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.
| Original language | American English |
|---|---|
| Pages (from-to) | 6533-6536 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 580 |
| Issue number | 28-29 |
| State | Published - 2006 |
Funding
The authors thank Dr. Timothy Hla (University of Connecticut) for the generous gift of the human COX-2 cDNA. These studies were supported by the Veterans Administration Merit Review Award and in part by the VA REAP and NASA Grants NCC-2-1361 and NAG-2-2981 awarded to M. H-F.
| Funders | Funder number |
|---|---|
| VA REAP | |
| Veterans Administration | |
| National Aeronautics and Space Administration | NCC-2-1361, NAG-2-2981 |
ASJC Scopus Subject Areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Keywords
- Animals
- Arachidonic Acid
- Asparagine
- COS Cells
- Cercopithecus aethiops
- Cyclooxygenase 2
- Glycosylation
- Humans
- Isoenzymes
- Membrane Proteins
- Mutagenesis
- Glycoforms
- Post-translational regulation
- Site-directed mutagenesis
- Cyclooxygenase-2
- Enzyme turnover
Disciplines
- Life Sciences
- Medicine and Health Sciences