WordNet

be a contributing factor; "make things factor into a companys profitability"
any of the numbers (or symbols) that form a product when multiplied together
an independent variable in statistics
anything that contributes causally to a result; "a number of factors determined the outcome"
consider as relevant when making a decision; "You must factor in the recent developments" (同)factor in, factor out
resolve into factors; "a quantum computer can factor the number 15" (同)factor in, factor out
an event known to have happened or something known to have existed; "your fears have no basis in fact"; "how much of the story is fact and how much fiction is hard to tell"
a concept whose truth can be proved; "scientific hypotheses are not facts"
a piece of information about circumstances that exist or events that have occurred; "first you must collect all the facts of the case"
a statement or assertion of verified information about something that is the case or has happened; "he supported his argument with an impressive array of facts"

PrepTutorEJDIC

(…の)『要因』,(…を生み出す)要素《+『in』+『名』(do『ing』)》 / 囲数,約数 / 代理人,《おもに英》仲買人 / =factorize
〈C〉『事実』,実際にある(あった)事 / 〈U〉真相,真実(truth) / 《the~》(法律用語で)犯行
凝固,凝結
Virgin Islands

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/01/15 11:29:45」(JST)

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Factor VII (formerly known as proconvertin) is one of the proteins that causes blood to clot in the coagulation cascade. It is an enzyme (EC 3.4.21.21) of the serine protease class. A recombinant form of human factor VIIa (NovoSeven, eptacog alfa [activated]) 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 manufacturing by AryoGen Biopharma and since 2012 is available 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 most important substrates for FVIIa-TF are Factor X and Factor IX.

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 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,^[2] but its role in this setting is controversial with insufficient evidence to support its use outside of clinical trials.^[3] The first report of its use in hemorrhage was in an Israeli soldier with uncontrollable bleeding in 1999.^[4] Risks of its use include an increase in arterial thrombosis.^[3]

Recombinant human factor VII while initially looking promising in intracerebral hemorrhage falled to show benefit following further study and this is no longer recommended.^[5]^[6]

Interactions

Factor VII has been shown to interact with Tissue factor.^[7]^[8]

References

^ Banner, D. W.; d'Arcy, A.; Chène, C.; Winkler, F. K.; Guha, A.; Konigsberg, W. H.; Nemerson, Y.; Kirchhofer, D. (1996). "The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor". Nature 380 (6569): 41–46. doi:10.1038/380041a0. PMID 8598903. edit
^ Roberts H, Monroe D, White G (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.
^ ^a ^b Simpson, E; Lin, Y; Stanworth, S; Birchall, J; Doree, C; Hyde, C (2012 Mar 14). "Recombinant factor VIIa for the prevention and treatment of bleeding in patients without haemophilia.". Cochrane database of systematic reviews (Online) 3: CD005011. 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 S, Brun N, Begtrup K, Broderick J, Davis S, Diringer M, Skolnick B, 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, et al. (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. http://www.nejm.org/doi/full/10.1056/NEJMoa0707534.
^ Carlsson, Karin; Freskgård Per-Ola, Persson Egon, Carlsson Uno, Svensson Magdalena (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. (Germany) 270 (12): 2576–82. doi:10.1046/j.1432-1033.2003.03625.x. ISSN 0014-2956. 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. (ENGLAND) 285 (5): 2089–104. doi:10.1006/jmbi.1998.2452. ISSN 0022-2836. PMID 9925787.

External links

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

UpToDate Contents

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1. 非血友病患者における遺伝子組換え第VIIa凝固因子の治療使用 therapeutic uses of recombinant coagulation factor viia in non hemophiliacs
2. 血友病患者における第VIIIおよび第IX因子阻害物質 factor viii and factor ix inhibitors in patients with hemophilia
3. 外傷に伴う凝固障害 coagulopathy associated with trauma
4. 血漿分画製剤および組換えDNA産生凝固因子 plasma derivatives and recombinant dna produced coagulation factors
5. 先天性および後天性血小板機能障害 congenital and acquired disorders of platelet function

English Journal

The hypercoagulable profile of patients with stent thrombosis.

Loeffen R1, Godschalk TC2, van Oerle R1, Spronk HM1, Hackeng CM3, Ten Berg JM2, Ten Cate H1.
Heart (British Cardiac Society).Heart.2015 Jul 15;101(14):1126-32. doi: 10.1136/heartjnl-2014-306685. Epub 2015 May 21.
OBJECTIVE: Coronary stent thrombosis is a devastating complication after percutaneous coronary intervention (PCI). The mechanisms underlying stent thrombosis are multifactorial. Whether the coagulation system is involved in the pathophysiology of stent thrombosis is unclear. We hypothesised that thr
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Hemostatic resuscitation in postpartum hemorrhage - a supplement to surgery.

Ekelund K1, Hanke G1, Stensballe J2,3, Wikkelsøe A4, Albrechtsen CK1, Afshari A1.
Acta obstetricia et gynecologica Scandinavica.Acta Obstet Gynecol Scand.2015 Jul;94(7):680-92. doi: 10.1111/aogs.12607. Epub 2015 Mar 5.
BACKGROUND: Postpartum hemorrhage is a potentially life-threatening albeit preventable condition that persists as a leading cause of maternal death. Identification of safe and cost-effective hemostatic treatment options remains crucial as a supplement to surgery and uterotonic agents.OBJECTIVE: This
PMID 25660118

Factor VIIa for Annulus Rupture After Transcatheter Aortic Valve Replacement.

Keenan JE1, Vavalle JP2, Ganapathi AM1, Wang H1, Harrison JK2, Wang A2, Hughes GC3.
The Annals of thoracic surgery.Ann Thorac Surg.2015 Jul;100(1):313-5. doi: 10.1016/j.athoracsur.2014.09.063.
Over the last decade, transcatheter aortic valve replacement (TAVR) has emerged as an effective treatment for inoperable and selected high surgical-risk patients with aortic stenosis. However, management of procedural complications with TAVR represents a major challenge as most TAVR patients carry p
PMID 26140778

Japanese Journal

Reversal of Rivaroxaban-Induced Alterations on Hemostasis by Different Coagulation Factor Concentrates : In Vitro Studies With Steady and Circulating Human Blood

Circulation journal : official journal of the Japanese Circulation Society 79(2), 331-338, 2015-02
NAID 40020333930

血液凝固第VII 因子の構造と機能および臨床応用

日本血栓止血学会誌 26(5), 562-575, 2015
NAID 130005102999

A Synthetic Serine Protease Inhibitor, Nafamostat Mesilate, Is a Drug Potentially Applicable to the Treatment of Ebola Virus Disease

The Tohoku Journal of Experimental Medicine 237(1), 45-50, 2015
NAID 130005096764

「活性化第VII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, 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
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; • serine-type peptidase activity;
Cellular component	• extracellular region; • extracellular space; • endoplasmic reticulum lumen; • Golgi lumen; • plasma membrane;
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; • negative regulation of apoptotic process; • response to estrogen stimulus; • post-translational protein modification; • cellular protein metabolic process; • positive regulation of positive chemotaxis; • positive regulation of protein kinase B signaling cascade; • response to growth hormone stimulus;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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