Glycosylation regulates turnover of cyclooxygenase-2.
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Sevigny MB, Li CF, Alas M, Hughes-Fulford M
Glycosylation regulates turnover of cyclooxygenase-2.
FEBS Lett. 2006 Dec 11;580(28-29):6533-6. Epub 2006 Nov 9.
- PubMed ID
- 17113084 [ View in PubMed]
- Abstract
Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the prostanoid biosynthesis pathway, converting arachidonic acid into prostaglandin H(2). COX-2 exists as 72 and 74kDa glycoforms, the latter resulting from an additional oligosaccharide chain at residue Asn(580). In this study, Asn(580) was mutated to determine the biological significance of this variable glycosylation. COS-1 cells transfected with the mutant gene were unable to express the 74kDa glycoform and were found to accumulate more COX-2 protein and have five times greater COX-2 activity than cells expressing both glycoforms. Thus, COX-2 turnover appears to depend upon glycosylation of the 72kDa glycoform.