Stuart factor

関

coagulation factors, factor X

WordNet

1. be a contributing factor; "make things factor into a companys profitability"
2. any of the numbers (or symbols) that form a product when multiplied together
3. an independent variable in statistics
4. anything that contributes causally to a result; "a number of factors determined the outcome"
5. consider as relevant when making a decision; "You must factor in the recent developments" (同)factor in, factor out
6. resolve into factors; "a quantum computer can factor the number 15" (同)factor in, factor out
7. 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"
8. a concept whose truth can be proved; "scientific hypotheses are not facts"
9. a piece of information about circumstances that exist or events that have occurred; "first you must collect all the facts of the case"
10. 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"
11. United States painter best known for his portraits of George Washington (1755-1828) (同)Gilbert Stuart, Gilbert Charles Stuart
12. a member of the royal family that ruled Scotland and England
13. the royal family that ruled Scotland from 1371-1714 and ruled England from 1603 to 1649 and again from 1660 to 1714

PrepTutorEJDIC

1. (…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
2. 〈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
3. (また Stewart)英国の王室の名

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/10/05 00:06:40」(JST)

wiki en

[Wiki en表示]

For other uses, see Factor X (disambiguation).

Coagulation factor X
PDB rendering based on 1c5m.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1C5M, 1EZQ, 1F0R, 1F0S, 1FAX, 1FJS, 1G2L, 1G2M, 1HCG, 1IOE, 1IQE, 1IQF, 1IQG, 1IQH, 1IQI, 1IQJ, 1IQK, 1IQL, 1IQM, 1IQN, 1KSN, 1LPG, 1LPK, 1LPZ, 1LQD, 1MQ5, 1MQ6, 1NFU, 1NFW, 1NFX, 1NFY, 1P0S, 1V3X, 1WU1, 1XKA, 1XKB, 1Z6E, 2BMG, 2BOH, 2BOK, 2BQ6, 2BQ7, 2BQW, 2CJI, 2D1J, 2EI6, 2EI7, 2EI8, 2FZZ, 2G00, 2GD4, 2H9E, 2J2U, 2J34, 2J38, 2J4I, 2J94, 2J95, 2JKH, 2P16, 2P3F, 2P3T, 2P3U, 2P93, 2P94, 2P95, 2PHB, 2PR3, 2Q1J, 2RA0, 2UWL, 2UWO, 2UWP, 2VH0, 2VH6, 2VVC, 2VVU, 2VVV, 2VWL, 2VWM, 2VWN, 2VWO, 2W26, 2W3I, 2W3K, 2WYG, 2WYJ, 2XBV, 2XBW, 2XBX, 2XBY, 2XC0, 2XC4, 2XC5, 2Y5F, 2Y5G, 2Y5H, 2Y7X, 2Y7Z, 2Y80, 2Y81, 2Y82, 3CEN, 3CS7, 3ENS, 3FFG, 3HPT, 3IIT, 3K9X, 3KL6, 3KQB, 3KQC, 3KQD, 3KQE, 3LIW, 3M36, 3M37, 3Q3K, 3SW2, 3TK5, 3TK6, 4A7I
Identifiers
Symbols	F10; FX; FXA
External IDs	OMIM: 613872 MGI: 103107 HomoloGene: 30976 ChEMBL: 244 GeneCards: F10 Gene
EC number	3.4.21.6
Gene Ontology Molecular function • serine-type endopeptidase activity • serine-type endopeptidase activity • calcium ion binding • protein binding • phospholipid binding Cellular component • extracellular region • extracellular region • endoplasmic reticulum lumen • microsome • Golgi lumen • plasma membrane • intrinsic to external side of plasma membrane Biological process • proteolysis • blood coagulation • blood coagulation • blood coagulation, intrinsic pathway • blood coagulation, extrinsic pathway • peptidyl-glutamic acid carboxylation • positive regulation of cell migration • post-translational protein modification • cellular protein metabolic process • positive regulation of protein kinase B signaling cascade Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2159	14058
Ensembl	ENSG00000126218	ENSMUSG00000031444
UniProt	P00742	O88947
RefSeq (mRNA)	NM_000504.3	NM_001242368.1
RefSeq (protein)	NP_000495.1	NP_001229297.1
Location (UCSC)	Chr 13: 113.78 – 113.8 Mb	Chr 8: 13.04 – 13.06 Mb
PubMed search	[1]	[2]

Factor X, also known by the eponym Stuart-Prower factor or as prothrombinase, is an enzyme (EC 3.4.21.6) of the coagulation cascade. It is a serine endopeptidase (protease group S1).

