Insulin but not phorbol ester treatment increases phosphorylation of vinculin by protein kinase C in BC3H-1 myocytes

FEBS Lett. 1987 Apr 6;214(1):122-6. doi: 10.1016/0014-5793(87)80025-x.

Abstract

Insulin was found to increase protein kinase C activity in BC3H-1 myocytes as determined by in vitro phosphorylation of both a lysine-rich histone fraction (histone III-S) and vinculin. TPA treatment for 20 min or 18 h provoked an apparent loss of histone-directed but not vinculin-directed phosphorylation by cytosolic C-kinase. Thus, chronic TPA-induced 'desensitization' or 'depletion' of cellular protein kinase C is more apparent than real, and is not a valid means for evaluating the role of C-kinase in hormone action.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cells, Cultured
  • Histones / metabolism
  • Insulin / pharmacology*
  • Muscle Proteins / metabolism*
  • Muscles / drug effects
  • Muscles / metabolism
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Tetradecanoylphorbol Acetate / pharmacology
  • Vinculin

Substances

  • Histones
  • Insulin
  • Muscle Proteins
  • Vinculin
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate