Bioelectrics Seminar
<p> <strong>“</strong><strong>Protein Phosphatase 4A3 is a Metastasis Associated Regulator of Vascular Endothelial Growth Factor Signaling”</strong></p> <p> </p> <p> <strong>John S. Lazo, Ph.D.</strong></p> <p> Professor of Pharmacology & Chemistry</p> <p> Associate Dean for Basic Research</p> <p> University of Virginia</p> <p> Charlottesville, VA</p> <p> </p> <p> </p> <p> <strong>Tuesday, March 3, 2014, 9-10AM</strong></p> <p> <strong>IRP2 First Floor Conference Room</strong></p> <p> <strong>4211 Monarch Way</strong></p> <p> <strong>All are invited</strong></p> <p> </p> <p> Protein phosphorylation is a central mechanism by which eukaryotic cells regulate enzyme activity and respond to extracellular signals. This reversible phosphorylation is regulated by the dynamic interplay of kinases and counterbalancing phosphatases and allows for efficient control of both constitutive as well as adaptive cellular processes. The role of phosphatases has been widely ignored. Protein-tyrosine phosphatase 4A3 (also known as PRL-3) is an enigmatic, oncogenic and metastasis associated dual-specificity phosphatase. In this seminar I will describe our efforts to understand its function both in tumor and endothelial cells using our recently generated PTP4A3 deficient mouse model. These mice exhibit reduced sensitivity to chemical carcinogenesis, vascular endothelial growth factor (VEGF)-mediated endothelial cell motility and signaling, and vascular permeability. Our hypothesis is that PTP4A3 reciprocally regulates VEGF signaling pathways and is an attractive molecular target for pharmacological intervention.</p>
Posted By: Loree Heller
Date: Tue Feb 25 11:07:01 EST 2014