大鼠卵巢中的热稳定蛋白激酶C（PKC）刺激因子可能使PKC在不依赖细胞膜脂质的情况下保持活性。

The heat-stable protein kinase C (PKC) stimulatory factor in the rat ovary may allow PKC to be active independent of cell membrane lipids.

作者信息

Eyster K M

机构信息

Department of Physiology and Pharmacology, University of South Dakota, School of Medicine, Vermillion 57069-2390, USA.

出版信息

Cell Signal. 1995 Jul;7(5):457-61. doi: 10.1016/0898-6568(95)00015-h.

DOI:10.1016/0898-6568(95)00015-h

PMID:8562306

Abstract

A protein kinase C (PKC) stimulatory factor in heat-treated ovarian cytosol appears to be protein in nature as it was susceptible to proteinase K digestion and strong acid, and its lipid-substituting properties were retained after extraction of lipids. Phosphorylation of substrate by PKC stimulated by the factor from heat-treated ovarian cytosol in the absence of lipids was subject to dephosphorylation by the ovarian phosphatase. The factor stimulated purified PKC obtained from a commercial source as well as PKC partially purified from rat brain. Heat-treated ovarian cytosol stimulated PKC phosphorylation of myelin basic protein, but not protamine sulphate, in a calcium-dependent manner.

摘要

热处理的卵巢细胞质溶胶中的一种蛋白激酶C（PKC）刺激因子似乎本质上是蛋白质，因为它易受蛋白酶K消化和强酸作用，并且在脂质提取后仍保留其脂质替代特性。在无脂质情况下，由热处理的卵巢细胞质溶胶中的因子刺激的PKC对底物的磷酸化会被卵巢磷酸酶去磷酸化。该因子能刺激从商业来源获得的纯化PKC以及从大鼠脑部分纯化的PKC。热处理的卵巢细胞质溶胶以钙依赖的方式刺激髓鞘碱性蛋白的PKC磷酸化，但不刺激硫酸鱼精蛋白的磷酸化。