coagulation factor X

• 凝固第X因子

関

blood coagulation factor X、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. the 24th letter of the Roman alphabet (同)x, ex

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. Christ / Christian
4. 凝固,凝結
5. x-axis

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/31 14:59:43」(JST)

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[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, 1FXY, 1G2L, 1G2M, 1HCG, 1IOE, 1IQE, 1IQF, 1IQG, 1IQH, 1IQI, 1IQJ, 1IQK, 1IQL, 1IQM, 1IQN, 1KSN, 1LPG, 1LPK, 1LPZ, 1LQD, 1MQ5, 1MQ6, 1MSX, 1NFU, 1NFW, 1NFX, 1NFY, 1NL8, 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, 4BTI, 4BTT, 4BTU
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 • calcium ion binding • protein binding • phospholipid binding Cellular component • extracellular region • endoplasmic reticulum lumen • Golgi lumen • plasma membrane • intrinsic component of external side of plasma membrane Biological process • proteolysis • 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 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	NM_001242368
RefSeq (protein)	NP_000495	NP_001229297
Location (UCSC)	Chr 13: 113.12 – 113.15 Mb	Chr 8: 13.04 – 13.06 Mb
PubMed search	[1]	[2]

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

Physiology

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

Factor X is activated, by hydrolysis, 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. To date, 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 three ligand binding domains: 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 (V - T)

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 or unaffected	Prolonged	Unaffected
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
C1INH deficiency	Unaffected	Shortened	Unaffected	Unaffected

Therapeutic use

Factor X is part of fresh frozen plasma and the prothrombinase complex. There are two commercially available Factor X concentrates: "Factor X P Behring" manufactured by CSL Behring, and "Coagadex" produced by Bio Products Laboratory and approved for use in the United States by the FDA in October 2015.

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 the sequence Ile-Glu/Asp-Gly-Arg, IEGR or IDGR) 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 1960s 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, so-called vitamin K antagonists (VKA), inhibit the vitamin K-dependent carboxylation of Factors II (prothrombin), VII, IX, X in the hepatocyte. This carboxylation after the translation is essential for the physiological activity.

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).

Interactions

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

References

External links

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

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. 
• 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. 
• 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. 
• 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

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• 1. 止血の概要 overview of hemostasis
• 2. 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
• 3. 肝臓の合成能の検査（アルブミン、凝固因子、プロトロンビン時間など） tests of the livers biosynthetic capacity eg albumin coagulation factors prothrombin time
• 4. 凝固検査の臨床使用 clinical use of coagulation tests
• 5. 後天性の凝固因子阻害物質 acquired inhibitors of coagulation

English Journal

• The pharmacokinetics of edoxaban for the prevention and treatment of venous thromboembolism.

• Escolar G, Diaz-Ricart M, Arellano-Rodrigo E, Galán AM.Author information Universitat de Barcelona, Hematologist, Hospital Clinic, Servicio de Hemoterapia y Hemostasia , Villarroel 170, 08036 Barcelona , Spain 34 93 227 54 00 Ext: 2571 ; 34 93 227 93 69 ; gescolar@clinic.ub.es.AbstractIntroduction: Thromboembolic diseases will become the most important contributors to mortality and morbidity for modern societies. Current antithrombotic strategies using heparins or vitamin K antagonists are inconvenient, with limitations and inherent side effects. A series of new oral anticoagulants with powerful and reliable antithrombotic actions have been developed in the last decade. Areas covered: Edoxaban is a direct and specific inhibitor of activated factor X, delivered orally. This article reviews literature from PubMed and articles referenced within. The text explores the pharmacological aspects of its antithrombotic action. Pharmacokinetics, metabolism and drug interactions are examined. The review places the results of recent clinical trials that have evaluated the antithrombotic potential of edoxaban versus standard antithrombotic therapies in the prophylaxis and treatment of venous thromboembolism into perspective. The possible relationship between the pharmacokinetic profile of edoxaban and the favorable results in clinical trials is discussed. Expert opinion: Edoxaban is perceived as a major advance, compared to vitamin K antagonists, in the prevention and treatment of thromboembolic disease given its favorable efficacy, safety, pharmacokinetic profile and renal clearance. The results of ongoing large international trials exploring the prevention of thrombotic complications in patients in different clinical settings should ensure the approval of edoxaban to treat new indications.
• Expert opinion on drug metabolism & toxicology.Expert Opin Drug Metab Toxicol.2014 Mar;10(3):445-58. doi: 10.1517/17425255.2014.882897. Epub 2014 Jan 28.
• Introduction: Thromboembolic diseases will become the most important contributors to mortality and morbidity for modern societies. Current antithrombotic strategies using heparins or vitamin K antagonists are inconvenient, with limitations and inherent side effects. A series of new oral anticoagulan
• PMID 24471416

