Coagulation factor X (F10) (F10)

Coagulation factor X (F10) is a vitamin K-dependent serine protease that serves as a critical convergence point in the blood coagulation cascade, where the intrinsic and extrinsic pathways meet to initiate the common pathway [1, 15]. It is synthesized in the liver and circulates in the plasma as an inactive zymogen until it is activated to form Factor Xa (FXa) [2, 15]. Once activated, Factor Xa assembles with its cofactor, Factor Va, on phospholipid surfaces to form the prothrombinase complex, which is responsible for the rapid conversion of prothrombin into thrombin [1, 15]. Thrombin then catalyzes the conversion of fibrinogen to fibrin, leading to the formation and stabilization of blood clots [10, 12]. Beyond its role in hemostasis, Factor Xa also functions as a signaling molecule by activating protease-activated receptors (PARs), thereby influencing inflammatory and fibroproliferative processes [6, 11, 13]. Due to its central role in thrombin generation, Factor Xa is a major therapeutic target for anticoagulation therapy [10, 15]. Direct oral anticoagulants (DOACs), such as rivaroxaban and apixaban, specifically inhibit Factor Xa to prevent and treat thromboembolic conditions like deep vein thrombosis, pulmonary embolism, and stroke in patients with atrial fibrillation [7, 14, 18]. While these drugs offer predictable pharmacokinetics and reduced monitoring requirements compared to traditional therapies like warfarin, the primary safety concern remains the risk of major bleeding [3, 14, 19]. Genetic mutations in the F10 gene can lead to Factor X deficiency, a rare but serious bleeding disorder characterized by impaired clot formation and hemorrhagic symptoms [1, 15].

Other names

Stuart factorStuart-Prower factorThrombokinaseActivated factor XaFXFXa

Direct Factor Xa inhibitors (e.g., rivaroxaban, apixaban) bind directly and reversibly to the active site of Factor Xa, inhibiting its ability to convert prothrombin to thrombin [7, 12, 18]. Indirect inhibitors (e.g., heparin, fondaparinux) act by binding to antithrombin, which then undergoes a conformational change to rapidly inactivate Factor Xa [12]. These mechanisms disrupt the final common pathway of the coagulation cascade, preventing fibrin formation and thrombus stabilization [10, 12].