| pubmed-article:1722393 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1722393 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
| pubmed-article:1722393 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:1722393 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:1722393 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1722393 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:1722393 | lifeskim:mentions | umls-concept:C0915518 | lld:lifeskim |
| pubmed-article:1722393 | pubmed:dateCreated | 1992-2-11 | lld:pubmed |
| pubmed-article:1722393 | pubmed:abstractText | Insulin causes a dramatic and rapid increase in phosphatidylinositol 3-kinase activity in the anti-phosphotyrosine immunoprecipitates of cells overexpressing the human insulin receptor. This enzyme may therefore be a mediator of insulin signal transduction [Endemann, Yonezawa & Roth (1990) J. Biol. Chem. 265, 396-400; Ruderman, Kapeller, White & Cantley (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 1411-1415]. At least two questions remain to be elucidated. Firstly, does the insulin receptor tyrosine kinase phosphorylate phosphatidylinositol 3-kinase directly, or does it phosphorylate a protein associated with the 3-kinase? Second, if the enzyme is a direct substrate for the insulin receptor tyrosine kinase, does tyrosine phosphorylation of phosphatidylinositol 3-kinase by the kinase alter the specific enzyme activity, or does the amount of the tyrosine-phosphorylated form of the phosphatidylinositol 3-kinase increase, with no change in the specific activity? We report here evidence that the 85 kDa subunit of highly purified phosphatidylinositol 3-kinase is phosphorylated on the tyrosine residue by the activated normal insulin receptor in vitro, but not by a mutant insulin receptor which lacks tyrosine kinase activity. We found that an increase in enzyme activity was detected in response to insulin not only in the anti-phosphotyrosine immunoprecipitates of the cytosol, but also in the cytosolic fraction before immunoprecipitation. In addition, we partially separated the tyrosine-phosphorylated form from the unphosphorylated form of the enzyme, by using a f.p.l.c. Mono Q column. The insulin-stimulated phosphatidylinositol 3-kinase activity was mainly detected in the fraction containing almost all of the tyrosine-phosphorylated form. This result suggests that tyrosine phosphorylation of phosphatidylinositol 3-kinase by the insulin receptor kinase may increase the specific activity of the former enzyme in vivo. | lld:pubmed |
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| pubmed-article:1722393 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1722393 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1722393 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1722393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1722393 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1722393 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1722393 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1722393 | pubmed:author | pubmed-author:HayashiHH | lld:pubmed |
| pubmed-article:1722393 | pubmed:author | pubmed-author:MiyajiSS | lld:pubmed |
| pubmed-article:1722393 | pubmed:author | pubmed-author:TakenawaTT | lld:pubmed |
| pubmed-article:1722393 | pubmed:author | pubmed-author:EbinaYY | lld:pubmed |
| pubmed-article:1722393 | pubmed:author | pubmed-author:ShibasakiFF | lld:pubmed |
| pubmed-article:1722393 | pubmed:author | pubmed-author:KanaiFF | lld:pubmed |
| pubmed-article:1722393 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1722393 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1722393 | pubmed:volume | 280 ( Pt 3) | lld:pubmed |
| pubmed-article:1722393 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1722393 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1722393 | pubmed:pagination | 769-75 | lld:pubmed |
| pubmed-article:1722393 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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