| Literature DB >> 3260266 |
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.Entities:
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Year: 1988 PMID: 3260266 PMCID: PMC2189673 DOI: 10.1084/jem.167.6.1895
Source DB: PubMed Journal: J Exp Med ISSN: 0022-1007 Impact factor: 14.307