Glycosylation regulates turnover of cyclooxygenase-2

Mary B. Sevigny, Chai-Fei Li, Monika Alas, Millie Hughes-Fulford

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the prostanoid biosynthesis pathway, converting arachidonic acid into prostaglandin H2. COX-2 exists as 72 and 74 kDa glycoforms, the latter resulting from an additional oligosaccharide chain at residue Asn580. In this study, Asn580 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.

Original languageEnglish (US)
Pages (from-to)6533-6536
Number of pages4
JournalFEBS Letters
Volume580
Issue number28-29
DOIs
StatePublished - Dec 11 2006
Externally publishedYes

Fingerprint

Glycosylation
Cyclooxygenase 2
Prostaglandin H2
COS Cells
Biosynthesis
Oligosaccharides
Arachidonic Acid
Prostaglandins
Genes
Cells
Proteins

Keywords

  • Cyclooxygenase-2
  • Enzyme turnover
  • Glycoforms
  • Glycosylation
  • Post-translational regulation
  • Site-directed mutagenesis

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Sevigny, M. B., Li, C-F., Alas, M., & Hughes-Fulford, M. (2006). Glycosylation regulates turnover of cyclooxygenase-2. FEBS Letters, 580(28-29), 6533-6536. https://doi.org/10.1016/j.febslet.2006.10.073

Glycosylation regulates turnover of cyclooxygenase-2. / Sevigny, Mary B.; Li, Chai-Fei; Alas, Monika; Hughes-Fulford, Millie.

In: FEBS Letters, Vol. 580, No. 28-29, 11.12.2006, p. 6533-6536.

Research output: Contribution to journalArticle

Sevigny, MB, Li, C-F, Alas, M & Hughes-Fulford, M 2006, 'Glycosylation regulates turnover of cyclooxygenase-2', FEBS Letters, vol. 580, no. 28-29, pp. 6533-6536. https://doi.org/10.1016/j.febslet.2006.10.073
Sevigny, Mary B. ; Li, Chai-Fei ; Alas, Monika ; Hughes-Fulford, Millie. / Glycosylation regulates turnover of cyclooxygenase-2. In: FEBS Letters. 2006 ; Vol. 580, No. 28-29. pp. 6533-6536.
@article{392f0966b61b46a7b81b195491340a03,
title = "Glycosylation regulates turnover of cyclooxygenase-2",
abstract = "Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the prostanoid biosynthesis pathway, converting arachidonic acid into prostaglandin H2. COX-2 exists as 72 and 74 kDa glycoforms, the latter resulting from an additional oligosaccharide chain at residue Asn580. In this study, Asn580 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.",
keywords = "Cyclooxygenase-2, Enzyme turnover, Glycoforms, Glycosylation, Post-translational regulation, Site-directed mutagenesis",
author = "Sevigny, {Mary B.} and Chai-Fei Li and Monika Alas and Millie Hughes-Fulford",
year = "2006",
month = "12",
day = "11",
doi = "10.1016/j.febslet.2006.10.073",
language = "English (US)",
volume = "580",
pages = "6533--6536",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "28-29",

}

TY - JOUR

T1 - Glycosylation regulates turnover of cyclooxygenase-2

AU - Sevigny, Mary B.

AU - Li, Chai-Fei

AU - Alas, Monika

AU - Hughes-Fulford, Millie

PY - 2006/12/11

Y1 - 2006/12/11

N2 - Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the prostanoid biosynthesis pathway, converting arachidonic acid into prostaglandin H2. COX-2 exists as 72 and 74 kDa glycoforms, the latter resulting from an additional oligosaccharide chain at residue Asn580. In this study, Asn580 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.

AB - Cyclooxygenase-2 (COX-2) catalyzes the rate-limiting step in the prostanoid biosynthesis pathway, converting arachidonic acid into prostaglandin H2. COX-2 exists as 72 and 74 kDa glycoforms, the latter resulting from an additional oligosaccharide chain at residue Asn580. In this study, Asn580 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.

KW - Cyclooxygenase-2

KW - Enzyme turnover

KW - Glycoforms

KW - Glycosylation

KW - Post-translational regulation

KW - Site-directed mutagenesis

UR - http://www.scopus.com/inward/record.url?scp=34848904215&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34848904215&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2006.10.073

DO - 10.1016/j.febslet.2006.10.073

M3 - Article

C2 - 17113084

AN - SCOPUS:34848904215

VL - 580

SP - 6533

EP - 6536

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 28-29

ER -