Bronfman M, Morales M N, Orellana A
Department of Cell Biology, P. Universidad Católica de Chile, Santiago.
Biochem Biophys Res Commun. 1988 May 16;152(3):987-92. doi: 10.1016/s0006-291x(88)80381-4.
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.
在存在二酰基甘油、磷脂酰丝氨酸和Ca²⁺的情况下，使用两种不同的测定系统（脂质以超声分散液形式添加或与 Triton X - 100形成混合胶束形式添加），发现微摩尔量的长链酰基辅酶A可使大鼠脑蛋白激酶C的活性大幅增加。这种增强现象需要二酰基甘油和磷脂酰丝氨酸同时存在；在这些效应物的低浓度和饱和浓度下均能观察到，并且在高浓度、非生理性的Ca²⁺浓度下受到抑制。在类似条件下，单独的脂肪酸或辅酶A没有效果。这些数据有力地表明，在磷脂酶C/磷脂酰肌醇途径激活该酶后，细胞内浓度水平的酰基辅酶A在蛋白激酶C的调节中很重要。
