Activation of protein kinase C by cis- and trans-octadecadienoic acids in intact human platelets and its potentiation by diacylglycerol

Biochem Biophys Res Commun. 1987 Dec 16;149(2):762-8. doi: 10.1016/0006-291x(87)90433-5.

Abstract

Octadecadienoic acids (linoleic acid and linolelaidic acid) and the diacylglycerol, 1-oleoyl-2-acetyl-rac-glycerol (OAG) concentration-dependently induced activation of gel-filtered human platelets, i.e. aggregation and phosphorylation of 20 kDa and 47 kDa peptides. In contrast, octadecenoic acids (oleic and elaidic acid) and octadecanoic (stearic) acid were inactive. Octadecadienoic acid-induced platelet activation was suppressed by the protein kinase C inhibitor, polymyxin B, but not by the cyclooxygenase inhibitor, indomethacin. OAG-induced activation was potentiated by octadecadienoic acids present at non-stimulatory concentrations. Our data suggest that octadecadienoic acids and diacylglycerol synergistically induce platelet activation via protein kinase C. Furthermore, linolelaidic acid may provide a useful experimental tool to study fatty acid regulation of protein kinase C in intact cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Platelets / enzymology*
  • Diglycerides / pharmacology*
  • Enzyme Activation / drug effects
  • Glycerides / pharmacology*
  • Humans
  • Phosphorylation
  • Platelet Aggregation / drug effects
  • Protein Kinase C / analysis*
  • Proteins / metabolism
  • Stearic Acids / pharmacology*

Substances

  • Diglycerides
  • Glycerides
  • Proteins
  • Stearic Acids
  • stearic acid
  • Protein Kinase C