The rate of cellular hydrogen peroxide removal shows dependency on GSH: Mathematical insight intoin vivoH2O2and GPx concentrations

Ng, Charles W. W.; Schäfer, Freya; Buettner, Garry R.; Rodgers, V.G.J.

doi:10.1080/10715760701625075

Cited by 109 publications

(69 citation statements)

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“…Further, it has been previously proposed that the rate of removal of H 2 O 2 is a direct function of GPx activity × GSH 29 . The highest levels of GSH observed and the intense diminution of intracellular GSH levels in C. albicans (Figure 1), together with the GPx activities previously observed for this species 20 (Abegg et al unpublished results), may indicate a more efficient detoxification system of H 2 O 2 through GPx/GSH in C. albicans than in other Candida sp.…”

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confidence: 99%

“…The H 2 O 2 (0.5 mM/1h treatment) used to induce oxidative stress was probably detoxified in part through the action of the enzyme glutathione-peroxidase (GPx) and the concomitant conversion of GSH into GSSG 29 . Increasing GSSG levels can potentially inhibit protein synthesis in animal and plant cells 40,41 , and because of this, Candida cells are likely to export GSSG under conditions of oxidative stress, resulting in a decrease in total intracellular glutathione levels.…”

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confidence: 99%

“…This would seem especially true for H 2 O 2 28 . According to Ng et al 29 the network of enzymes that detoxify H 2 O 2 in biological systems has at least 3 nodes: catalase (which is the longest known enzyme for the removal of H 2 O 2 and requires no cofactors), 6 members of the peroxiredoxin family of enzymes, and the glutathione peroxidases that rely on GSH as the electron donor and specific cofactor.The GSH levels (90-152) observed by Fekete et al 30 in untreated C. albicans isolates were similar to the levels found in this study (Figure 1). …”

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confidence: 99%

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Glutathione levels in and total antioxidant capacity of Candida sp. cells exposed to oxidative stress caused by hydrogen peroxide

Abegg

Alabarse

Schüller

et al. 2012

Rev. Soc. Bras. Med. Trop.

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Candida albicans, C. glabrata, C. tropicalis, and C. parapsilosis account for approximately 95% of identifiable Candida infections. Other species, including C. krusei, C. lusitaniae, and C. guilliermondii, account for less than 5% of cases of invasive candidiasis. The most common causative agent is still C. albicans, but its incidence is declining and the frequencies of other species are increasing. Recently, Furlaneto et al. 1 noted that non-albicans Candida was the predominant species in different clinical specimens, with the exception of urine samples, in a Brazilian tertiary-care hospital. Invasive candidiasis has a mortality rate that approaches 40% 2,3 . Although most people are colonized by Candida sp., the majority never develop invasive candidiasis. Alterations in host immunity, physiological features, or normal microflora, rather than the acquisition of novel or hypervirulent factors by Candida, are suggested to degenerate the commensal-host interaction and lead to an opportunistic infection 4 .During the course of a systemic infection, Candida cells are engulfed by host phagocytes, where they are exposed to reactive oxygen species (ROS) 5 . ROS contribute to the killing of C. albicans in both cultured cells and entire organisms [6][7][8][9] . Upon incubation with macrophages, C. albicans deoxyribonucleic acid (DNA) repair genes are transcriptionally induced, suggesting that DNA damage indeed occurs in the phagosome and that genotoxic hypersensitivity stress would be disadvantageous to the pathogen 10 . Recently, it was demonstrated that a large proportion of C. albicans cell surface antigens related to acute candidemia are involved in oxidative stress 4 . In C. albicans, hyphal cells ABSTRACT Introduction: The capacity to overcome the oxidative stress imposed by phagocytes seems to be critical for Candida species to cause invasive candidiasis. Methods: To better characterize the oxidative stress response (OSR) of 8 clinically relevant Candida sp., glutathione, a vital component of the intracellular redox balance, was measured using the 5,5'-dithiobis-(2-nitrobenzoic acid (DTNB)-glutathione disulfide (GSSG) reductase reconversion method; the total antioxidant capacity (TAC) was measured using a modified method based on the decolorization of the 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic) acid radical cation (ABTS* + ). Both methods were used with cellular Candida sp. extracts treated or not with hydrogen peroxide (0.5 mM). Results: Oxidative stress induced by hydrogen peroxide clearly reduced intracellular glutathione levels. This depletion was stronger in Candida albicans and the levels of glutathione in untreated cells were also higher in this species. The TAC demonstrated intra-specific variation. Conclusions: Glutathione levels did not correlate with the measured TAC values, despite this being the most important non-enzymatic intracellular antioxidant molecule. The results indicate that the isolated measurement of TAC does not give a clear picture of the ability of a given Candida sp. to resp...

