Microsomal glutathione transferase 1 is not S-nitrosylated in rat liver microsomes or in endotoxin challenged rats
- 作者：Shi ; Qiang ; Lou ; Yi-jia
- 关键词：Microsomal glutathione transferase 1 ; S-Nitrosylation ; Proteomics ; Microsomes ; Endotoxin
- 刊名：Pharmacological Research
- 出版年：2005
- 期刊代码：54_10436618
- 类别：pha
- 出版时间：April, 2005
- 卷：51
- 期：4
- 页码：303-310
- 文件大小：230 K
摘要
In vitro activation of purified rat microsomal glutathione transferase 1 (MGST1) by S-nitrosylation has been recently reported. This study was designated to explore its in vivo relevance. Unexpectedly, we failed to detect S-nitrosylated MGST1 in rat liver microsomes treated with S-nitrosoglutathione (GSNO); neither did we observe MGST1 S-nitrosylation in endotoxin challenged rats. However, by using matrix-assisted laser dissociation/ionization time-of-flight mass spectrometry (MALDI-TOF MS), we identified several other proteins which are susceptible to S-nitrosylation in liver microsomes, including retinol dehydrogenase type I (RODH I), aldolase B, cytochrome P4502C11, and peroxiredoxin 1. Our results suggest that MGST1 S-nitrosylation is unlikely to be involved in the protection mechanism against nitrosative stress caused by endotoxin challenge. Further studies on the novel S-nitrosylable microsomal proteins are also warranted.