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

Authors

Genna Roan, Dominican University of California
Grace Alexander, Dominican University of California
Klarisse Cruz, Dominican University of California
Janelle Nguyen, Dominican University of California
Mary B. Sevigny, Dominican University of CaliforniaFollow

Files

Description

Cyclooxygenase-2 (COX-2) is an enzyme that helps catalyze the formation of prostaglandins, which promote inflammation, pain, and fever and maintain other normal physiological functions throughout the body. However, the overexpression of COX-2 has been found to play a role in various diseases including breast cancer. COX-2 exists as two major glycoforms— 72 kDa and 74 kDa— due to the glycosylation site Asn580 which is glycosylated 50% of the time. Past studies from our lab have shown that this glycosylation regulates COX-2 protein turnover in the cell3. The proteins E-cadherin— a tumor suppressor— and β-catenin— a tumor driver— can be regulated by COX-2 activity

Department

Natural Sciences and Mathematics

Publication Date

4-2021

Sponsorship/Conference/Institution

Experimental Biology Meeting, virtual conference

Keywords

COX-2, Cancer, Cyclooxygenase-2, Breast Cancer

Disciplines

Biology | Cancer Biology | Cell and Developmental Biology