automated-analytics/bionlp2004 · Datasets at AI快站

100

We have examined the role of cell surface molecules in these responses .

101

Normal T lymphocytes whose surface expression of CD3 was depleted showed impaired UV-induced tyrosine phosphorylation and Ca2+ signals .

Normal <cell_type>T lymphocytes</cell_type> whose surface expression of <protein>CD3</protein> was depleted showed impaired UV-induced tyrosine phosphorylation and Ca2+ signals .

102

Similarly , Jurkat T cell lines deficient in CD3 or CD45 expression also gave impaired UV responses .

Similarly , <cell_line>Jurkat T cell lines</cell_line> deficient in CD3 or CD45 expression also gave impaired UV responses .

103

However , all these cell types still gave strong Ca2+ and tyrosine phosphorylation responses to H2O2 .

104

The T cell tyrosine kinase ZAP-70 was found to be highly responsive to UV and H2O2 treatment .

The T cell tyrosine <protein>kinase ZAP-70</protein> was found to be highly responsive to UV and H2O2 treatment .

105

ZAP-70 responsiveness to UV required expression of both CD3 and CD45 , whereas only CD3 was required for the response to H2O2 .

<protein>ZAP-70</protein> responsiveness to UV required expression of both <protein>CD3</protein> and <protein>CD45</protein> , whereas only <protein>CD3</protein> was required for the response to H2O2 .

106

UV-induced activation of NF-kappa B was blocked by CD3 depletion , indicating the importance of such cell surface molecules in biological responses to UV .

UV-induced activation of <protein>NF-kappa B</protein> was blocked by <protein>CD3</protein> depletion , indicating the importance of such <protein>cell surface molecules</protein> in biological responses to UV .

107

In nonlymphoid cells , the epidermal growth factor receptor displayed increased tyrosine phosphorylation within seconds of UV irradiation .

In <cell_type>nonlymphoid cells</cell_type> , the <protein>epidermal growth factor receptor</protein> displayed increased tyrosine phosphorylation within seconds of UV irradiation .

108

These results suggest that UV-induced signal transduction is mediated via cell surface receptors that normally respond to biological stimulation , whereas H2O2 is able to partially bypass this requirement .

These results suggest that UV-induced signal transduction is mediated via <protein>cell surface receptors</protein> that normally respond to biological stimulation , whereas H2O2 is able to partially bypass this requirement .

109

Inhibition of the differentiation of human myeloid cell lines by redox changes induced through glutathione depletion .

Inhibition of the differentiation of <cell_line>human myeloid cell lines</cell_line> by redox changes induced through glutathione depletion .

110

We have investigated the effect of redox changes in vivo on the differentiation of two human myeloid cell lines , HL-60 and KG-1 .

We have investigated the effect of redox changes in vivo on the differentiation of two <cell_line>human myeloid cell lines</cell_line> , <cell_line>HL-60</cell_line> and <cell_line>KG-1</cell_line> .

111

The glutathione-depleting agent diethyl maleate ( DEM ) prevented the development of differentiated features in response to phorbol esters , including adherence of the cells to plastic surfaces and repression of the myeloperoxidase and CD34 genes .

The glutathione-depleting agent diethyl maleate ( DEM ) prevented the development of differentiated features in response to phorbol esters , including adherence of the cells to plastic surfaces and repression of the <dna>myeloperoxidase and CD34 genes</dna> .

112

Moreover , DEM abolished phorbol 12-myristate 13-acetate-induced activation of the transcription factors AP-1 and Egr-1 , suggesting that inhibition of differentiation may be due , at least in part , to redox modifications of these proteins .

Moreover , DEM abolished phorbol 12-myristate 13-acetate-induced activation of the <protein>transcription factors</protein> <protein>AP-1</protein> and <protein>Egr-1</protein> , suggesting that inhibition of differentiation may be due , at least in part , to redox modifications of these <protein>proteins</protein> .

113

Lipopolysaccharide induction of tissue factor gene expression in monocytic cells is mediated by binding of c-Rel/p65 heterodimers to a kappa B-like site .

Lipopolysaccharide induction of <dna>tissue factor gene</dna> expression in <cell_type>monocytic cells</cell_type> is mediated by binding of <protein>c-Rel/p65 heterodimers</protein> to a <dna>kappa B-like site</dna> .

114

Exposure of monocytic cells to bacterial lipopolysaccharide ( LPS ) activates the NF-kappa B/Rel family of proteins and leads to the rapid induction of inflammatory gene products , including tissue factor ( TF ) .

