Down regulation of prothrombinase by activated protein C during prothrombin activation
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چکیده
منابع مشابه
Activation of Human Prothrombin by Human Prothrombinase
The kinetics of the activation of human prothrombin catalyzed by human prothrombinase was studied using the fluorescent a-thrombin inhibitor dansylarginineN-(3-ethyl-1,5-pentanediyl)amide(DAPA). Prothrombinase proteolytically activates prothrombin to athrombin by cleavages at Arg273-Thr274 (bond A) and Arg322-Ile323 (bond B). The differential fluorescence properties of DAPA complexed with the...
متن کاملFate of membrane-bound reactants and products during the activation of human prothrombin by prothrombinase.
Membrane binding by prothrombin, mediated by its N-terminal fragment 1 (F1) domain, plays an essential role in its proteolytic activation by prothrombinase. Thrombin is produced in two cleavage reactions. One at Arg(320) yields the proteinase meizothrombin that retains membrane binding properties. The second, at Arg(271), yields thrombin and severs covalent linkage with the N-terminal fragment ...
متن کاملInhibition of activated protein C anticoagulant activity by prothrombin.
In this study, we test the hypothesis that prothrombin levels may modulate activated protein C (APC) anticoagulant activity. Prothrombin in purified systems or plasma dramatically inhibited the ability of APC to inactivate factor Va and to anticoagulate plasma. This was not due solely to competition for binding to the membrane surface, as prothrombin also inhibited factor Va inactivation by APC...
متن کاملActivated Protein C Inhibits Platelet Prothrombin-
Bovine platelets that have been activated factor Xa is able to protect the platelet by thrombin facilitate the conversion of prothrombin-converting activity from macprothrombin to thrombin in the presence of tivation by activated protein C. The acticalcium ions and factor Xa. Activated vated protein C causes a parallel loss of protein C, a vitamin-K-dependent plasma factor Xa receptor sites and...
متن کاملSpecific contribution of different phospholipid surfaces to the activation of prothrombin by the fully assembled prothrombinase.
This paper addresses, in thermodynamic and kinetic terms, the reasons for the acidic lipid specificity of the human prothrombinase complex. We obtained, from the measured lipid titrations of the initial rates of prothrombin activation, the empirical binding constants for prothrombinase assembly on different membranes. These favored assembly on phosphatidylserine (PS)- as opposed to phosphatidyl...
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ژورنال
عنوان ژورنال: Thrombosis and Haemostasis
سال: 2010
ISSN: 0340-6245,2567-689X
DOI: 10.1160/th09-09-0650