Replacing the Factor VIII C1 Domain with a Second C2 Domain Reduces Factor VIII Stability and Affinity for Factor IXa
نویسندگان
چکیده
منابع مشابه
FACTOR V AND VIII INHIBITOR IN PATIENTS WITH COMBINED FACTOR V AND VIII DEFICIENCY
Patients with coagulation factor(s) deficiency who use coagulation therapy are susceptible to forming inhibitors against coagulation factor(s). In this survey we detected factor V and VIII inhibitor in ten patients with combined deficiency of factors V and VIII from north east of Iran (Khorassan province). It was revealed in our survey that eight patients had both factor V and factor VIII i...
متن کاملActivation of factor VIII by factor IXa.
Thrombin causes an increase in factor VIII coagulant (VIII:C) activity, which is followed by a decay of VIII:C activity to below baseline levels. It has been suggested that a similar interaction of trace amounts of thrombin and factor VIII is a necessary prerequisite before factor VIII can participate in the coagulation cascade. In the current study, factor IXa, a serine protease with structura...
متن کاملA membrane-interactive surface on the factor VIII C1 domain cooperates with the C2 domain for cofactor function.
Factor VIII binds to phosphatidylserine (PS)-containing membranes through its tandem, lectin-homology, C1 and C2 domains. However, the details of C1 domain membrane binding have not been delineated. We prepared 4 factor VIII C1 mutations localized to a hypothesized membrane-interactive surface (Arg2090Ala/Gln2091Ala, Lys2092Ala/Phe2093Ala, Gln2042Ala/Tyr2043Ala, and Arg2159Ala). Membrane bindin...
متن کاملMembrane-binding properties of the Factor VIII C2 domain.
Factor VIII functions as a cofactor for Factor IXa in a membrane-bound enzyme complex. Membrane binding accelerates the activity of the Factor VIIIa-Factor IXa complex approx. 100000-fold, and the major phospholipid-binding motif of Factor VIII is thought to be on the C2 domain. In the present study, we prepared an fVIII-C2 (Factor VIII C2 domain) construct from Escherichia coli, and confirmed ...
متن کاملThe factor VIII C1 domain contributes to platelet binding.
Activated factor VIII (FVIIIa) forms a procoagulant complex with factor IXa on negatively charged membranes, including activated platelet surfaces. Membrane attachment involves the FVIII C2 domain; involvement of the adjacent C1 domain has not been established. Binding of recombinant FVIII C1C2 and C2 proteins to platelets was detected by flow cytometry using (1) anti-C2 monoclonal antibody ESH...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2013
ISSN: 0021-9258
DOI: 10.1074/jbc.m113.497289