Exposure of <cell_type>monocytic cells</cell_type> to bacterial lipopolysaccharide ( LPS ) activates the <protein>NF-kappa B/Rel family</protein> of proteins and leads to the rapid induction of <protein>inflammatory gene products</protein> , including <protein>tissue factor</protein> ( <protein>TF</protein> ) .

115

TF is the primary cellular initiator of the coagulation protease cascades .

<protein>TF</protein> is the primary cellular initiator of the <protein>coagulation protease</protein> cascades .

116

Here we report the characterization of a nuclear complex from human monocytic cells that bound to a kappa B-like site , 5'-CGGAGTTTCC-3 ' , in the 5'-flanking region of the human TF gene .

Here we report the characterization of a <protein>nuclear complex</protein> from human <cell_type>monocytic cells</cell_type> that bound to a <dna>kappa B-like site</dna> , <dna>5'-CGGAGTTTCC-3 '</dna> , in the <dna>5'-flanking region</dna> of the <dna>human TF gene</dna> .

117

This nuclear complex was activated by LPS with kinetics that preceded induction of the TF gene .

This <protein>nuclear complex</protein> was activated by LPS with kinetics that preceded induction of the <dna>TF gene</dna> .

118

In vitro binding studies demonstrated that the TF site bound translated c-Rel and p65 homodimers but not p50/p65 heterodimers or p50 homodimers .

In vitro binding studies demonstrated that the <dna>TF site</dna> bound translated <protein>c-Rel and p65 homodimers</protein> but not <protein>p50/p65 heterodimers</protein> or <protein>p50 homodimers</protein> .

119

Base-pair substitutions in the TF site indicated that the presence of a cytosine at position 1 precluded binding of NF-kappa B .

Base-pair substitutions in the <dna>TF site</dna> indicated that the presence of a cytosine at <protein>position 1</protein> precluded binding of <protein>NF-kappa B</protein> .

120

In fact , under low-ionic-strength conditions , the TF complex did not migrate with translated p50/p65 dimers but instead comigrated with c-Rel/p65 dimers .

In fact , under low-ionic-strength conditions , the <protein>TF complex</protein> did not migrate with translated <protein>p50/p65 dimers</protein> but instead comigrated with <protein>c-Rel/p65 dimers</protein> .

121

Antibodies against the NF-kappa B and Rel proteins and UV cross-linking studies revealed the presence of c-Rel and p65 and the absence of p50 in the TF complex and further showed that c-Rel/p65 heterodimers selectively bound to the TF kappa B-like site .

Antibodies against the <protein>NF-kappa B</protein> and Rel proteins and UV cross-linking studies revealed the presence of <protein>c-Rel</protein> and p65 and the absence of <protein>p50</protein> in the <protein>TF complex</protein> and further showed that <protein>c-Rel/p65 heterodimers</protein> selectively bound to the <dna>TF kappa B-like site</dna> .

122

Functional studies indicated that the TF site conferred LPS inducibility on a heterologous promoter and was transactivated by c-Rel or p65 .

Functional studies indicated that the <dna>TF site</dna> conferred LPS inducibility on a <dna>heterologous promoter</dna> and was transactivated by <protein>c-Rel</protein> or p65 .

123

Taken together , our results demonstrated that binding of c-Rel/p65 heterodimers to a novel kappa B-like site mediated LPS induction of TF gene expression in monocytic cells .

Taken together , our results demonstrated that binding of <protein>c-Rel/p65 heterodimers</protein> to a novel <dna>kappa B-like site</dna> mediated LPS induction of <protein>TF</protein> gene expression in <cell_type>monocytic cells</cell_type> .

124

Inhibition of T cell activation by the extracellular matrix protein tenascin .

Inhibition of T cell activation by the <protein>extracellular matrix protein</protein> <protein>tenascin</protein> .

125

Tenascin ( TN ) is an extracellular matrix protein that is expressed widely in the fetus and sparingly in the adult , but reappears at high levels in certain areas of tissue insult such as tumor matrices and sites of wound healing .

<protein>Tenascin</protein> ( <protein>TN</protein> ) is an <protein>extracellular matrix protein</protein> that is expressed widely in the fetus and sparingly in the adult , but reappears at high levels in certain areas of tissue insult such as tumor matrices and sites of wound healing .

126

We show here that soluble TN inhibits proliferation of human T cells in response to alpha CD3 Ab co-immobilized with the extracellular matrix protein fibronectin ( FN ) .

