Nishizuka Y
Department of Biochemistry, Kobe University School of Medicine, Japan.
JAMA. 1989 Oct 6;262(13):1826-33.
Protein kinase C, an enzyme that is activated by diacylglycerol resulting from the receptor-mediated hydrolysis of inositol phospholipids, relays information of a variety of extracellular signals across the cell membrane to regulate many intracellular processes. Since this enzyme also serves as a major receptor for phorbol esters, a class of tumor promoters, it has attracted great attention from biologists interested in the mechanism of signal transduction and carcinogenesis. Recent analysis has revealed that protein kinase C is a large family of proteins, with the multiple subspecies that possess subtle individual enzymological characteristics. Biochemical and immunohistochemical studies indicate that the protein kinase C subspecies may be differently distributed in particular cell types and with limited intracellular locations. Presumably, each member of the family plays discrete roles in the processing of various physiological and pathological responses to external signals, such as in the modulation of membrane functions and the activation of gene transcription.
蛋白激酶C是一种由受体介导的肌醇磷脂水解产生的二酰基甘油激活的酶,它将各种细胞外信号的信息传递过细胞膜,以调节许多细胞内过程。由于这种酶也是一类肿瘤促进剂佛波酯的主要受体,它引起了对信号转导和致癌机制感兴趣的生物学家的极大关注。最近的分析表明,蛋白激酶C是一个庞大的蛋白质家族,有多个具有细微个体酶学特征的亚种。生化和免疫组织化学研究表明,蛋白激酶C亚种可能在特定细胞类型中分布不同,且细胞内定位有限。据推测,该家族的每个成员在处理对外部信号的各种生理和病理反应中发挥着不同的作用,例如在调节膜功能和激活基因转录方面。