2008 Eighth Annual Beckman Scholars Symposium
Thursday Poster Session - July 27, 2006

The epidermal growth factor receptor (EGFR) has been found to be mutated or over activated in many cancer cells. The EGFR plays an important role in regulating cell proliferation, differentiation, and migration. Recent studies suggest that this receptor and a number of other highly regulated signaling membrane proteins can be found in membrane invaginations called caveolae. Caveolin-1, the major structural protein of caveolae, has been found to modulate the activity of the EGFR. Determining the role of caveolin-1 has become an important focus of research because of its part in cell transformation and cancer progression. To investigate this importance, the production of caveolin-1 was knocked out using siRNA technology. A431 epidermoid carcinomas cells were used because they are known to over-express the EGFR and modulate caveolin upon EGF treatment. The autophosphorylation of the receptor, triggered by EGF treatment, initiates the phosphorylation of downstream signaling molecules, such as Grb-2, Src, and their intracellular signaling pathways. In these studies, I determined that by knocking out caveolin-1, the activity of the EGFR was altered in response to EGF treatment. The knockdown of caveolin-1 was seen after two days of treatment with siRNA. After the two day incubation, cells underwent a timecourse treatment of EGF and the activity of the downstream signaling molecules was evaluated using western blotting techniques. Their activity appeared to decrease in response to caveolin-1 knockdown and treatment of EGF. This suggests caveolin-1 as a positive regulator of EGFR kinase activity when the receptor is over-expressed.