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

Miguel Bronfman, M. Nelly Morales, Ariel Orellana

Resultado de la investigación: Contribución a una revistaArtículo

72 Citas (Scopus)

Resumen

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.

Idioma originalInglés
Páginas (desde-hasta)987-992
Número de páginas6
PublicaciónBiochemical and Biophysical Research Communications
Volumen152
N.º3
DOI
EstadoPublicada - 16 may 1988

Áreas temáticas de ASJC Scopus

  • Bioquímica
  • Biofísica
  • Biología molecular

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