在钙离子存在的情况下蛋白激酶C与中性粒细胞膜的结合及其被一种需要钙离子的蛋白酶激活。
Binding of protein kinase C to neutrophil membranes in the presence of Ca2+ and its activation by a Ca2+-requiring proteinase.
作者信息
Melloni E, Pontremoli S, Michetti M, Sacco O, Sparatore B, Salamino F, Horecker B L
出版信息
Proc Natl Acad Sci U S A. 1985 Oct;82(19):6435-9. doi: 10.1073/pnas.82.19.6435.
Abstract
In the presence of micromolar concentrations of Ca2+, both protein kinase C and a cytosolic Ca2+-requiring neutral proteinase of human neutrophils become associated with the neutrophil membrane. Binding to the membrane results in activation of the proteinase, which then catalyzes limited proteolysis of the kinase to produce a form that is fully active in the absence of Ca2+ and phospholipid. This irreversibly activated protein kinase is released from the membrane and may thus have access, in the intact cell, to intracellular protein substrates. In the absence of the proteinase, Ca2+ promotes the binding of protein kinase C, but conversion to the Ca2+/phospholipid-independent form does not occur and the kinase remains associated with the membrane fraction.
摘要
在存在微摩尔浓度的Ca2+时，蛋白激酶C和人类中性粒细胞的一种需要胞质Ca2+的中性蛋白酶都会与中性粒细胞膜结合。与膜结合会导致蛋白酶激活，然后该蛋白酶催化激酶的有限蛋白水解，从而产生一种在没有Ca2+和磷脂的情况下仍具有完全活性的形式。这种不可逆激活的蛋白激酶从膜上释放出来，因此在完整细胞中可能能够接触到细胞内的蛋白质底物。在没有蛋白酶的情况下，Ca2+促进蛋白激酶C的结合，但不会转化为不依赖Ca2+/磷脂的形式，激酶仍与膜部分结合。
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