Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 485, Issue 1, Pages 56-62Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2009.03.001
Keywords
Glutathione reductase inhibitor; Thiol redox state; Protein thiols; GSH; GSSG
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Funding
- National Institutes of Health [CA098810-01, CA120062-01]
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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 [gamma-glutamylcysteine synthetase and glutathione synthetase]. (C) 2009 Elsevier Inc. All rights reserved.
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