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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
1998-7-16
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pubmed:abstractText |
CD43, the most abundant membrane protein of T lymphocytes, is able to initiate signals that lead to Ca2+ mobilization and interleukin-2 production, yet the molecular events involved in signal transduction pathway of the CD43 molecule are only beginning to be understood. We have shown recently that cross-linking CD43 on the cell surface of human T lymphocytes with the anti-CD43 monoclonal antibody L10 leads to CD43-Fyn kinase interactions and to Fyn phosphorylation on tyrosine residues. This interaction seems to be mediated by the SH3 domain of Fyn and a proline-rich sequence located in the cytoplasmic domain of CD43. Here we show that CD43-specific activation of human T lymphocytes induced tyrosine phosphorylation of the adaptor protein Shc and of the guanine exchange factor Vav, as well as the formation of a macromolecular complex that comprises Shc, GRB2, and Vav. CD43 ligation resulted in enhanced formation of Vav.SLP-76 complexes and in the activation and nuclear translocation of ERK2. Cross-linking of the CD43 molecule in 3T3-CD43(+) cells induced luciferase activity from a construct under the control of the Fos serum responsive element. Altogether, these data suggest that the mitogen-activated protein kinase pathway is involved in CD43-dependent interleukin-2 gene expression.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD43,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Grb2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-vav,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Shc1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Spn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/UN1 sialoglycoprotein, human,
http://linkedlifedata.com/resource/pubmed/chemical/VAV1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Vav1 protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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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 |
5
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14218-24
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pubmed:dateRevised |
2011-9-7
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pubmed:meshHeading |
pubmed-meshheading:9603925-3T3 Cells,
pubmed-meshheading:9603925-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9603925-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:9603925-Animals,
pubmed-meshheading:9603925-Antigens, CD,
pubmed-meshheading:9603925-Antigens, CD43,
pubmed-meshheading:9603925-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9603925-Cross-Linking Reagents,
pubmed-meshheading:9603925-GRB2 Adaptor Protein,
pubmed-meshheading:9603925-Gene Expression Regulation,
pubmed-meshheading:9603925-Genes, Reporter,
pubmed-meshheading:9603925-Genes, fos,
pubmed-meshheading:9603925-Humans,
pubmed-meshheading:9603925-Interleukin-2,
pubmed-meshheading:9603925-Mice,
pubmed-meshheading:9603925-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:9603925-Oncogene Proteins,
pubmed-meshheading:9603925-Phosphorylation,
pubmed-meshheading:9603925-Proteins,
pubmed-meshheading:9603925-Proto-Oncogene Proteins c-vav,
pubmed-meshheading:9603925-Shc Signaling Adaptor Proteins,
pubmed-meshheading:9603925-Sialoglycoproteins,
pubmed-meshheading:9603925-Signal Transduction,
pubmed-meshheading:9603925-T-Lymphocytes,
pubmed-meshheading:9603925-Transfection,
pubmed-meshheading:9603925-Tyrosine
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pubmed:year |
1998
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pubmed:articleTitle |
T cell activation through the CD43 molecule leads to Vav tyrosine phosphorylation and mitogen-activated protein kinase pathway activation.
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pubmed:affiliation |
Instituto de Biotecnología/UNAM, APDO. Postal 510-3 Cuernavaca, Morelos, 62250, México.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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