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同: cyclooxygenase 1

同: cyclooxygenase 1

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the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system
act as the coxswain, in a boat race

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carbonの化学記号
=coxswain
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/07/15 13:32:01」(JST)

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"COX-1" redirects here. COX-1 may also refer to mitochondrial cytochrome c oxidase subunit 1 (cox1).

Cyclooxygenase-1 (COX-1), also known as prostaglandin G/H synthase 1, prostaglandin-endoperoxide synthase 1 or prostaglandin H2 synthase 1, is an enzyme that in humans is encoded by the PTGS1 gene.^[1]^[2]

History

Cyclooxygenase (COX) is the central enzyme in the biosynthetic pathway to prostaglandins from arachidonic acid. This protein was purified more than 20 years ago and cloned in 1988.^[3]^[4]

Gene and isozymes

There are two isozymes of COX encoded by distinct gene products: a constitutive COX-1 (this enzyme) and an inducible COX-2, which differ in their regulation of expression and tissue distribution. The expression of these two transcripts is differentially regulated by relevant cytokines and growth factors.^[5] A splice variant of COX-1 termed COX-3 was identified in the CNS of dogs, but does not result in a functional protein in humans. Two smaller COX-1-derived proteins (the partial COX-1 proteins PCOX-1A and PCOX-1B) have also been discovered, but their precise roles are yet to be described.^[6]

Function

Prostaglandin-endoperoxide synthase (PTGS), also known as cyclooxygenase (COX), is the key enzyme in prostaglandin biosynthesis. It converts free arachidonic acid, released from membrane phospholipids at the sn-2 ester binding site by the enzymatic activity of phospholipase A2, to prostaglandin (PG) H2. The reaction involves both cyclooxygenase (dioxygenase) and hydroperoxidase (peroxidase) activity. The cyclooxygenase activity incorporates two oxygen molecules into arachidonic acid or alternate polyunsaturated fatty acid substrates, such as linoleic acid and eicosapentaenoic acid. Metabolism of arachidonic acid forms a labile intermediate peroxide, PGG2, which is reduced to the corresponding alcohol, PGH2, by the enzyme’s hydroperoxidase activity. There are two isozymes of COX encoded by distinct gene products: a constitutive COX-1 (this enzyme) and an inducible COX-2, which differ in their regulation of expression and tissue distribution. (A splice variant of COX-1, initially termed COX-3 was identified in the CNS of dogs, but does not result in a functional protein in humans.) This gene encodes COX-1, which regulates angiogenesis in endothelial cells. COX-1 is also involved in cell signaling and maintaining tissue homeostasis.

COX-1 promotes the production of the natural mucus lining that protects the inner stomach and contribute to reduced acid secretion and reduced pepsin content.^[7]^[8] COX-1 is normally present in a variety of areas of the body, including not only the stomach but any site of inflammation.^[9]^[7]

Clinical significance

COX-1 is inhibited by nonsteroidal anti-inflammatory drugs (NSAIDs) such as aspirin. TXA2, the major product of COX-1 in platelets, induces platelet aggregation.^[10]^[11] Research has shown that the inhibition of COX-1 is sufficient to explain why aspirin is effective at reducing cardiac events.

References

^ Yokoyama C, Tanabe T (December 1989). "Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme". Biochem. Biophys. Res. Commun. 165 (2): 888–94. DOI:10.1016/S0006-291X(89)80049-X. PMID 2512924.
^ Funk CD, Funk LB, Kennedy ME, Pong AS, Fitzgerald GA (June 1991). "Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment". FASEB J. 5 (9): 2304–12. PMID 1907252.
^ Bakhle YS (1999). "Structure of COX-1 and COX-2 enzymes and their interaction with inhibitors". Drugs Today 35 (4-5): 237–50. PMID 12973429.
^ Sakamoto C (October 1998). "Roles of COX-1 and COX-2 in gastrointestinal pathophysiology". J. Gastroenterol. 33 (5): 618–24. DOI:10.1007/s005350050147. PMID 9773924.
^ "Entrez Gene: PTGS1 prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5742.
^ Chandrasekharan NV, Dai H, Roos KL, Evanson NK, Tomsik J, Elton TS, Simmons DL (October 2002). "COX-3, a cyclooxygenase-1 variant inhibited by acetaminophen and other analgesic/antipyretic drugs: cloning, structure, and expression". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13926–31. DOI:10.1073/pnas.162468699. PMC 129799. PMID 12242329. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=129799.
^ ^a ^b MedicineNet.com[Internet]. New York:WebMD. [updated 2003 March 3; cited 2010 February 1] Available from: http://www.medterms.com/script/main/art.asp?articlekey=7123
^ Bruton LL, Lazo JS, Parker KL. Goodman & Gilman’s: the pharmacological basis of therapeutics. 11th edition. New York: McGraw-Hill; 2006. p. 661.
^ AWS-Law.com [Internet]. Florida. [cited 2010 February 1] Available from: http://www.aws-law.com/about.asp.
^ Bruton LL, Lazo JS, Parker KL. Goodman & Gilman’s: the pharmacological basis of therapeutics. 11th edition. New York: McGraw-Hill; 2006. p. 1126.
^ Weitz Jeffrey I, "Chapter 112. Antiplatelet, Anticoagulant, and Fibrinolytic Drugs" (Chapter). Fauci AS, Braunwald E, Kasper DL, Hauser SL, Longo DL, Jameson JL, Loscalzo J: Harrison's Principles of Internal Medicine, 17e: http://www.accessmedicine.com/content.aspx?aID=2891975.

