Granulocyte elastase cleaves human high molecular weight kininogen and destroys its clot-promoting activity

doi:10.1084/jem.167.6.1895

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Granulocyte elastase cleaves human high molecular weight kininogen and destroys its clot-promoting activity

J Kleniewski and V Donaldson
Department of Pediatrics, University of Cincinnati College of Medicine, Children's Hospital Research Foundation, Ohio 45229.

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.
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