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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
37
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pubmed:dateCreated |
1995-10-12
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pubmed:abstractText |
Stimulation of the activity of protein kinase C by pretreatment of cells with phorbol esters was tested for its ability to inhibit signaling by four members of the insulin receptor family, including the human insulin and insulin-like growth factor-I receptors, the human insulin receptor-related receptor, and the Drosophila insulin receptor. Activation of overexpressed protein kinase C alpha resulted in a subsequent inhibition of the ligand-stimulated increase in antiphosphotyrosine-precipitable phosphatidylinositol 3-kinase mediated by the kinase domains of all four receptors. This inhibition varied from 97% for the insulin receptor-related receptor to 65% for the Drosophila insulin receptor. In addition, the activation of protein kinase C alpha inhibited the in situ ligand-stimulated increase in tyrosine phosphorylation of the GTPase-activating protein-associated p60 protein as well as Shc mediated by these receptors. The mechanism for this inhibition was further studied in the case of the insulin-like growth factor-I receptor. Although the in situ phosphorylation of insulin-receptor substrate-1 and p60 by this receptor was inhibited by prior stimulation of protein kinase C alpha, the in vitro tyrosine phosphorylation of these two substrates by this receptor was not decreased by prior stimulation of the protein kinase C alpha in the cells that served as a source of the substrates. Finally, the insulin-like growth factor-I-stimulated increase in cell proliferation was found to be inhibited by prior activation of protein kinase C alpha.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant |
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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/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/IRS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin Receptor Substrate Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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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 |
15
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21600-5
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7545165-Amino Acid Sequence,
pubmed-meshheading:7545165-Animals,
pubmed-meshheading:7545165-CHO Cells,
pubmed-meshheading:7545165-Cattle,
pubmed-meshheading:7545165-Cell Division,
pubmed-meshheading:7545165-Cricetinae,
pubmed-meshheading:7545165-Drosophila,
pubmed-meshheading:7545165-Enzyme Activation,
pubmed-meshheading:7545165-GTPase-Activating Proteins,
pubmed-meshheading:7545165-Humans,
pubmed-meshheading:7545165-Insulin Receptor Substrate Proteins,
pubmed-meshheading:7545165-Insulin Resistance,
pubmed-meshheading:7545165-Insulin-Like Growth Factor I,
pubmed-meshheading:7545165-Isoenzymes,
pubmed-meshheading:7545165-Kinetics,
pubmed-meshheading:7545165-Molecular Sequence Data,
pubmed-meshheading:7545165-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:7545165-Phosphoproteins,
pubmed-meshheading:7545165-Phosphorylation,
pubmed-meshheading:7545165-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:7545165-Phosphotyrosine,
pubmed-meshheading:7545165-Protein Kinase C,
pubmed-meshheading:7545165-Proteins,
pubmed-meshheading:7545165-Receptor, IGF Type 1,
pubmed-meshheading:7545165-Receptor, Insulin,
pubmed-meshheading:7545165-Recombinant Proteins,
pubmed-meshheading:7545165-Sequence Homology, Amino Acid,
pubmed-meshheading:7545165-Signal Transduction,
pubmed-meshheading:7545165-Tetradecanoylphorbol Acetate,
pubmed-meshheading:7545165-Transfection,
pubmed-meshheading:7545165-Tyrosine
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pubmed:year |
1995
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pubmed:articleTitle |
Activation of protein kinase C alpha inhibits signaling by members of the insulin receptor family.
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pubmed:affiliation |
Department of Molecular Pharmacology, Stanford University School of Medicine, California 94305, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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