Dimethyl sulfoxide elevates hydrogen peroxide-mediated cell death in Saccharomyces cerevisiae by inhibiting the antioxidant function of methionine sulfoxide reductase A

Kwak, Geun-Hee; Choi, Seung Hee; Kim, Hwa-Young

doi:10.3858/bmbrep.2010.43.9.622

Cited by 4 publications

(6 citation statements)

References 31 publications

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“…It has been reported that DMSO affects the oxidative stress-induced cytotoxicity in two completely different ways on yeast and mammalian cells (Kwak et al, 2010). In sharp contrast to its cytotoxic effect in yeast under oxidative stress, DMSO showed a protective effect on oxidative stress-induced cytotoxicity in human SK-Hep1 cells (Kwak et al, 2010). In sharp contrast to its cytotoxic effect in yeast under oxidative stress, DMSO showed a protective effect on oxidative stress-induced cytotoxicity in human SK-Hep1 cells (Kwak et al, 2010).…”

Section: Introductionmentioning

confidence: 97%

“…It is an effective penetration enhancer and is routinely used as a cryoprotectant (Kashino et al, 2010;Kwak et al, 2010). Its amphiphilic nature appears to be an important characteristic defining its action on membranes.…”

Section: Introductionmentioning

confidence: 99%

“…It has been reported that DMSO affects the oxidative stress-induced cytotoxicity in two completely different ways on yeast and mammalian cells (Kwak et al, 2010). It has been reported that DMSO affects the oxidative stress-induced cytotoxicity in two completely different ways on yeast and mammalian cells (Kwak et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…The reasons for these cellular differences in DMSO effects are unclear (Qi et al, 2008). In the yeast, DMSO was found to inhibit in vivo methionine-S-sulfoxide reduction by competitively inhibiting methionine sulfoxide reductase A activity (Kwak et al, 2010). DMSO reduced also arsenite-or hydrogen peroxide (H 2 O 2 )-induced intracellular ROS production in human hamster hybrid and mouse embryo cells and was capable of trapping nitric oxide free radicals in human umbilical vein endothelial cells.…”

Section: Introductionmentioning

confidence: 99%

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Dimethyl sulfoxide induces oxidative stress in the yeastSaccharomyces cerevisiae

et al. 2013

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Dimethyl sulfoxide (DMSO) is used as a cryoprotectant for the preservation of cells, including yeast, and as a solvent for chemical compounds. We report that DMSO induces oxidative stress in the yeast. Saccharomyces cerevisiae wt strain EG-103 and its mutants Δsod1, Δsod2, and Δsod1 Δsod2 were used. Yeast were subjected to the action of 1-14% DMSO for 1 h at 28 °C. DMSO induced a concentration-dependent inhibition of yeast growth, the effect being more pronounced for mutants devoid of SOD (especially Δsod1 Δsod2). Cell viability was compromised. DMSO-concentration-dependent activity loss of succinate dehydrogenase, a FeS enzyme sensitive to oxidative stress, was observed. DMSO enhanced formation of reactive oxygen species, estimated with dihydroethidine in a concentration-dependent manner, the effect being again more pronounced in mutants devoid of superoxide dismutases. The content of cellular glutathione was increased with increasing DMSO concentrations, which may represent a compensatory response. Membrane fluidity, estimated by fluorescence polarization of DPH, was decreased by DMSO. These results demonstrate that DMSO, although generally considered to be antioxidant, induces oxidative stress in yeast cells.

