PTGS2

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See also: cyclooxygenase
Prostaglandin-endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase)
PDB rendering based on 6COX
Available structures: PDB 6COX, 1CX2, 3PGH, 4COX, 5COX, 1PXX, 1CVU, 1DDX
Identifiers
Symbols PTGS2; COX2; PGG/HS; COX-2; PGHS-2; PHS-2; hCox-2
External IDs OMIM: 600262 MGI: 97798 HomoloGene: 31000
EC number 1.14.99.1
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5743 19225
Ensembl ENSG00000073756 ENSMUSG00000032487
Uniprot P35354 Q3UMR6
Refseq NM_000963 (mRNA)
NP_000954 (protein)		 NM_011198 (mRNA)
NP_035328 (protein)
Location Chr 1: 184.91 - 184.92 Mb Chr 1: 151.86 - 151.87 Mb
Pubmed search [1] [2]

Prostaglandin-endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase), also known as PTGS2, is a human gene.

Prostaglandin-endoperoxide synthase (PTGS), also known as cyclooxygenase, is the key enzyme in biosynthesis of the prostanoids, (prostaglandins, prostacyclin and thromboxanes.) It acts both as a dioxygenase and as a peroxidase. There are two isozymes of PTGS: a constitutive PTGS1 and an inducible PTGS2, which differ in their regulation of expression and tissue distribution. This gene encodes PTGS2, which shows 86% - 89% amino acid sequence identity with mouse, rat, sheep, bovine, horse and rabbit PTGS2 proteins, respectively. Human PTGS2 is expressed in a limited number of cell types and regulated by specific stimulatory events, suggesting that it is responsible for the prostanoid biosynthesis involved in inflammation and mitogenesis. The expression of this gene is deregulated in epithelial tumors.[1]

References

  1. ^ "Entrez Gene: PTGS2 prostaglandin-endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase)".

Further reading

  • Richards JA, Petrel TA, Brueggemeier RW (2002). "Signaling pathways regulating aromatase and cyclooxygenases in normal and malignant breast cells.". J. Steroid Biochem. Mol. Biol. 80 (2): 203–12. PMID 11897504. 
  • Koki AT, Khan NK, Woerner BM, et al. (2003). "Characterization of cyclooxygenase-2 (COX-2) during tumorigenesis in human epithelial cancers: evidence for potential clinical utility of COX-2 inhibitors in epithelial cancers.". Prostaglandins Leukot. Essent. Fatty Acids 66 (1): 13–8. doi:10.1054/plef.2001.0335. PMID 12051953. 
  • Saukkonen K, Rintahaka J, Sivula A, et al. (2003). "Cyclooxygenase-2 and gastric carcinogenesis.". APMIS 111 (10): 915–25. PMID 14616542. 
  • Sinicrope FA, Gill S (2004). "Role of cyclooxygenase-2 in colorectal cancer.". Cancer Metastasis Rev. 23 (1-2): 63–75. PMID 15000150. 
  • Jain S, Khuri FR, Shin DM (2004). "Prevention of head and neck cancer: current status and future prospects.". Current problems in cancer 28 (5): 265–86. PMID 15375804. 
  • Saba N, Jain S, Khuri F (2004). "Chemoprevention in lung cancer.". Current problems in cancer 28 (5): 287–306. PMID 15375805. 
  • Cardillo I, Spugnini EP, Verdina A, et al. (2006). "Cox and mesothelioma: an overview.". Histol. Histopathol. 20 (4): 1267–74. PMID 16136507. 
  • Brueggemeier RW, Díaz-Cruz ES (2006). "Relationship between aromatase and cyclooxygenases in breast cancer: potential for new therapeutic approaches.". Minerva Endocrinol. 31 (1): 13–26. PMID 16498361. 
  • Fujimura T, Ohta T, Oyama K, et al. (2006). "Role of cyclooxygenase-2 in the carcinogenesis of gastrointestinal tract cancers: a review and report of personal experience.". World J. Gastroenterol. 12 (9): 1336–45. PMID 16552798. 
  • Bingham S, Beswick PJ, Blum DE, et al. (2007). "The role of the cylooxygenase pathway in nociception and pain.". Semin. Cell Dev. Biol. 17 (5): 544–54. doi:10.1016/j.semcdb.2006.09.001. PMID 17071117. 
  • Minghetti L, Pocchiari M (2007). "Cyclooxygenase-2, prostaglandin E2, and microglial activation in prion diseases.". Int. Rev. Neurobiol. 82: 265–75. doi:10.1016/S0074-7742(07)82014-9. PMID 17678966. 
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