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- Title
Glycosylation regulates turnover of cyclooxygenase-2
- Authors
Sevigny, Mary B.; Li, Chai-Fei; Alas, Monika; Hughes-Fulford, Millie
- Abstract
Abstract: Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the prostanoid biosynthesis pathway, converting arachidonic acid into prostaglandin H2. COX-2 exists as 72 and 74kDa glycoforms, the latter resulting from an additional oligosaccharide chain at residue Asn580. In this study, Asn580 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.
- Subjects
ENZYME-linked immunosorbent assay; ARACHIDONIC acid; ESTERIFICATION
- Publication
FEBS Letters, 2006, Vol 580, Issue 28/29, p6533
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2006.10.073