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: Article

54 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 originalEnglish
Páginas (desde-hasta)57-61
Número de páginas5
PublicaciónEuropean Journal of Biochemistry
Volumen190
N.º1
DOI
EstadoPublished - 1990

Huella dactilar

Phosphatidylserines
Protein Kinase C
Enzymes
Platelets
Phosphotransferases
Diglycerides
Coenzymes
Substrates
Histones
Rats
Assays
Brain
Blood Platelets
Adenosine Triphosphate
ciprofibrate
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Citar esto

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title = "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",
abstract = "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.",
author = "Ariel ORELLANA and HIDALGO, {Perla C.} and MORALES, {Maria N.} and Diego MEZZANO and Miguel BRONFMAN",
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T1 - 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

AU - ORELLANA, Ariel

AU - HIDALGO, Perla C.

AU - MORALES, Maria N.

AU - MEZZANO, Diego

AU - BRONFMAN, Miguel

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

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SP - 57

EP - 61

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

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