Tunicamycin Effects on Cell-Cell adhesion and surface carbohydrates in Embryogenesis

Students: Melody Valdez, Desiree Salcedo

Faculty Mentor: Lisa Hua

Biology

College of Science, Technology, and Business

This study examines the role of protein glycosylation in the fundamental process of cell-cell recognition during embryogenesis. Using sea urchin embryos as a model system, an experiment was conducted to investigate the role of protein glycosylation during early development in the sea urchin life cycle. To test the significance of surface-bound glycoproteins, embryos were treated with the glycosylation inhibitor tunicamycin. Tunicamycin blocks the transfer of N-acetylglucosamine to membrane-bound dolichol phosphate, an early and essential step in the synthesis of glycoproteins in the endoplasmic reticulum. Embryos treated with tunicamycin displayed clear developmental defects, including abnormal cell adhesion, suggesting that disruption of glycoprotein formation impairs critical cell-cell interactions. In contrast, untreated embryos developed normally, exhibiting expected stages of embryogenesis without abnormalities. These findings support the hypothesis that surface-bound glycoproteins play a critical role in the cell-cell interaction process necessary for proper embryonic development.