Human neutrophil elastase does not bind to alpha 1-protease inhibitor that has been exposed to activated human neutrophils.
Human neutrophil elastase does not bind to alpha 1-protease inhibitor that has been exposed to activated human neutrophils.
复制标题
人中性粒细胞弹性蛋白酶不会与暴露于活化人中性粒细胞的 α1-蛋白酶抑制剂结合。
DOI：
10.1164/arrd.1983.128.3.434
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Franzblau,C
中科院分区：
文献类型：
--
作者：
Zaslow,MC;Clark,RA;Stone,PJ;Calore,JD;Snider,GL;Franzblau,C
The effect of leukocyte-derived oxidants on the elastase-inhibitory capacity of α1- protease inhibitor was examined in anin vitrosystem using cells and purified proteins from human sources. The exposure of α1-protease inhibitor to the myeloperoxidase-hydrogen peroxide-halide system resulted in a nearly complete loss of its ability to bind and inactivate purified human neutrophil elastase. A similar loss of binding to and inactivation of human neutrophil elastase was observed on exposure of α1-protease inhibitor to human neutrophils in the presence of a halide and the neutrophil-activating agent, phorbol myristate acetate. This loss of elastase binding activity was abrogated by the addition of azide or catalase but not superoxide dismutase or heated catalase. The data suggest oxidative inactivation of α1-protease inhibitor by secreted myeloperoxidase and hydrogen peroxide. Thus, the reported effects of leukocyte oxidants, especially the myeloperoxidase system, on α1-protease inhibitor have been confirmed using the most pathophysiologically relevant protease, human neutrophil elastase, as the test enzyme. The role of the neutrophil in the pathogenesis of emphysema may, therefore, include the secretion of both elastase and oxidants that impair antielastase defenses.
