGE2 in human monocytes . | We have investigated the effects of acetylsalicylic acid and sodium salicylate on the LPS-induced synthesis of the pro-coagulant protein tissue factor ( TF ) and the pro-inflammatory protein tumor necrosis factor-alpha ( <protein>TNF-alpha</protein> ) , as well as the <protein>prostaglandin PGE2</protein> in <cell_type>human monocytes</cell_type> . |
784 | Both drugs dose-dependently inhibited LPS-induced TF and TNF-alpha synthesis at the mRNA and the protein level , and reduced PGE2 production . | Both drugs dose-dependently inhibited <protein>LPS-induced TF</protein> and <protein>TNF-alpha</protein> synthesis at the <rna>mRNA</rna> and the protein level , and reduced <protein>PGE2</protein> production . |
785 | As evidenced by electro mobility shift assay ( EMSA ) and the use of a NF-kappa B prototypic probe , these drugs probably exert their inhibitory effects by interference with the nuclear translocation of NF-kappa B/c-Rel proteins . | As evidenced by electro mobility shift assay ( EMSA ) and the use of a <dna>NF-kappa B prototypic probe</dna> , these drugs probably exert their inhibitory effects by interference with the nuclear translocation of <protein>NF-kappa B/c-Rel proteins</protein> . |
786 | These data may expand the understanding of the anti-thrombotic and anti-inflammatory effects of these drugs when activation of monocytes occurs . | These data may expand the understanding of the anti-thrombotic and anti-inflammatory effects of these drugs when activation of <cell_type>monocytes</cell_type> occurs . |
787 | Interferon augments PML and PML/RAR alpha expression in normal myeloid and acute promyelocytic cells and cooperates with all-trans retinoic acid to induce maturation of a retinoid-resistant promyelocytic cell line . | Interferon augments <protein>PML</protein> and <protein>PML/RAR alpha</protein> expression in normal <cell_type>myeloid</cell_type> and <cell_type>acute promyelocytic cells</cell_type> and cooperates with all-trans retinoic acid to induce maturation of a <cell_line>retinoid-resistant promyelocytic cell line</cell_line> . |
788 | The PML gene is fused to the retinoic acid receptor alpha gene ( RAR alpha ) in the acute promyelocytic leukemia ( APL ) 15 ; 17 translocation . | The <dna>PML gene</dna> is fused to the <dna>retinoic acid receptor alpha gene</dna> ( <dna>RAR alpha</dna> ) in the acute promyelocytic leukemia ( APL ) 15 ; 17 translocation . |
789 | PML is expressed in diverse tissues and cell lines and localized in the nucleus with a typical speckled pattern . | <protein>PML</protein> is expressed in diverse tissues and cell lines and localized in the nucleus with a typical speckled pattern . |
790 | In the bone marrow , it is preferentially expressed in myeloid cells . | In the bone marrow , it is preferentially expressed in <cell_type>myeloid cells</cell_type> . |
791 | PML appears to be transcriptionally regulated by class I and II interferons , which raises the possibility that interferons modulate the function and growth and differentiation potential of normal myeloid cells and precursors by activating PML -dependent pathways . | <protein>PML</protein> appears to be transcriptionally regulated by <protein>class I and II interferons</protein> , which raises the possibility that interferons modulate the function and growth and differentiation potential of normal <cell_type>myeloid cells</cell_type> and precursors by activating <protein>PML</protein> -dependent pathways . |
792 | Similarly , interferons could act on APL cells , alone or in combination with all-trans retinoic acid ( RA ) , especially if the PML/RAR alpha fusion transcript that results from the t ( 15 ; 17 ) is induced by interferon . | Similarly , interferons could act on <cell_type>APL cells</cell_type> , alone or in combination with all-trans retinoic acid ( RA ) , especially if the <rna>PML/RAR alpha fusion transcript</rna> that results from the <dna>t ( 15 ; 17 )</dna> is induced by <protein>interferon</protein> . |
793 | We report here that PML is expressed at low levels or not expressed in normal circulating human monocytes , lymphocytes , and polymorphonucleate cells , but is markedly induced by interferon ; that PML and PML/RAR alpha expression is augmented by interferon in the NB4 APL cell line , which carries the t ( 15 ; 17 ) , and in APL blasts from patients ; that interferon inhibits growth and survival of NB4 APL cells in cooperation with RA ; that interferons alone have minimal maturation effect on NB4 cells ; and , finally , that interferon gamma , but not alpha or beta , induces maturation and growth suppression of NB4 cells with de novo retinoid resistance , and partially restores RA response . | We report here that <protein>PML</protein> is expressed at low levels or not expressed in normal circulating <cell_type>human monocytes</cell_type> , <cell_type>lymphocytes</cell_type> , and <cell_type>polymorphonucleate cells</cell_type> , but is markedly induced by <protein>interferon</protein> ; that <protein>PML</protein> and <protein>PML/RAR alpha</protein> expression is augmented by <protein>interferon</protein> in the <cell_line>NB4 APL cell line</cell_line> , which carries the <dna>t ( 15 ; 17 )</dna> , and in <cell_type>APL blasts</cell_type> from patients ; that <protein>interferon</protein> inhibits growth and survival of NB4 <cell_type>APL cells</cell_type> in cooperation with RA ; that interferons alone have minimal maturation effect on <cell_line>NB4 cells</cell_line> ; and , finally , that <protein>interferon gamma , but not alpha or beta</protein> , induces maturation and growth suppression of <cell_line>NB4 cells</cell_line> with de novo retinoid resistance , and partially restores RA response . |
794 | Effects of Ara-C on neutral sphingomyelinase and mitogen- and stress- activated protein kinases in T-lymphocyte cell lines . | Effects of Ara-C on <protein>neutral sphingomyelinase</protein> and <protein>mitogen- and stress- activated protein kinases</protein> in <cell_line>T-lymphocyte cell lines</cell_line> . |
795 | Neutral sphingomyelinase ( SMase ) can be activated by extracellular signals to produce ceramide , which may affect mitogen-activated protein kinase ( MAPK ) activities . | <protein>Neutral sphingomyelinase</protein> ( <protein>SMase</protein> ) can be activated by extracellular signals to produce ceramide , which may affect <protein>mitogen-activated protein kinase</protein> ( <protein>MAPK</protein> ) activities . |
796 | Neutral SMase activity was assessed in membranes from Jurkat , a human T-cell line , and EL4 , a murine T-cell line . | Neutral <protein>SMase</protein> activity was assessed in membranes from <cell_line>Jurkat</cell_line> , a <cell_line>human T-cell line</cell_line> , and <cell_line>EL4</cell_line> , a <cell_line>murine T-cell line</cell_line> . |
797 | Ara-C activated SMase with 10 minutes in both Jurkat and EL4 cells , while phorbol ester ( PMA ) had no effect . | Ara-C activated <protein>SMase</protein> with 10 minutes in both Jurkat and <cell_line>EL4 cells</cell_line> , while phorbol ester ( PMA ) had no effect . |
798 | PMA , but not Ara-C or ceramides , activated ERK MAPKS , in Jurkat and EL4 . | PMA , but not Ara-C or ceramides , activated <protein>ERK MAPKS</protein> , in <cell_line>Jurkat</cell_line> and <cell_line>EL4</cell_line> . |
799 | PMA acted synergistically with ionomycin to activate JNK MAPKs in Jurkat and EL4 within 10 minutes . | PMA acted synergistically with ionomycin to activate <protein>JNK MAPKs</protein> in <cell_line>Jurkat</cell_line> and <cell_line>EL4</cell_line> within 10 minutes . |
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