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pubmed-article:7726827pubmed:abstractTextWe investigated epidermal growth factor (EGF)-induced activation of 85-kDa/110-kDa phosphatidylinositol (PI)-3-kinase and 70-kDa S6 kinase in Chinese hamster ovary cells expressing the human EGF receptor. EGF-induced activation of p70 S6 kinase was comparable to that induced by insulin, whereas that of PI-3-kinase in anti-phosphotyrosine immunoprecipitates was very small compared with insulin. Wortmannin, a p85/p110 PI-3-kinase inhibitor, inhibited EGF-induced activation of p70 S6 kinase in a dose-dependent manner. Given that several proteins homologous to catalytic subunit of p85/p110 PI-3-kinase have been identified and that wortmannin inhibits distinct form of PI-3-kinase, the present results suggest that wortmannin-sensitive kinases that resemble catalytic subunit of p85/p110 PI-3-kinase may participate in the signaling pathway from EGF receptors to p70 S6 kinase.lld:pubmed
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pubmed-article:7726827pubmed:articleTitleEGF-induced activation of 70-kDa S6 kinase in CHO cells expressing human EGF receptors.lld:pubmed
pubmed-article:7726827pubmed:affiliationSecond Department of Internal Medicine, Kobe University School of Medicine, Japan.lld:pubmed
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pubmed-article:7726827pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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