Huang C K, Devanney J F, Kennedy S P
Department of Pathology, University of Connecticut Health Center, Farmington 06032.
Biochem Biophys Res Commun. 1988 Feb 15;150(3):1006-11. doi: 10.1016/0006-291x(88)90728-0.
Evidence is shown that vimentin, the intermediate filament protein, is a substrate for protein kinase C: (a) Purified vimentin from Chinese hamster ovary cells can be phosphorylated by protein kinase C prepared from rabbit peritoneal neutrophils. Tryptic peptic analysis reveals multiple sites of phosphorylation distinct from those phosphorylated by cAMP-dependent protein kinase. (b) phosphorylation of membrane associated vimentin is stimulated in phorbol 12-myristate 13-acetate treated neutrophil membranes, suggesting that vimentin can be a substrate for membrane associated protein kinase C and (c) phorbol 12-myristate 13-acetate also stimulates the phosphorylation of vimentin in 32P-labeled intact neutrophils.
有证据表明,中间丝蛋白波形蛋白是蛋白激酶C的底物:(a) 从中国仓鼠卵巢细胞中纯化的波形蛋白可被从兔腹膜中性粒细胞制备的蛋白激酶C磷酸化。胰蛋白酶消化分析显示,磷酸化位点与环磷酸腺苷依赖性蛋白激酶磷酸化的位点不同。(b) 在佛波醇12-肉豆蔻酸酯13-乙酸酯处理的中性粒细胞膜中,膜相关波形蛋白的磷酸化受到刺激,这表明波形蛋白可能是膜相关蛋白激酶C的底物,并且 (c) 佛波醇12-肉豆蔻酸酯13-乙酸酯也能刺激32P标记的完整中性粒细胞中波形蛋白的磷酸化。