Involvement of Glyoxalase I in NO-induced Oxidative Stress

Abstract

To understand the molecular dynamics in response to nitric oxide-induced oxidative stress under infectious and inflammatory conditions, we have analyzed protein expression patterns of human endothelial cells with or without treatment of nitric oxide donors. We identified glyoxalase I as a novel nitric oxide responsive protein using two-dimensional polyacrylamide gel electrophoresis. Mammalian glyoxalase I can interact with S-nitrosoglutathione at the substrate recognition site, resulting in an inactive from with a reductant reversible chemical modification. The oxidative response of glyoxalase I is specific to nitric oxide and more sensitive than that of glyceraldehyde-3-phosphate dehydrogenase which is a well-known enzyme inactivated by nitric oxide. In this review, we introduce the characteristics of glyoxalase I as a nitric oxide responsive protein and hypothesize the roles of glyoxalase I under nitrosative stress conditions.