蛋白激酶C在磷脂酶C刺激磷脂酰胆碱合成中的作用。
The role of protein kinase C in the stimulation of phosphatidylcholine synthesis by phospholipase C.
作者信息
Jones G A, Kent C
机构信息
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
出版信息
Arch Biochem Biophys. 1991 Aug 1;288(2):331-6. doi: 10.1016/0003-9861(91)90203-u.
The role of protein kinase C in the stimulation of phosphatidylcholine (PC) synthesis by phospholipase C was investigated. Phospholipase C treatment of Chinese hamster ovary cells (CHO) generates diacylglycerol, which is an activator of protein kinase C. The protein kinase C activator, 12-O-tetradecanoyl-phorbol-13-acetate (TPA) stimulated choline incorporation into two CHO cell lines, a wild-type cell line, WTB, and a mutant cell line, DTG 1-5-4. DTG 1-5-4 is a mutant defective in receptor-mediated endocytosis. A 3-h phospholipase C treatment resulted in the activation and translocation of CTP:phosphocholine cytidylyltransferase in both cell lines. TPA treatment, however, resulted in only a slight (20%) translocation of cytidylyltransferase in WTB; no detectable translocation of cytidylyltransferase was observed in DTG 1-5-4. A decrease in the phosphocholine pools was observed in response to TPA treatment in both cell lines, which indicated that the cytidylyltransferase step was being activated. Phospholipase C stimulated choline incorporation into PC even when protein kinase C had been down-regulated in both cell lines. It was concluded that phospholipase C does not activate PC synthesis by activating protein kinase C.
研究了蛋白激酶C在磷脂酶C刺激磷脂酰胆碱（PC）合成中的作用。用磷脂酶C处理中国仓鼠卵巢细胞（CHO）可产生二酰基甘油，它是蛋白激酶C的激活剂。蛋白激酶C激活剂12 - O - 十四烷酰佛波醇 - 13 - 乙酸酯（TPA）刺激胆碱掺入两种CHO细胞系，一种是野生型细胞系WTB，另一种是突变细胞系DTG 1 - 5 - 4。DTG 1 - 5 - 4是一种在受体介导的内吞作用方面存在缺陷的突变体。3小时的磷脂酶C处理导致两种细胞系中CTP：磷酸胆碱胞苷转移酶的激活和易位。然而，TPA处理仅导致WTB中胞苷转移酶有轻微（20%）的易位；在DTG 1 - 5 - 4中未观察到胞苷转移酶的可检测易位。在两种细胞系中，TPA处理均导致磷酸胆碱池减少，这表明胞苷转移酶步骤正在被激活。即使在两种细胞系中蛋白激酶C已被下调，磷脂酶C仍能刺激胆碱掺入PC。得出的结论是，磷脂酶C不会通过激活蛋白激酶C来激活PC合成。
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