Recent Trends in Glutathione Biochemistry—Glutathione–Protein Interactions: A Molecular Link between Oxidative Stress and Cell Proliferation?

Cotgreave, Ian A.; Gerdes, Robert

doi:10.1006/bbrc.1997.7812

Cited by 428 publications

(255 citation statements)

References 120 publications

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“…GSH also provides, directly or secondarily, reducing equivalents for the elimination of peroxides. In addition, GSH forms protein mixed disulfides with thiyl radicals of protein cysteinyl residues (Wardman, 1995;Cotgreave and Gerdes, 1998;Droge, 2002). This reaction is reversible and affords protection for protein thiols against further oxidation, and may act as a mechanism for the redox-based regulation of biosignaling and gene transcription.…”

Section: Discussionmentioning

confidence: 99%

“…One consequence of oxidation of GSH and/or protein cysteinyl residues is the uncatalyzed formation of protein-glutathionyl mixed disulfides. This reversible interaction has been postulated to serve as a regulatory mechanism for proteins involved in a variety of functions such as biosignaling, gene transcription, and catalytic activities (Cotgreave and Gerdes, 1998;Droge, 2002). An age-associated, prooxidizing shift in glutathione redox state and an elevation of protein mixed disulfides (protein-SSG) have been previously reported in Drosophila melanogaster (Rebrin et al, 2004) and different tissues of C57BL/6 mice (Rebrin et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

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Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice

2007

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The main purpose of the present study was to determine whether specific regions of the mouse brain exhibit different age-related changes in oxidative stress, as indicated by glutathione redox state and the level of protein-glutathionyl mixed disulfides. Comparison of 3-and 21-month-old mice indicated an age-related decrease in the ratio of reduced to oxidized glutathione (GSH:GSSG) as well as a prooxidizing shift in the calculated redox potential (ranging from 6 to 15 mV) in the cortex, hippocampus, striatum and cerebellum, whereas there was little change in the brainstem. This pro-oxidizing shift in redox state was due to a modest decrease in GSH content occurring in all the brain regions examined, and elevations in GSSG amount that were most pronounced in the striatum and cerebellum. The regional changes in glutathione redox state were paralleled by increases in the amounts of protein-mixed disulfides. A reduction of caloric intake by 40% for a short period (7 weeks), implemented in relatively old mice (17 months), increased the GSH:GSSG ratio and redox potential at 19 months in the same brain regions that exhibited age-related decreases. The effects of age and caloric restriction were qualitatively similar in C57BL/6 and DBA/2 mice. However, young DBA/2 mice, which do not show extension of life span in response to long-term caloric restriction, had lower GSH:GSSG ratios and higher protein-mixed disulfides than age-matched C57BL/6 mice. The current findings demonstrate that oxidative stress, as reflected by glutathione redox state, increases in the aging brain in regions linked to age-associated losses of function and neurodegenerative diseases.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice

2007

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“…28). Cys-SOH is an intermediate form involved in redox regulation and catalysis by protein sulfhydryl groups (reviewed in 6).…”

Section: Discussionmentioning

confidence: 99%

20 S Proteasome from Saccharomyces cerevisiae Is Responsive to Redox Modifications and IsS-Glutathionylated

Demasi

Silva

Netto

2003

Journal of Biological Chemistry

114

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“…Redox status affects virtually all cellular processes including DNA synthesis, transcriptional activation, enzyme kinetics, and protein folding (Sen and Packer, 1996;Cotgreave and Gerdes, 1998) and trafficking (Pfau, et al, 2004). Differentiation processes, then, are inevitably impacted by redox potential changes.…”

Section: Introductionmentioning

confidence: 99%

A reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle

Hansen

Klass

Harris

et al. 2007

Cell Biology International

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Intracellular redox potential of skeletal muscle becomes progressively more oxidized with aging, negatively impacting regenerative ability. We examined the effects of oxidizing redox potential on terminal differentiation of cultured C2C12 myoblasts. Redox potentials were manipulated by changing the culture O 2 environment, by free radical scavenging, or addition of H 2 O 2. Intracellular reactive oxygen species (ROS) production was higher in 20% environmental O 2 and in this condition, redox potential became progressively oxidized compared to cultures in 6% O 2. Treatment with a ROS trapping agent (phenyl-N-tert-butylnitrone, PBN) caused reducing redox potentials and enhanced C2C12 differentiation, while addition of 25 μM H 2 O 2 to cells in 20% O 2 dramatically slowed differentiation. Under these most oxidative conditions, quantitative PCR showed a significant decrease in myogenic basic helix-loop-helix transcription factor expression compared to cultures treated with phenyl PBN or grown in 6% O 2 . Thus, oxidative intracellular environments impair myoblast differentiation, while reducing environments favor myogenesis.

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Recent Trends in Glutathione Biochemistry—Glutathione–Protein Interactions: A Molecular Link between Oxidative Stress and Cell Proliferation?

Cited by 428 publications

References 120 publications

Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice

Effects of age and caloric intake on glutathione redox state in different brain regions of C57BL/6 and DBA/2 mice

20 S Proteasome from Saccharomyces cerevisiae Is Responsive to Redox Modifications and IsS-Glutathionylated

A reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle

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