We show here that soluble <protein>TN</protein> inhibits proliferation of <cell_type>human T cells</cell_type> in response to <protein>alpha CD3 Ab</protein> co-immobilized with the <protein>extracellular matrix protein</protein> <protein>fibronectin</protein> ( <protein>FN</protein> ) .

127

TN also inhibits proliferation driven by alpha CD3/IL-2 or by phorbol ester/IL-2 , and it prevents high level induction of IL-2R .

<protein>TN</protein> also inhibits proliferation driven by <protein>alpha CD3/IL-2</protein> or by <protein>phorbol ester/IL-2 ,</protein> and it prevents high level induction of <protein>IL-2R</protein> .

128

The presence of TN in culture medium does not detectably alter the pattern of tyrosine phosphorylation resulting from T cell triggering with alpha CD3 , but at later time points prevents the appearance of functional NF-AT1 transcription factor complexes in T cell nuclear extracts .

The presence of <protein>TN</protein> in culture medium does not detectably alter the pattern of tyrosine phosphorylation resulting from T cell triggering with <protein>alpha CD3</protein> , but at later time points prevents the appearance of functional <protein>NF-AT1 transcription factor complexes</protein> in T cell nuclear extracts .

129

These findings are consistent with the postulated role for TN as a natural antagonist to FN action , and suggest that T cell responses occurring at tissue sites in which TN is expressed could be influenced by its presence .

These findings are consistent with the postulated role for <protein>TN</protein> as a natural antagonist to <protein>FN</protein> action , and suggest that T cell responses occurring at tissue sites in which <protein>TN</protein> is expressed could be influenced by its presence .

130

Human immunodeficiency virus type 1 Nef protein down-regulates transcription factors NF-kappa B and AP-1 in human T cells in vitro after T-cell receptor stimulation .

Human immunodeficiency virus type 1 Nef protein down-regulates <protein>transcription factors</protein> <protein>NF-kappa B</protein> and <protein>AP-1</protein> in <cell_type>human T cells</cell_type> in vitro after T-cell receptor stimulation .

131

Human immunodeficiency virus type 1 ( HIV-1 ) negative factor ( Nef ) has been shown to down-regulate the transcription factors NF-kappa B and AP-1 in vitro .

Human immunodeficiency virus type 1 ( HIV-1 ) <protein>negative factor</protein> ( <protein>Nef</protein> ) has been shown to down-regulate the <protein>transcription factors</protein> <protein>NF-kappa B</protein> and <protein>AP-1</protein> in vitro .

132

To define the mechanism of action of the Nef protein , the signal transduction pathways which may be affected in T cells by constitutive expression of the nef gene were examined .

To define the mechanism of action of the <protein>Nef</protein> protein , the signal transduction pathways which may be affected in <cell_type>T cells</cell_type> by constitutive expression of the nef gene were examined .

133

Stimulation of T cells with tumor necrosis factor , interleukin-1 , or lipopolysaccharide resulted in the recruitment of transcriptional factors to a similar level whether or not the cells expressed the nef gene .

Stimulation of <cell_type>T cells</cell_type> with tumor necrosis factor , interleukin-1 , or lipopolysaccharide resulted in the recruitment of transcriptional factors to a similar level whether or not the cells expressed the nef gene .

134

On the other hand , stimulation of T cells by mitogens or antibodies to the T-cell receptor ( TCR ) - CD3 complex resulted in the down-regulation of transcriptional factors NF-kappa B and AP-1 in cells expressing the nef gene compared with cells not expressing the nef gene .

On the other hand , stimulation of <cell_type>T cells</cell_type> by mitogens or antibodies to the T-cell receptor ( TCR ) - <protein>CD3</protein> complex resulted in the down-regulation of transcriptional factors <protein>NF-kappa B</protein> and <protein>AP-1</protein> in cells expressing the nef gene compared with cells not expressing the nef gene .

135

Because the Nef protein does not affect the surface expression of the CD3 -TCR complex , we conclude that the Nef protein down-regulates the transcriptional factors NF-kappa B and AP-1 in T cells in vitro through an effect on the TCR-dependent signal transduction pathway .

Because the <protein>Nef</protein> protein does not affect the surface expression of the <protein>CD3</protein> -TCR complex , we conclude that the <protein>Nef</protein> protein down-regulates the transcriptional factors <protein>NF-kappa B</protein> and <protein>AP-1</protein> in <cell_type>T cells</cell_type> in vitro through an effect on the TCR-dependent signal transduction pathway .

