NDLI: Association of p21ras with phosphatidylinositol 3-kinase.

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Association of p21ras with phosphatidylinositol 3-kinase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sjölander, A. Huber, B. E. Yamamoto, K. Lapetina, E. G.
Description	Author Affiliation: Sjölander A ( Division of Cell Biology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.);
Abstract	In mammalian cells, ras genes code for 21-kDa GTP-binding proteins. Increased expression and mutations in specific amino acids have been closely linked to alterations of normal cell morphology, growth, and differentiation and, in particular, to neoplastic transformation. The signal transduction induced by these p21ras proteins is largely unknown; however, the signaling pathways of several growth factors have been reported to involve phosphatidylinositol (PtdIns) 3-kinase. In the present study of a Ha-ras-transformed epithelial cell line, we demonstrated increased PtdIns 3-kinase activity in anti-phosphotyrosine and anti-receptor (insulin and hybrid insulin-like growth factor I) immunoprecipitates of cells that had been stimulated with insulin or insulin-like growth factor I. The PtdIns 3-kinase activity was also immunoprecipitated in these experiments by the anti-Ras monoclonal antibody Y13-259. The specificity of this association with p21ras was ascertained by the neutralizing effect of the antigen peptide and the absence of PtdIns 3-kinase activity in Y13-259 immunoprecipitates from cells in which the ras gene was turned off. These data indicate that PtdIns 3-kinase activity is an important step in the cascade of reactions in p21ras signal transduction, suggesting that the alterations of the cytoskeleton and growth in ras-transformed cells could be mediated by PtdIns 3-kinase activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Phosphotransferases Metabolism Proto-Oncogene Proteins P21(ras) 1-Phosphatidylinositol 4-Kinase Animals Cells, Cultured In Vitro Techniques Insulin Pharmacology Insulin-Like Growth Factor I Liver Cytology Phosphatidylinositols Phosphotyrosine Signal Transduction Tyrosine Analogs & Derivatives Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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