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Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Dimethyl sulfoxide induces oxidative stress in the yeastSaccharomyces cerevisiae

et al. 2013

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“…Dimethyl sulfoxide, which competitively inhibits methionine sulfoxide reduction activity of MsrA, was able to enhance hydrogen peroxide‐mediated S . cerevisiae cell death and markedly accumulate protein‐carbonyl under oxidative stress . However, differences in defensive roles of MsrA and MsrB under various stress conditions currently remain unclear.…”

Section: Discussionmentioning

confidence: 99%

Protective roles of methionine‐R‐sulfoxide reductase against stresses in Schizosaccharomyces pombe

Cho

et al. 2013

J. Basic Microbiol.

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The Schizosaccharomyces pombe msrB(+) gene encoding methionine-R-sulfoxide reductase (MsrB) was cloned into the shuttle vector pRS316 to generate the recombinant plasmid pFMetSO. The msrB(+) mRNA level was significantly increased in the S. pombe cells harboring pFMetSO, indicating that the cloned msrB(+) gene is functioning. In the presence of 0.1 mM L-methionine-(R,S)-sulfoxide, the S. pombe cells harboring pFMetSO could grow normally but the growth of the vector control cells was almost arrested. The S. pombe cells harboring pFMetSO exhibited the enhanced growth on the minimal medium plates with stress-inducing agents, such as hydrogen peroxide, superoxide radical-generating menadione (MD), nitric oxide (NO)-generating sodium nitroprusside (SNP), and cadmium (Cd), when compared with the vector control cells. They also gave rise to the enhanced growth at the high incubation temperature of 37 °C than the vector control cells. The S. pombe cells harboring pFMetSO contained lower reactive oxygen species (ROS) and higher total glutathione (GSH) levels than the vector control cells. In brief, the S. pombe MsrB plays a protective role against oxidative, nitrosative, and thermal stresses, and is involved in diminishing intracellular ROS level.

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Methionine Sulfoxide Reductase A Negatively Controls Microglia-Mediated Neuroinflammation via Inhibiting ROS/MAPKs/NF-κB Signaling Pathways Through a Catalytic Antioxidant Function

Fan

Zhang

et al. 2015

Antioxidants & Redox Signaling

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Aims: Oxidative burst is one of the earliest biochemical events in the inflammatory activation of microglia. Here, we investigated the potential role of methionine sulfoxide reductase A (MsrA), a key antioxidant enzyme, in the control of microglia-mediated neuroinflammation. Results: MsrA was detected in rat microglia and its expression was upregulated on microglial activation. Silencing of MsrA exacerbated lipopolysaccharide (LPS)-induced activation of microglia and the production of inflammatory markers, indicating that MsrA may function as an endogenous protective mechanism for limiting uncontrolled neuroinflammation. Application of exogenous MsrA by transducing Tat-rMsrA fusion protein into microglia attenuated LPS-induced neuroinflammatory events, which was indicated by an increased Iba1 (a specific microglial marker) expression and the secretion of pro-inflammatory cytokines, and this attenuation was accompanied by inhibiting multiple signaling pathways such as p38 and ERK mitogen-activated protein kinases (MAPKs) and nuclear factor kappaB (NF-jB). These effects were due to MsrA-mediated reactive oxygen species (ROS) elimination, which may be derived from a catalytic effect of MsrA on the reaction of methionine with ROS. Furthermore, the transduction of Tat-rMsrA fusion protein suppressed the activation of microglia and the expression of pro-inflammatory factors in a rat model of neuroinflammation in vivo. Innovation: This study provides the first direct evidence for the biological significance of MsrA in microglia-mediated neuroinflammation. Conclusion: Our data provide a profound insight into the role of endogenous antioxidative defense systems such as MsrA in the control of microglial function. Antioxid. Redox Signal. 22, 832-847.

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Dimethyl sulfoxide elevates hydrogen peroxide-mediated cell death in Saccharomyces cerevisiae by inhibiting the antioxidant function of methionine sulfoxide reductase A

Cited by 4 publications

References 31 publications

Dimethyl sulfoxide induces oxidative stress in the yeastSaccharomyces cerevisiae

Dimethyl sulfoxide induces oxidative stress in the yeastSaccharomyces cerevisiae

Protective roles of methionine‐R‐sulfoxide reductase against stresses in Schizosaccharomyces pombe

Methionine Sulfoxide Reductase A Negatively Controls Microglia-Mediated Neuroinflammation via Inhibiting ROS/MAPKs/NF-κB Signaling Pathways Through a Catalytic Antioxidant Function

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