Direct activation of purified protein kinase C by unsaturated fatty acids (oleate and arachidonate) in the absence of phospholipids and Ca2+

Kentaro Murakami*, Aryeh Routtenberg

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

241 Scopus citations

Abstract

Unsaturated fatty acids (oleic acid and arachidonic acid) activate purified protein kinase C independently of phospholipid and Ca2+. Oleic acid activation of protein kinase C is as effective as phosphatidylserine and Ca2+. Ka, values for oleic acid and arachidonic acid are 50 and 53 μM, respectively. In contrast to the cis fatty acids, a trans form (elaidic acid) or a saturated fatty acid (stearic acid) has little or no effect on protein kinase C activation. If cis fatty acid liberation is physiologically important, this suggests that another mechanism may exist for protein kinase C activation, in addition to phospholipase C/phosphatidylinositol turnover signaling, possibly via the liberation of cis fatty acids by the Ca2+-dependent phospholipase A2 system.

Original languageEnglish (US)
Pages (from-to)189-193
Number of pages5
JournalFEBS Letters
Volume192
Issue number2
DOIs
StatePublished - Nov 18 1985

Keywords

  • Phospholipase A
  • Protein kinase C
  • Unsaturated fatty acid

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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