Assay for quantitative determination of glutathione and glutathione disulfide levels using enzymatic recycling method

Rahman, Irfan; Kode, Aruna; Biswas, Saibal K

doi:10.1038/nprot.2006.378

Cited by 1,805 publications

(1,154 citation statements)

References 18 publications

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“…measured GSH and ROS levels in acute GDAP1 knockdown cells by the enzymatic recycling method and 2,7-dichlorofluorescin (DCF) fluorescence intensity measurements, respectively [17,29]. Cellular GSH levels after GDAP1 knockdown by two individual shRNAs showed no significant difference to control cells ( Fig 2B).…”

Section: Gdap1 In Peroxisomal Fissionmentioning

confidence: 95%

Charcot‐Marie‐Tooth disease‐associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission

et al. 2013

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Mitochondria and peroxisomes can be fragmented by the process of fission. The fission machineries of both organelles share a set of proteins. GDAP1 is a tail-anchored protein of mitochondria and induces mitochondrial fragmentation. Mutations in GDAP1 lead to Charcot-Marie-Tooth disease (CMT), an inherited peripheral neuropathy, and affect mitochondrial dynamics. Here, we show that GDAP1 is also targeted to peroxisomes mediated by the import receptor Pex19. Knockdown of GDAP1 leads to peroxisomal elongation that can be rescued by re-expressing GDAP1 and by missense mutated forms found in CMT patients. GDAP1-induced peroxisomal fission is dependent on the integrity of its hydrophobic domain 1, and on Drp1 and Mff, as is mitochondrial fission. Thus, GDAP1 regulates mitochondrial and peroxisomal fission by a similar mechanism. However, our results reveal also a more critical role of the amino-terminal GDAP1 domains, carrying most CMT-causing mutations, in the regulation of mitochondrial compared to peroxisomal fission.

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Section: Gdap1 In Peroxisomal Fissionmentioning

confidence: 95%

Charcot‐Marie‐Tooth disease‐associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission

et al. 2013

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“…Reduced (GSH) and oxidized (GSSG) glutathione content were determined according to Rahman et al (2007), using reduced and oxidized glutathione standards (0-60 μmol/L). Absorbance was measured at 412 nm.…”

Section: Indicators Of Oxidative Stressmentioning

confidence: 99%

Chronic toxicity of the antiepileptic carbamazepine on the clam Ruditapes philippinarum

Almeida

Freitas

Calisto

et al. 2015

Comparative Biochemistry and Physiology Part C: Toxicology &

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The impacts of carbamazepine (CBZ) on aquatic organisms are yet not well investigated. The present study aimed to better understand the chronic effects of environmentally relevant concentrations of CBZ. The experiment was performed by exposing the filter feeding clam Ruditapes philippinarum to 0.00, 0.03, 0.30, 3.00 and 9.00 μg/L, during 28 days. To assess the chronic toxicity of the drug a battery of biomarkers related with health status and oxidative stress was applied. In order to quantify CBZ in the clam's tissues and in water samples ELISA was used. The present study showed three types of responses on the clams after a chronic exposure to CBZ. For control condition and the lower concentrations (0.03 and 0.30 μg/L) a "similar" metabolic state was observed and the most efficient antioxidant status leading to the elimination of reactive oxygen species formed during the metabolism of CBZ. The concentration of 3.00 μg/L seemed to be a "threshold" concentration, beyond which the concentration levels of CBZ began to exert a toxic effect, compromising the activity of biotransformation and antioxidant enzymes, with notorious effects at the highest CBZ concentration (9.00 μg/L). CBZ also seemed to alter the energy-related responses, especially the glycogen and electron system responses, revealing a slowdown in metabolism at the higher exposure concentrations (3.00 and 9.00 μg/L). Overall, the present study demonstrated that the higher CBZ concentrations can lead to the impairment of antioxidant enzymes compromising the neutralization of reactive oxygen species, and thus the ability to cope with oxidative stress.

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“…(A) Superimposition of homology-modelled ChaC1 structure (cyan colour) on g-GCT structure (yellow colour). (B) Putative active site residues of ChaC1 ( 39 YGSL 42 and E 116 , cyan in colour) were superimposed on corresponding active site residues of g-GCT ( 22 YGSN 25 and E 98 , yellow in colour). g-GCT residues are labelled in yellow colour.…”

Section: Chac Proteins Allow Utilization Of Glutathione In Yeastsmentioning

confidence: 99%

Mammalian proapoptotic factor ChaC1 and its homologues function as γ‐glutamyl cyclotransferases acting specifically on glutathione

et al. 2012

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ChaC1 is a mammalian proapoptic protein of unknown function induced during endoplasmic reticulum stress. We show using in vivo studies and novel in vitro assays that the ChaC family of proteins function as c-glutamyl cyclotransferases acting specifically to degrade glutathione but not other c-glutamyl peptides. The overexpression of these proteins (but not the catalytically dead E4Q mutants) led to glutathione depletion and enhanced apoptosis in yeast. The ChaC family is conversed across all phyla and represents a new pathway for glutathione degradation in living cells, and the first cytosolic pathway for glutathione degradation in mammalian cells.

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Assay for quantitative determination of glutathione and glutathione disulfide levels using enzymatic recycling method

Cited by 1,805 publications

References 18 publications

Charcot‐Marie‐Tooth disease‐associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission

Charcot‐Marie‐Tooth disease‐associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission

Chronic toxicity of the antiepileptic carbamazepine on the clam Ruditapes philippinarum

Mammalian proapoptotic factor ChaC1 and its homologues function as γ‐glutamyl cyclotransferases acting specifically on glutathione

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