Title

Glycosylation regulates turnover of cyclooxygenase-2.

Department

Natural Sciences and Mathematics

Document Type

Article

Source

FEBS Letters

Publication Date

12-11-2006

ISSN

0014-5793

Volume

580

Issue

28-29

First Page

6533

Last Page

6536

Digital Object Identifier / DOI

10.1016/j.febslet.2006.10.073

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.

PubMed ID

7113084

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