136

Effects of alpha-lipoic acid and dihydrolipoic acid on expression of proto-oncogene c-fos .

Effects of alpha-lipoic acid and dihydrolipoic acid on expression of <dna>proto-oncogene c-fos</dna> .

137

The transcription factor AP-1 is an important human mediator of the cellular response to serum , growth factors , and phorbol esters such as 12-O-tetradecanoyl-phorbol-13 acetate ( TPA ) .

The <protein>transcription factor</protein> <protein>AP-1</protein> is an important human mediator of the cellular response to serum , <protein>growth factors</protein> , and phorbol esters such as 12-O-tetradecanoyl-phorbol-13 acetate ( TPA ) .

138

The AP-1 complex consists of distinct protein heterodimers encoded by the proto-oncogene c-fos and c-jun mRNA whose gene expression can be induced by TPA , cyclic AMP and growth factors .

The <protein>AP-1</protein> complex consists of distinct <protein>protein heterodimers</protein> encoded by the <dna>proto-oncogene c-fos</dna> and <rna>c-jun mRNA</rna> whose gene expression can be induced by TPA , cyclic AMP and <protein>growth factors</protein> .

139

Recent findings suggest an involvement of reactive oxygen species in the pathway of TPA and protein kinase C leading to expression of c-fos and c-jun mRNA .

Recent findings suggest an involvement of reactive oxygen species in the pathway of TPA and <protein>protein kinase C</protein> leading to expression of <rna>c-fos and c-jun mRNA</rna> .

140

To investigate the role of reactive oxygen species we studied the effects of alpha-lipoic acid and dihydrolipoic acid ( natural thiol antioxidants ) on the expression of c-fos mRNA in human Jurkat T cells .

To investigate the role of reactive oxygen species we studied the effects of alpha-lipoic acid and dihydrolipoic acid ( natural thiol antioxidants ) on the expression of <rna>c-fos mRNA</rna> in <cell_line>human Jurkat T cells</cell_line> .

141

When cells were preincubated with dihydrolipoic acid ( 0.2 mM ) the expression of c-fos mRNA was suppressed at 30 min after stimulation of TPA ( 0.5 microM ) whereas in the case of preincubation of alpha-lipoic acid ( 0.2 microM ) , the expression was enhanced at 30 min .

When cells were preincubated with dihydrolipoic acid ( 0.2 mM ) the expression of <rna>c-fos mRNA</rna> was suppressed at 30 min after stimulation of TPA ( 0.5 microM ) whereas in the case of preincubation of alpha-lipoic acid ( 0.2 microM ) , the expression was enhanced at 30 min .

142

These studies support the idea that superoxide anion radical plays a role in the expression of c-fos mRNA .

These studies support the idea that superoxide anion radical plays a role in the expression of <rna>c-fos mRNA</rna> .

143

Appraisal of potential therapeutic index of antioxidants on the basis of their in vitro effects on HIV replication in monocytes and interleukin 2 -induced lymphocyte proliferation .

Appraisal of potential therapeutic index of antioxidants on the basis of their in vitro effects on HIV replication in <cell_type>monocytes</cell_type> and <protein>interleukin 2</protein> -induced lymphocyte proliferation .

144

Antioxidant molecules have been suggested to be of therapeutic value in the treatment of HIV-infected patients .

145

To evaluate this possibility , we examined in vitro the effects of two types of antioxidant molecules in terms of inhibition of HIV replication in monocytes , one of the main reservoirs of HIV , and also in terms of modulation of the immune competence as measured by PBMC proliferation .

To evaluate this possibility , we examined in vitro the effects of two types of antioxidant molecules in terms of inhibition of HIV replication in <cell_type>monocytes</cell_type> , one of the main reservoirs of HIV , and also in terms of modulation of the immune competence as measured by <cell_type>PBMC</cell_type> proliferation .

146

We tested the effects of BHA , a phenolic , lipid-soluble , chain-breaking antioxidant , and NAC , a known glutathione precursor with some direct free-radical scavenging properties as well , on the regulation of HIV-1 expression in latently infected U1 cells and in productively and chronically infected U937 cells .

We tested the effects of BHA , a phenolic , lipid-soluble , chain-breaking antioxidant , and NAC , a known glutathione precursor with some direct free-radical scavenging properties as well , on the regulation of HIV-1 expression in latently infected <cell_line>U1 cells</cell_line> and in productively and chronically infected <cell_line>U937 cells</cell_line> .

