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a coagulation factor formed in the kidney under the influence of vitamin K (同)cothromboplastin, stable_factor, factor_VII

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/19 23:59:41」(JST)

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Factor VII (EC 3.4.21.21, blood-coagulation factor VIIa, activated blood coagulation factor VII, formerly known as proconvertin) is one of the proteins that causes blood to clot in the coagulation cascade. It is an enzyme of the serine protease class. A recombinant form of human factor VIIa (eptacog alfa [activated], NovoSeven) has U.S. Food and Drug Administration approval for uncontrolled bleeding in hemophilia patients. It is sometimes used unlicensed in severe uncontrollable bleeding, although there have been safety concerns. A biosimilar form of recombinant activated factor VII (AryoSeven) is also available, but does not play any considerable role in the market.

Physiology

The main role of factor VII (FVII) is to initiate the process of coagulation in conjunction with tissue factor (TF/factor III). Tissue factor is found on the outside of blood vessels - normally not exposed to the bloodstream. Upon vessel injury, tissue factor is exposed to the blood and circulating factor VII. Once bound to TF, FVII is activated to FVIIa by different proteases, among which are thrombin (factor IIa), factor Xa, IXa, XIIa, and the FVIIa-TF complex itself. The complex of factor VIIa with TF catalyzes the conversion of factor IX and factor X into the active proteases, factor IXa and factor Xa, respectively.^[2]

The action of the factor is impeded by tissue factor pathway inhibitor (TFPI), which is released almost immediately after initiation of coagulation. Factor VII is vitamin K dependent; it is produced in the liver. Use of warfarin or similar anticoagulants decreases hepatic synthesis of FVII.

Genetics

The gene for factor VII is located on chromosome 13 (13q34).

Role in disease

Deficiency is rare (congenital proconvertin deficiency) and inherits recessively. Factor VII deficiency presents as a hemophilia-like bleeding disorder. It is treated with recombinant factor VIIa (NovoSeven or AryoSeven).

Medical uses

Recombinant factor VIIa, marketed under the trade names AryoSeven and NovoSeven, is used for people with hemophilia (with Factor VIII or IX deficiency) who have developed inhibitors against replacement coagulation factor.

It has also been used in the setting of uncontrollable hemorrhage,^[3]^[4] but its role in this setting is controversial with insufficient evidence to support its use outside of clinical trials.^[5] The first report of its use in hemorrhage was in an Israeli soldier with uncontrollable bleeding in 1999.^[6] Risks of its use include an increase in arterial thrombosis.^[5]

Recombinant human factor VII while initially looking promising in intracerebral hemorrhage failed to show benefit following further study and this is no longer recommended.^[7]^[8]

Interactions

Factor VII has been shown to interact with tissue factor.^[9]^[10]

References

^ Banner DW, D'Arcy A, Chène C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y, Kirchhofer D (1996). "The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor". Nature 380 (6569): 41–6. doi:10.1038/380041a0. PMID 8598903.
^ Wajima T, Isbister GK, Duffull SB (2009). "A comprehensive model for the humoral coagulation network in humans". Clin Pharmacol Ther 86 (3): 290–8. doi:10.1038/clpt.2009.87. PMID 19516255.
^ Roberts HR, Monroe DM, White GC (2004). "The use of recombinant factor VIIa in the treatment of bleeding disorders". Blood 104 (13): 3858–64. doi:10.1182/blood-2004-06-2223. PMID 15328151.
^ Uncontrolled Bleeding and Injury Lawsuit Claims
^ ^a ^b Simpson E, Lin Y, Stanworth S, Birchall J, Doree C, Hyde C (Mar 14, 2012). "Recombinant factor VIIa for the prevention and treatment of bleeding in patients without haemophilia.". Cochrane database of systematic reviews (Online) 3: CD005011. doi:10.1002/14651858.CD005011.pub4. PMID 22419303.
^ Kenet G, Walden R, Eldad A, Martinowitz U (1999). "Treatment of traumatic bleeding with recombinant factor VIIa". Lancet 354 (9193): 1879. doi:10.1016/S0140-6736(99)05155-7. PMID 10584732.
^ Mayer SA, Brun NC, Begtrup K, Broderick J, Davis S, Diringer MN, Skolnick BE, Steiner T (2005). "Recombinant activated factor VII for acute intracerebral hemorrhage". N. Engl. J. Med. 352 (8): 777–85. doi:10.1056/NEJMoa042991. PMID 15728810.
^ Mayer SA, Brun NC, Begtrup K, Broderick J, Davis S, Diringer MN, Skolnick BE, Steiner T (May 2008). "Efficacy and safety of recombinant activated factor VII for acute intracerebral hemorrhage". N. Engl. J. Med. 358 (20): 2127–37. doi:10.1056/NEJMoa0707534. PMID 18480205.
^ Carlsson K, Freskgård PO, Persson E, Carlsson U, Svensson M (Jun 2003). "Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor-factor VIIa-factor Xa-tissue factor pathway inhibitor". Eur. J. Biochem. 270 (12): 2576–82. doi:10.1046/j.1432-1033.2003.03625.x. PMID 12787023.
^ Zhang E, St Charles R, Tulinsky A (Feb 1999). "Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant". J. Mol. Biol. 285 (5): 2089–104. doi:10.1006/jmbi.1998.2452. PMID 9925787.

