Physiological Thiols as Promoters of Glutathione Oxidation and Modifying Agents in Protein S-Thiolation

Corso, Antonella Del; Vilardo, Pier Giuseppe; Cappiello, Mario; Cecconi, I; Monte, Massimo Dal; Barsacchi, D; Mura, Umberto

doi:10.1006/abbi.2001.2678

Cited by 22 publications

(15 citation statements)

References 37 publications

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“…Whether this contributes also to the etiology of the cardiomyopathy remains to be evaluated. Such studies appears to be warranted, given that HNE binding to mNADP ϩ -ICDH, if predominantly occurring at cysteine residues (5), could potentially be reversed by aldehyde-sequestering drugs (12,19,22,32). In fact, the reversal of HNE binding to proteins could be part of the mechanism by which N-acetylcysteine prevents cardiac hypertrophy in rats infused with angiotensin II (48).…”

Section: Discussionmentioning

confidence: 91%

Decreased cardiac mitochondrial NADP⁺-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development

Benderdour

Charron

Comte

et al. 2004

American Journal of Physiology-Heart and Circulatory Physiology

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Mitochondrial dysfunction subsequent to increased oxidative stress and alterations in energy metabolism is considered to play a role in the development of cardiac hypertrophy and its progression to failure, although the sequence of events remains to be elucidated. This study aimed at characterizing the impact of hypertrophy development on the activity and expression of mitochondrial NADP+-isocitrate dehydrogenase (mNADP+-ICDH), a metabolic enzyme that controls redox and energy status. We expanded on our previous finding of its inactivation through posttranslational modification by the lipid peroxidation product 4-hydroxynonenal (HNE) in 7-wk-old spontaneously hypertensive rat (SHR) hearts before hypertrophy development (Benderdour et al. J Biol Chem 278: 45154-45159, 2003). In this study, we used 7-, 15-, and 30-wk-old SHR and Sprague-Dawley (SD) rats with abdominal aortic coarctation. Compared with age-matched control Wistar-Kyoto (WKY) rats, SHR hearts showed a significant 25% decrease of mNADP+-ICDH activity, which preceded in time 1) the decline in its protein and mRNA expression levels (between 10% and 35%) and 2) the increase in hypertrophy markers. The chronic and persistent loss of mNADP+-ICDH activity in SHR was associated with enhanced tissue accumulation of HNE-mNADP+-ICDH and total HNE-protein adducts at all ages and contrasted with the profile of changes in the activity of other mitochondrial enzymes involved in antioxidant or energy metabolism. Two-way ANOVA of the data also revealed a significant effect of age on most parameters measured in SHR and WKY hearts. The mNADP+-ICDH activity, protein, and mRNA expression were reduced between 25% and 35% in coarctated SD rats and were normalized by treatment of SHR or coarctated SD rats with renin-angiotensin system inhibitors, which prevented or attenuated hypertrophy. Altogether, our data show that cardiac mNADP+-ICDH activity and expression are differentially and sequentially affected in hypertrophy development and, to a lesser extent, with aging. Decreased cardiac mNADP+-ICDH activity, which is attributed at least in part to HNE adduct formation, appears to be a relevant early and persistent marker of mitochondrial oxidative stress-related alterations in hypertrophy development. Potentially, this could also contribute to the aetiology of cardiomyopathy.

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Section: Discussionmentioning

confidence: 91%

Decreased cardiac mitochondrial NADP⁺-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development

Benderdour

Charron

Comte

et al. 2004

American Journal of Physiology-Heart and Circulatory Physiology

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“…It has been hypothesised that GSH may also be involved as a physiological buffer for controlling cellular oxygen tension [75]. In a community-based study, cigarette smokers were found to have ,20% more glutathiolated proteins in their plasma compared with nonsmokers [76].…”

