Proteome Analysis of Oxidative Stress: Glutathionyl Hemoglobin in Diabetic and Uremic Patients

Niwa, Toshimitsu

doi:10.1002/0471973122.ch20

Cited by 3 publications

(1 citation statement)

References 31 publications

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“…Glutathionyl hemoglobin has been widely documented in disease states such as uremia or diabetes (Niwa, 2006); since it is currently believed to be a consequence of the oxidative stress underlying these diseases, it might be a very useful marker of oxidative stress in such pathological conditions. Sarcoplasmic/endoplasmic reticulum Ca 2+ ATPase (SERCA) is a protein regulating the intracellular storage of Ca…”

Section: Protein S-glutathiolationmentioning

confidence: 99%

Glutathione Metabolism: Favorable Versus Unfavorable Effects

Cimino

Saija

2008

Oxidants in Biology

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The aim of this paper is to review current knowledge concerning the different perspectives that are actually investigated to better clarify the role of GSH in organism health.Glutathione (GSH) is widely found in all forms of life and plays an essential role especially in aerobic organisms. In animals, including humans, and in plants, GSH is the predominant non-protein thiol and acts as a redox buffer, in particular keeping with its own SH groups those of proteins in a reduced condition. Because of the cysteine residue, GSH is readily oxidized non-enzymatically to glutathione disulfide (GSSG) by electrophilic substances; GSSG is in turn reduced to GSH by the NADPH-dependent glutathione reductase. Cellular GSH concentrations are markedly reduced in response to oxidative stress and the GSH/GSSG ratio is often used as an indicator of the cellular redox state. Furthermore, GSH acts as an endogenous trapping for reactive intermediates derived from exogenous and endogenous chemicals preventing unwanted reactions of chemically reactive molecules with important cell constituents. In fact, GSH is able to form adducts with a wide range of reactive intermediates, such as quinoneimines, nitrenium ions, arene oxides, quinones, imine methides, Michael acceptors and 4-hydroxy-2-nonenal.Although GSH conjugation has been identified as an important detoxification reaction, other biological and/or toxic effects of some GSH-adducts have been described. For example, oxyeicosanoid GSH-adducts do not represent just inactivation products, but they can both retain or show novel biological activities. However, several papers describe the biotransformation and bioactivation of a range of nephrotoxic compounds, evidencing that this bioactivation is dependent on GSH S-conjugate formation and activation of cysteine S-conjugates by cysteine conjugate β-lyase. Furthermore, recent evidences show that GSH may conjugate to nitric oxide (NO) to form an S-nitroso-glutathione (GSNO) adduct. GSNO represents one of the major transport forms of NO in biological systems, may give rise to transnitrosation and S-thiolation reactions. GSNO has been shown to have several pharmacological activities, including the inhibition of platelet aggregation and a protective effect during the exposure of cells to oxidants. Finally, recent studies have also highlighted the ability of GSH and of its catabolites to promote oxidative processes, by participating in metal-ion-mediated reactions leading to formation of reactive oxygen species and free radicals.

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Section: Protein S-glutathiolationmentioning

confidence: 99%

Glutathione Metabolism: Favorable Versus Unfavorable Effects

Cimino

Saija

2008

Oxidants in Biology

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Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences

Martínez‐Ruiz

Lamas

2007

Cardiovascular Research

163

143

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The role of nitric oxide in several signalling routes has been clearly established. In recent years increasing attention has been paid to its ability to produce covalent protein post-translational modifications in conjunction with other reactive oxygen and nitrogen species. Among these, the modification of cysteine residues has been shown to be of particular importance due to the functional relevance of many of them. In this review, we focus on the modification of the cysteine thiol by incorporation of a NO moiety (S-nitrosylation) or of a glutathione moiety (S-glutathionylation). Both modifications are produced by different reactions induced by nitric oxide-related species. We discuss the differences and similarities of both modifications, and their relationships, in regard to the biochemical mechanisms that produce them, including the enzymatic activities that may catalyze some of them and their subcellular compartmentalization. Even when biochemical knowledge is one step ahead of the demonstration of their pathophysiological relevance, we also describe the potential role of both modifications in several processes in which both post-translational modifications are involved.

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