147

Both antioxidants inhibited TNF -or PMA-induced NF-kappa B activity in U1 cells , as well as the sustained NF-kappa B activity permanently induced by the virus itself in chronically HIV-infected U937 cells .

Both antioxidants inhibited <protein>TNF</protein> -or PMA-induced <protein>NF-kappa B</protein> activity in <cell_line>U1 cells</cell_line> , as well as the sustained <protein>NF-kappa B</protein> activity permanently induced by the virus itself in chronically HIV-infected <cell_line>U937 cells</cell_line> .

148

This resulted in only a partial inhibition of TNF -or PMA- induced HIV replication in U1 cells , and no detectable effect on HIV replication in chronically infected U937 cells .

This resulted in only a partial inhibition of <protein>TNF</protein> -or PMA- induced HIV replication in <cell_line>U1 cells</cell_line> , and no detectable effect on HIV replication in <cell_line>chronically infected U937 cells</cell_line> .

149

This may be the first limitation to potential antiviral effects of antioxidant therapies .

150

Another limitation is that antioxidant concentrations high enough to block NK-kappa B activation were shown to have a suppressive effect on immune functions in vitro , because NAC and BHA blocked IL-2-induced PBMC proliferation .

Another limitation is that antioxidant concentrations high enough to block <protein>NK-kappa B</protein> activation were shown to have a suppressive effect on immune functions in vitro , because NAC and BHA blocked <cell_type>IL-2-induced PBMC</cell_type> proliferation .

151

These data warrant prudence in the design of antioxidant-based therapies aimed at suppressing HIV replication .

152

Isolation and characterization of gelatinase granules from human neutrophils .

Isolation and characterization of gelatinase granules from <cell_type>human neutrophils</cell_type> .

153

We recently confirmed the existence of gelatinase granules as a subpopulation of peroxidase-negative granules by double-labeling immunogold electron microscopy on intact cells and by subcellular fractionation .

154

Further characterization of gelatinase granules has been hampered by poor separation of specific and gelatinase granules on both two-layer Percoll gradients and sucrose gradients .

155

We have developed a three-layer Percoll density gradient that allows separation of the different granules and vesicles from human neutrophils ; in particular , it allows separation of specific and gelatinase granules .

We have developed a three-layer Percoll density gradient that allows separation of the different granules and vesicles from <cell_type>human neutrophils</cell_type> ; in particular , it allows separation of specific and gelatinase granules .

156

This allows us to characterize these two granule populations with regard to their content of membrane proteins , which become incorporated into the plasma membrane during exocytosis .

This allows us to characterize these two granule populations with regard to their content of <protein>membrane proteins</protein> , which become incorporated into the plasma membrane during exocytosis .

157

We found that gelatinase granules , defined as peroxidase-negative granules containing gelatinase but lacking lactoferrin , contain 50 % of total cell gelatinase , with the remaining residing in specific granules .

We found that gelatinase granules , defined as peroxidase-negative granules containing <protein>gelatinase</protein> but lacking <protein>lactoferrin</protein> , contain 50 % of total cell <protein>gelatinase</protein> , with the remaining residing in specific granules .

158

Furthermore , we found that 20 % to 25 % of both the adhesion protein Mac-1 and the NADPH-oxidase component cytochrome b558 is localized in gelatinase granules .

Furthermore , we found that 20 % to 25 % of both the <protein>adhesion protein Mac-1</protein> and the <protein>NADPH-oxidase component cytochrome</protein> <protein>b558</protein> is localized in <protein>gelatinase</protein> granules .

159

Although no qualitative difference was observed between specific granules and gelatinase granules with respect to cytochrome b558 and Mac-1 , stimulation of the neutrophil with FMLP resulted in a selective mobilization of the least dense peroxidase-negative granules , ie , gelatinase granules , which , in concert with secretory vesicles , furnish the plasma membrane with Mac-1 and cytochrome b558 .

Although no qualitative difference was observed between specific granules and <protein>gelatinase</protein> granules with respect to <protein>cytochrome b558</protein> and <protein>Mac-1</protein> , stimulation of the <cell_type>neutrophil</cell_type> with <protein>FMLP</protein> resulted in a selective mobilization of the least dense peroxidase-negative granules , ie , <protein>gelatinase</protein> granules , which , in concert with secretory vesicles , furnish the plasma membrane with <protein>Mac-1</protein> and <protein>cytochrome b558</protein> .

160

This shows that gelatinase granules are functionally important relative to specific granules in mediating early inflammatory responses .

