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• W2004615772 abstract "The effect of reactive nitrogen species on rat liver microsomal glutathione S-transferase (MGST1) was investigated using microsomes and purified MGST1. When microsomes or the purified enzyme were incubated with peroxynitrite (ONOO−), the GST activity was increased to 2.5–6.5 fold in concentration-dependent manner and a small amount of the MGST1 dimer was detected. MGST1 activity was increased by ONOO− in the presence of high amounts of reducing agents including glutathione (GSH) and the activities increased by ONOO− or ONOO− plus GSH treatment were decreased by 30–40% by further incubation with dithiothreitol (DTT, reducing disulfide) or by sodium arsenite (reducing sulfenic acid). Furthermore, GSH was detected by HPLC from the MGST1 which was incubated with ONOO− plus GSH or S-nitrosoglutathione followed by DTT treatment. In addition, the MGST1 activity increased by nitric oxide (NO) donors such as S-nitrosoglutathione, S-nitrosocysteine or the non-thiol NO donor 1-hydroxy-2-oxo-3 (3-aminopropyl)-3-isopropyl was restored by the DTT treatment. Since DTT can reduce S-nitrosothiol and disulfide bond to thiol, S-nitrosylation and a mixed disulfide bond formation of MGST1 were suggested. Thus, it was demonstrated that MGST1 is activated by reactive nitrogen species through a forming dimeric protein, mixed disulfide bond, nitrosylation and sulfenic acid." @default.
• W2004615772 created "2016-06-24" @default.
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• W2004615772 date "2006-05-01" @default.
• W2004615772 modified "2023-09-27" @default.
• W2004615772 title "Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase" @default.
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• W2004615772 doi "https://doi.org/10.1016/j.lfs.2005.11.026" @default.
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