Roddick V L, Krebs C R, Kucera L S, Daniel L W, Waite M
Department of Biochemistry, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, N.C.
Oncology. 1988;45(3):197-201. doi: 10.1159/000226561.
Increased cytosolic phospholipid-sensitive, Ca2+-dependent protein kinase C (PK-C) activity is correlated with the highly tumorigenic potential of rat embryo fibroblasts transformed by herpes simplex virus type 2 (HSV-2). Treatment of the cells with 12-O-tetradecanoylphorbol-13-acetate (TPA) caused a decrease in the cytosolic PK-C with a concomitant increase in PK-C recovered in the membrane fraction. Translocation of the PK-C was dependent upon length of exposure to the phorbol diester. PK-C activity in the cytosolic fraction could be stimulated by TPA without the addition of phosphatidylserine and diacylglycerol. It is tempting to speculate that HSV-2 induction of cellular PK-C activity may be important in phosphorylation of proteins needed for promotion of HSV-2-induced carcinogenesis.
胞质磷脂敏感的、Ca2+ 依赖性蛋白激酶 C（PK-C）活性增加与单纯疱疹病毒 2 型（HSV-2）转化的大鼠胚胎成纤维细胞的高致瘤潜力相关。用 12-O-十四烷酰佛波醇-13-乙酸酯（TPA）处理细胞导致胞质 PK-C 减少，同时膜部分中回收的 PK-C 增加。PK-C 的转位取决于佛波酯的暴露时间。在不添加磷脂酰丝氨酸和二酰基甘油的情况下，TPA 可刺激胞质部分中的 PK-C 活性。很容易推测，HSV-2 诱导细胞 PK-C 活性可能在促进 HSV-2 诱导的致癌作用所需蛋白质的磷酸化中起重要作用。
