SERPIN Regulation of Factor XIa
نویسندگان
چکیده
منابع مشابه
Inactivation of factor XIa in human plasma assessed by measuring factor XIa-protease inhibitor complexes: major role for C1-inhibitor.
From experiments with purified proteins, it has been concluded that factor XIa (FXIa) is inhibited in plasma mainly by alpha 1-antitrypsin (a1AT), followed by antithrombin III (ATIII), C1-inhibitor (C1Inh), and alpha 2-antiplasmin (a2AP). However, the validity of this concept has never been studied in plasma. We established the relative contribution of different inhibitors to the inactivation o...
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From experiments with purified proteins, it has been concluded that factor Xla (FXla) is inhibited in plasma mainly by a,-antitrypsin (alAT), followed by antithrombin 111 (ATIll), Cl-inhibitor (Cllnh), and a2-antiplasmin (a2AP). However, the validity of this concept has never been studied n plasma. We established the relative contribution of different inhibitors to the inactivation of FXla in h...
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Studies of the mechanisms of blood coagulation zymogen activation demonstrate that exosites (sites on the activating complex distinct from the protease active site) play key roles in macromolecular substrate recognition. We investigated the importance of exosite interactions in recognition of factor IX by the protease factor XIa. Factor XIa cleavage of the tripeptide substrate S2366 was inhibit...
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We have studied the interaction between purified human factor XIa and antithrombin in the presence and absence of well-characterized preparations of heparin. The concentrations of hemostatic enzyme. protease inhibitor. and mucopolysaccharide were 5.76 x iO8 mol/L. 5.76 x iO mol/L. and either 5.88 x iO mol/L or 0. respectively. Kinetic investigation of this process using a tritiated factor IX su...
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The dose-limiting issue with available anticoagulant therapies is bleeding. Is there an approach that could provide antithrombotic protection with reduced bleeding? One hypothesis is that targeting proteases upstream from the common pathway provides a reduction in thrombin sufficient to impede occlusive thrombosis yet allows enough thrombin generation to support hemostasis. The impairment of in...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.m003909200