S-glutathionylation in protein redox regulation

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

doi:10.1016/j.freeradbiomed.2007.06.014

Cited by 427 publications

(398 citation statements)

References 139 publications

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“…In addition, free sulphydryl groups can also form disulphide bridges with low molecular weight sulphydryl compounds present in the protein environment, such as free cysteine, and glutathione [59][60][61][62]. S-glutathionylation is in most cases a permanent modification, except if a second cysteine is present in the close vicinity, and is available for disulphide bridge formation.…”

Section: Protein Thiols and Thioethersmentioning

confidence: 99%

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Barelli

Canellini

Thadikkaran

et al. 2008

Proteomics Clinical Apps

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Protein oxidation mechanisms result in a wide array of modifications, from backbone cleavage or protein crosslinking to more subtle modifications such as side chain oxidations. Protein oxidation occurs as part of normal regulatory processes, as a defence mechanism against oxidative stress, or as a deleterious processes when antioxidant defences are overcome. Because blood is continually exposed to reactive oxygen and nitrogen species, blood proteomics should inherently adopt redox proteomic strategies. In this review, we recall the biochemical basis of protein oxidation, review the proteomic methodologies applied to analyse redox modifications, and highlight some physiological and in vitro responses to oxidative stress of various blood components.

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Section: Protein Thiols and Thioethersmentioning

confidence: 99%

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Barelli

Canellini

Thadikkaran

et al. 2008

Proteomics Clinical Apps

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“…Protein S-glutathionylation may occur in physiological conditions but is generally facilitated by oxidative stress when excessive ROS are present and GSH is locally available to the target protein (33). The ratio of reduced and oxidized glutathione (GSH/GSSG) and deglutathionylation enzymes also contribute to the protein S-glutathionylation.…”

Section: S-glutathionylation Overviewmentioning

confidence: 99%

“…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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“…Glutathione (GSH), a tripeptide (L-γ-glutamyl-L-cysteinyl glycine) thiol, exists in most mammal cells and plays an important role in various biological processes (Dalle-Donne et al, 2007). GSH is a critical component of the antioxidant defense system.…”

Section: Introductionmentioning

confidence: 99%

Differential Cell Death and Bcl-2 Expression in Mouse Retina after Glutathione Decrease by Systemic D,L-Buthionine Sulphoximine Administration

Park

Kim

Moon

et al. 2013

Molecules and Cells

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Glutathione (GSH) plays a critical role in cellular defense against unregulated oxidative stress in mammalian cells including neurons. We previously demonstrated that GSH decrease using [D, L]-buthionine sulphoximine (BSO) induces retinal cell death, but the underlying mechanisms of this are still unclear. Here, we demonstrated that retinal GSH level is closely related to retinal cell death as well as expression of an anti-apoptotic molecule, Bcl-2, in the retina. We induced differential expression of retinal GSH by single and multiple administrations of BSO, and examined retinal GSH levels and retinal cell death in vivo. Single BSO administration showed a transient decrease in the retinal GSH level, whereas multiple BSO administration showed a persistent decrease in the retinal GSH level. Retinal cell death also showed similar patterns: transient increase of retinal cell death was observed after single BSO administration, whereas persistent increase of retinal cell death was observed after multiple BSO administration. Changes in the retinal GSH level affected Bcl-2 expression in the retina. Immunoblot and immunohistochemical analyses showed that single and multiple administration of BSO induced differential expressions of Bcl-2 in the retina. Taken together, the results of our study suggest that the retinal GSH is important for the survival of retinal cells, and retinal GSH appears to be deeply related to Bcl-2 expression in the retina. Thus, alteration of Bcl-2 expression may provide a therapeutic tool for retinal degenerative diseases caused by retinal oxidative stress such as glaucoma or retinopathy.

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S-glutathionylation in protein redox regulation

Cited by 427 publications

References 139 publications

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Oxidation of proteins: Basic principles and perspectives for blood proteomics

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

Differential Cell Death and Bcl-2 Expression in Mouse Retina after Glutathione Decrease by Systemic D,L-Buthionine Sulphoximine Administration

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