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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1995-11-6
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pubmed:abstractText |
Thy-1 molecules, which lack a transmembrane domain, can nonetheless induce T cell activation; it has thus been suggested that a separate transmembrane molecule associated with Thy-1 is required for signal transduction. We have previously characterized a transmembrane protein with an Mr of 100,000 (p100), which is non-covalently bound to two glycosyl-phosphatidylinositol (GPI)-linked molecules, Thy-1 and ThB. p100 is selectively expressed on the T cell surface and divides peripheral CD4 cells into two subpopulations. This differential expression on CD4 cells allowed us to investigate the role of p100 in signal transduction through Thy-1 molecules. Here we report that only p100+ CD4 cells proliferate and release cytokines in response to cross-linkage of Thy-1, although both p100+ and p100- CD4 cells strongly express Thy-1 on their surfaces. Control stimulation by anti-CD3 antibodies or concanavalin A induces identical thymidine uptake by the two CD4 cell populations. Interestingly, these two populations of CD4 cells had different cytokine release profiles after activation through CD3: only p100+ CD4 cells released high amounts of IL-2 and IFN-gamma, whereas both populations released IL-4. p100 expression correlates with the induction of homotypic aggregation of T cells after Thy-1 triggering. p100 is associated with kinase activity (fyn and lck), and phosphorylated proteins of 90, 59, 57 and 33 kDa co-precipitate with Thy-1 only in p100+ CD4 cells. Altogether, these data suggest that p100 is involved in signal transduction through Thy-1. p100 expression by activated CD4 cells in vivo may be relevant to the proposed function of Thy-1 as an accessory signaling molecule in cell activation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Thy-1,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
607-16
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7547688-Animals,
pubmed-meshheading:7547688-Antigens, Surface,
pubmed-meshheading:7547688-Antigens, Thy-1,
pubmed-meshheading:7547688-CD4-Positive T-Lymphocytes,
pubmed-meshheading:7547688-Cell Aggregation,
pubmed-meshheading:7547688-Cytokines,
pubmed-meshheading:7547688-Female,
pubmed-meshheading:7547688-Lymphocyte Activation,
pubmed-meshheading:7547688-Male,
pubmed-meshheading:7547688-Membrane Proteins,
pubmed-meshheading:7547688-Mice,
pubmed-meshheading:7547688-Mice, Inbred BALB C,
pubmed-meshheading:7547688-Mice, Inbred C3H,
pubmed-meshheading:7547688-Mice, Inbred C57BL,
pubmed-meshheading:7547688-Mice, Inbred NOD,
pubmed-meshheading:7547688-Protein Kinases,
pubmed-meshheading:7547688-T-Lymphocyte Subsets
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pubmed:year |
1995
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pubmed:articleTitle |
T cell activation through Thy-1 is associated with the expression of a surface protein (p100) on a subset of CD4 cells.
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pubmed:affiliation |
Institut National de la Santé et de la Recherche Médicale, Hôpital Necker, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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