Inactivation of protein tyrosine phosphatase 1B (PTP1B) by the endogenous/dietary aldehyde acrolein

TOXI 16

Derrick R. Seiner, drs4zc@mizzou.edu1, Jason LaButti, jason.labutti@mizzou.edu1, and Kent S. Gates, GatesK@missouri.edu2. (1) Department of Chemistry, University of Missouri-Columbia, 601 South College Avenue, Columbia, MO 65211, (2) Departments of Chemistry and Biochemistry, University of Missouri - Columbia, 601 S. College Ave., Columbia, MO 65211
PTP1B dephosphorylates the insulin receptor and the insulin receptor substrate, thus serving as the primary negative regulator that “switches off” the insulin signaling pathway. Inhibition of PTP1B activity can potentiate the action of insulin, thus yielding significant biological effects. The α,β-unsaturated aldehyde acrolein occurs naturally in the human diet and is a product of endogenous lipid peroxidation. In the work presented here, we have examined the inactivation of PTP1B by acrolein and have investigated the mechanism underlying phosphatase inactivation by this endogenous aldehyde.
 

Young Investigator Session
8:15 AM-12:00 PM, Monday, August 20, 2007 BCEC -- 258C, Oral

Division of Chemical Toxicology

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007