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cyclooxygenase-2 (COX2, PGH synthase-2, prostaglandin endoperoxide synthase-2)
Function:
- may have a role as a major mediator of inflammation &/or a role for prostanoid signaling in activity-dependent plasticity
- fatty acids biosynthesis; prostaglandin biosynthesis
- acts both as a dioxygenase & as a peroxidase
- in endothelial cells, COX2 produces prostacyclin. [3,4]
Cofactor:
- binds 1 heme B (iron-protoporphyrin IX) group per subunit (putative)
Structure:
- homodimer (putative)
- belongs to the prostaglandin G/H synthase family
- contains 1 EGF-like domain
Compartment:
- microsome membrane, peripheral membrane
Expression:
- not found in resting cells, but is rapidly induced in fibroblasts, endothelial cells & smooth muscle cells by cytokines, growth factors, phorbol esters & lipopolysaccharide
- induced by cytokines & mitogens
Pathology:
- likely to play a role in inflammatory diseases such as rheumatoid arthritis
Pharmacology:
- target of nonsteroidal anti-inflammatory drugs (NSAIDs) & the COX2 inhibitors (celecoxib)
- acute anti-inflammatory properties of NSAIDs are due to inhibition of COX2
Related
cyclooxygenase 2 gene; COX2 gene; PGH synthase 2 gene
cyclooxygenase-2 (COX-2) specific inhibitor
cyclooxygenase-2 Ag in tissue
General
cyclooxygenase (prostaglandin endoperoxide synthase, COX)
glycoprotein
Properties
SIZE: entity length = 604 aa
MW = 69 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-17}
EGF domain {18-55}
MOTIF: cysteine residue {C21}
MODIFICATION: cysteine residue {C32}
cysteine residue {C22}
MODIFICATION: cysteine residue {C145}
cysteine residue {C26}
MODIFICATION: cysteine residue {C42}
cysteine residue {C32}
MODIFICATION: cysteine residue {C21}
cysteine residue {C42}
MODIFICATION: cysteine residue {C26}
cysteine residue {C44}
MODIFICATION: cysteine residue {C54}
N-glycosylation site {N53}
cysteine residue {C54}
MODIFICATION: cysteine residue {C44}
N-glycosylation site {N130}
cysteine residue {C145}
MODIFICATION: cysteine residue {C22}
histidine residue {H193}
tyrosine residue {Y371}
Iron [Fe]-binding site
SITE: 374-374
N-glycosylation site {N396}
Ser phosphorylation site {S437}
Tyr phosphorylation site {Y446}
serine residue {516-516}
cysteine residue {C555}
MODIFICATION: cysteine residue {C561}
cysteine residue {C561}
MODIFICATION: cysteine residue {C555}
N-glycosylation site {N580}
Database Correlations
OMIM 600262
UniProt P35354
PFAM correlations
KEGG correlations
References
- UniProt :accession P35354
- Mayo Internal Medicine Board Review, 1998-99, Prakash UBS (ed)
Lippincott-Raven, Philadelphia, 1998, pg 14, 851-53
- Journal Watch 22(10):78, 2002
Cheng Y, Austin SC, Rocca B, Koller BH, Coffman TM, Grosser T,
Lawson JA, FitzGerald GA.
Role of prostacyclin in the cardiovascular response to thromboxane A2.
Science. 2002 Apr 19;296(5567):539-41.
PMID: 11964481
Vane JR, Science 296:474, 2002
- Journal Watch 25(2):15, 2005
Egan KM, Lawson JA, Fries S, Koller B, Rader DJ, Smyth EM,
Fitzgerald GA.
COX-2-derived prostacyclin confers atheroprotection on female mice.
Science. 2004 Dec 10;306(5703):1954-7. Epub 2004 Nov 18.
PMID: 15550624
- Atlas of genetics & cytogenetics in oncology & Haematology
http://atlasgeneticsoncology.org/genes/PTGS2ID509ch1q31.html