Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage
Saccharomyces cerevisiae mutants deficient in superoxide dismutase genes (sod1delta, sod2delta and the double mutant) were subjected to H2O2 stress in the stationary phase. The highest sensitivity was observed in the sod2delta mutant, while the sod1deltasod2delta double mutant was not sensitive. Sod...
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| Format: | Article |
| Language: | English |
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Associação Brasileira de Divulgação Científica
2004-02-01
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| Series: | Brazilian Journal of Medical and Biological Research |
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| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000200001&tlng=en |
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| author | V. Manfredini R. Roehrs M.C.R. Peralba J.A.P. Henriques J. Saffi A.L.L.P. Ramos M.S. Benfato |
| author_facet | V. Manfredini R. Roehrs M.C.R. Peralba J.A.P. Henriques J. Saffi A.L.L.P. Ramos M.S. Benfato |
| author_sort | V. Manfredini |
| collection | DOAJ |
| description | Saccharomyces cerevisiae mutants deficient in superoxide dismutase genes (sod1delta, sod2delta and the double mutant) were subjected to H2O2 stress in the stationary phase. The highest sensitivity was observed in the sod2delta mutant, while the sod1deltasod2delta double mutant was not sensitive. Sod mutants had lower catalase activity (44%) than wild-type cells, independent of H2O2 stress. Untreated cells of sod1deltasod2delta double mutants showed increased glutathione peroxidase activity (126%), while sod1delta had lower activity (77%) than the wild type. Glutathione levels in sod1delta were increased (200-260%) after exposure to various H2O2 concentrations. In addition, the highest malondialdehyde levels could be observed without H2O2 treatment in sod1delta (167%) and sod2delta (225%) mutants. In contrast, the level of malondialdehyde in the sod1deltasod2delta double mutant was indistinguishable from that of the wild type. These results suggest that resistance to H2O2 by sod1deltasod2delta cells depends on the induction of glutathione peroxidase and is independent of catalase, and that glutathione is a primary antioxidant in the defense against H2O2 in stationary phase sod1delta mutants. |
| first_indexed | 2024-04-11T16:43:14Z |
| format | Article |
| id | doaj.art-f6ad4e0db7ec4100aaf436fc9e3fb56c |
| institution | Directory Open Access Journal |
| issn | 1414-431X |
| language | English |
| last_indexed | 2024-04-11T16:43:14Z |
| publishDate | 2004-02-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-f6ad4e0db7ec4100aaf436fc9e3fb56c2022-12-22T04:13:37ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research1414-431X2004-02-0137215916510.1590/S0100-879X2004000200001Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damageV. Manfredini0R. Roehrs1M.C.R. Peralba2J.A.P. Henriques3J. Saffi4A.L.L.P. Ramos5M.S. Benfato6Universidade Federal do Rio Grande do SulUniversidade Federal do Rio Grande do SulUniversidade Federal do Rio Grande do SulUniversidade Federal do Rio Grande do SulUniversidade Federal do Rio Grande do SulUniversidade Federal do Rio Grande do SulUniversidade Federal do Rio Grande do SulSaccharomyces cerevisiae mutants deficient in superoxide dismutase genes (sod1delta, sod2delta and the double mutant) were subjected to H2O2 stress in the stationary phase. The highest sensitivity was observed in the sod2delta mutant, while the sod1deltasod2delta double mutant was not sensitive. Sod mutants had lower catalase activity (44%) than wild-type cells, independent of H2O2 stress. Untreated cells of sod1deltasod2delta double mutants showed increased glutathione peroxidase activity (126%), while sod1delta had lower activity (77%) than the wild type. Glutathione levels in sod1delta were increased (200-260%) after exposure to various H2O2 concentrations. In addition, the highest malondialdehyde levels could be observed without H2O2 treatment in sod1delta (167%) and sod2delta (225%) mutants. In contrast, the level of malondialdehyde in the sod1deltasod2delta double mutant was indistinguishable from that of the wild type. These results suggest that resistance to H2O2 by sod1deltasod2delta cells depends on the induction of glutathione peroxidase and is independent of catalase, and that glutathione is a primary antioxidant in the defense against H2O2 in stationary phase sod1delta mutants.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000200001&tlng=enCatalaseSuperoxide dismutaseGlutathioneHydrogen peroxideSaccharomyces cerevisiaeReactive oxygen species |
| spellingShingle | V. Manfredini R. Roehrs M.C.R. Peralba J.A.P. Henriques J. Saffi A.L.L.P. Ramos M.S. Benfato Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage Brazilian Journal of Medical and Biological Research Catalase Superoxide dismutase Glutathione Hydrogen peroxide Saccharomyces cerevisiae Reactive oxygen species |
| title | Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage |
| title_full | Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage |
| title_fullStr | Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage |
| title_full_unstemmed | Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage |
| title_short | Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage |
| title_sort | glutathione peroxidase induction protects saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage |
| topic | Catalase Superoxide dismutase Glutathione Hydrogen peroxide Saccharomyces cerevisiae Reactive oxygen species |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000200001&tlng=en |
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