Skip to main content
Article
Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors
Pharmacological Research (2012)
  • Mary Sevigny, Department of Natural Sciences and Mathematics, Dominican University of California
  • Kamara Graham, Department of Natural Sciences and Mathematics, Dominican University of California
  • Esmeralda Ponce, Department of Natural Sciences and Mathematics, Dominican University of California
  • Maggie Louie, Department of Natural Sciences and Mathematics, Dominican University of California
  • Kylie Mitchell, Department of Natural Sciences and Mathematics, Dominican University of California
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 Asn580. In this study, Asn580 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 Asn580 decreases the efficacy of some inhibitors.
Keywords
  • cancer,
  • cyclooxygenase-2,
  • cox-2,
  • COX-2 inhibitors
Disciplines
Publication Date
April, 2012
Citation Information
Mary Sevigny, Kamara Graham, Esmeralda Ponce, Maggie Louie, et al.. "Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors" Pharmacological Research Vol. 65 Iss. 4 (2012) p. 445 - 450 ISSN: 1043-6618
Available at: http://works.bepress.com/maggie_louie/12/