Redox Signaling and Regulation in Biology and Medicine 2009
DOI: 10.1002/9783527627585.ch5
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Protein Glutathiolation

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Cited by 9 publications
(12 citation statements)
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“…However, oxidative stress is the principal force in regulating redox signaling (Ghezzi and Di Simplicio 2009;Sohal and Orr 2012). Moreover, the glutathione role in cell signaling could be independent from oxidative stress.…”
Section: Discussionmentioning
confidence: 99%
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“…However, oxidative stress is the principal force in regulating redox signaling (Ghezzi and Di Simplicio 2009;Sohal and Orr 2012). Moreover, the glutathione role in cell signaling could be independent from oxidative stress.…”
Section: Discussionmentioning
confidence: 99%
“…However, considering the role of glutathione in cell signaling (Jones 2006;Ghezzi and Di Simplicio 2009) and the fact that this antioxidant is present in every tissue (Wu et al 2004), a general regulatory mechanism can also be proposed. At first glance, the results suggest a compensatory (hormetic) response against a mild stressor, which may improve fitness (Costantini et al 2010).…”
Section: Discussionmentioning
confidence: 99%
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“… 119 Once formed, disulfides are relatively stable to most physiological nucleophiles and are generally cleaved by other thiols as in thiol-disulfide exchange (nucleophilic substitution) reactions (Figure 5 ). 120 The thiol in a disulfide with the lower p K a will be the better leaving group and often dictates which cysteine is released in thiol-disulfide exchange. Indeed, this strategy is employed by the thiol-disulfide exchange catalysts in the cell, such as protein disulfide isomerases (PDI).…”
Section: Reactive Oxygen Species (Ros) In Biological Systemsmentioning
confidence: 99%
“…Under oxidative conditions, excessive GSSG can react with thiol groups of proteins, a process known as glutathionylation, leading to alterations of protein functioning (Hawkins et al, 2010;Hurd et al, 2005). The loss of cellular GSH/GSSG redox control makes glutathionylation a deleterious event (Ghezzi and Di Simplicio, 2009), and therefore GSSG is generally exported from the cell to the extracellular matrix (Garcia et al, 2010;Han et al, 2006). Given this, our findings suggest that juvenile C. gigas antioxidant capacity at the highest hypercapnia level (pH 7.0) was exceeded, with excess glutathione oxidation, and GSSG excretion resulting in lower total glutathione content, as seen in other bivalve species experiencing oxidative stress (Hannam et al, 2010;Peña-Llopis et al, 2002Regoli et al, 1998.…”
Section: Antioxidant Scavengers and Cellular Damagementioning
confidence: 99%