Physiology

Factor X is synthesized in the liver and requires vitamin K for its synthesis.

Factor X is activated into factor Xa by both factor IX (with its cofactor, factor VIII in a complex known as intrinsic Xase) and factor VII with its cofactor, tissue factor (a complex known as extrinsic Xase). It is therefore the first member of the final common pathway or thrombin pathway.

It acts by cleaving prothrombin in two places (an arg-thr and then an arg-ile bond), which yields the active thrombin. This process is optimized when factor Xa is complexed with activated co-factor V in the prothrombinase complex.

Factor Xa is inactivated by protein Z-dependent protease inhibitor (ZPI), a serine protease inhibitor (serpin). The affinity of this protein for factor Xa is increased 1000-fold by the presence of protein Z, while it does not require protein Z for inactivation of factor XI. Defects in protein Z lead to increased factor Xa activity and a propensity for thrombosis.

The half life of factor X is 40-45 hours.

Structure of Factor Xa

The first crystal structure of human factor Xa was deposited in May 1993. Till now total 191 crystal structures of factor Xa with various inhibitors have been deposited in the protein data bank. The active site of factor Xa is divided into four sub pockets as S1, S2, S3 and S4. The S1 subpocket determines the major component of selectivity and binding. The S2 sub-pocket is small, shallow and not well defined. It merges with the S4 subpocket. The S3 sub-pocket is located on the rim of the S1 pocket and is quite exposed to solvent. The S4 sub-pocket has 3 ligand binding domains, namely the “hydrophobic box”, the “cationic hole” and the water site. Factor Xa inhibitors generally bind in an L-shaped conformation, where one group of the ligand occupies the anionic S1 pocket lined by residues Asp189, Ser195, and Tyr228, and another group of the ligand occupies the aromatic S4 pocket lined by residues Tyr99, Phe174, and Trp215. Typically, a fairly rigid linker group bridges these two interaction sites.

Genetics

The human factor X gene is located on the thirteenth chromosome (13q34).

Role in disease

Inborn deficiency of factor X is very rare (1:500,000), and may present with epistaxis (nosebleeds), hemarthrosis (bleeding into joints) and gastrointestinal blood loss. Apart from congenital deficiency, low factor X levels may occur occasionally in a number of disease states. For example, factor X deficiency may be seen in amyloidosis, where factor X is adsorbed to the amyloid fibrils in the vasculature.

Deficiency of vitamin K or antagonism by warfarin (or similar medication) leads to the production of an inactive factor X. In warfarin therapy, this is desirable to prevent thrombosis. As of late 2007, four out of five emerging anti-coagulation therapeutics targeted this enzyme.

Inhibiting Factor Xa would offer an alternate method for anticoagulation. Direct Xa inhibitors are popular anticoagulants.

Laboratory findings in various platelet and coagulation disorders

Condition	Prothrombin time	Partial thromboplastin time	Bleeding time	Platelet count
Vitamin K deficiency or warfarin	Prolonged	Normal or mildly prolonged	Unaffected	Unaffected
Disseminated intravascular coagulation	Prolonged	Prolonged	Prolonged	Decreased
Von Willebrand disease	Unaffected	Prolonged	Prolonged	Decreased and or Rejected
Hemophilia	Unaffected	Prolonged	Unaffected	Unaffected
Aspirin	Unaffected	Unaffected	Prolonged	Unaffected
Thrombocytopenia	Unaffected	Unaffected	Prolonged	Decreased
Liver failure, early	Prolonged	Unaffected	Unaffected	Unaffected
Liver failure, end-stage	Prolonged	Prolonged	Prolonged	Decreased
Uremia	Unaffected	Unaffected	Prolonged	Unaffected
Congenital afibrinogenemia	Prolonged	Prolonged	Prolonged	Unaffected
Factor V deficiency	Prolonged	Prolonged	Unaffected	Unaffected
Factor X deficiency as seen in amyloid purpura	Prolonged	Prolonged	Unaffected	Unaffected
Glanzmann's thrombasthenia	Unaffected	Unaffected	Prolonged	Unaffected
Bernard-Soulier syndrome	Unaffected	Unaffected	Prolonged	Decreased or unaffected
Factor XII deficiency	Unaffected	Prolonged	Unaffected	Unaffected

Therapeutic use

Factor X is part of fresh frozen plasma and the prothrombinase complex. The only commercially available concentrate is 'Factor X P Behring' manufactured by CSL Behring.

