F10

Official Full Name

coagulation factor X

Organism

Homo sapiens

GeneID

2159

Background

This gene encodes the vitamin K-dependent coagulation factor X of the blood coagulation cascade. This factor undergoes multiple processing steps before its preproprotein is converted to a mature two-chain form by the excision of the tripeptide RKR. Two chains of the factor are held together by 1 or more disulfide bonds; the light chain contains 2 EGF-like domains, while the heavy chain contains the catalytic domain which is structurally homologous to those of the other hemostatic serine proteases. The mature factor is activated by the cleavage of the activation peptide by factor IXa (in the intrisic pathway), or by factor VIIa (in the extrinsic pathway). The activated factor then converts prothrombin to thrombin in the presence of factor Va, Ca+2, and phospholipid during blood clotting. Mutations of this gene result in factor X deficiency, a hemorrhagic condition of variable severity. Alternative splicing results in multiple transcript variants encoding different isoforms that may undergo similar proteolytic processing to generate mature polypeptides. [provided by RefSeq, Aug 2015]

Synonyms

FX; FXA;

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Detailed Information

Coagulation Factor X Recent Research Progress

Functions

Coagulation factor is a general term for substances that are directly involved in blood clotting in plasma and tissues. Coagulation factor X (F10) is a plasma glycoprotein that plays an important role in the coagulation process. Its activated form, F10a can activate prothrombin to thrombin with the help of coagulation factors V, Ca²⁺ and phospholipids. In addition, blood coagulation factor X exerts different effects on adenovirus entry into human lymphocytes. Moreover, hemostatic system components, including factor X (F10), contribute to cancer progression.

Mechanism

Th Luxor's toxin contains an enzyme that activates F10 (RVV-X), which can directly activate F10 in the presence of Ca²⁺. The colony diffusion of tumor cells may be related to the activation of F10.It has been proposed that blood coagulation factors, principally factor X (F10), enhance the uptake of human adenovirus type 5 (Ad5) into cultured epithelial cells by bridging the viral hexon capsid protein and cell-surface heparan sulphate proteoglycans (HSPGs).Daudi, a B-cell line and Jurkat, a T-cell line, as well as primary peripheral blood lymphocytes (PBL) and HeLa epithelial cells using either replication-deficient Ad5, or a derivative in which the Ad5 fiber was replaced with that of another Ad type, Ad35, termed Ad5F35. PBL and NK92MI were resistant to Ad5 transduction. Transduction of Jurkat and Daudi cells by Ad5 was reduced by F10 but without discernible effects on cell-surface Ad5 binding. F10 cut down virus binding and transduction of all lymphoid cell lines by Ad5F35, as well as transduction of the T- and Natural Killer (NK)-cell populations of PBL. Flow cytometry analysis showed that all lymphoid cell lines were negative for HSPG components, in contrast to HeLa cells. F10 reduced transduction of an HSPG-negative mutant Chinese hamster ovary cell line (CHOpgsA745) by Ad5 and Ad5F35. These results point to fiber-dependent differences (Ad5 versus Ad35 fiber) in Ad binding and transduction of human lymphoid and epithelial cells in the presence of F10.

Figure 1.X-ray diffraction pattern of rivaroxaban and coagulation Xa factor (Xiong Gang ,2017)

Furthermore, expression of F10 was visualized in association with endothelial cells. In turn, colon cancer-associated macrophages were characterized by F10 presence. ISH studies revealed the presence of F10 mRNA in colon cancer cells indicating induced synthesis of these proteins. The localization of F10 in colon cancer cells indicates that it may contribute to anticoagulant events at the tumor site. Strong co-localization of F10 in cancer cells, and the presence of the mRNAs encoding the proteins, suggests their role in the tumor’s biology.

References:

Elsevier Ltd, et al. Co-localization of Protein Z, Protein Z-Dependent protease inhibitor and coagulation factor X in human colon cancer tissue: Implications for coagulation regulation on tumor cells. Thrombosis Research, 2012, e112-e118.
Findlay James S, et al. Blood Coagulation Factor X Exerts Differential Effects on Adenovirus Entry into Human Lymphocytes.Viruses, 2018, 10.3390/v10010020.
Suangding Wu, et al. Activation of coagulation factor X and inhibition of activated factor X,Journal of China university of Science and Technology ,2000, Vol.30,No.6.
Adrijana Leonardi, et al. Two coagulation factor X activators from Vipera a. ammodytes venom with potential to treat patients with dysfunctional factors IXa or VIIa, Toxicon, 2008, 628-637.

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