Epoxide hydrolase 3 (Ephx3) gene disruption reduces ceramide linoleate epoxide hydrolysis and impairs skin barrier function
Matthew L. Edin, Haruto Yamanashi, William E. Boeglin, Joan P. Graves, Laura M. DeGraff, Fred B. Lih, Darryl C. Zeldin, Alan Brash
Abstract
epidermis of the major trihydroxy isomer 9R,10S,13R-trihydroxy-11E-octadecenoate. We conclude that EPHX3 (and not EPHX1 or EPHX2) catalyzes hydrolysis of the 12R-LOX/eLOX3-derived epoxyalcohol esterified in acylceramide and may function to control flux through the alternative and crucial route of metabolism via the dehydrogenation pathway of SDR9C7. Importantly, our findings also identify a functional role for EPHX3 in transformation of a naturally esterified epoxide substrate, pointing to its potential contribution in other tissues.
Topics & Concepts
EpoxideEpoxide hydrolaseCeramideEpoxide hydrolase 2ChemistryHydrolysisBarrier functionBiochemistryCell biologyBiologyEnzymeCatalysisMicrosomeApoptosisEicosanoids and Hypertension PharmacologyFatty Acid Research and HealthCardiovascular, Neuropeptides, and Oxidative Stress Research