Activation of protein kinase C by cis- and trans-fatty acids and its potentiation by diacylglycerol

Biochem Biophys Res Commun. 1988 Jul 15;154(1):20-6. doi: 10.1016/0006-291x(88)90643-2.

Abstract

Both cis- and trans-unsaturated but not saturated fatty acids activated protein kinase C purified to apparent homogeneity from rat brain. Fatty-acid-induced enzyme activation was not more than additive with that by phospholipids and was potentiated by diacylglycerol. Recently, we demonstrated that cis- and trans-unsaturated fatty acids induced platelet aggregation and phosphorylation of specific proteins. Both events were potentiated by a cell-permeable diacylglycerol [(1987) Biochem. Biophys. Res. Commun. 149, 762-768]. Thus, trans-unsaturated fatty acids may provide useful experimental tools for the study of protein kinase C activation in vitro and in vivo. Our results suggest that fatty acids and diacylglycerol may synergistically be involved in hormonal stimulation of protein kinase C, as certain hormonal stimuli cause release of diacylglycerol and fatty acids from phospholipids by parallel activation of phospholipases C and A2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain / enzymology*
  • Calcium / pharmacology
  • Diglycerides / pharmacology*
  • Enzyme Activation
  • Fatty Acids, Unsaturated / pharmacology*
  • Glycerides / pharmacology*
  • Kinetics
  • Protein Kinase C / isolation & purification
  • Protein Kinase C / metabolism*
  • Rats
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Diglycerides
  • Fatty Acids, Unsaturated
  • Glycerides
  • Protein Kinase C
  • Calcium