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Glycosylation regulates turnover of cyclooxygenase‐2
Author(s) -
Sevigny Mary B.,
Li Chai-Fei,
Alas Monika,
Hughes-Fulford Millie
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.073
Subject(s) - glycosylation , biochemistry , cyclooxygenase , chemistry , arachidonic acid , mutant , enzyme , transfection , prostaglandin , gene
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 74 kDa 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 74 kDa 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 72 kDa glycoform.