• MAX mutations status in Swedish patients with pheochromocytoma and paraganglioma tumours.

• Crona J, Maharjan R, Delgado Verdugo A, Stålberg P, Granberg D, Hellman P, Björklund P.Author information Department of Surgical, Uppsala University, Akademiska sjukhuset, ing 70, 3tr, FOA2, 75185, Uppsala, Sweden, joakim.crona@surgsci.uu.se.AbstractPheochromocytoma (PCC) and Paraganglioma are rare tumours originating from neuroendocrine cells. Up to 60 % of cases have either germline or somatic mutation in one of eleven described susceptibility loci, SDHA, SDHB, SDHC, SDHD, SDHAF2, VHL, EPAS1, RET, NF1, TMEM127 and MYC associated factor-X (MAX). Recently, germline mutations in MAX were found to confer susceptibility to PCC and paraganglioma (PGL). A subsequent multicentre study found about 1 % of PCCs and PGLs to have germline or somatic mutations in MAX. However, there has been no study investigating the frequency of MAX mutations in a Scandinavian cohort. We analysed tumour specimens from 63 patients with PCC and PGL treated at Uppsala University hospital, Sweden, for re-sequencing of MAX using automated Sanger sequencing. Our results show that 0 % (0/63) of tumours had mutations in MAX. Allele frequencies of known single nucleotide polymorphisms rs4902359, rs45440292, rs1957948 and rs1957949 corresponded to those available in the Single Nucleotide Polymorphism Database. We conclude that MAX mutations remain unusual events and targeted genetic screening should be considered after more common genetic events have been excluded.
• Familial cancer.Fam Cancer.2014 Mar;13(1):121-5. doi: 10.1007/s10689-013-9666-3.
• Pheochromocytoma (PCC) and Paraganglioma are rare tumours originating from neuroendocrine cells. Up to 60 % of cases have either germline or somatic mutation in one of eleven described susceptibility loci, SDHA, SDHB, SDHC, SDHD, SDHAF2, VHL, EPAS1, RET, NF1, TMEM127 and MYC associated factor-X (MA
• PMID 23743562

• Calnexin silencing in mouse neonatal cardiomyocytes induces Ca2+ cycling defects, ER stress, and apoptosis.

