Oxidative stress response: a proteomic view

Rabilloud, Thierry; Chevallet, Mireille; Luche, Sylvie; Leize‐Wagner, Emmanuelle

doi:10.1586/14789450.2.6.949

Cited by 19 publications

(13 citation statements)

References 60 publications

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“…A number of the regulated proteins like superoxide dismutase, heat shock protein, peroxiredoxin and elongation factor-1 alpha found in this study are consistent with a general oxidative stress response [24], [73], [74]. Homologues to superoxide dismutase (SOD) (such as SSO0316), participate in the scavenging of highly reactive oxygen species across all domains [75], [76].…”

Section: Resultssupporting

confidence: 77%

“…phosphorylation, sulfation, glycosylation, carbonylation and cysteine oxidation) are important regulators of protein activity. As discussed above with respect to DPSL and rubrerythrin, these modifications can alter the charge of a protein, which will shift the position on a 2D gel [73]. Of the 19 regulated proteins found in this study, 5 were identified in more than one spot; DPSL (SSO2079), superoxide dismutase (SSO0316), peroxiredoxin (SSO2121), rubrerythrin (SSO2642), elongation factor 1-alpha (SSO0216) and thermosome alpha subunit (SSO0862).…”

Section: Resultsmentioning

confidence: 67%

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Something Old, Something New, Something Borrowed; How the Thermoacidophilic Archaeon Sulfolobus solfataricus Responds to Oxidative Stress

et al. 2009

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To avoid molecular damage of biomolecules due to oxidation, all cells have evolved constitutive and responsive systems to mitigate and repair chemical modifications. Archaea have adapted to some of the most extreme environments known to support life, including highly oxidizing conditions. However, in comparison to bacteria and eukaryotes, relatively little is known about the biology and biochemistry of archaea in response to changing conditions and repair of oxidative damage. In this study transcriptome, proteome, and chemical reactivity analyses of hydrogen peroxide (H2O2) induced oxidative stress in Sulfolobus solfataricus (P2) were conducted. Microarray analysis of mRNA expression showed that 102 transcripts were regulated by at least 1.5 fold, 30 minutes after exposure to 30 µM H2O2. Parallel proteomic analyses using two-dimensional differential gel electrophoresis (2D-DIGE), monitored more than 800 proteins 30 and 105 minutes after exposure and found that 18 had significant changes in abundance. A recently characterized ferritin-like antioxidant protein, DPSL, was the most highly regulated species of mRNA and protein, in addition to being post-translationally modified. As expected, a number of antioxidant related mRNAs and proteins were differentially regulated. Three of these, DPSL, superoxide dismutase, and peroxiredoxin were shown to interact and likely form a novel supramolecular complex for mitigating oxidative damage. A scheme for the ability of this complex to perform multi-step reactions is presented. Despite the central role played by DPSL, cells maintained a lower level of protection after disruption of the dpsl gene, indicating a level of redundancy in the oxidative stress pathways of S. solfataricus. This work provides the first “omics” scale assessment of the oxidative stress response for an archeal organism and together with a network analysis using data from previous studies on bacteria and eukaryotes reveals evolutionarily conserved pathways where complex and overlapping defense mechanisms protect against oxygen toxicity.

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Section: Resultssupporting

confidence: 77%

Section: Resultsmentioning

confidence: 67%

Something Old, Something New, Something Borrowed; How the Thermoacidophilic Archaeon Sulfolobus solfataricus Responds to Oxidative Stress

et al. 2009

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“…However, only a very small increase in mRNA and protein levels has been observed in such conditions, suggesting no direct role of SsPDO in the oxidative stress response [131]. In agreement with these data, a recent transcriptomic, proteomic, and chemical reactivity analysis, performed in oxidative stress conditions, failed to show any up-regulation of SsPDO, unlike other antioxidant enzymes [140][141][142][143]. By contrast, similar studies conducted on P. furiosus showed that PfPDO is one of the most strongly up-regulated proteins in response to cold adaptation from 95 to 72°C [144].…”

Section: Insight Into Pdo Functionssupporting

confidence: 54%

Multiple catalytically active thioredoxin folds: a winning strategy for many functions

Pedone

Limauro

D’Ambrosio

et al. 2010

Cell. Mol. Life Sci.

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The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs).

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“…Large scale experiments that allow analysis of oxidative modifications on a proteome-wide scale can now be performed. The modifications that are produced in vivo are attractive biomarker targets, possibly facilitating early diagnosis of a number of diseases [57,61,62]. Peroxynitrite is a reactive nitrogen species (RNS) that may be formed from NO by peroxidase activity and can give rise to nitration products.…”

Section: Protein Side-chain Modification: Mimicking In Vivo Oxidationmentioning

confidence: 99%

Electrochemistry-Mass Spectrometry in Drug Metabolism and Protein Research

Permentier¹,

Bruins²,

Bischoff

2008

MRMC

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The combination of electrochemistry coupled on-line to mass spectrometry (EC-MS) forms a powerful analytical technique with unique applications in the fields of drug metabolism and proteomics. In this review the latest developments are surveyed from both instrumental and application perspectives. The limitations and solutions for coupling an electrochemical system to a mass spectrometer are discussed. The electrochemical mimicking of drug metabolism, specifically by Cytochrome P450, is high-lighted as an application with high biomedical relevance. The EC-MS analysis of proteins also has promising new applications for both proteomics research and biomarker discovery. EC-MS has furthermore advantages for improved analyte detection with mass spectrometry, both for small molecules and large biomolecules. Finally, potential future directions of development of the technique are briefly discussed.

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Oxidative stress response: a proteomic view

Cited by 19 publications

References 60 publications

Something Old, Something New, Something Borrowed; How the Thermoacidophilic Archaeon Sulfolobus solfataricus Responds to Oxidative Stress

Something Old, Something New, Something Borrowed; How the Thermoacidophilic Archaeon Sulfolobus solfataricus Responds to Oxidative Stress

Multiple catalytically active thioredoxin folds: a winning strategy for many functions

Electrochemistry-Mass Spectrometry in Drug Metabolism and Protein Research

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