Natural Sciences and Mathematics | Faculty Research Posters



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A cancer cell’s most threatening property is its ability to metastasize or detach from the primary tumor and migrate to other locations in the body. Previous studies have shown that overexpression of the enzyme cyclooxygenase-2 (COX-2) can increase the metastatic potential of several cell types. COX-2 is the rate-limiting enzyme in the prostanoid biosynthesis pathway, converting arachidonic acid to prostaglandin H2, an important signaling molecule in the body. Glycosylation of COX-2 at the amino acid site Asn580 occurs about 50% of the time, and this results in two forms of the enzyme with molecular weights 72 and 74kDa. The purpose of this study was to investigate the impact of glycosylation of COX-2 at the Asn580 site on the metastatic potential of cells. COS-1 cells were first transfected with either an Asn580-mutant human COX-2 gene or the wild-type human COX-2 gene. A cell migration assay was then carried out on these two groups of cells. Briefly, 5x104 cells were plated onto the membrane of a Boyden Chamber, and cells were incubated for 12 hours. Cells that migrated to the underside of the membrane were fixed, stained, visualized via light microscopy, and counted. Our results revealed that cells transfected with the Asn580-mutant gene migrated faster through the membrane. This indicates that a lack of glycosylation at the Asn580 site of the COX-2 enzyme may lead to an enhanced metastatic potential in cells. Future studies will analyze the effect of variable COX-2 glycoform expression on the migratory potential of tumor cell lines such as MCF-7 and T-47D.


Natural Sciences and Mathematics

Publication Date



Annual Meeting of the American Society for Cell Biology


New Orleans, LA


cyclooxygenase-2, COX-2



Glycosylation of cyclooxygenase-2 (COX-2) influences the migratory potential of COS-1 cells

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Biochemistry Commons