Oxidation Proteomics: The Role of Thiol Modifications

Riederer, Beat M.

doi:10.2174/157016409787847448

Cited by 20 publications

(16 citation statements)

References 182 publications

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“…Oxidation of proteins can be classified into two types: reversible and irreversible [30, 31]. Cysteine (Cys) and methionine (Met) residues on proteins are typical targets of reversible oxidative modification because of their low pKa thiols that react with oxidative species [32–34]. Reversible oxidation occurs in the presence of ROS such as H 2 O 2 , O 2 •− , and RNS like peroxynitrite [35, 36], initially producing sulfenic acid residues (-SOH) that can then react with glutathione (GSH) or other sulfhydryl groups to form glutathione disulfide (GSSG), intra- or extra-molecular disulfide bonds (RS-SR′), and S-glutathionylated proteins (R-SSG) [36–39] (Figure 1).…”

Section: The Actin Cytoskeleton As a Target Of Oxidantsmentioning

confidence: 99%

Redox regulation of the actin cytoskeleton and its role in the vascular system

Huff

Fujii

et al. 2017

Free Radical Biology and Medicine

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The actin cytoskeleton is critical for form and function of vascular cells, serving mechanical, organizational and signaling roles. Because many cytoskeletal proteins are sensitive to reactive oxygen species, redox regulation has emerged as a pivotal modulator of the actin cytoskeleton and its associated proteins. Here, we summarize work implicating oxidants in altering actin cytoskeletal proteins and focus on how these alterations affect cell migration, proliferation and contraction of vascular cells. Finally, we discuss the role of oxidative modification of the actin cytoskeleton in vivo and highlight its importance for vascular diseases.

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Section: The Actin Cytoskeleton As a Target Of Oxidantsmentioning

confidence: 99%

Redox regulation of the actin cytoskeleton and its role in the vascular system

Huff

Fujii

et al. 2017

Free Radical Biology and Medicine

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“…Reversible oxidative modifications on protein thiols have been recognized as important and ubiquitous posttranslational modifications that are essential for redox signaling and regulation in normal physiological and pathological processes [1–4]. In particular, several forms of reversible oxidation of cysteine thiols, including S-nitrosylation, S-glutathionylation, and S-sulfenic acid, have been increasingly emphasized for their roles in integrating both reactive oxygen and reactive nitrogen species (ROS/RNS) 1 to mediate cellular signaling pathways [1,5,6].…”

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confidence: 99%

Quantitative site-specific reactivity profiling of S-nitrosylation in mouse skeletal muscle using cysteinyl peptide enrichment coupled with mass spectrometry

Shukla

Chen

et al. 2013

Free Radical Biology and Medicine

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S-nitrosylation, the formation of S-nitrosothiol (SNO), is an important reversible thiol oxidation event that has been increasingly recognized for its role in cell signaling. Although many proteins susceptible to S-nitrosylation have been reported, site-specific identification of physiologically relevant SNO modifications remains an analytical challenge because of the low abundance and labile nature of this modification. Herein we present further improvement and optimization of the recently reported resin-assisted cysteinyl peptide enrichment protocol for SNO identification and its application to mouse skeletal muscle to identify specific cysteine sites sensitive to S-nitrosylation by a quantitative reactivity profiling strategy. Our results indicate that the protein- and peptide-level enrichment protocols provide comparable specificity and coverage of SNO-peptide identifications. S-nitrosylation reactivity profiling was performed by quantitatively comparing the site-specific SNO modification levels in samples treated with S-nitrosoglutathione, an NO donor, at two different concentrations (i.e., 10 and 100 μM). The reactivity profiling experiments led to the identification of 488 SNO-modified sites from 197 proteins with specificity of ~95% at the unique peptide level, i.e., ~95% of enriched peptides contain cysteine residues as the originally SNO-modified sites. Among these sites, 281 from 145 proteins were considered more sensitive to S-nitrosylation based on the ratios of observed SNO levels between the two treatments. These SNO-sensitive sites are more likely to be physiologically relevant. Many of the SNO-sensitive proteins are localized in mitochondria, contractile fiber, and actin cytoskeleton, suggesting the susceptibility of these subcellular compartments to redox regulation. Moreover, these observed SNO-sensitive proteins are primarily involved in metabolic pathways, including the tricarboxylic acid cycle, glycolysis/gluconeogenesis, glutathione metabolism, and fatty acid metabolism, suggesting the importance of redox regulation in muscle metabolism and insulin action.

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“…We are focusing on the oxidised Cys and Met and its chemistry and biochemistry in the consequences of diseases (32). During the lifetime, living organisms are constantly exposed to one or more conditions that generate highly reactive oxygen and nitrogen species (ROS/ RNS) that either serve as second messengers in signal transduction or may damage protein, nucleic acid and lipid (33). As we know that alteration in signal transduction pathways can cause several chronic disorders like defects in map kinase pathway (MAPK) causes apoptosis, cancer.…”

Section: Amino Acid Oxidationmentioning

confidence: 99%

Protein oxidation an overview of metabolism of sulphur containing amino acid cysteine

et al. 2017

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The available data suggest that among cellular constituents, proteins are the major target for oxidation primarily because of their quantity and high rate of interactions with ROS. Proteins are susceptible to ROS modifications of amino acid side chains which alter protein structure. Among the amino acids, Cysteine (Cys) is more prone to oxidation by ROS because of its high nucleophilic property. The reactivity of Cys with ROS is due to the presence of thiol group. In the oxidised form, Cys forms disulfide bond, which are primary covalent cross-link found in proteins, and which stabilize the native conformation of a protein. Indirect evidence suggests that thiol modifications by ROS may be involved in neurodegenerative disorders, but the significance and precise extent of the contributions are poorly understood. Here, we review the role of oxidized Cys in different pathological consequences and its biochemistry may increase the research in the discovery of new therapies. The purpose of this review is to re-examine the role and biochemistry of oxidised Cys residues.

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Oxidation Proteomics: The Role of Thiol Modifications

Cited by 20 publications

References 182 publications

Redox regulation of the actin cytoskeleton and its role in the vascular system

Redox regulation of the actin cytoskeleton and its role in the vascular system

Quantitative site-specific reactivity profiling of S-nitrosylation in mouse skeletal muscle using cysteinyl peptide enrichment coupled with mass spectrometry

Protein oxidation an overview of metabolism of sulphur containing amino acid cysteine

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