Diacylglycerol activation of protein kinase C is modulated by long-chain acyl-CoA

Biochem Biophys Res Commun. 1988 May 16;152(3):987-92. doi: 10.1016/s0006-291x(88)80381-4.


The activity of rat brain protein kinase C, measured in the presence of diacylglycerol, phosphatidylserine and Ca+2, was found to be greatly increased by micromolar amounts of long chain acyl-CoAs, using two different assay systems (lipids added as sonicated dispersion or as mixed micelles with Triton X-100). The potentiation phenomenon required the presence of both diacylglycerol and phosphatidylserine; it was observed at low and saturating concentrations of these effectors, and it was inhibited at high, non physiological Ca+2 concentrations. Under similar conditions, fatty acids alone or coenzyme A were ineffective. The data strongly suggest that acyl-CoAs at the intracellular concentration levels, are important in the modulation of protein kinase C, after activation of the enzyme by the phospholipase C/phosphatidylinositol pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / pharmacology*
  • Animals
  • Brain / enzymology
  • Calcium / pharmacology
  • Diglycerides / pharmacology*
  • Drug Synergism
  • Enzyme Activation
  • Glycerides / pharmacology*
  • Octoxynol
  • Phosphatidylserines / pharmacology
  • Polyethylene Glycols
  • Protein Kinase C / metabolism*
  • Rats
  • Structure-Activity Relationship


  • Acyl Coenzyme A
  • Diglycerides
  • Glycerides
  • Phosphatidylserines
  • Polyethylene Glycols
  • Octoxynol
  • Protein Kinase C
  • Calcium