粒细胞弹性蛋白酶可裂解人高分子量激肽原并破坏其促凝活性。
Granulocyte elastase cleaves human high molecular weight kininogen and destroys its clot-promoting activity.
作者信息
Kleniewski J, Donaldson V
机构信息
Department of Pediatrics, University of Cincinnati College of Medicine, Children's Hospital Research Foundation, Ohio 45229.
出版信息
J Exp Med. 1988 Jun 1;167(6):1895-907. doi: 10.1084/jem.167.6.1895.
Abstract
Purified human granulocyte elastase cleaved purified human high molecular weight (HMW) kininogen into multiple low molecular weight fragments, and destroyed the clot-promoting activity of the HMW kininogen. Elastase digestion did not release kinin or destroy the bradykinin portion of the HMW kininogen molecule; kallikrein could release kinin from the elastase-induced low molecular weight digestion products of HMW kininogen. Purified alpha 1-antitrypsin prevented the destruction of the clot-promoting activity of HMW kininogen by elastase; it also delayed the clotting of normal plasma. Elastase may play a significant role in altered hemostasis as well as fibrinolysis, in areas of inflammation to which polymorphonuclear leukocytes have been attracted.
摘要
纯化的人粒细胞弹性蛋白酶将纯化的人高分子量（HMW）激肽原切割成多个低分子量片段，并破坏了HMW激肽原的促凝活性。弹性蛋白酶消化不会释放激肽或破坏HMW激肽原分子的缓激肽部分；激肽释放酶可从弹性蛋白酶诱导的HMW激肽原低分子量消化产物中释放激肽。纯化的α1-抗胰蛋白酶可防止弹性蛋白酶对HMW激肽原促凝活性的破坏；它还会延迟正常血浆的凝固。在多形核白细胞被吸引到的炎症区域，弹性蛋白酶可能在改变的止血以及纤维蛋白溶解中起重要作用。
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本文引用的文献
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