Proteolytic cleavage of human von Willebrand factor induced by enzyme(s) released from polymorphonuclear cells.
Proteolytic cleavage of human von Willebrand factor induced by enzyme(s) released from polymorphonuclear cells.
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由多形核细胞释放的酶诱导人血管性血友病因子的蛋白水解裂解。
DOI：
10.1182/blood.v67.5.1281.1281
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发表时间：
1986
期刊：
影响因子：
20.3
通讯作者：
M. Howard
中科院分区：
文献类型：
--
作者：
E. Thompson;M. Howard
在弥散性血管内凝血患者血浆、VIII因子浓缩物和正常血清中，放射性交叉免疫电泳（CIE）证实了血管性血友病因子抗原（vWF：Ag）分子的体内片段化。本文报道的实验表明，多形核白细胞（PMN）细胞含有一种非钙依赖性蛋白酶，当释放并与vWF：Ag孵育时，在放射性CIE上产生额外的vWF：Ag峰。与PMN细胞孵育产生的片段vWF：Ag发生在一个时间依赖性的方式。负责的蛋白酶被二异丙基氟磷酸盐、大豆胰蛋白酶抑制剂和抑肽酶抑制，但不被苯甲脒、叠氮化物、Epicron或水蛭素抑制。柠檬酸盐、EDTA和亮抑酶肽对PMN细胞酶的活性也没有影响，表明该酶不是钙依赖性的。负责vWF：Ag片段化的PMN细胞酶位于细胞内，并通过冷冻溶解或钙或钙离子载体A23187的细胞活化而释放。
In vivo fragmentation of the von Willebrand factor antigen (vWF:Ag) molecule has been demonstrated on radiocrossed immunoelectrophoresis (CIE) in the plasma from patients with disseminated intravascular coagulation, in factor VIII concentrates, and in normal serum. Experiments reported here show that polymorphonuclear (PMN) cells contain a non-calcium-dependent protease(s) that when released and incubated with vWF:Ag results in an additional vWF:Ag peak on radio-CIE. Production of fragments of vWF:Ag by incubation with PMN cells occurred in a time-dependent manner. The protease(s) responsible was inhibited by diisopropyl fluorophosphate, soybean trypsin inhibitor, and aprotinin, but not by benzamidine, azide, epicron, or hirudin. Citrate, EDTA, and leupeptin also had no effect on the PMN cell enzyme's activity, indicating that the enzyme(s) is not calcium dependent. The PMN cell enzyme responsible for vWF:Ag fragmentation is located intracellularly and released by freezethaw lysis or cell activation by calcium or the calcium ionophore A23187.
血小板钙激活蛋白酶对人血管性血友病因子的裂解。
影响因子：
20.3
作者：
Kunicki,TJ;Montgomery,RR;Schullek,J
通讯作者：
Schullek,J