Location Determines PKC Specificity
Animation of KAI Pharmaceutical's Selective Modulators
KAI Pharmaceuticals, Inc.
on July 29, 2009
Efforts to target individual PKC isozymes with small molecules for therapeutic applications have been largely unsuccessful due to the lack of specificity of such compounds. Expanding on technology developed in the lab of Dr. Daria Mochly-Rosen at Stanford University, KAI’s technology has yielded a portfolio of selective peptide-based PKC inhibitors and activators that overcome this limitation by focusing on modulating the unique intracellular translocation of individual isozymes rather than their catalytic activity, which is poorly differentiated across the PKC enzyme family.
Utilizing peptide-based rational design, KAI has developed and can optimize highly selective modulators of all eight PKC isozymes by targeting the interaction between the individual isozyme and its unique subcellular receptor, or RACK. With this approach, KAI’s PKC modulators can selectively activate or inhibit each of the individual PKC isozymes without affecting highly homologous kinases within the same cells. As such, KAI’s selective PKC isozyme modulators represent novel, first-in-class agents in each therapeutic area currently under development.
This video demonstrates the mechanisms of subcellular PKC isozyme localization.
Tags: protein kinase C, PKC, isozyme, PKC isozymes, PKC modulators