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J.Health Sci., 45(6), 367-376, 1999
- Minireview -
Involvement of Glyoxalase I in NO-induced Oxidative Stress[in Japanese]
Atsushi Mitsumoto and Yasuhito Nakagawa*
Laboratory of Hygienic Chemistry, School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan
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 form 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.
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