Digital Object Identifier / DOI

https://doi.org/10.1016/j.phrs.2012.01.001

Department

Department of Natural Sciences and Mathematics

Document Type

Article

Source

Pharmacological Research

Publication Date

4-1-2012

ISSN

1096-1186

Volume

65

Issue

4

First Page

445

Last Page

450

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

Included in

Biochemistry Commons

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