Linked Life Data

7774645

Source:http://linkedlifedata.com/resource/pubmed/id/7774645

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-7-13
pubmed:abstractText
Using the CD4+ human T cell clone P28, we demonstrated that the HIV-1 glycoprotein gp120 inhibited CD3-induced inositol trisphosphate production, calcium influx and T cell proliferation. Additionally, gp120 was shown to dissociate the tyrosine kinase p56lck from CD4 in CEM cells, with a concommittant inhibition of CD4-linked kinase activity. We have addressed the question whether disruption of CD4/p56lck or CD4/CD3-T cell receptor interactions, or both, could account for the inhibitory effect of gp120 in P28 cells. By comparing the effects of various anti-CD4 monoclonal antibodies (mAb) with those of gp120, we show that gp120 and IOT4a modulate CD4 expression, and decrease CD4-associated p56lck and CD4-linked kinase activity at the plasma membrane. In contrast, OKT4A and OKT4 anti-CD4 mAb have no inhibitory effect. Interestingly, gp120 also inhibits CD3-induced Lck activation and cellular tyrosine phosphorylation, particularly of phosphoinositide-specific phospholipase C-gamma-1. Kinetic experiments reveal that the inhibitory effect of gp120 on CD3-induced tyrosine phosphorylation appears as early as 30 min, but culminate when CD4-p56lck complexes disappear from the cell surface after 4 h. These results suggest that a negative signal is triggered by gp120 that results, after a few hours, in down-modulation of CD4-p56lck complexes and the impairment of CD3 signaling. Supporting this hypothesis, gp120 inhibits CD3-linked kinase activity as shown by the inhibition of the phosphorylation of CD3 chains, leading to the inhibition of subsequent signal transduction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1417-25
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7774645-Antibodies, Monoclonal, pubmed-meshheading:7774645-Antigens, CD3, pubmed-meshheading:7774645-Antigens, CD4, pubmed-meshheading:7774645-Clone Cells, pubmed-meshheading:7774645-HIV Antibodies, pubmed-meshheading:7774645-HIV Envelope Protein gp120, pubmed-meshheading:7774645-HIV-1, pubmed-meshheading:7774645-Humans, pubmed-meshheading:7774645-Kinetics, pubmed-meshheading:7774645-Lymphocyte Activation, pubmed-meshheading:7774645-Lymphocyte Specific Protein Tyrosine Kinase p56(lck), pubmed-meshheading:7774645-Phosphoproteins, pubmed-meshheading:7774645-Phosphorylation, pubmed-meshheading:7774645-Protein Processing, Post-Translational, pubmed-meshheading:7774645-Proto-Oncogene Proteins, pubmed-meshheading:7774645-Receptor-CD3 Complex, Antigen, T-Cell, pubmed-meshheading:7774645-Signal Transduction
pubmed:year
1995
pubmed:articleTitle
HIV-1 glycoprotein gp120 disrupts CD4-p56lck/CD3-T cell receptor interactions and inhibits CD3 signaling.
pubmed:affiliation
Laboratoire d'Immunologie Cellulaire et Tissulaire, CNRS URA 625, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't