Granulocyte elastase cleaves human high molecular weight kininogen and destroys its clot-promoting activity.
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.
Kleniewski
J
J
Department of Pediatrics, University of Cincinnati College of Medicine, Children's Hospital Research Foundation, Ohio 45229.
Donaldson
V
V
D001777:Blood Coagulation; D006801:Humans; D066298:In Vitro Techniques; D007704:Kininogens / Q000378:metabolism*; D007705:Kinins / Q000378:metabolism; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D000515:alpha 1-Antitrypsin / Q000494:pharmacology
D007704:Kininogens; D007705:Kinins; D010446:Peptide Fragments; D000515:alpha 1-Antitrypsin; D010196:Pancreatic Elastase