Protein S-glutathionylation: a regulatory device from bacteria to humans

Dalle‐Donne, Isabella; Rossi, Ranieri; Colombo, Graziano; Giustarini, Daniela; Milzani, Aldo

doi:10.1016/j.tibs.2008.11.002

Cited by 566 publications

(512 citation statements)

References 88 publications

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“…Gluthationylation can be triggered by oxidative stress when the GSH : GSSG ratio is reduced (not seen here), but it can also be generated by specific enzymes potentially acting independently of oxidative stress (Ghezzi 2013). Glutathionylation has attracted the attention of biomedicine because it is a potent mechanism for posttranslational modification of metabolic and regulatory proteins, influencing pathways from energy metabolism to inflammation and apoptosis (Dalle-Donne et al 2009;Zhang and Forman 2012;Ghezzi 2013). However, its function in the physiological systems of the organism of animals as a whole is still poorly understood, with most information being inferred from in vitro studies on cell lines or tissues (Ghezzi 2013).…”

Section: Discussionmentioning

confidence: 90%

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The Level of an Intracellular Antioxidant during Development Determines the Adult Phenotype in a Bird Species: A Potential Organizer Role for Glutathione

Romero-Haro

Alonso‐Álvarez

2015

The American Naturalist

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Online enhancement: appendix. Dryad data: http://dx.doi.org/10.5061/dryad.1rd58.abstract: Life-history traits are often involved in trade-offs whose outcome would depend on the availability of resources but also on the state of specific molecular signals. Early conditions can influence trade-offs and program the phenotype throughout the lifetime, with oxidative stress likely involved in many taxa. Here we address the potential regulatory role of a single intracellular antioxidant in lifehistory trade-offs. Blood glutathione levels were reduced in a large sample of birds (zebra finch Taeniopygia guttata) during development using the synthesis inhibitor buthionine sulfoximine (BSO). Results revealed several modifications in the adult phenotype. BSO-treated nestlings showed lower glutathione and plasma antioxidant levels. In adulthood, BSO birds endured greater oxidative damage in erythrocytes but stronger expression of a sexual signal. Moreover, adult BSO females also showed weaker resistance to oxidative stress but were heavier and showed better body condition. Results suggest that low glutathione values during growth favor the investment in traits that should improve fitness returns, probably in the form of early reproduction. Higher oxidative stress in adulthood may be endured if this cost is paid later in life. Either the presence of specific signaling mechanisms or the indirect effect of increased oxidative stress can explain our findings.

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Section: Discussionmentioning

confidence: 90%

“…We can only speculate about how glutathionylation may have mediated our results. For instance, reduced glutathionylation may have favored the activity of glycolytic enzymes, leading to cell proliferation (Dalle-Donne et al 2009). …”

Section: Discussionmentioning

confidence: 99%

The Level of an Intracellular Antioxidant during Development Determines the Adult Phenotype in a Bird Species: A Potential Organizer Role for Glutathione

Romero-Haro

Alonso‐Álvarez

2015

The American Naturalist

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“…Glutathione, a highly abundant tripeptide (γ-Glu-Cys-Gly), occurring mostly in its reduced form (GSH), is one of the major cellular antioxidant redox buffers in most organisms [84]. Moreover, glutathione can form a mixed disulfide bridge between its cysteine thiol and an accessible free thiol on a protein, which termed as protein S-glutathionylation [85,86]. Glutathionylation is a reversible PTM that seems to occur mostly under oxidative or nitrosative stress conditions.…”

Section: Glutathionylomementioning

confidence: 99%

“…Glutathionylation is a reversible PTM that seems to occur mostly under oxidative or nitrosative stress conditions. It is a crucial mechanism of redox signaling by protecting specific cysteine residues or by modulating protein activity [85,87].…”

Section: Glutathionylomementioning

confidence: 99%

Proteomic analysis of post translational modifications in cyanobacteria

Xiong

Chen

2016

Journal of Proteomics

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“…The ratio of reduced and oxidized glutathione (GSH/GSSG) and deglutathionylation enzymes also contribute to the protein S-glutathionylation. S-glutathionylation has been found in a large number of proteins, affecting a variety of cellular processes (32,51). Many different thiol modification mechanisms have been associated with oxidative stress but as GSH is naturally abundant within the cells, GSH is likely to serve as a major electron donor, making S-glutathionylation a preferred mechanism for protein modification during oxidative stress (33,44).…”

Section: S-glutathionylation Overviewmentioning

confidence: 99%

S-Glutathionylation of Ion Channels: Insights into the Regulation of Channel Functions, Thiol Modification Crosstalk, and Mechanosensing

Yang

Jin²,

Jiang³

2014

Antioxidants & Redox Signaling

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Significance: Ion channels control membrane potential, cellular excitability, and Ca ++ signaling, all of which play essential roles in cellular functions. The regulation of ion channels enables cells to respond to changing environments, and post-translational modification (PTM) is one major regulation mechanism. Recent Advances: Many PTMs (e.g., S-glutathionylation, S-nitrosylation, S-palmitoylation, S-sulfhydration, etc.) targeting the thiol group of cysteine residues have emerged to be essential for ion channels regulation under physiological and pathological conditions. Critical Issues: Under oxidative stress, S-glutathionylation could be a critical PTM that regulates many molecules. In this review, we discuss S-glutathionylation-mediated structural and functional changes of ion channels. Criteria for testing S-glutathionylation, methods and reagents used in ion channel S-glutathionylation studies, and thiol modification crosstalk, are also covered. Mechanotransduction, and S-glutathionylation of the mechanosensitive K ATP channel, are discussed. Future Directions: Further investigation of the ion channel S-glutathionylation, especially the physiological significance of S-glutathionylation and thiol modification crosstalk, could lead to a better understanding of the thiol modifications in general and the ramifications of such modifications on cellular functions and related diseases. Antioxid. Redox Signal. 20, 937-951.

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Protein S-glutathionylation: a regulatory device from bacteria to humans

Cited by 566 publications

References 88 publications

The Level of an Intracellular Antioxidant during Development Determines the Adult Phenotype in a Bird Species: A Potential Organizer Role for Glutathione

The Level of an Intracellular Antioxidant during Development Determines the Adult Phenotype in a Bird Species: A Potential Organizer Role for Glutathione

Proteomic analysis of post translational modifications in cyanobacteria

S-Glutathionylation of Ion Channels: Insights into the Regulation of Channel Functions, Thiol Modification Crosstalk, and Mechanosensing

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