This shows that <protein>gelatinase</protein> granules are functionally important relative to specific granules in mediating early inflammatory responses .

161

Regulation of interleukin-2 receptor alpha chain expression and nuclear factor.kappa B activation by protein kinase C in T lymphocytes .

Regulation of <protein>interleukin-2 receptor alpha chain</protein> expression and <protein>nuclear factor.kappa B</protein> activation by <protein>protein kinase C</protein> in <cell_type>T lymphocytes</cell_type> .

162

Autocrine role of tumor necrosis factor alpha .

Autocrine role of <protein>tumor necrosis factor alpha</protein> .

163

The regulation of interleukin-2 receptor alpha chain ( IL-2R alpha ) expression and nuclear factor ( NF ) activation by protein kinase C ( PKC ) in resting T cells , has been studied .

The regulation of <protein>interleukin-2 receptor alpha chain</protein> ( <protein>IL-2R alpha</protein> ) expression and <protein>nuclear factor</protein> ( NF ) activation by <protein>protein kinase C</protein> ( <protein>PKC</protein> ) in <cell_type>resting T cells</cell_type> , has been studied .

164

Treatment of human resting T cells with phorbol esters strongly induced the expression of IL-2R alpha and the activation of NF.kappa B .

Treatment of human <cell_type>resting T cells</cell_type> with phorbol esters strongly induced the expression of <protein>IL-2R alpha</protein> and the activation of <protein>NF.kappa B</protein> .

165

This activation was due to the translocation of p65 and c-Rel NF.kappa B proteins from cytoplasmic stores to the nucleus , where they bound the kappa B sequence of the IL-2R alpha promoter either as p50.p65 or as p50.c-Rel heterodimers .

This activation was due to the translocation of <protein>p65</protein> and <protein>c-Rel</protein> <protein>NF.kappa B</protein> proteins from cytoplasmic stores to the nucleus , where they bound the <dna>kappa B sequence</dna> of the <dna>IL-2R alpha promoter</dna> either as <protein>p50.p65</protein> or as <protein>p50.c-Rel</protein> heterodimers .

166

Interestingly , all of those events were largely indirect and mediated by endogenously secreted tumor necrosis factor alpha ( TNF alpha ) , as they were strongly inhibited by a neutralizing anti-TNF alpha monoclonal antibody .

Interestingly , all of those events were largely indirect and mediated by endogenously secreted <protein>tumor necrosis factor alpha</protein> ( <protein>TNF alpha</protein> ) , as they were strongly inhibited by a <protein>neutralizing anti-TNF alpha monoclonal antibody</protein> .

167

Furthermore , cyclosporin A , which blocked TNF alpha production induced by PKC , strongly inhibited IL-2R alpha and NF.kappa B activation .

Furthermore , cyclosporin A , which blocked <protein>TNF alpha</protein> production induced by <protein>PKC</protein> , strongly inhibited <protein>IL-2R alpha</protein> and <protein>NF.kappa B</protein> activation .

168

The addition of either TNF alpha or IL-2 partially recovered cyclosporin A-induced IL-2R alpha inhibition , but only TNF alpha completely recovered NF.kappa B activation .

The addition of either <protein>TNF alpha</protein> or <protein>IL-2</protein> partially recovered cyclosporin A-induced <protein>IL-2R alpha</protein> inhibition , but only <protein>TNF alpha</protein> completely recovered <protein>NF.kappa B</protein> activation .

169

Those results indicate that , in resting T cells , PKC activation has only a triggering role , whereas the endogenously secreted TNF alpha plays an essential role in the quantitative control of the expression of IL-2R alpha chain or NF.kappa B activation .

Those results indicate that , in <cell_type>resting T cells</cell_type> , <protein>PKC</protein> activation has only a triggering role , whereas the endogenously secreted <protein>TNF alpha</protein> plays an essential role in the quantitative control of the expression of <protein>IL-2R alpha</protein> chain or <protein>NF.kappa B</protein> activation .

170

Superantigens activate HIV-1 gene expression in monocytic cells .

<protein>Superantigens</protein> activate HIV-1 gene expression in <cell_type>monocytic cells</cell_type> .

171

Binding of superantigens to MHC class II molecules results in transduction of biochemical signals leading to cellular activation and gene expression .

Binding of superantigens to <protein>MHC class II molecules</protein> results in transduction of biochemical signals leading to cellular activation and gene expression .