Use in Biochemistry

The Factor Xa protease can be used in biochemistry to cleave off protein tags that improve expression or purification of a protein of interest. Its preferred cleavage site (after the arginine in ile-glu/asp-gly-arg) can easily be engineered between a tag sequence and the protein of interest. After expression and purification, the tag is then proteolytically removed by Factor Xa.

Factor Xa

Blood coagulation pathways in vivo showing the central role played by thrombin

Factor Xa is the activated form of the coagulation factor thrombokinase, known eponymously as Stuart-Prower factor. Factor X is an enzyme, a serine endopeptidase, which plays a key role at several stages of the coagulation system. Factor X is synthesized in the liver. The most commonly used anticoagulants in clinical practice, warfarin and the heparin series of anticoagulants and fondaparinux, act to inhibit the action of Factor Xa in various degrees.

Traditional models of coagulation developed in the 1960’s envisaged two separate cascades, the extrinsic (tissue factor (TF)) pathway and the intrinsic pathway. These pathways converge to a common point, the formation of the Factor Xa/Va complex which together with calcium and bound on a phospholipids surface generate thrombin (Factor IIa) from prothrombin (Factor II).

A new model, the cell-based model of anticoagulation appears to explain more fully the steps in coagulation. This model has three stages: 1) initiation of coagulation on TF-bearing cells, 2) amplification of the procoagulant signal by thrombin generated on the TF-bearing cell and 3) propagation of thrombin generation on the platelet surface. Factor Xa plays a key role in all three of these stages.

In stage 1, Factor VII binds to the transmembrane protein TF on the surface of cells and is converted to Factor VIIa. The result is a Factor VIIa/TF complex which catalyzes the activation of Factor X and Factor IX. Factor Xa formed on the surface of the TF-bearing cell interacts with Factor Va to form the prothrombinase complex which generates small amounts of thrombin on the surface of TF-bearing cells.

In stage 2, the amplification stage, if enough thrombin has been generated, then activation of platelets and platelet associated cofactors occurs.

In stage 3, thrombin generation, Factor XIa activates free Factor IX on the surface of activated platelets. The activated Factor IXa with Factor VIIIa forms the "tenase" complex. This "tenase" complex activates more Factor X, which in turn forms new prothrombinase complexes with Factor Va. Factor Xa is the prime component of the prothrombinase complex which converts large amounts of prothrombin—the "thrombin burst". Each molecule of Factor Xa can generate 1000 molecules of thrombin. This large burst of thrombin is responsible for fibrin polymerization to form a thrombus.

Inhibition of the synthesis or activity of Factor X is the mechanism of action for many anticoagulants in use today. Warfarin, a synthetic derivative of coumarin, is the most widely used oral anticoagulant in the US. In some European countries, other coumarin derivatives (phenprocoumon and acenocoumarol) are used. These agents are vitamin K antagonists (VKA). Vitamin K is essential for the hepatic synthesis of Factors II (prothrombin), VII, IX and X.

Heparin (unfractionated heparin) and its derivatives low molecular weight heparin (LMWH) bind to a plasma cofactor, antithrombin (AT) to inactivate several coagulation factors IIa, Xa, XIa and XIIa. The affinity of unfractionated heparin and the various LMWHs for Factor Xa varies considerably. The efficacy of heparin-based anticoagulants increases as selectivity for Factor Xa increases. LMWH shows increased inactivation of Factor Xa compared to unfractionated heparin, and fondaparinux, an agent based on the critical pentasacharide sequence of heparin, shows more selectivity than LMWH. This inactivation of Factor Xa by heparins is termed "indirect" since it relies on the presence of AT and not a direct interaction with Factor Xa.

Recently a new series of specific, direct acting inhibitors of Factor Xa has been developed. These include the drugs rivaroxaban, apixaban, betrixaban, LY517717, darexaban (YM150), edoxaban and 813893. These agents have several theoretical advantages over current therapy. They may be given orally. They have rapid onset of action. And they may be more effective against Factor Xa in that they inhibit both free Factor Xa and Factor Xa in the prothrombinase complex.