• Bousette N, Abbasi C, Chis R, Gramolini AO.Author information Department of Physiology, University of Toronto, Toronto, Ontario, Canada; Heart and Stroke/Richard Lewar Centre of Excellence, University of Toronto, Toronto, Ontario, Canada.AbstractCalnexin (CNX) is an endoplasmic reticulum (ER) quality control chaperone that has been implicated in ER stress. ER stress is a prominent pathological feature of various pathologic conditions, including cardiovascular diseases. However, the role of CNX and ER stress has not been studied in the heart. In the present study, we aimed to characterize the role of CNX in cardiomyocyte physiology with respect to ER stress, apoptosis, and cardiomyocyte Ca(2+) cycling. We demonstrated significantly decreased CNX mRNA and protein levels by LentiVector mediated transduction of targeting shRNAs. CNX silenced cardiomyocytes exhibited ER stress as evidenced by increased GRP78 and ATF6 protein levels, increased levels of spliced XBP1 mRNA, ASK-1, ERO1a, and CHOP mRNA levels. CNX silencing also led to significant activation of caspases-3 and -9. This activation of caspases was associated with hallmark morphological features of apoptosis including loss of sarcomeric organization and nuclear integrity. Ca(2+) imaging in live cells showed that CNX silencing resulted in Ca(2+) transients with significantly larger amplitudes but decreased frequency and Ca(2+) uptake rates in the basal state. Interestingly, 5 mM caffeine stimulated Ca(2+) transients were similar between control and CNX silenced cardiomyocytes. Finally, we demonstrated that CNX silencing induced the expression of the L-type voltage dependent calcium channel (CAV1.2) but reduced the expression of the sarcoplasmic reticulum ATPase (SERCA2a). In conclusion, this is the first study to demonstrate CNX has a specific role in cardiomyocyte viability and Ca(2+) cycling through its effects on ER stress, apoptosis and Ca(2+) channel expression.
• Journal of cellular physiology.J Cell Physiol.2014 Mar;229(3):374-83. doi: 10.1002/jcp.24459.
• Calnexin (CNX) is an endoplasmic reticulum (ER) quality control chaperone that has been implicated in ER stress. ER stress is a prominent pathological feature of various pathologic conditions, including cardiovascular diseases. However, the role of CNX and ER stress has not been studied in the heart
• PMID 24037923

Japanese Journal

• 経験 全自動血液凝固分析装置COAGTRON-350におけるBerichrom F？？を用いた血液凝固第？？因子活性測定条件の検討

• 菅野 信子,金子 誠,田辺 久美子 他
• 臨床病理 : 日本臨床検査医学会誌 60(12), 1131-1138, 2012-12-00
• NAID 40019559597

• Impaired dimer assembly and decreased stability of naturally recurring R260C mutant A subunit for coagulation factor ？

• Maeda Shoko,Zhang Wei Guang,Souri Masayoshi 他
• The journal of biochemistry 152(5), 471-478, 2012-11-00
• NAID 40019507425

• Stable complex formation between serine protease inhibitor and zymogen : coagulation factor Χ cleaves the Arg393-Ser394 bond in a reactive centre loop of antithrombin in the presence of heparin

• Nakatomi Yasushi,Tsuji Manami,Gokudan Soutaro 他
• The journal of biochemistry 152(5), 463-470, 2012-11-00
• NAID 40019507414

Related Links

• Factor X - Wikipedia, the free encyclopedia

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).

• Coagulation factor X precursor - Homo sapiens (Human)

Function. Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. Catalytic activity. Selective cleavage of Arg-|-Thr and then Arg-|-Ile ...

Related Pictures

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★リンクテーブル★

リンク元	「凝固第X因子」
拡張検索	「blood coagulation factor XIII」「coagulation factor XIII」「blood coagulation factor XI」「blood coagulation factor X」「coagulation factor Xa」
関連記事	「fact」「factor」「coagulation factor」「X」

「凝固第X因子」

　　[★]

英

coagulation factor X

関

第X因子、血液凝固第X因子

「blood coagulation factor XIII」

　　[★]

• 血液凝固第XIII因子

関

coagulation factor XIII、factor XIII

「coagulation factor XIII」

　　[★]

• 凝固第XIII因子

関

blood coagulation factor XIII、factor XIII

「blood coagulation factor XI」

　　[★]

• 血液凝固第XI因子

関

coagulation factor XI、factor XI

「blood coagulation factor X」

　　[★]

• 血液凝固第X因子

関

coagulation factor X、factor X

「coagulation factor Xa」

　　[★]

• 活性化第X因子

関

activated factor X、factor Xa

「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

　 　 　 　 　 　 　

「coagulation factor」

　　[★] 血液凝固因子

同

coagulation factors

「X」

　　[★] キサントシン, xanthosine