Pharmacological evidence for system-dependent involvement of protein kinase C isoenzymes in phorbol ester-suppressed gap junctional communication

Exp Cell Res. 2001 Aug 15;268(2):150-61. doi: 10.1006/excr.2001.5275.

Abstract

Several phorbol esters are potent activators of protein kinase C. They down-regulate gap junctional intercellular communication and induce phosphorylation of connexin43, but the sensitivity and extent of responses vary much between systems. We asked whether the total protein kinase C enzyme activity or the protein kinase C isoenzyme constitution was of importance for such variations. Some fibroblastic culture systems were compared. It was concluded that the total protein kinase C enzyme activity did not determine the sensitivity to phorbol esters. Furthermore, the use of isotype-specific inhibitors of protein kinase C indicated that protein kinase C alpha, delta, and epsilon may be involved to different extents in different fibroblastic systems in the response to phorbol esters.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbazoles / pharmacology
  • Cell Communication / drug effects
  • Cells, Cultured
  • Connexin 43 / metabolism
  • Dose-Response Relationship, Drug
  • Gap Junctions / drug effects*
  • Indoles / pharmacology
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / metabolism
  • Maleimides / pharmacology
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism*
  • Protein Kinase C-delta
  • Protein Kinase C-epsilon
  • Tetradecanoylphorbol Acetate / pharmacology*

Substances

  • Carbazoles
  • Connexin 43
  • Indoles
  • Isoenzymes
  • Maleimides
  • Go 6976
  • protein kinase D
  • Protein Kinase C
  • Protein Kinase C-delta
  • Protein Kinase C-epsilon
  • bisindolylmaleimide I
  • Tetradecanoylphorbol Acetate