History

American and British scientists described deficiency of factor X independently in 1953 and 1956, respectively. As with some other coagulation factors, the factor was initially named after these patients, a Mr Rufus Stuart (1921) and a Miss Audrey Prower (1934).

External links

• The MEROPS online database for peptidases and their inhibitors: S01.216
• med/3495 at eMedicine
• Factor X deficiency

Interactions

Factor X has been shown to interact with Tissue factor pathway inhibitor.

References

Further reading

• Cooper DN, Millar DS, Wacey A, et al. (1997). "Inherited factor X deficiency: molecular genetics and pathophysiology". Thromb. Haemost. 78 (1): 161–72. PMID 9198147. 
• Hassan HJ, Leonardi A, Chelucci C, et al. (1990). "Blood coagulation factors in human embryonic-fetal development: preferential expression of the FVII/tissue factor pathway". Blood 76 (6): 1158–64. PMID 1698100. 
• Messier TL, Pittman DD, Long GL, et al. (1991). "Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X". Gene 99 (2): 291–4. doi:10.1016/0378-1119(91)90141-W. PMID 1902434. 
• Krishnaswamy S (1990). "Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation". J. Biol. Chem. 265 (7): 3708–18. PMID 2303476. 
• España F, Berrettini M, Griffin JH (1989). "Purification and characterization of plasma protein C inhibitor". Thromb. Res. 55 (3): 369–84. doi:10.1016/0049-3848(89)90069-8. PMID 2551064. 
• Fung MR, Hay CW, MacGillivray RT (1985). "Characterization of an almost full-length cDNA coding for human blood coagulation factor X". Proc. Natl. Acad. Sci. U.S.A. 82 (11): 3591–5. doi:10.1073/pnas.82.11.3591. PMC 397831. PMID 2582420. //www.ncbi.nlm.nih.gov/pmc/articles/PMC397831/. 
• Jagadeeswaran P, Reddy SV, Rao KJ, et al. (1990). "Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X". Gene 84 (2): 517–9. doi:10.1016/0378-1119(89)90529-5. PMID 2612918. 
• Reddy SV, Zhou ZQ, Rao KJ, et al. (1989). "Molecular characterization of human factor XSan Antonio". Blood 74 (5): 1486–90. PMID 2790181. 
• Kaul RK, Hildebrand B, Roberts S, Jagadeeswaran P (1986). "Isolation and characterization of human blood-coagulation factor X cDNA". Gene 41 (2–3): 311–4. doi:10.1016/0378-1119(86)90112-5. PMID 3011603. 
• Broze GJ, Warren LA, Novotny WF, et al. (1988). "The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: insight into its possible mechanism of action". Blood 71 (2): 335–43. PMID 3422166. 
• Gilgenkrantz S, Briquel ME, André E, et al. (1986). "Structural genes of coagulation factors VII and X located on 13q34". Ann. Genet. 29 (1): 32–5. PMID 3487272. 
• Leytus SP, Foster DC, Kurachi K, Davie EW (1986). "Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C". Biochemistry 25 (18): 5098–102. doi:10.1021/bi00366a018. PMID 3768336. 
• Leytus SP, Chung DW, Kisiel W, et al. (1984). "Characterization of a cDNA coding for human factor X". Proc. Natl. Acad. Sci. U.S.A. 81 (12): 3699–702. doi:10.1073/pnas.81.12.3699. PMC 345286. PMID 6587384. //www.ncbi.nlm.nih.gov/pmc/articles/PMC345286/. 
• McMullen BA, Fujikawa K, Kisiel W, et al. (1983). "Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid". Biochemistry 22 (12): 2875–84. doi:10.1021/bi00281a016. PMID 6871167. 
• Marchetti G, Castaman G, Pinotti M, et al. (1995). "Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain". Br. J. Haematol. 90 (4): 910–5. doi:10.1111/j.1365-2141.1995.tb05214.x. PMID 7669671. 
• Morgenstern KA, Sprecher C, Holth L, et al. (1994). "Complementary DNA cloning and kinetic characterization of a novel intracellular serine proteinase inhibitor: mechanism of action with trypsin and factor Xa as model proteinases". Biochemistry 33 (11): 3432–41. doi:10.1021/bi00177a037. PMID 8136380. 
• Heeb MJ, Rosing J, Bakker HM, et al. (1994). "Protein S binds to and inhibits factor Xa". Proc. Natl. Acad. Sci. U.S.A. 91 (7): 2728–32. doi:10.1073/pnas.91.7.2728. PMC 43443. PMID 8146182. //www.ncbi.nlm.nih.gov/pmc/articles/PMC43443/. 
• Inoue K, Morita T (1993). "Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X". Eur. J. Biochem. 218 (1): 153–63. doi:10.1111/j.1432-1033.1993.tb18361.x. PMID 8243461. 
• Padmanabhan K, Padmanabhan KP, Tulinsky A, et al. (1993). "Structure of human des(1-45) factor Xa at 2.2 A resolution". J. Mol. Biol. 232 (3): 947–66. doi:10.1006/jmbi.1993.1441. PMID 8355279. 
• Sinha U, Wolf DL (1993). "Carbohydrate residues modulate the activation of coagulation factor X". J. Biol. Chem. 268 (5): 3048–51. PMID 8428982. 

