Protein denitration/modification by glutathione-S-transferase and glutathione peroxidase.
Peroxynitrite (PN)-pretreated histone III-S (NH) and reduced glutathione (GSH)-treated NH (NH(GSH)) were incubated with glutathione-S-transferase (GST) and glutathione peroxidase (GPX). Western blot analysis revealed decreased 3-nitrotyrosine immunoreactivity for NH(GSH), but not for NH. Additionally, increased nitrate was noted as an end product of these enzymatic reactions. The findings imply that GSH-treatment of NH may facilitate its conformational change in favor of subsequent enzymatic denitration and/or modification, which could be vital in relieving cellular oxidative stress and regulating NO/PN-mediated signal transduction cascade.
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, FL 32114, USA. kuow@cookman.edu
Wu-Nan
WN
Kuo
Joseph M
JM
Kocis
Madhvi
M
Mewar
D000818:Animals; D002417:Cattle; D005978:Glutathione / Q000378:metabolism / Q000494:pharmacology; D005979:Glutathione Peroxidase / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism*; D006657:Histones / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism*; D066298:In Vitro Techniques; D008954:Models, Biological; D009569:Nitric Oxide / Q000378:metabolism; D018384:Oxidative Stress; D030421:Peroxynitrous Acid / Q000378:metabolism / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects; D015398:Signal Transduction
D006657:Histones; D030421:Peroxynitrous Acid; D009569:Nitric Oxide; D005979:Glutathione Peroxidase; D005982:Glutathione Transferase; D005978:Glutathione