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Article
Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
Natural Sciences and Mathematics | Faculty Scholarship
Department
Department of Natural Sciences and Mathematics
Document Type
Article
Source
Pharmacological Research
Publication Date
4-1-2012
Disciplines
Abstract
Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer. The rate-limiting step in the prostanoid biosynthesis pathway is catalyzed by cyclooxygenase-2 (COX-2). COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580). In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib. Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
PubMed ID
22245433
Creative Commons License
Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International
Citation Information
Mary B. Sevigny, Kamara Graham, Esmeralda Ponce, Maggie Louie, et al.. "Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors." Vol. 65 Iss. 4 (2012) p. 445 - 450 ISSN: 1096-1186 Available at: http://works.bepress.com/mary-sevigny/23/