UpToDate Contents

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1. COX-2選択的阻害剤の概要 overview of selective cox 2 inhibitors
2. 非ステロイド性抗炎症剤（NSAIDs）：作用機序 nsaids mechanism of action
3. 非ステロイド性抗炎症剤（NSAIDs）（アスピリンを含む）：胃十二指腸障害の病因 nsaids including aspirin pathogenesis of gastroduodenal toxicity
4. COX-2阻害剤および胃十二指腸障害：大規模臨床試験 cox 2 inhibitors and gastroduodenal toxicity major clinical trials
5. 非ステロイド性抗炎症剤（NSAIDs）（アスピリンを含む）：アレルギー反応および偽アレルギー反応 nsaids including aspirin allergic and pseudoallergic reactions

English Journal

Liquid chromatography-tandem mass spectrometry for simultaneous measurement of thromboxane B2 and 12(S)-hydroxyeicosatetraenoic acid in serum.

Squellerio I1, Porro B2, Songia P3, Veglia F4, Caruso D5, Tremoli E6, Cavalca V7.
Journal of pharmaceutical and biomedical analysis.J Pharm Biomed Anal.2014 Aug 5;96:256-62. doi: 10.1016/j.jpba.2014.04.004. Epub 2014 Apr 13.
Arachidonic acid (AA) is metabolized in human platelets by two main pathways: via cyclooxygenase (COX-1) to prostaglandins and thromboxane (TX)A2 and via 12-lipoxygenase (12-LOX) to 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE). While COX products are known to regulate platelet reactivity, the rol
PMID 24786190

Aspirin may modify tumor microenvironment via antiplatelet effect.

Su BB1, Chen JH2, Shi H1, Chen QQ1, Wan J3.
Medical hypotheses.Med Hypotheses.2014 Aug;83(2):148-50. doi: 10.1016/j.mehy.2014.05.007. Epub 2014 May 20.
High-quality evidence suggests that aspirin is a promising agent for cancer prevention and treatment. Direct inhibition of cyclooxygenase-2 (COX-2) pathway is generally thought to be the main mechanism by which aspirin inhibits cancer development. However, either pharmacological properties of aspiri
PMID 24908358

Protective effect of nimesulide against hepatic ischemia/reperfusion injury in rats: Effects on oxidant/antioxidants, DNA mutation and COX-1/COX-2 levels.

Demiryilmaz I1, Turan MI2, Kisaoglu A3, Gulapoglu M4, Yilmaz I5, Suleyman H6.
Pharmacological reports : PR.Pharmacol Rep.2014 Aug;66(4):647-52. doi: 10.1016/j.pharep.2014.02.015. Epub 2014 Mar 11.
BACKGROUND: Nimesulide is a pharmacological agent and selective COX-2 inhibitor. It has anti-inflammatory, analgesic and antipyretic properties. The purpose of this study was to investigate the effect of nimesulide on oxidant/antioxidant, DNA mutation and COX-1/COX-2 activities in rat liver tissue w
PMID 24948067

Japanese Journal

The comprehensive assessment of local immune status of ovarian cancer by the clustering of multiple immune factors.

Hamanishi Junzo,Mandai Masaki,Abiko Kaoru,Matsumura Noriomi,Baba Tsukasa,Yoshioka Yumiko,Kosaka Kenzo,Konishi Ikuo
Clinical immunology 141(3), 338-347, 2011-12
… The numbers of CD1α+, CD4+, CD8+, CD57+, forkhead box P3+ and programmed cell death-1+ cells were counted, and the intensity of immunosuppressive factors, such as programmed cell death-1 ligand (PD-L)1, PD-L2, cyclooxygenase (COX)-1, COX-2 and transforming growth factor β1, were evaluated in 70 ovarian cancer specimens stained by immunohistochemistry. …
NAID 120003610113

An intact mitochondrial cox1 gene and a pseudogene with different genomic configurations are present in apple cultivars 'Golden Delicious' and 'Delicious': Evolutionary aspects

