Elucidating the mechanism of PI3K when interacting with TRPV1.

Abstract

The interaction between Transient Receptor Potential Cation Channel Subfamily V member 1 (TRPV1), Phosphoinositide 3-Kinase (PI3K), and Receptor Tyrosine Kinase (RTK) provides us with a positive feedback loop that is responsible for recruiting Pi3K, a protein responsible for phosphorylating Phosphatidylinositol Bisphosphate (PIP2) into Phosphatidylinositol Trisphosphate (PIP3), and recruit TRPV1, an ion channel responsible for regulating heat and pain sensation, to specific areas in the plasma membrane (PM). In this study, we use ELISA immunoassay, microscopy, and other techniques to elucidate PI3K's functionality under the influence of TRPV1. Ultimately, we want to investigate this positive feedback loop and determine if we can interfere with excess TRPV1 activation and potentially stop excess pain and inflammation.