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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1993-2-4
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pubmed:abstractText |
Engagement of the TCR by specific antigen results in activation of a tyrosine kinase pathway. A candidate for the kinase responsible for the rapid tyrosine phosphorylation detected with T cell activation is p60fyn, a member of the src kinase family. In an earlier study [Samelson et al. (1990) Proc. Natl Acad. Sci. USA 87:4358] this enzyme was co-immunoprecipitated with the TCR from T cells solubilized in digitonin. In that study a sensitive in vitro kinase assay was used to detect the associated p60fyn. It was subsequently found that the reproducibility of the interaction depended on lot-to-lot variations in digitonin. To eliminate the possibility that the association of antigen receptor and kinase is an artifact of solubilization with ill-defined digitonin preparations, a cross-linking protocol was developed to stabilize the interaction between the TCR and p60fyn. T cells were permeabilized with tetanolysin and proteins were cross-linked with the water soluble chemical cross-linker, 3,3' dithiobis(sulfosuccinimidylpropionate). These experiments allowed the confirmation of the interaction between the TCR, p60fyn, and several additional proteins. The cross-linking studies also enabled the mapping of the interaction of p60fyn and associated proteins to the TCR zeta-chain. This technique should have a general use in stabilizing interactions between other receptors and molecules required for intracellular signaling.
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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/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Digitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Fyn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Specific Protein...,
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
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:geneSymbol |
fyn,
src
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1211-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1472474-Animals,
pubmed-meshheading:1472474-Cross-Linking Reagents,
pubmed-meshheading:1472474-Digitonin,
pubmed-meshheading:1472474-Immunoblotting,
pubmed-meshheading:1472474-Lymphocyte Specific Protein Tyrosine Kinase p56(lck),
pubmed-meshheading:1472474-Mice,
pubmed-meshheading:1472474-Protein Binding,
pubmed-meshheading:1472474-Protein-Tyrosine Kinases,
pubmed-meshheading:1472474-Proto-Oncogene Proteins,
pubmed-meshheading:1472474-Proto-Oncogene Proteins c-fyn,
pubmed-meshheading:1472474-Receptors, Antigen, T-Cell,
pubmed-meshheading:1472474-Reproducibility of Results,
pubmed-meshheading:1472474-T-Lymphocytes
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pubmed:year |
1992
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pubmed:articleTitle |
Characterization of the T cell antigen receptor--p60fyn protein tyrosine kinase association by chemical cross-linking.
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pubmed:affiliation |
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20982.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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