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

Miguel Bronfman, M. Nelly Morales, Ariel Orellana

Research output: Contribution to journalArticlepeer-review

72 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)987-992
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume152
Issue number3
DOIs
Publication statusPublished - 16 May 1988

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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