Amiloride sensitive activation of S6 kinase by angiotensin II in cultured vascular smooth muscle cells

Biochem Biophys Res Commun. 1988 Feb 29;151(1):583-9. doi: 10.1016/0006-291x(88)90634-1.

Abstract

Angiotensin II was shown to activate S6-kinase in cultured vascular smooth muscle cells (VSMC) in a dose- (10(-9)-10(-6) M) and time-dependent manner. Pretreatment of quiescent cells with 12-O-Tetradecanoylphorbol-13-acetate had no effect on the activation levels of the kinase at the hormone levels used. However, stimulation of S6-kinase activity by angiotensin II was markedly inhibited by the inclusion of amiloride hydrochloride in serum-free medium during activation procedures. Angiotensin was not mitogenic for VSMC at even the highest doses used (10(-6) M). These findings support the notion that raised intracellular pH results in the activation of protein synthesis in quiescent cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amiloride / pharmacology*
  • Angiotensin II / pharmacology*
  • Animals
  • Cell Division / drug effects
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Enzyme Activation / drug effects
  • Hydrogen-Ion Concentration
  • Kinetics
  • Muscle, Smooth, Vascular / cytology
  • Muscle, Smooth, Vascular / drug effects
  • Muscle, Smooth, Vascular / enzymology*
  • Protein Biosynthesis
  • Protein Kinases / metabolism*
  • Rats
  • Rats, Inbred SHR
  • Ribosomal Protein S6 Kinases
  • Tetradecanoylphorbol Acetate / pharmacology

Substances

  • Angiotensin II
  • Amiloride
  • Protein Kinases
  • Ribosomal Protein S6 Kinases
  • Tetradecanoylphorbol Acetate