Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage
dc.contributor.author | Manfredini, Vanusa | pt_BR |
dc.contributor.author | Roehrs, Rafael | pt_BR |
dc.contributor.author | Peralba, Maria do Carmo Ruaro | pt_BR |
dc.contributor.author | Henriques, João Antonio Pêgas | pt_BR |
dc.contributor.author | Saffi, Jenifer | pt_BR |
dc.contributor.author | Ramos, Ana Ligia Lia de Paula | pt_BR |
dc.contributor.author | Benfato, Mara da Silveira | pt_BR |
dc.date.accessioned | 2010-04-24T04:15:35Z | pt_BR |
dc.date.issued | 2004 | pt_BR |
dc.identifier.issn | 0100-879X | pt_BR |
dc.identifier.uri | http://hdl.handle.net/10183/21176 | pt_BR |
dc.description.abstract | Saccharomyces cerevisiae mutants deficient in superoxide dismutase genes (sod1∆, sod2∆and the double mutant) were subjected to H2O2 stress in the stationary phase. The highest sensitivity was observed in the sod2∆mutant, while the sod1∆sod2∆double mutant was not sensitive. sod mutants had lower catalase activity (44%) than wildtype cells, independent of H2O2 stress. Untreated cells of sod1∆sod2∆ double mutants showed increased glutathione peroxidase activity (126%), while sod1∆had lower activity (77%) than the wild type. Glutathione levels in sod1∆were increased (200-260%) after exposure to various H2O2 concentrations. In addition, the highest malondialdehyde levels could be observed without H2O2 treatment in sod1∆ (167%) and sod2∆(225%) mutants. In contrast, the level of malondialdehyde in the sod1∆sod2∆double mutant was indistinguishable from that of the wild type. These results suggest that resistance to H2O2 by sod1∆sod2∆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 sod1∆ mutants. | en |
dc.format.mimetype | application/pdf | pt_BR |
dc.language.iso | eng | pt_BR |
dc.relation.ispartof | Brazilian journal of medical and biological research = Revista brasileira de pesquisas médicas e biológicas. Ribeirão Preto, SP. Vol. 37, no. 2 (2004), p. 159-165 | pt_BR |
dc.rights | Open Access | en |
dc.subject | Catalase | en |
dc.subject | Catalase | pt_BR |
dc.subject | Glutationa | pt_BR |
dc.subject | Superoxide dismutase | en |
dc.subject | Glutathione | en |
dc.subject | Saccharomyces cerevisiae : Gene : Mutacao | pt_BR |
dc.subject | Superóxido dismutase | pt_BR |
dc.subject | Hydrogen peroxide | en |
dc.subject | Peróxido de hidrogênio | pt_BR |
dc.subject | Saccharomyces cerevisiae | en |
dc.subject | Espécies reativas de oxigênio | pt_BR |
dc.subject | Reactive oxygen species | en |
dc.title | Glutathione peroxidase induction protects Saccharomyces cerevisiae sod1deltasod2delta double mutants against oxidative damage | pt_BR |
dc.type | Artigo de periódico | pt_BR |
dc.identifier.nrb | 000406308 | pt_BR |
dc.type.origin | Nacional | pt_BR |
Este item está licenciado na Creative Commons License
-
Artigos de Periódicos (39074)Ciências Exatas e da Terra (5943)
-
Artigos de Periódicos (39074)Ciências Biológicas (3009)