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

• 1. 凝固検査の臨床使用clinical use of coagulation tests [show details]
  …of 2 to 3 corresponds to a chromogenic factor X assay of approximately 20 to 30 percent. Of note, the chromogenic factor X assay is different from the anti-factor Xa activity assay used to monitor heparins …
• 2. 稀な遺伝性凝固異常rare inherited coagulation disorders [show details]
  …have been reported . Factor X deficiency (F10D; OMIM 227600) – Approximately three-fourths of patients have missense mutations that result in low but measurable levels of factor X activity . Factor VII …
• 3. 止血の概要overview of hemostasis [show details]
  …VIIa) as the protease, tissue factor as the cofactor, and factor X (Stuart factor) as the substrate . Tissue factor/FVIIa activate both factor X and factor IX . Intrinsic X-ase (ten-ase) – Consists of …
• 4. 直接経口抗凝固薬（DOAC）と非経口直接作用型抗凝固薬：用量および副作用direct oral anticoagulants doacs and parenteral direct acting anticoagulants dosing and adverse effects [show details]
  …because one molecule of factor Xa can cleave over 1000 molecules of prothrombin to thrombin . Direct factor Xa inhibitors bind to the active site of factor Xa and inhibit factor Xa activity without a requirement …
• 5. ヘパリンおよびLMWヘパリン：用量および副作用heparin and lmw heparin dosing and adverse effects [show details]
  …units/mL by chromogenic anti-factor Xa assay) for each batch of thromboplastin reagent (for the aPTT) or anti-factor Xa assay used . Exceptions to the use of the aPTT or anti-factor Xa activity for monitoring …

English Journal

• Caffeine supplementation and peak anaerobic power output.

• Glaister M1, Muniz-Pumares D, Patterson SD, Foley P, McInnes G.
• European journal of sport science.Eur J Sport Sci.2015 Aug;15(5):400-6. doi: 10.1080/17461391.2014.962619. Epub 2014 Oct 2.
• The aim of this study was to investigate the effects of caffeine supplementation on peak anaerobic power output (Wmax). Using a counterbalanced, randomised, double-blind, placebo-controlled design, 14 well-trained men completed three trials of a protocol consisting of a series of 6-s cycle ergometer
• PMID 25275888

• Heparin-Calibrated Chromogenic Anti-Xa Activity Measurements in Patients Receiving Rivaroxaban: Can This Test Be Used to Quantify Drug Level?

• Gosselin RC1, Francart SJ2, Hawes EM2, Moll S3, Dager WE1, Adcock DM4.
• The Annals of pharmacotherapy.Ann Pharmacother.2015 Jul;49(7):777-83. doi: 10.1177/1060028015578451. Epub 2015 Apr 8.
• BACKGROUND: Determination of plasma rivaroxaban concentration may be necessary in certain clinical situations. Rivaroxaban concentration can be accurately and rapidly determined using a chromogenic anti-activated factor X (factor Xa) assay with specific drug calibrator material. However, there are c
• PMID 25855705

• Added value of semi-quantitative breast-specific gamma imaging in the work-up of suspicious breast lesions compared to mammography, ultrasound and 3-T MRI.

