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蛋白激酶C对一种20 kDa细胞骨架多肽的磷酸化作用增强了其对钙蛋白酶消化的敏感性。

Phosphorylation by protein kinase C of a 20-kDa cytoskeletal polypeptide enhances its susceptibility to digestion by calpain.

作者信息

Pontremoli S, Melloni E, Michetti M, Sparatore B, Salamino F, Sacco O, Horecker B L

出版信息

Proc Natl Acad Sci U S A. 1987 Jan;84(2):398-401. doi: 10.1073/pnas.84.2.398.

DOI:10.1073/pnas.84.2.398
PMID:3025869
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC304214/
Abstract

Incubation of the cytoskeletal fraction from human neutrophils with the proteolytically activated form of protein kinase C results in the phosphorylation of several components, including a 20-kDa polypeptide, probably consisting of myosin light chains. The 20-kDa polypeptide is also specifically phosphorylated by activated protein kinase C in a solubilized 20-kDa/80-kDa complex that was obtained after sonication of the insoluble cytoskeletal fraction. Phosphorylation of this polypeptide, in either the insoluble cytoskeletal fraction or the soluble 20-kDa/80-kDa complex, greatly enhances its susceptibility to digestion by the Ca2+-requiring proteinase (calpain, EC 3.4.22.17) of human neutrophils. Thus, signals that activate calpain by mobilizing intracellular calcium would lead to proteolytic activation of protein kinase C, phosphorylation of cytoskeletal proteins, and remodeling of the cytoskeleton by proteolysis of at least one cytoskeletal component.

摘要

将人中性粒细胞的细胞骨架组分与蛋白激酶C的蛋白水解激活形式一起温育，会导致几种成分发生磷酸化，包括一种20 kDa的多肽，可能由肌球蛋白轻链组成。在对不溶性细胞骨架组分进行超声处理后获得的可溶性20 kDa/80 kDa复合物中，活化的蛋白激酶C也会使20 kDa多肽发生特异性磷酸化。无论是在不溶性细胞骨架组分中还是在可溶性20 kDa/80 kDa复合物中，该多肽的磷酸化都会大大增强其对人中性粒细胞中需要Ca2+的蛋白酶（钙蛋白酶，EC 3.4.22.17）消化的敏感性。因此，通过动员细胞内钙来激活钙蛋白酶的信号将导致蛋白激酶C的蛋白水解激活、细胞骨架蛋白的磷酸化以及通过至少一种细胞骨架成分的蛋白水解对细胞骨架进行重塑。

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Phosphorylation by protein kinase C of a 20-kDa cytoskeletal polypeptide enhances its susceptibility to digestion by calpain.蛋白激酶C对一种20 kDa细胞骨架多肽的磷酸化作用增强了其对钙蛋白酶消化的敏感性。
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