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S-glutathionylation: relevance in diabetes and potential role as a biomarker

AuthorsSánchez Gómez, Francisco Javier; Espinosa-Díez, Cristina ; Dubey, Megha; Dikshit, Madhu; Lamas Peláez, Santiago
Issue Date12-Jun-2013
PublisherWalter de Gruyter
CitationBiological Chemistry 394(10): 1263- 1280 (2013)
AbstractGlutathione is considered the main regulator of redox balance in the cellular milieu due to its capacity for detoxifying deleterious molecules. The oxidative stress induced as a result of a variety of stimuli promotes protein oxidation, usually at cysteine residues, leading to changes in their activity. Mild oxidative stress, which may take place in physiological conditions, induces the reversible oxidation of cysteines to sulfenic acid form, while pathological conditions are associated with higher rates of reactive oxygen species production, inducing the irreversible oxidation of cysteines. Among these, neurodegenerative disorders, cardiovascular diseases and diabetes have been proposed to be pathogenetically linked to this state. In diabetes-associated vascular complications, lower levels of glutathione and increased oxidative stress have been reported. S-glutathionylation has been proposed as a posttranslational modification able to protect proteins from over-oxidizing environments. S-glutathionylation has been identified in proteins involved in diabetic models both in vitro and in vivo. In all of them, S-glutathionylation represents a mechanism that regulates the response to diabetic conditions, and has been described to occur in erythrocytes and neutrophils from diabetic patients. However, additional studies are necessary to discern whether this modification represents a biomarker for the early onset of diabetic vascular complications.
Identifiersdoi: 10.1515/hsz-2013-0150
issn: 1431-6730
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