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Blood coagulation factor X is a vitamin K-dependent serine protease synthesized in the liver that plays a pivotal role in the coagulation cascade, acting as the first enzyme of the common pathway in both intrinsic and extrinsic blood clotting routes[1][2][3][6]. In its active form, factor Xa, it converts prothrombin to thrombin in the presence of factor Va, calcium ions, and phospholipids, catalyzing the key final steps of clot formation[1][3][6]. Due to this central function, it is a validated therapeutic target for anticoagulant drugs, especially direct oral anticoagulants (DOACs)[1][5]. Factor X deficiency results in bleeding disorders, whereas overactivity contributes to thrombotic diseases[1][2][3]. Factor X is also known as Stuart factor or thrombokinase and is encoded by the F10 gene[3][6]. Its molecular structure contains Gla and EGF-like domains important for membrane binding and enzymatic activity[5][6]. Clinical modulation of factor Xa activity is central to the management of thrombosis and bleeding risk in numerous cardiovascular conditions[1][3][5].
Inhibition of factor Xa activity to prevent thrombin generation; Reduction of prothrombinase complex activity; Attenuation of blood coagulation cascade
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