PROTEOLYTIC CLEAVAGE OF HUMAN VONWILLEBRAND-FACTOR INDUCED BY ENZYME(S) RELEASED FROM POLYMORPHONUCLEAR CELLS

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  • 1 May 1986
    • journal article
    • research article
    • Vol. 67  (5) , 1281-1285
Abstract
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 freeze-thaw lysis or cell activation by calcium or the calcium ionophore A23187.