Stimulation by a tumor-promoting phorbol ester of acetyl-CoA carboxylase activity in isolated rat hepatocytes

Biochem Biophys Res Commun. 1987 Jan 15;142(1):135-40. doi: 10.1016/0006-291x(87)90461-x.

Abstract

Acetyl-CoA carboxylase (EC 6.4.1.2) in hepatocytes from meal-fed rats was activated by phorbol myristate acetate (PMA) in a time- and concentration-dependent fashion. This activation can account for the PMA-induced stimulation of de novo fatty acid synthesis. Purified rat-liver acetyl-CoA carboxylase was found to be phosphorylated and activated by protein kinase C, thus providing a possible mechanism for the metabolic action of PMA in intact hepatocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyl-CoA Carboxylase / metabolism*
  • Allosteric Regulation
  • Animals
  • Dose-Response Relationship, Drug
  • Enzyme Activation / drug effects
  • Fatty Acids / biosynthesis
  • Hydrocarbons, Chlorinated
  • Lactates / metabolism
  • Ligases / metabolism*
  • Liver / enzymology*
  • Phosphorylation
  • Propionates / metabolism
  • Protein Kinase C / metabolism
  • Rats
  • Tetradecanoylphorbol Acetate / pharmacology*

Substances

  • Fatty Acids
  • Hydrocarbons, Chlorinated
  • Lactates
  • Propionates
  • 2-chloropropionic acid
  • Protein Kinase C
  • Ligases
  • Acetyl-CoA Carboxylase
  • Tetradecanoylphorbol Acetate