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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Requirement of glutathione for Sod1 activation during lifespan extension

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Author(s):
Mannarino, Sergio C. [1] ; Vilela, Leonardo F. [1] ; Brasil, Aline A. [1] ; Aranha, Juliana N. [1] ; Moradas-Ferreira, Pedro [2, 3] ; Pereira, Marcos D. [1] ; Costa, Vitor [2, 3] ; Eleutherio, Elis C. A. [1]
Total Authors: 8
Affiliation:
[1] UFRJ, Inst Quim, Dept Bioquim, BR-21941909 Rio De Janeiro - Brazil
[2] IBMC, P-4150180 Oporto - Portugal
[3] Univ Porto, Dept Biol Mol, ICBAS, P-4100 Oporto - Portugal
Total Affiliations: 3
Document type: Journal article
Source: YEAST; v. 28, n. 1, p. 19-25, JAN 2011.
Web of Science Citations: 13
Abstract

It has been shown that the activation of cytosolic superoxide dismutase (Sod1) in Saccharomyces cerevisiae is only dependent on Ccs1, which is responsible for insertion of copper into the enzyme catalytic center, and that glutathione (GSH) is not necessary for this process. In this work, we addressed an important role of GSH in Sod1 activation by a Ccs1-dependent mechanism during oxidative stress and its role in yeast lifespan. Exponential cells of Saccharomyces cerevisiae, treated or not with 0.5 mM menadione for 1 h, were used for evaluation of the effect of a mild oxidative stress pre-treatment on chronological lifespan. The results showed that menadione induced a lifespan extension in the wild-type (WT) strain but this adaptive response was repressed in gsh1 and in sod1 strains. Interestingly, menadione treatment increased SOD1 and CCS1 gene expression in both WT and gsh1 strains. However, while these strains showed the same Sod1 activity before treatment, only the WT presented an increase of Sod1 activity after menadione exposure. Glutathionylation seems to be essential for Sod1 activation since no increase in activity was observed after menadione treatment in grx1 and grx2 null mutants. Our results suggest that GSH and glutathionylation are fundamental to protect Sod1 sulfhydryl residues under mild oxidative stress, enabling Sod1 activation and lifespan extension. Copyright (C) 2010 John Wiley \& Sons, Ltd. (AU)

FAPESP's process: 04/10067-6 - Stress, transport and metabolism of alpha-glycosides in Saccharomyces cerevisiae
Grantee:Pedro Soares de Araujo
Support Opportunities: Research Projects - Thematic Grants