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

Granulocyte elastase cleaves human high molecular weight kininogen and destroys its clot-promoting activity.
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DOI:
10.1084/jem.167.6.1895
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发表时间:
1988-06-01
影响因子:
15.3
通讯作者:
DONALDSON, V
DONALDSON, V
中科院分区:
医学1区
文献类型:
--
作者:
KLENIEWSKI, J;DONALDSON, V

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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.
DOI: 10.1172/jci104308
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