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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1997-12-16
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pubmed:abstractText |
It has been previously demonstrated that the occupancy of CD4 molecules by the HIV-1 envelope glycoprotein gp120 results in marked inhibition of T cell receptor-CD3 complex (TCR/CD3) activation-induced IL-2 secretion. To elucidate the mechanism of inhibitory effects of gp160 on T cell signaling, we have investigated the intracellular biochemical events and biological output in response to anti-CD3 mAb activation of purified peripheral blood CD4+ T cells from healthy donors with and without prior exposure to HIV-1 gp160. Pretreatment with gp160 resulted in marked inhibition of tyrosine phosphorylation of p59(fyn), PLC-gamma1, ras activation, and TNF-alpha secretion in anti-CD3 mAb activated CD4+ T cells, and a subset of CD4+ cells underwent activation-induced cell death. The data presented here provide insight into the mechanism by which the interaction of HIV-1 envelope glycoproteins with CD4 molecules may alter TCR/CD3-activation-induced signal transduction resulting in anergy and apoptosis with consequent functional deficiency of CD4+ T cells.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp160,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0090-1229
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1997 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
195-201
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9344703-Antigens, CD3,
pubmed-meshheading:9344703-Antigens, CD95,
pubmed-meshheading:9344703-Apoptosis,
pubmed-meshheading:9344703-CD4-Positive T-Lymphocytes,
pubmed-meshheading:9344703-Gene Expression Regulation,
pubmed-meshheading:9344703-Genes, ras,
pubmed-meshheading:9344703-HIV Envelope Protein gp120,
pubmed-meshheading:9344703-HIV Envelope Protein gp160,
pubmed-meshheading:9344703-HIV-1,
pubmed-meshheading:9344703-Humans,
pubmed-meshheading:9344703-Interleukin-2,
pubmed-meshheading:9344703-Lymphocyte Activation,
pubmed-meshheading:9344703-Phosphorylation,
pubmed-meshheading:9344703-Protein-Tyrosine Kinases,
pubmed-meshheading:9344703-Receptors, Antigen, T-Cell,
pubmed-meshheading:9344703-Signal Transduction,
pubmed-meshheading:9344703-Tumor Necrosis Factor-alpha
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pubmed:year |
1997
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pubmed:articleTitle |
Signals transduced through the CD4 molecule interfere with TCR/CD3-mediated ras activation leading to T cell anergy/apoptosis.
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pubmed:affiliation |
Department of Pediatrics, North Shore University Hospital-New York University School of Medicine, Manhasset, New York 11030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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