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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
1994-10-20
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pubmed:abstractText |
We evaluated in Jurkat T cells the time-dependent responses of Fyn, Lck, Syk, and Zap following antibody-mediated cross-linking of the T cell antigen receptor. Our results show that the protein kinase activities of Fyn and Lck were activated within seconds of receptor cross-linking. Fyn activity, as measured by autophosphorylation and tyrosine phosphorylation of an exogenous substrate, was maximal 5 s to 1 min following receptor cross-linking. Lck was also found to be activated within 5 s of antigen receptor cross-linking but differed from Fyn in that Lck activity was elevated for at least 30 min. Syk and Zap protein kinase activities were found to peak between 5 and 10 min following receptor cross-linking, returning to approximately basal activity levels by 60 min. The protein kinase activities of both Syk and Zap were found to parallel their reactivity in immunoblotting experiments with anti-phosphotyrosine antibodies. Both Syk and Zap were found to associate with the tyrosine-phosphorylated zeta subunit of the T cell antigen receptor. These observations imply that T cell antigen receptor signal transduction involves the activation of multiple members of at least two different families of non-transmembrane protein tyrosine kinases.
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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/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/FYN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Specific Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fyn,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP-70 Protein-Tyrosine Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP70 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
269
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pubmed:geneSymbol |
Zap
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23642-7
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:7522230-Amino Acid Sequence,
pubmed-meshheading:7522230-Cell Line,
pubmed-meshheading:7522230-Enzyme Activation,
pubmed-meshheading:7522230-Enzyme Precursors,
pubmed-meshheading:7522230-Humans,
pubmed-meshheading:7522230-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:7522230-Lymphocyte Specific Protein Tyrosine Kinase p56(lck),
pubmed-meshheading:7522230-Molecular Sequence Data,
pubmed-meshheading:7522230-Phosphotyrosine,
pubmed-meshheading:7522230-Protein-Tyrosine Kinases,
pubmed-meshheading:7522230-Proto-Oncogene Proteins,
pubmed-meshheading:7522230-Proto-Oncogene Proteins c-fyn,
pubmed-meshheading:7522230-Receptors, Antigen, T-Cell,
pubmed-meshheading:7522230-Signal Transduction,
pubmed-meshheading:7522230-Tyrosine,
pubmed-meshheading:7522230-ZAP-70 Protein-Tyrosine Kinase
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pubmed:year |
1994
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pubmed:articleTitle |
Temporal regulation of non-transmembrane protein tyrosine kinase enzyme activity following T cell antigen receptor engagement.
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pubmed:affiliation |
Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey 08543.
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pubmed:publicationType |
Journal Article,
In Vitro
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