Huang K P
Section on Metabolic Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Biofactors. 1990 Jul;2(3):171-8.
Protein kinase C (PKC) consists of a family of closely related enzymes ubiquitously present in animal tissues. These enzymes respond to second messengers, Ca2+, diacylglycerol and arachidonic acid, to express their activities at membrane locations. Numerous hormones, neurotransmitters, growth factors and antigens are believed to transmit their signals by activation of a variety of phospholipases to generate these messengers. The various PKC isozymes, which exhibit distinct biochemical characteristics and unique cellular and subcellular localizations, may be differentially stimulated depending on the duration and strength of these messengers. Activation of PKC has been linked to the regulation of cell surface receptors, ion channels, secretion, gene expression, and neuronal plasticity and toxicity. The mechanisms of action of PKC in the regulation of these cellular functions are not entirely clear. Further study to identify the target substrates relevant to the various cellular functions is essential to define the functional diversity of this enzyme family.
蛋白激酶C（PKC）由一组密切相关的酶组成，广泛存在于动物组织中。这些酶对第二信使、钙离子、二酰基甘油和花生四烯酸作出反应，在膜位置发挥其活性。许多激素、神经递质、生长因子和抗原被认为通过激活各种磷脂酶来产生这些信使，从而传递它们的信号。各种PKC同工酶具有不同的生化特性以及独特的细胞和亚细胞定位，可能会根据这些信使的持续时间和强度受到不同的刺激。PKC的激活与细胞表面受体、离子通道、分泌、基因表达以及神经元可塑性和毒性的调节有关。PKC在调节这些细胞功能中的作用机制尚不完全清楚。进一步研究以确定与各种细胞功能相关的靶底物对于定义该酶家族的功能多样性至关重要。
