Palmitoyl‐CoA and the acyl‐CoA thioester of the carcinogenic peroxisome‐proliferator ciprofibrate potentiate diacylglycerol‐activated protein kinase C by decreasing the phosphatidylserine requirement of the enzyme

Ariel ORELLANA, Perla C. HIDALGO, Maria N. MORALES, Diego MEZZANO, Miguel BRONFMAN

Resultado de la investigación: Contribución a una revistaArtículo

55 Citas (Scopus)

Resumen

To gain insight into the mechanism by which long‐chain acyl‐CoA thioesters potentiate diacylglycerol‐activated protein kinase C, the cofactor dependence of this activating effect was studied with purified rat brain enzyme and histone H1 as substrate. Using two different assay systems, palmitoyl‐CoA was found to decrease greatly the amount of phosphatidylserine required to activate the kinase. No relative changes were observed in the dependence of the enzyme for other cofactors (diacylglycerol, ATP, and Ca2+) in the presence of palmitoyl‐CoA. The potentiating effect of palmitoyl‐CoA and the decrease in phosphatidylserine requirement of the kinase was also demonstrated using the 47‐kDa protein of human platelets as substrate and platelet protein kinase C as source of enzyme. The acyl‐CoA thioester of the carcinogenic peroxisome‐proliferator ciprofibrate was also found to decrease the phosphatidylserine requirement of protein kinase C. The data suggest that acyl‐CoAs may play a role in the regulation of protein kinase C activity.

Idioma originalInglés
Páginas (desde-hasta)57-61
Número de páginas5
PublicaciónEuropean Journal of Biochemistry
Volumen190
N.º1
DOI
EstadoPublicada - 1990

    Huella digital

Áreas temáticas de ASJC Scopus

  • Bioquímica
  • Biología celular
  • Biología molecular

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