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Effects of glutathione reductase inhibition on cellular thiol redox state and related systems |
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| Authors: | Yong Zhao Wei Chen Duane Matthees Xiangming Guan |
| Institution: | a Department of Physiology, Michigan State University, East Lansing, MI 48824, USA b Department of Pharmaceutical Sciences, College of Pharmacy, South Dakota State University, Brookings, SD 57007, USA c Department of Biology and Microbiology, College of Agriculture and Biological Sciences, South Dakota State University, Brookings, SD 57007, USA d Department of Veterinary Science, College of Agriculture and Biological Sciences, South Dakota State University, Brookings, SD 57007, USA |
| Abstract: | Although inhibition of glutathione reductase (GR) has been demonstrated to cause a decrease in reduced glutathione (GSH) and increase in glutathione disulfide (GSSG), a systematic study of the effects of GR inhibition on thiol redox state and related systems has not been noted. By employing a monkey kidney cell line as the cell model and 2-acetylamino-3-4-(2-acetylamino-2-carboxy-ethylsulfanylthio carbonylamino)phenylthiocarbamoylsulfanyl]propionic acid (2-AAPA) as a GR inhibitor, an investigation of the effects of GR inhibition on cellular thiol redox state and related systems was conducted. Our study demonstrated that, in addition to a decrease in GSH and increase in GSSG, 2-AAPA increased the ratios of NADH/NAD+ and NADPH/NADP+. Significant protein glutathionylation was observed. However, the inhibition did not affect the formation of reactive oxygen species or expression of antioxidant defense enzyme systems GR, glutathione peroxidase, catalase, and superoxide dismutase] and enzymes involved in GSH biosynthesis γ-glutamylcysteine synthetase and glutathione synthetase]. |
| Keywords: | Glutathione reductase inhibitor Thiol redox state Protein thiols GSH GSSG |
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