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malfunction
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enzyme inhibition by anticoagulants are recommended for numerous medical conditions, including the prevention and treatment of venous thromboembolism, stroke prevention in patients with atrial fibrillation, and secondary prevention in acute coronary syndromes
malfunction
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enzyme inhibition is beneficial in prevention and treatment of thromboembolic disorders
malfunction
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factor Xa deficiency is a rare inherited autosomal recessive trait, a patient harboring the mutation is affected by a severe bleeding diathesis
malfunction
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enzyme inhibition reduces thioacetamide-induced murine liver fibrosis
metabolism
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the enzyme is involved in the blood coagulation cascade, overview
metabolism
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constituents of platelet membranes regulate the activity of the prothrombinase complex. Membranes containing phosphatidylcholine and phosphatidylethanolamine bind factor Va with high affinity in the absence of phosphatidylserine, specific protein-PE interactions appear to contribute to the effects of phosphatidylethanolamine
physiological function
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factor Xa is a serine protease located at the confluence of the intrinsic and extrinsic pathways of the blood coagulation cascade, that catalyzes the conversion of prothrombin to thrombin via the prothrombinase complex, the enzyme is required for blood coagulation, overview
physiological function
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factor Xa is part of the blood coagulation cascade
physiological function
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factor Xa plays a role in blood coagulation. And FXa also plays a key role in cell migration, and is involved in a mechanism of PAR-1-mediated inhibition of migration via Rho and Src dependent pathways
physiological function
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FXa plays a critical role in coagulation. Together with FVa and calcium ions on a phospholipid surface, FXa forms the prothrombinase complex, which is responsible for the conversion of prothrombin to thrombin, the final effector of coagulation. Regulation of thrombin generation is the primary physiologic function of FXa
physiological function
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the final serine proteinase zymogen activation step of the blood coagulation pathway is the proteolytic activation of prothrombin to thrombin by prothrombinase. Prothrombinase consists of the proteinase, factor Xa, bound to its protein cofactor, factor Va, assembled in the presence of calcium on phospholipid membranes containing phosphatidylserine
physiological function
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the final serine proteinase zymogen activation step of the blood coagulation pathway is the proteolytic activation of prothrombin to thrombin by prothrombinase. Prothrombinase consists of the proteinase, factor Xa, bound to its protein cofactor, factor Va, assembled in the presence of calcium on phospholipid membranes containing phosphatidylserine
physiological function
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activated blood coagulation factor X (FXa) induces angiogenic growth factor expression in human retinal pigment epithelial (RPE) cells. FXa induced chemotaxis of RPE cells via activation of the p38 mitogen-activated protein kinase signal transduction pathway. FXa also induces expression of vascular endothelial growth factor, heparin-binding epidermal growth factor-like growth factor, and basic fibroblast growth factor, as well as release of these factors from RPE cells
physiological function
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activated factor Xa is an important player in the coagulation cascade responsible for thrombin generation, which is activated during atrial fibrillation. Factor Xa induces an inflammatory signalling by activation of protease-activated receptors in human atrial tissue. FXa and tachyarrhythmia act synergistically to increase expression of protease-activated receptors and inflammatory mediators
physiological function
apart from the natural activation pathway, human prothrombin can also be activated by prothrombin activators in snake venoms. Oscutarin depends on calcium and phospholipids but not on factor Va for activity and generation of thrombin
physiological function
apart from the natural activation pathway, human prothrombin can also be activated by prothrombin activators in snake venoms. Trocarin depends on calcium and phospholipids as well as factor Va for activity and generation of thrombin
physiological function
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factor Xa i spart of the prothrombinase complex
physiological function
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factor-Xa-induced mitogenesis and migration require sphingosine kinase activity and sphingosine-1-phosphate formation in human vascular smooth muscle cells. Factor Xa induces sphingosine kinase-1 expression and increases sphingosine-1-phosphate formation independent of thrombin, involving the activation of Rho A and protein kinase C signalling
physiological function
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the membrane-dependent interaction of factor Xa with factor Va forms prothrombinase and drives thrombin formation essential for hemostasis
physiological function
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the enzyme induces inflammation by activating protease-activated receptor 1 and protease-activated receptor 2
physiological function
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the enzyme promotes stellate cell contractility and activation
additional information
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factor Va is the non-enzymatic cofactor of prothrombinase, which comprises, along with FVa, the enzyme factor Xa, a negatively charged phospholipid surface, and calcium ions
additional information
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prothrombin specifically active site-labeled with D-Phe-Pro-Arg-CH2Cl shows altered activity in vitro and in vivo compared to the wild-type protein, overview
additional information
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prothrombin specifically active site-labeled with D-Phe-Pro-Arg-CH2Cl shows altered activity in vitro and in vivo compared to the wild-type protein. [AF660]FPR-mouse ProT binds to fibroblast membranes in mouse plasma, overview
additional information
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the mechanism for the activation of prothrombin to thrombin by prothrombinase is achieved through two distinct intermediate pathways, overview
additional information
the enzyme is similar to human coagulation factor X
additional information
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the enzyme is similar to human coagulation factor X
additional information
the enzyme is similar to human coagulation factor X
additional information
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the enzyme is similar to human coagulation factor X