• Meissnitzer T1, Seymer A2, Keinrath P3, Holzmannhofer J3, Pirich C3, Hergan K1, Meissnitzer MW1.
• The British journal of radiology.Br J Radiol.2015 Jul;88(1051):20150147. doi: 10.1259/bjr.20150147. Epub 2015 Apr 17.
• OBJECTIVE: To prospectively analyse the diagnostic value of semi-quantitative breast-specific gamma imaging (BSGI) in the work-up of suspicious breast lesions compared with that of mammography (MG), breast ultrasound and MRI of the breast.METHODS: Within a 15-month period, 67 patients with 92 breast
• PMID 25882690

Related Links

• Stuart factor - definition of Stuart factor by Medical dictionary

Stu·art factor (stōō′ərt) or Stuart-Prow·er factor (-prou′ər) n. See prothrombinase. factor X A vitamin K-dependent enzyme which is the key protein in all—intrinsic, extrinsic, and common—coagulation pathways, converting prothrombin ...

• Stuart-Prower factor - definition of Stuart-Prower factor by ...

factor [fak´ter] an agent or element that contributes to the production of a result. accelerator factor factor V, one of the coagulation factors. factor I see coagulation factors. factor II see coagulation factors. factor III see coagulation ...

---

★リンクテーブル★

リンク元	「血液凝固因子」
関連記事	「fact」「factor」「Stuart」

「血液凝固因子」

　　[★]

英

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

関

ビタミンK

血液凝固因子

• 第I因子
• 第II因子
• 第III因子
• 第IV因子
• 第V因子
• 第VII因子
• 第VIII因子
• 第IX因子
• 第X因子
• 第XI因子
• 第XII因子
• 第XIII因子

表

• PT.261

型	名称	同義語	分子量 (kDa)	血漿中濃度 (μg/ml)	半減期 (day)
内因系のプロ酵素	XII	Hageman因子	80	29	2
	プレカリクレイン	Fletcher因子	88	45
	XI	PTA	160	4	2.5
ビタミンK依存	VII	proconvertin	50	0.5	0.2
凝固プロ酵素	IX	Christmas因子	57	4	1
	X	Stuart因子	57	8	1.5
	II	プロトロンビン	70	150	3
補助因子	III	組織因子		0
	血小板ホスホリピド
	高分子量キニノゲン		120	70
	V	proaccelerin	330	7	1.5
	VIII	抗血友病因子			0.5
フィブリン堆積因子	I	フィブリノゲン	340	2500	4.5
	XIII	フィブリン安定因子	320	8	7
抑制物質	アンチトロンビンIII		58	150	2.5

• 標準血液病学 p.217

15種類ある

凝固因子	慣用語・同義語	ビタミンK依存	血液中半減期(hr)	産生器官	染色体座乗部位
I	fibrinogen		100-150	肝臓	4q26
II	prothronbin	○	50-80	肝臓	11p141-q12
III	tissue thromboplastin			体の各組織	1pter-p21
IV	calcium ion			肝臓
V	labile factor/proaccelerin		24	肝臓	1q21-q25
VII	stable factor/proconvertin	○	6	肝臓	13q34
VIII	antihemophilic factor		12	細網系?	xq28
IX	Christmas factor	○	24	肝臓	xq26.3-q27.2
X	Stuart factor	○	25-60	肝臓	13q34
XI	plasma thromboplastin antecedent		40-80	肝臓	4q35
XII	Hageman factor		50-70	肝臓	5q33-qter
XIII	fibrin stabilizing factor		150	肝臓	6p24-p21.3
prekallikrein	Fletcher factor		35	肝臓	4q35
hight molecular weight kininogen	Fitzgerold factor		150	肝臓	3q26-qter
von Willebrand factor			24	血管内皮 血小板 糸球体	12pter-p12

産生部位

• ほとんどが肝臓
• 例外：

• 第III因子(F III)：組織トロンボプラスチン：組織
• 第VIII因子(F VIII)：組織トロンボプラスチン：細網組織？

臨床関連

• ビタミンK欠乏
• 妊娠により第XI因子、第XIII因子を除き、血液凝固因子の濃度が上昇する

-凝固因子

「fact」

　　[★]

• n.

• 事実、現状、実際、実態

関

actual、actually、in fact、in practice、indeed、practically

　 　 　 　 　

「factor」

　　[★]

• n.

• 因子、要因、要素、ファクター

関

element、elementary、factorial、parameter

　 　 　 　 　 　 　

「Stuart」

　　[★]

スチュワート