Effects of glutathione reductase inhibition on cellular thiol redox state and related systems

Zhao, Y., Seefeldt, T., Chen, W., Wang, X., Matthees, D., Hu, Y. and Guan, X. (2009) Effects of glutathione reductase inhibition on cellular thiol redox state and related systems. Archives of Biochemistry and Biophysics, 485 (1). pp. 56-62.

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].

Item Type:	Journal Article
Publisher:	Elsevier
Copyright:	© 2009 Elsevier Inc.
URI:	http://researchrepository.murdoch.edu.au/id/eprint/65341

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