External links

Official website
The MEROPS online database for peptidases and their inhibitors: S01.215

Molecular and Cellular Biology portal

UpToDate Contents

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1. 抗リン脂質抗体症候群の治療 treatment of the antiphospholipid syndrome
2. 凝固検査の臨床使用 clinical use of coagulation tests

English Journal

Activation of a cryptic splice site in a potentially lethal coagulation defect accounts for a functional protein variant.

Cavallari N, Balestra D, Branchini A, Maestri I, Chuamsunrit A, Sasanakul W, Mariani G, Pagani F, Bernardi F, Pinotti M.SourceDepartment of Biochemistry and Molecular Biology, and LTTA, University of Ferrara, Italy.
Biochimica et biophysica acta.Biochim Biophys Acta.2012 Jul;1822(7):1109-13. Epub 2012 Mar 9.
Changes at the invariable donor splice site +1 guanine, relatively frequent in human genetic disease, are predicted to abrogate correct splicing, and thus are classified as null mutations. However, their ability to direct residual expression, which might have pathophysiological implications in sever
PMID 22426302

Bioconversion of car-3-ene by a dioxygenase of Pleurotus sapidus.

Lehnert N, Krings U, Sydes D, Wittig M, Berger RG.SourceInstitut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167 Hannover, Germany.
Journal of biotechnology.J Biotechnol.2012 Jun 30;159(4):329-35. Epub 2011 Jun 23.
Mycelium of the basidiomycete Pleurotus sapidus known to contain a novel dioxygenase was used for the bioconversion of car-3-ene [I]. After 4h of incubation 25.3mgL(-1) car-3-en-5-one [V], 5.4mgL(-1) car-3-en-2-one [VII], and 7.3mgL(-1) car-2-en-4-one [XV] accumulated as major oxidation products. Th
PMID 21723336

Japanese Journal

Activation of bovine factor VII (proconvertin) by factor XIIa (activated Hageman factor)

KISIEL W
Biochemistry 16, 4189-4194, 1977
NAID 80014863654

A clinical and family study of hereditary proconvertin (factor VII) deficiency

HALL CA.
Am J Med 37, 172-181, 1964
NAID 30008553521

「血液凝固因子」

Coagulation factor VII (serum prothrombin conversion accelerator)
	Anchoring of coagulation factor VIIa (PDB 1dan) to the membrane through its Gla domain
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1BF9, 1CVW, 1DAN, 1DVA, 1F7E, 1F7M, 1FAK, 1FF7, 1FFM, 1J9C, 1JBU, 1KLI, 1KLJ, 1NL8, 1O5D, 1QFK, 1W0Y, 1W2K, 1W7X, 1W8B, 1WQV, 1WSS, 1WTG, 1WUN, 1WV7, 1YGC, 1Z6J, 2A2Q, 2AEI, 2AER, 2B7D, 2B8O, 2BZ6, 2C4F, 2EC9, 2F9B, 2FIR, 2FLB, 2FLR, 2PUQ, 2ZP0, 2ZWL, 2ZZU, 3ELA, 3TH2, 3TH3, 3TH4, 4IBL, 4ISH, 4ISI, 4JYU, 4JYV, 4JZD, 4JZE, 4JZF, 4NA9, 4NG9, 4NGA, 4X8S, 4X8T, 4X8U, 4X8V, 4YT6, 4YT7
Identifiers
Symbols	F7 ; SPCA
External IDs	OMIM: 613878 MGI: 109325 HomoloGene: 7710 ChEMBL: 3991 GeneCards: F7 Gene
EC number	3.4.21.21
Gene ontology
Molecular function	• glycoprotein binding; • serine-type endopeptidase activity; • receptor binding; • calcium ion binding; • protein binding; • serine-type peptidase activity;
Cellular component	• extracellular region; • extracellular space; • endoplasmic reticulum lumen; • Golgi lumen; • plasma membrane; • vesicle;
Biological process	• positive regulation of leukocyte chemotaxis; • proteolysis; • blood coagulation; • blood coagulation, extrinsic pathway; • circadian rhythm; • positive regulation of platelet-derived growth factor receptor signaling pathway; • peptidyl-glutamic acid carboxylation; • positive regulation of blood coagulation; • positive regulation of cell migration; • organ regeneration; • response to vitamin K; • response to estrogen; • post-translational protein modification; • cellular protein metabolic process; • positive regulation of positive chemotaxis; • positive regulation of protein kinase B signaling; • response to growth hormone;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;

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英: coagulation factor (Z), clotting factor, blood coagulation factor, blood coagulation factors
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