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

Miguel Bronfman, M. Nelly Morales, Ariel Orellana

Resultado de la investigación: Article

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

Huella dactilar

Acyl Coenzyme A
Phosphatidylserines
Diglycerides
Protein Kinase C
Chemical activation
Enzyme Activation
Octoxynol
Micelles
Type C Phospholipases
Coenzyme A
Phosphatidylinositols
Rats
Assays
Brain
Fatty Acids
Modulation
Lipids
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Citar esto

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Diacylglycerol activation of protein kinase C is modulated by long-chain acyl-CoA. / Bronfman, Miguel; Morales, M. Nelly; Orellana, Ariel.

En: Biochemical and Biophysical Research Communications, Vol. 152, N.º 3, 16.05.1988, p. 987-992.

Resultado de la investigación: Article

TY - JOUR

T1 - Diacylglycerol activation of protein kinase C is modulated by long-chain acyl-CoA

AU - Bronfman, Miguel

AU - Morales, M. Nelly

AU - Orellana, Ariel

PY - 1988/5/16

Y1 - 1988/5/16

N2 - 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.

AB - 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.

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DO - 10.1016/S0006-291X(88)80381-4

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JO - Biochemical and Biophysical Research Communications

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