rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
|
pubmed:dateCreated |
1990-6-7
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pubmed:abstractText |
T cell receptor-CD3 complex (TCR-CD3)-mediated signal transduction was analyzed in HPB-ALL and Jurkat T cell lines. Both cell lines express high levels of TCR-CD3 complex on the cell surface, but provide different model systems for TCR-CD3 signaling in T cells. Jurkat responds with both inositol phosphate generation and intracellular Ca2+ mobilization after triggering of TCR-CD3, whereas TCR-CD3 triggering of HPB-ALL induces Ca2+ mobilization without detectable inositol phosphate generation. By employing a permeabilized cell system, we show that the HPB-ALL line expressed normal levels of Ca2(+)-induced phospholipase C activity. However, the TCR-CD3 on this cell line seems to be uncoupled from phospholipase C activation. In agreement with this result we also show, by analysis of protein kinase C-dependent phosphorylation of three distinct substrates, that TCR-CD3 in HPB-ALL is apparently uncoupled from protein kinase C activation. These findings may have implications for understanding signal-transducing pathways in T cells at various stages of differentiation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD2,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-1767
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
144
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3651-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1970588-Antigens, CD,
pubmed-meshheading:1970588-Antigens, CD2,
pubmed-meshheading:1970588-Antigens, CD3,
pubmed-meshheading:1970588-Antigens, Differentiation, T-Lymphocyte,
pubmed-meshheading:1970588-Calcium,
pubmed-meshheading:1970588-Cell Differentiation,
pubmed-meshheading:1970588-Enzyme Activation,
pubmed-meshheading:1970588-Humans,
pubmed-meshheading:1970588-Inositol Phosphates,
pubmed-meshheading:1970588-Protein Kinase C,
pubmed-meshheading:1970588-Receptors, Antigen, T-Cell,
pubmed-meshheading:1970588-Receptors, Immunologic,
pubmed-meshheading:1970588-Recombinant Proteins,
pubmed-meshheading:1970588-Signal Transduction,
pubmed-meshheading:1970588-T-Lymphocytes,
pubmed-meshheading:1970588-Tumor Cells, Cultured,
pubmed-meshheading:1970588-Type C Phospholipases
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pubmed:year |
1990
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pubmed:articleTitle |
Signal transduction through the T cell receptor-CD3 complex. Evidence for heterogeneity in receptor coupling.
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pubmed:affiliation |
Unit of Applied Cell and Molecular Biology, University of Umeå, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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