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Blood coagulation pathways in vivo showing the central role played by thrombin. Factor Xa is the activated form of the coagulation factor X, also known as thrombokinase. Factor X is an enzyme, a serine endopeptidase, which plays a key role at several stages of the coagulation system. Factor X is synthesized in the liver.
Factor X deficiency (X as Roman numeral ten) is a bleeding disorder characterized by a lack in the production of factor X (FX), an enzyme protein that causes blood to clot in the coagulation cascade. Produced in the liver FX when activated cleaves prothrombin to generate thrombin in the intrinsic pathway of coagulation.
Coagulation factor concentrates are used to treat hemophilia, to reverse the effects of anticoagulants, and to treat bleeding in people with impaired coagulation factor synthesis or increased consumption. Prothrombin complex concentrate, cryoprecipitate and fresh frozen plasma are commonly used coagulation factor products.
In coagulation, the coagulation factor X can be activated into factor Xa in two ways: either extrinsically or intrinsically. The activating complexes are together called tenase. Tenase is a blend word of "ten" and the suffix "-ase", which means, that the complex activates its substrate (inactive factor X) by cleaving it. [1]
Factors VII, IX, and X all play key roles in blood coagulation and also share a common domain architecture. [10] The factor IX protein is composed of four protein domains: the Gla domain, two tandem copies of the EGF domain and a C-terminal trypsin-like peptidase domain which carries out the catalytic cleavage.
The activation of factor X is a common point between the intrinsic and extrinsic pathway of blood coagulation. [1] Activated factor X (FXa) is the sole enzyme that catalyzes the conversion of prothrombine into thrombin, which is vital in the coagulation cascade. [ 1 ]
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