Angiotensin II controls p21ras activity via pp60c-src

Bernhard Schieffer, William G. Paxton, Qing Chai, Mario B. Marrero, Kenneth E. Bernstein

Research output: Contribution to journalArticle

134 Scopus citations

Abstract

Angiotensin II is the major effector peptide of the renin-angiotensin system, and it exerts its physiologic functions via a G protein-coupled cell surface receptor called AT1. We found that in rat aortic smooth muscle cells, angiotensin II stimulated the formation of Ras-GTP, Ras-Raf-1 complex formation, and the tyrosine phosphorylation of two important Ras GTPase-activating proteins (GAPs), p120 Ras-GAP and p190 Rho-GAP. Electroporation of anti-pp60c-src antibody into cultured, adherent smooth muscle cells blocked the angiotensin II stimulation of Ras-GAP and Rho-GAP tyrosine phosphorylation. In contrast electroporation of antibodies against c-Yes or c-Fyn had no effect. Anti-pp60c-src antibody also blocked angiotensin II-stimulated Ras activation and Ras-Raf-1 complex formation. These data strongly suggest that a G protein-coupled receptor such as the AT1 receptor can activate the Ras protein cascade via the tyrosine kinase pp60c-src.

Original languageEnglish (US)
Pages (from-to)10329-10333
Number of pages5
JournalJournal of Biological Chemistry
Volume271
Issue number17
DOIs
StatePublished - Apr 26 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Schieffer, B., Paxton, W. G., Chai, Q., Marrero, M. B., & Bernstein, K. E. (1996). Angiotensin II controls p21ras activity via pp60c-src. Journal of Biological Chemistry, 271(17), 10329-10333. https://doi.org/10.1074/jbc.271.17.10329