Bignon E, Kishimoto A, Pons M, Crastes de Paulet A, Gilbert J, Miquel J F, Nishizuka Y
Department of Biochemistry, Kobe University School of Medicine, Japan.
Biochem Biophys Res Commun. 1990 Feb 14;166(3):1471-8. doi: 10.1016/0006-291x(90)91033-o.
Protein kinase C (PKC) I (gamma), II (beta) and III (alpha) subspecies are all activated by 1,1-di-(p-hydroxyphenyl)ethylene derivatives (DPE) at micromolar concentrations. This PKC activation depends on the presence of both Ca2+ and phosphatidylserine (PS) but does not require diacylglycerol (DG). DPEs enhance PKC activity at low PS concentrations, but not at saturating PS concentrations. Like DG, DPEs increase the apparent affinity of PKC for PS as well as for Ca2+, but lead to a decrease in the catalytic activity (Vmax). In the presence of saturating DG concentrations, DPEs exhibit an inhibitory action. The derivatives also inhibit the activity of the proteolytic fragment of PKC, protein kinase M. It is concluded that DPEs are mixed-type inhibitors, probably interacting with the catalytic domain of the enzyme.
蛋白激酶C（PKC）的I（γ）、II（β）和III（α）亚型均能被微摩尔浓度的1,1-二-（对羟基苯基）乙烯衍生物（DPE）激活。这种PKC激活依赖于Ca2+和磷脂酰丝氨酸（PS）的存在，但不需要二酰基甘油（DG）。DPE在低PS浓度下增强PKC活性，但在饱和PS浓度下则不然。与DG一样，DPE增加了PKC对PS以及对Ca2+的表观亲和力，但导致催化活性（Vmax）降低。在饱和DG浓度存在的情况下，DPE表现出抑制作用。这些衍生物还抑制PKC的蛋白水解片段蛋白激酶M的活性。结论是DPE是混合型抑制剂，可能与该酶的催化结构域相互作用。
