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Factor X

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Official Full Name
Factor X
Background
Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, factor VIIIa, cellular surface and calcium ions) or the extrinsic factor Xase complex (factor VIIa, tissue factor, cellular surface and calcium ions). Activation of human factor X by either complex results in cleavage at Arg52-Ile53 of the COOH-terminal heavy chain and subsequent release of a 52 amino acid activation glycopeptide. Factor Xa then serves as the enzyme component of the prothrombinase complex which is responsible for the rapid conversion of prothrombin to thrombin. The gla residues enable factor X/Xa to bind phospholipid (i.e. cell surfaces) in a calcium dependent manner; a requirement for assembly of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains. Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured in a factor X clotting assay.
Synonyms
Human Factor X; Factor X
Catalog Product Name EC No. CAS No. Source Price
CZY-007 Mouse Factor X Mouse Inquiry
CZY-006 Bovine Factor X 9002-05-5 Bovine Inquiry
CZY-005 Human gla-domainless Factor X Human Inquiry
CZY-004 Human Factor X 9001-29-0 Human Inquiry

Related Reading

Introduction

Factor X is a key enzyme in the coagulation cascade, playing a crucial role in the formation of blood clots. Factor X is a serine protease that is synthesized in the liver and circulates in the bloodstream in an inactive form. When a blood vessel is injured, the coagulation cascade is initiated, leading to the activation of Factor X by either the intrinsic or extrinsic pathways. Once activated, Factor X cleaves prothrombin to form thrombin, which is a critical step in the formation of a blood clot.

Structure

The structure of Factor X consists of a light chain and a heavy chain, connected by a disulfide bond. The light chain contains the catalytic domain, responsible for the enzymatic activity of the protein, while the heavy chain contains the Gla domain, which allows Factor X to bind to phospholipids on the surface of platelets and other cells.

Functions

Factor X plays a central role in hemostasis, the process of stopping bleeding after a blood vessel is injured. In the initial phase of hemostasis, platelets adhere to the site of injury and release chemical signals that activate Factor X. Once activated, Factor X forms a complex with other clotting factors on the surface of activated platelets, leading to the conversion of prothrombin to thrombin. Thrombin then cleaves fibrinogen to form a mesh-like structure called fibrin, which reinforces the platelet plug and stabilizes the blood clot.

Applications

Factor X has a wide range of applications in both clinical and research settings. In the clinical setting, Factor X concentrate is used to treat individuals with Factor X deficiency or other bleeding disorders. It is also used in surgical procedures to promote blood clotting and prevent excessive bleeding. In research, Factor X is used to study the coagulation cascade and develop new therapies for bleeding disorders.

Clinical Significance

Dysregulation of Factor X can lead to several disease states, including thrombosis and bleeding disorders. Inherited mutations in Factor X can result in Factor X deficiency, a rare bleeding disorder characterized by prolonged bleeding times and abnormal blood clotting. Acquired conditions, such as liver disease or vitamin K deficiency, can also impair Factor X activation and lead to bleeding complications.

On the other hand, excessive activation of Factor X can result in thrombosis, a condition characterized by the formation of blood clots within the circulation. Thrombosis can lead to serious complications, such as heart attacks and strokes, if the clots block blood flow to vital organs. Patients with inherited or acquired prothrombotic conditions may require anticoagulant therapy to inhibit Factor X and prevent clot formation.

Conclusion

Factor X is a crucial enzyme in the coagulation cascade, playing a central role in the formation of blood clots. Its activation and regulation are tightly controlled to maintain hemostasis and prevent excessive clotting. Dysregulation of Factor X can lead to bleeding disorders or thrombotic complications, highlighting the importance of understanding its structure and function in health and disease. Further research on Factor X may lead to the development of novel therapeutic strategies for managing coagulation disorders and preventing thrombotic events.