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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1987-7-22
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pubmed:abstractText |
Of fundamental importance in understanding the events involved in T cell activation is the identification and characterization of the relevant cell surface molecules. Antigen-induced stimulation and subsequent activation of the T cell are initiated through interactions with the T cell antigen receptor. Several lines of evidence have demonstrated the intimate association between the T cell antigen receptor and T3, thus forming the so-called T3-T cell receptor complex. First, in immunoprecipitates with either anti-T3 monoclonal antibodies, or with anti-T cell receptor antibodies, five polypeptide chains have been detected. These are two disulfide bridged variable glycoproteins (alpha and beta chains) and three invariable structures the T3-gamma, delta, and epsilon chains with molecular weights of 25, 20, and 20 kdaltons, respectively. Second, mutants of a T leukemic cell line which were selected for the loss of the T3 complex from their surface by treatment with an anti-T3 antibody and complement concomitantly lost expression of the clonotypic heterodimer. Third, monoclonal antibodies directed at either the T cell receptor alpha and beta chains or at the T3 chains affect T cell functions in an identical fashion. Thus, we see that the complex formed between the T cell receptor and the T3 molecules is functionally as well as structurally central to the immune response. The structure, biosynthesis, and regulation of gene expression of the T3-T cell receptor complex will be discussed. An attempt will be made to relate the structural information to the function of the T3-T cell receptor complex.
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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, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell
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pubmed:status |
MEDLINE
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pubmed:issn |
1040-8401
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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 |
131-67
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2953555-Animals,
pubmed-meshheading:2953555-Antigens, CD3,
pubmed-meshheading:2953555-Antigens, Surface,
pubmed-meshheading:2953555-Cell Differentiation,
pubmed-meshheading:2953555-Cytotoxicity, Immunologic,
pubmed-meshheading:2953555-Humans,
pubmed-meshheading:2953555-Lymphocyte Activation,
pubmed-meshheading:2953555-Macromolecular Substances,
pubmed-meshheading:2953555-Membrane Proteins,
pubmed-meshheading:2953555-Protein Kinase C,
pubmed-meshheading:2953555-Receptors, Antigen, T-Cell,
pubmed-meshheading:2953555-T-Lymphocytes
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pubmed:year |
1987
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pubmed:articleTitle |
A review of the structure and function of the T-cell receptor-T3 complex.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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