Section: Protein-thiol (Sh) Alterations: a Novel Redox Signalling Mecmentioning

confidence: 99%

Oxidative stress and redox regulation of lung inflammation in COPD

Rahman

Adcock²

2006

Eur Respir J

783

599

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Reactive oxygen species, either directly or via the formation of lipid peroxidation products, may play a role in enhancing inflammation through the activation of stress kinases (cJun activated kinase, extracellular signal-regulated kinase, p38) and redox-sensitive transcription factors, such as nuclear factor (NF)-kB and activator protein-1. This results in increased expression of a battery of distinct pro-inflammatory mediators. Oxidative stress activates NF-kBmediated transcription of pro-inflammatory mediators either through activation of its activating inhibitor of kB-a kinase or the enhanced recruitment and activation of transcriptional coactivators. Enhanced NF-kB-co-activator complex formation results in targeted increases in histone modifications, such as acetylation leading to inflammatory gene expression.Emerging evidence suggests the glutathione redox couple may entail dynamic regulation of protein function by reversible disulphide bond formation on kinases, phosphatases and transcription factors. Oxidative stress also inhibits histone deacetylase activity and in doing so further enhances inflammatory gene expression and may attenuate glucocorticoid sensitivity.The antioxidant/anti-inflammatory effects of thiol molecules (glutathione, N-acetyl-L-cysteine and N-acystelyn, erdosteine), dietary polyphenols (curcumin-diferuloylmethane, cathechins/ quercetin and reserveratol), specific spin traps, such as a-phenyl-N-tert-butyl nitrone, a catalytic antioxidant (extracellular superoxide dismutase (SOD) mimetic, SOD mimetic M40419 and SOD, and catalase manganic salen compound, eukarion-8), porphyrins (AEOL 10150 and AEOL 10113) and theophylline have all been shown to play a role in either controlling NF-kB activation or affecting histone modifications with subsequent effects on inflammatory gene expression in lung epithelial cells.Thus, oxidative stress regulates both key signal transduction pathways and histone modifications involved in lung inflammation. Various approaches to enhance lung antioxidant capacity and clinical trials of antioxidant compounds in chronic obstructive pulmonary disease are also discussed.

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“…In addition, growing evidence supports a role of HNE as a (patho)physiological modulator of signal transduction, transcriptional regulation, and PTM [46][47][48][49][50]. PTM is currently considered to be the primary mechanism of protein activity and propriety changes [51,52]. It is noteworthy that many signaling molecules and transcription factors modulated by HNE (for e.g.…”

Section: -Hydroxynonenal: a (Patho)physio-logical Modulator In Arthrmentioning

confidence: 97%

“…One candidate mechanism is glutathionylation and is currently emerging as a PTM mechanism, very much like phosphorylation, for the acute control of protein activity by redox status through the reversible modification of their sulfhydryl residues [51]. Interestingly, many HNE protein targets, namely myosin, actin and cytochrome C, were shown to be glutathionylated [64].…”

Section: Hne and Protein Ptmmentioning

confidence: 98%

Lipid Peroxidation End-Products as Modulators of Catabolic and Inflammatory Responses in Arthritis: A Review

Morquette¹,

Shi²,

Lavigne³

et al. 2005

CRR

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Lipid peroxidation (LPO) is a free radical-related process occurring in biologic systems under enzymatic or nonenzymatic control, e.g. for the generation of lipid-derived aldehydes. There is increasing evidence that these aldehydes are causally involved in the pathogenesis of numerous diseases including diabetes, heart failure, atherosclerosis, and neurodegenerative process.4-hydroxynonenal (HNE) is the most important aldehyde involved in oxidant injury. Classically, HNE was described for a long time as a marker of extensive oxidative stress in various tissues. Recent studies, however, showed that HNE can modulate cellular metabolism, inflammatory responses, as well as apoptosis via its effects on signaling/transcription regulation and protein modification. Interestingly, these pathological processes are all implicated to various degrees in arthritis, but no study has specifically reported the potential role of these aldehydes in rheumatic diseases. Therefore, this review focuses on the relevance of oxidative stress-induced HNE production to the pathophysiology of arthritis at inflammatory and catabolic levels.

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Physiological Thiols as Promoters of Glutathione Oxidation and Modifying Agents in Protein S-Thiolation

Cited by 22 publications

References 37 publications

Decreased cardiac mitochondrial NADP⁺-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development

Decreased cardiac mitochondrial NADP⁺-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development

Oxidative stress and redox regulation of lung inflammation in COPD

Lipid Peroxidation End-Products as Modulators of Catabolic and Inflammatory Responses in Arthritis: A Review

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Physiological Thiols as Promoters of Glutathione Oxidation and Modifying Agents in Protein S-Thiolation

Cited by 22 publications

References 37 publications

Decreased cardiac mitochondrial NADP+-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development

Decreased cardiac mitochondrial NADP+-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development

Oxidative stress and redox regulation of lung inflammation in COPD

Lipid Peroxidation End-Products as Modulators of Catabolic and Inflammatory Responses in Arthritis: A Review

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Decreased cardiac mitochondrial NADP⁺-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development

Decreased cardiac mitochondrial NADP⁺-isocitrate dehydrogenase activity and expression: a marker of oxidative stress in hypertrophy development