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Glutathione levels in and total antioxidant capacity of Candida sp. cells exposed to oxidative stress caused by hydrogen peroxide

Abegg

Alabarse

Schüller

et al. 2012

Rev. Soc. Bras. Med. Trop.

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“…CAT is a common enzyme and it can catalyze the decomposition of H2O2 to water and oxygen [32]. In addition, a previous study demonstrated that the rate of cellular H2O2 removal is partly dependent on GSH level [37]. These antioxidants' decrease might be due to FZD induced production of free radicals which in turn can impair the antioxidant defense system, finally resulting in exacerbating oxidative stress.…”

Section: Discussionmentioning

confidence: 99%

Curcumin Ameliorates Furazolidone Induced DNA Damage and Apoptosis in Human Hepatocyte L02 Cells via Inhibiting ROS Production and Mitochondrial Pathway

Dai

Gong

et al. 2016

Preprint

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Furazolidone (FZD), a synthetic nitrofuran derivative, has been widely used as an antibacterial and antiprotozoal agent. Recently, the potential toxicity of FZD has raised concerns, but its mechanism is still unclear. This study aimed to investigate the protective effect of curcumin on FZD induced cytotoxicity and the underlying mechanism in human hepatocyte L02 cells. The results showed that curcumin pre-treatment significantly ameliorated FZD induced oxidative stress, characterized by decreased reactive oxygen species (ROS) and malondialdehyde formations, and increased superoxide dismutase, catalase activities and glutathione contents. In addition, curcumin pre-treatment significantly ameliorated the loss of mitochondrial membrane potential, the activation of caspase-9 and -3, and apoptosis caused by FZD. Alkaline comet assay showed that curcumin markedly reduced FZD-induced DNA damage in a dose-dependent manner. Consistently, curcumin pre-treatment markedly down-regulated the mRNA expression levels of p53, Bax, caspase-9 and -3 and up-regulated the mRNA expression level of Bcl-2. Taken together, these results revealed that curcumin protects against FZD induced DNA damage and apoptosis via inhibiting oxidative stress and mitochondrial pathway. Our study indicated that curcumin may be a promising combiner with FZD to reduce FZD-related toxicity in the clinical applications.

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“…2GSH + H2O2 → GSSG + 2H2O (72) Kinetic behaviour of the overall reaction is discussed in detail in Ng et al [137].…”

Section: Glutathione Peroxidase (Gpx)mentioning

confidence: 99%

Oxidative Processes and Antioxidative Metaloenzymes

Vašková¹,

Vaško²,

Kron³

2012

Antioxidant Enzyme

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The rate of cellular hydrogen peroxide removal shows dependency on GSH: Mathematical insight intoin vivoH₂O₂and GPx concentrations

Cited by 109 publications

References 48 publications

Glutathione levels in and total antioxidant capacity of Candida sp. cells exposed to oxidative stress caused by hydrogen peroxide

Glutathione levels in and total antioxidant capacity of Candida sp. cells exposed to oxidative stress caused by hydrogen peroxide

Curcumin Ameliorates Furazolidone Induced DNA Damage and Apoptosis in Human Hepatocyte L02 Cells via Inhibiting ROS Production and Mitochondrial Pathway

Oxidative Processes and Antioxidative Metaloenzymes

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