Effect of Cyclooxygenase‐2 Glycosylation on Downstream Expression of E‐Cadherin and b‐Catenin in MCF‐7 Breast Cancer Cells

Cyclooxygenases (COXs) are enzymes that catalyze the formation of prostaglandins. Prostaglandins a class lipid mediators can promote inflammation, pain, and fever as well maintain variety normal physiological functions. exist in two forms, COX-1 COX-2, both which localized to luminal membrane endoplasmic reticulum. COX-2 expression is usually induced response certain stimuli, such infection. However, overexpression has been correlated numerous cancers, breast, colon prostate cancer. exists major glycoforms 72 74kDa, latter resulting from an additional oligosaccharide chain at amino acid residue Asn580. Past studies our lab have shown this glycosylation regulates protein turnover cell. The proteins E-cadherin— tumor suppressor— b-catenin—a driver— often regulated by expression. purpose study determine if Asn580 affects downstream E- cadherin b-catenin subsequent migratory potential MCF-7 breast cancer cells. cells were transiently transfected with either wild-type or Asn580-mutant gene empty plasmid (control). RNA isolated was subjected semi-quantitative RT-PCR, cell lysates analyzed via western blotting following immunostaining. Migratory determined three days after transfection using vitro transwell migration assays. No differences found amongst groups. We E-cadherin transcriptional translational levels reduced expressing mutant for hours. Interestingly, also 48 hours gene, though appeared unchanged. These results indicate although no changes could be discerned transfection, did decrease suppressor driver β-catenin line, thus obscuring role progression.