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