Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage

Manfredini, Vanusa; Roehrs, Rafael; Peralba, Maria do Carmo Ruaro; Henriques, João Antônio Pêgas; Saffi, Jenifer; Ramos, Ana Lı́gia Lia de Paula; Benfato, Mara da Silveira

doi:10.1590/s0100-879x2004000200001

Cited by 16 publications

(12 citation statements)

References 24 publications

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“…The reduced catalase levels with increasing amounts of paraquat (Fig. 3A,B) suggest that, as with the experiment described by Manfredini et al, 24 other antioxidant defenses (which were not measured by us) such as GPx or total glutathione content may be altered in these strains.…”

Section: Discussionsupporting

confidence: 79%

Antioxidant activity of L-ascorbic acid in wild-type and superoxide dismutase deficient strains ofSaccharomyces cerevisiae

et al. 2006

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Much has been published on the non-enzymatic antioxidant L-ascorbic acid (vitamin C), but even so its interaction with endogenous cellular defense systems has not yet been fully elucidated. Our study investigated the antioxidant activity of L-ascorbic acid in wild-type strain EG103 (SOD) Saccharomyces cerevisiae and isogenic mutant strains deficient in cytosolic superoxide dismutase (sod1delta), mitochondrial superoxide dismutase (sod2delta) or both (sod1delta sod2delta), metabolizing aerobically or anaerobically with and without the stressing agent paraquat. The results show that during both aerobic and anaerobic metabolism there was a significant increase in the survival of both wild-type S. cerevisiae cells and the mutant cells (sod1delta, sod2delta and sod1delta sod2delta) when pretreated with L-ascorbic acid before exposure to paraquat. Exposure to paraquat resulted in higher catalase activity but this significantly decreased when the cells were pre-treated with L-ascorbic acid. These results demonstrate that due to the damage caused by paraquat, the antioxidant protection of L-ascorbic acid seems to be mediated by catalase levels in yeast cells.

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Section: Discussionsupporting

confidence: 79%

Antioxidant activity of L-ascorbic acid in wild-type and superoxide dismutase deficient strains ofSaccharomyces cerevisiae

et al. 2006

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“…Untreated cells of sod1Δsod2Δ double mutant showed increased glutathione peroxidase activity (126%), while sod1Δ had lower activity (77%) than the wild-type. These results suggest that the resistance to H 2 O 2 by sod1Δsod2Δ cells depends on the induction of glutathione peroxidase and is independent of catalase in stationary phase and microaerophilic conditions (9). Because the level of oxygen modifies the concentration of ROS in the cell, the present investigation intends to evaluate the alterations occurring in the mechanisms of antioxidant defense of the yeast in conditions of high aeration, making a comparison with the results obtained in microaerophilic conditions.…”

Section: Introductionmentioning

confidence: 98%

“…Previous studies performed in our laboratory evaluated the activities of the antioxidant enzymes (CAT and GPx) and the sensibility of the sod mutants to H 2 O 2 in microaerophilic conditions (9). The highest sensitivity to H 2 O 2 was observed in the sod2Δ mutant, while the sod1Δsod2Δ double mutant was not sensitive.…”

Section: Introductionmentioning

confidence: 99%

“…Neither MnSOD nor CuZnSOD is strictly essential; however, the loss of CuZnSOD has dramatic phenotypic consequences in yeast. Yeast strains lacking CuZnSOD (sod1Δ) show reduced growth rates in glycerol and ethanol, auxotrophy for lysine and methionine or cysteine, a higher rate of spontaneous mutation and more rapid loss of viability in the stationary phase (3,7,9). sod2Δ mutants are oxygen-sensitive and, when required to utilize oxygen, grow poorly.…”

Section: Introductionmentioning

confidence: 99%

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High levels of catalase in sod mutants of Saccharomyces cerevisiae in high aeration conditions

Martins¹,

Manfredini²,

Benfato³

2005

Braz. J. Microbiol.

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Saccharomyces cerevisiae mutants deficient in superoxide dismutase genes (sod1Δ, sod2Δ and sod1Δsod2Δ mutants) in a stationary phase of growth under high aeration conditions were subjected to H2O2 stress. All the mutants were sensitive after H2O2 treatment. Glutathione peroxidase levels were significantly lower in sod1Δ and sod2Δ single mutants than in the wild-type without treatment. After exposure to H2O2 concentrations, glutathione peroxidase levels were increased in sod1Δsod2Δ double mutants and the sod2Δ single mutant, while sod1Δ maintained lower gluthatione peroxidase activities. The sod2Δ mutant demonstrated a similar catalase activity to that of the wild-type without treatment, whilst decreased catalase activity was observed in conditions of low aeration. Untreated sod1Δsod2Δ double mutant cells presented a lower catalase activity. Catalase levels were higher under high aeration conditions than under microaerophilic conditions, including in sod1Δsod2Δ cells that contain less H2O2, since SOD catalyzes the cleavage of superoxide producing H2O2 and oxygen. We suggest that catalase is not essential for sod mutants under normal conditions, but plays an important role in the acquisition of tolerance to oxidative stress induced by high aeration.

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“…Lee et al 37 found that a 6-h treatment with 0.1mM H 2 O 2 provoked a 3.14-fold elevation in GSH levels in Schizosaccharomyces pombe. Manfredini et al 38 reported an increase in GSH levels upon treatment with 0.5mM H 2 O 2 in wild-type S. cerevisiae cells and a significant reduction in those levels with 5mM H 2 O 2 . These differences regarding our results may be related to the duration of treatment, the use of different oxidants or lower doses of hydrogen peroxide, or to differences in the metabolic activities of the species.…”

mentioning

confidence: 99%

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 peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage

Cited by 16 publications

References 24 publications

Antioxidant activity of L-ascorbic acid in wild-type and superoxide dismutase deficient strains ofSaccharomyces cerevisiae

Antioxidant activity of L-ascorbic acid in wild-type and superoxide dismutase deficient strains ofSaccharomyces cerevisiae

High levels of catalase in sod mutants of Saccharomyces cerevisiae in high aeration conditions

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

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