172

We demonstrate that the staphylococcal superantigens toxic shock syndrome toxin-1 ( TSST-1 ) and staphylococcal enterotoxin A ( SEA ) activate HIV-1-LTR -driven transcription of chloramphenicol acetyl transferase in the human monocytic cell line THP-1 .

We demonstrate that the <protein>staphylococcal superantigens</protein> <protein>toxic shock syndrome toxin-1</protein> ( <protein>TSST-1</protein> ) and <protein>staphylococcal enterotoxin A</protein> ( <protein>SEA</protein> ) activate <dna>HIV-1-LTR</dna> -driven transcription of <protein>chloramphenicol acetyl transferase</protein> in the <cell_line>human monocytic cell line</cell_line> <cell_line>THP-1</cell_line> .

173

Induction of HIV-1- LTR -driven transcription in THP-1 cells by superantigens was associated with the induction of nuclear factor-kappa B DNA-binding activity .

Induction of HIV-1- <dna>LTR</dna> -driven transcription in <cell_line>THP-1 cells</cell_line> by <protein>superantigens</protein> was associated with the induction of <protein>nuclear factor-kappa B</protein> DNA-binding activity .

174

Superantigens also increased viral protein secretion from the granulocyte-macrophage colony-stimulating factor-pretreated chronically infected human monocytic cell line U1 .

<protein>Superantigens</protein> also increased viral protein secretion from the <cell_line>granulocyte-macrophage colony-stimulating factor-pretreated chronically infected human monocytic cell line U1</cell_line> .

175

Induction of HIV-1 gene expression in monocytic cells by superantigens occurred via tumor necrosis factor-alpha-dependent and -independent mechanisms .

Induction of HIV-1 gene expression in <cell_type>monocytic cells</cell_type> by <protein>superantigens</protein> occurred via tumor necrosis factor-alpha-dependent and -independent mechanisms .

176

Our results suggest that superantigens and other MHC class II ligands may activate HIV-1 gene expression in monocytes/macrophages .

Our results suggest that <protein>superantigens</protein> and other <protein>MHC class II ligands</protein> may activate HIV-1 gene expression in <cell_type>monocytes/macrophages</cell_type> .

177

Mitogen activation of human peripheral T lymphocytes induces the formation of new cyclic AMP response element-binding protein nuclear complexes .

Mitogen activation of <cell_type>human peripheral T lymphocytes</cell_type> induces the formation of new <protein>cyclic AMP response element-binding protein nuclear complexes</protein> .

178

A large body of evidence indicates that experimental agents which raise cellular cAMP levels inhibit T cell growth and division .

179

By contrast , many studies have reported that mitogen activation of T cells increases cAMP levels , implying a positive physiological role for cAMP in the activation process .

By contrast , many studies have reported that <protein>mitogen</protein> activation of <cell_type>T cells</cell_type> increases cAMP levels , implying a positive physiological role for cAMP in the activation process .

180

In the present study we demonstrate that mitogen activation of human peripheral T lymphocytes induces nuclear factors that form complexes with cyclic AMP response element-binding protein ( CREB ) .

In the present study we demonstrate that <protein>mitogen</protein> activation of <cell_type>human peripheral T lymphocytes</cell_type> induces nuclear factors that form complexes with <protein>cyclic AMP response element-binding protein</protein> ( <protein>CREB</protein> ) .

181

Four complexes are identified by the electrophoretic mobility shift assay , two of which are induced by mitogen activation .

Four complexes are identified by the electrophoretic mobility shift assay , two of which are induced by <protein>mitogen</protein> activation .

182

All four complexes contain CREB and are bound to the cAMP response element ( CRE ) core sequence ( TGACGTCA ) , as indicated by antibody and oligonucleotide competition experiments .

All four complexes contain <protein>CREB</protein> and are bound to the <dna>cAMP response element ( CRE ) core sequence</dna> ( TGACGTCA ) , as indicated by antibody and oligonucleotide competition experiments .

183

Binding of the four complexes to CRE is prevented by dephosphorylation of nuclear extracts and is restored by rephosphorylation with cAMP-dependent protein kinase or endogenous kinases .

Binding of the four complexes to <dna>CRE</dna> is prevented by dephosphorylation of nuclear extracts and is restored by rephosphorylation with <protein>cAMP-dependent protein kinase</protein> or <protein>endogenous kinases</protein> .

184

Similar complexes are detected in nuclear extracts of Jurkat cells .

Similar complexes are detected in nuclear extracts of <cell_line>Jurkat cells</cell_line> .