Wakatsuki Akihito,Kitazaki Kazuyoshi,Kato Sumie,Kishima Yuji,Mikami Tetsuo
Scientia Horticulturae 130(1), 49-53, 2011-08-26
… We have characterized the mitochondrial cox1 gene copies in two apple cultivars 'Golden Delicious' and 'Delicious'. … Both the cultivars contained an intact copy and a truncated copy of cox1. … The intact 'Golden Delicious' and 'Delicious' cox1 genes, designated G-cox1 and D-cox1, respectively, were both found to be actually transcribed to give an RNA of approximately 1.7 kb. …
NAID 120003898267

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関連記事	「C」「CO」「COX」

「C」

Prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase)
	; PDB rendering based on 1diy.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1cqe, 1diy, 1ebv, 1eqg, 1eqh, 1fe2, 1ht5, 1ht8, 1igx, 1igz, 1pge, 1pgf, 1pgg, 1prh, 1pth, 1q4g, 1u67, 2ayl
Identifiers
Symbols	PTGS1; COX1; COX3; PCOX1; PGG/HS; PGHS-1; PGHS1; PHS1; PTGHS
External IDs	OMIM: 176805 MGI: 97797 HomoloGene: 743 ChEMBL: 221 GeneCards: PTGS1 Gene
EC number	1.14.99.1
Gene Ontology
Molecular function	• peroxidase activity; • prostaglandin-endoperoxide synthase activity; • lipid binding; • oxidoreductase activity; • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; • heme binding; • metal ion binding;
Cellular component	• photoreceptor outer segment; • nucleus; • nuclear envelope; • cytoplasm; • endoplasmic reticulum; • endoplasmic reticulum membrane; • microsome; • Golgi apparatus; • plasma membrane; • intracellular membrane-bounded organelle; • cytoplasmic part;
Biological process	• prostaglandin biosynthetic process; • lipid metabolic process; • fatty acid biosynthetic process; • prostanoid metabolic process; • xenobiotic metabolic process; • response to oxidative stress; • aging; • regulation of blood pressure; • response to organic nitrogen; • negative regulation of norepinephrine secretion; • cyclooxygenase pathway; • negative regulation of epinephrine secretion; • regulation of cell proliferation; • small molecule metabolic process; • positive regulation of vasoconstriction; • positive regulation of smooth muscle contraction; • response to corticosterone stimulus;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

炭素 carbon
シトシン cytosine
システイン cysteine
シチジン
セルシウス度摂氏 degrees Celsius degree C
産婦人科領域で「子宮外頚子宮外頚部 exocervix」を表現するための略語

「CO」

　　[★]

「COX」

　　[★] シクロオキシゲナーゼ COX

[pmid2512924-0] Yokoyama C, Tanabe T (December 1989). "Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme". Biochem. Biophys. Res. Commun. 165 (2): 888–94. DOI:10.1016/S0006-291X(89)80049-X. PMID 2512924.

[pmid1907252-1] Funk CD, Funk LB, Kennedy ME, Pong AS, Fitzgerald GA (June 1991). "Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment". FASEB J. 5 (9): 2304–12. PMID 1907252.

[pmid12973429-2] Bakhle YS (1999). "Structure of COX-1 and COX-2 enzymes and their interaction with inhibitors". Drugs Today 35 (4-5): 237–50. PMID 12973429.

[pmid9773924-3] Sakamoto C (October 1998). "Roles of COX-1 and COX-2 in gastrointestinal pathophysiology". J. Gastroenterol. 33 (5): 618–24. DOI:10.1007/s005350050147. PMID 9773924.

[4] "Entrez Gene: PTGS1 prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5742.

[CDRETES1-5] Chandrasekharan NV, Dai H, Roos KL, Evanson NK, Tomsik J, Elton TS, Simmons DL (October 2002). "COX-3, a cyclooxygenase-1 variant inhibited by acetaminophen and other analgesic/antipyretic drugs: cloning, structure, and expression". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13926–31. DOI:10.1073/pnas.162468699. PMC 129799. PMID 12242329. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=129799.

[MedicineNetcomInternetNew-6] MedicineNet.com[Internet]. New York:WebMD. [updated 2003 March 3; cited 2010 February 1] Available from: http://www.medterms.com/script/main/art.asp?articlekey=7123

[7] Bruton LL, Lazo JS, Parker KL. Goodman & Gilman’s: the pharmacological basis of therapeutics. 11th edition. New York: McGraw-Hill; 2006. p. 661.

[8] AWS-Law.com [Internet]. Florida. [cited 2010 February 1] Available from: http://www.aws-law.com/about.asp.

[9] Bruton LL, Lazo JS, Parker KL. Goodman & Gilman’s: the pharmacological basis of therapeutics. 11th edition. New York: McGraw-Hill; 2006. p. 1126.

[10] Weitz Jeffrey I, "Chapter 112. Antiplatelet, Anticoagulant, and Fibrinolytic Drugs" (Chapter). Fauci AS, Braunwald E, Kasper DL, Hauser SL, Longo DL, Jameson JL, Loscalzo J: Harrison's Principles of Internal Medicine, 17e: http://www.accessmedicine.com/content.aspx?aID=2891975.

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