Oleate-induced translocation of protein kinase C to hepatic microsomal membranes

Biochem Biophys Res Commun. 1989 May 15;160(3):1243-9. doi: 10.1016/s0006-291x(89)80137-8.

Abstract

The incubation of rat liver homogenates in the presence of oleate induces the translocation of protein kinase C from the cytosol to the endoplasmic reticulum membranes. The half-maximal effect was obtained at 0.3 mM oleate. The redistribution of this enzyme induced by oleate was also obtained with purified protein kinase C and hepatic microsomal membranes. This effect seems to be mediated by long-chain fatty acids since translocation was not obtained with esterified derivatives.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Animals
  • Arachidonic Acid
  • Arachidonic Acids / pharmacology
  • Biological Transport / drug effects
  • Brain / enzymology
  • Calcium / pharmacology
  • Fatty Acids / pharmacology
  • Intracellular Membranes / enzymology
  • Isoenzymes / metabolism
  • Isoquinolines / pharmacology
  • Leupeptins / pharmacology
  • Microsomes, Liver / enzymology*
  • Oleic Acid
  • Oleic Acids / pharmacology*
  • Phorbol 12,13-Dibutyrate / pharmacology
  • Phosphatidate Phosphatase / metabolism
  • Piperazines / pharmacology
  • Protein Kinase C / metabolism*
  • Rats
  • Spermine / pharmacology

Substances

  • Arachidonic Acids
  • Fatty Acids
  • Isoenzymes
  • Isoquinolines
  • Leupeptins
  • Oleic Acids
  • Piperazines
  • Arachidonic Acid
  • Spermine
  • Oleic Acid
  • Phorbol 12,13-Dibutyrate
  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Protein Kinase C
  • Phosphatidate Phosphatase
  • leupeptin
  • Calcium