185

Mitogen induction of the electrophoretic mobility shift assay complexes is not accounted for by protein phosphorylation or by induction of CREB .

Mitogen induction of the <protein>electrophoretic mobility shift assay complexes</protein> is not accounted for by protein phosphorylation or by induction of <protein>CREB</protein> .

186

Rather , the data indicate that mitogen increases the levels of a nuclear factor ( s ) that dimerizes with CREB .

Rather , the data indicate that mitogen increases the levels of a nuclear factor ( s ) that dimerizes with <protein>CREB</protein> .

187

Induction of new CREB complexes implies a physiological role for cAMP in mitogen activation of T lymphocytes .

Induction of new <protein>CREB complexes</protein> implies a physiological role for cAMP in <protein>mitogen</protein> activation of <cell_type>T lymphocytes</cell_type> .

188

Alpha-tocopherol inhibits agonist-induced monocytic cell adhesion to cultured human endothelial cells .

Alpha-tocopherol inhibits agonist-induced monocytic cell adhesion to <cell_line>cultured human endothelial cells</cell_line> .

189

Antioxidants have been proposed to be anti-atherosclerotic agents ; however , the mechanisms underlying their beneficial effects are poorly understood .

190

We have examined the effect of alpha-tocopherol ( alpha-tcp ) on one cellular event in atherosclerotic plaque development , monocyte adhesion to stimulated endothelial cells ( ECs ) .

We have examined the effect of alpha-tocopherol ( alpha-tcp ) on one cellular event in atherosclerotic plaque development , monocyte adhesion to <cell_type>stimulated endothelial cells</cell_type> ( <cell_type>ECs</cell_type> ) .

191

Human umbilical vein ECs were pretreated with alpha-tcp before stimulation with known agonists of monocyte adhesion : IL-1 ( 10 ng/ml ) , LPS ( 10 ng/ml ) , thrombin ( 30 U/ml ) , or PMA ( 10 nM ) .

Human umbilical vein <cell_type>ECs</cell_type> were pretreated with alpha-tcp before stimulation with known agonists of monocyte adhesion : <protein>IL-1</protein> ( 10 ng/ml ) , LPS ( 10 ng/ml ) , <protein>thrombin</protein> ( 30 U/ml ) , or PMA ( 10 nM ) .

192

Agonist-induced monocytic cell adhesion , but not basal adhesion , was inhibited in a time- and concentration-dependent manner by alpha-tcp .

193

The IC50 of alpha-tcp on an IL-1 -induced response was 45 microM .

The IC50 of alpha-tcp on an <protein>IL-1</protein> -induced response was 45 microM .

194

The inhibition correlated with a decrease in steady state levels of E-selectin mRNA and cell surface expression of E-selectin which is consistent with the ability of a monoclonal antibody to E-selectin to inhibit monocytic cell adhesion in this system .

The inhibition correlated with a decrease in steady state levels of <rna>E-selectin mRNA</rna> and cell surface expression of <protein>E-selectin</protein> which is consistent with the ability of a <protein>monoclonal antibody</protein> to <protein>E-selectin</protein> to inhibit monocytic cell adhesion in this system .

195

Probucol ( 50 microM ) and N-acetylcysteine ( 20 mM ) also inhibited agonist-induced monocytic cell adhesion ; whereas , several other antioxidants had no significant effect .

196

Protein kinase C ( PKC ) does not appear to play a role in the alpha-tcp effect since no suppression of phosphorylation of PKC substrates was observed .

<protein>Protein kinase C</protein> ( <protein>PKC</protein> ) does not appear to play a role in the alpha-tcp effect since no suppression of phosphorylation of <protein>PKC</protein> substrates was observed .

197

Activation of the transcription factor NF-kappa B is reported to be necessary but not sufficient for E-selectin expression in EC .

Activation of the <protein>transcription factor</protein> <protein>NF-kappa B</protein> is reported to be necessary but not sufficient for <protein>E-selectin</protein> expression in <cell_line>EC</cell_line> .

198

Electrophoretic mobility shift assays failed to show an alpha-tcp-induced decrease in activation of this transcription factor after cytokine stimulation .

Electrophoretic mobility shift assays failed to show an alpha-tcp-induced decrease in activation of this <protein>transcription factor</protein> after <protein>cytokine</protein> stimulation .

199

It has been hypothesized that alpha-tcp acts as an anti-atherosclerotic molecule by inhibiting generation of oxidized LDL -- a putative triggering molecule in the atherosclerotic process .