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Cross-tissue deep profiling of redox proteome in obese mice

ABSTRACT: Cellular redox state, the balance between oxidation and reduction, is precisely regulated through cysteine thiol modification. In this study, we developed a novel method, in conjunction with directed data-independent acquisition (dDIA) for identifying and quantifying a substantial number of sulfhydryl sites. Our method provided a valuable tool for large-scale investigations of redox regulation and oxidative stress in disease.

ORGANISM(S): Mus Musculus

SUBMITTER: Jinlong Wang

PROVIDER: PXD066139 | iProX | Tue Jul 15 00:00:00 BST 2025

REPOSITORIES: iProX

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Cross-tissue deep profiling of redox proteome in obese mice using enhanced resin-assisted capture and data-independent acquisition.

Liu Jiyuan J Jiang Xinbo X Li Yunyu Y Shen Liye L Li Xiaoliang X Wang Xiaohui X Wang Jinlong J

Redox biology 20260128

Cysteine thiol modification plays a critical role in the precise regulation of the cellular redox state. Existing redox proteomic methodologies are often limited by their efficiency, complexity, and cost. To overcome these limitations, we developed and synthesized a series of novel enrichment resins. Three of these resins demonstrated a markedly enhanced enrichment efficiency. The application of one such resin, coupled with data-independent acquisition, allowed the systematic and reproducible qu ...[more]

PMID: 41621244

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S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics

Project description:Protein S-thiolation is a post-translational thiol-modification that controls redox-sensing transcription factors and protects active site cysteine residues against irreversible oxidation. In Bacillus subtilis the MarR-type repressor OhrR was shown to sense organic hydroperoxides via formation of mixed disulfides with the redox buffer bacillithiol (Cys-GlcN-Malate, BSH), termed as S-bacillithiolation. Here, we have studied changes in the transcriptome and redox proteome caused by the strong oxidant hypochloric acid in B. subtilis. The expression profile of NaOCl stress is indiciative of disulfide stess as shown by the induction of the thiol- and oxidative stress-specific Spx, CtsR and PerR regulons. Thiol redox proteomics identified only few cytoplasmic proteins with reversible thiol-oxidations in response to NaOCl stress that include GapA and MetE. Shotgun-LC-MS/MS analyses revealed that GapA, Spx and PerR are oxidized to intramolecular disulfides by NaOCl stress. Furthermore, we identified six S-bacillithiolated proteins in NaOCl-treated cells, including the OhrR repressor, two methionine synthases MetE and YxjG, the inorganic pyrophosphatase PpaC, the 3-D-phophoglycerate dehydrogenase SerA and the putative bacilliredoxin YphP. S-bacillithiolation of the OhrR repressor leads to up-regulation of the OhrA peroxiredoxin that confers together with BSH specific protection against NaOCl. S-bacillithiolation of MetE, YxjG, PpaC and SerA causes hypochlorite-induced methionine starvation as supported by the induction of the S-box regulon. The mechanism of S-glutathionylation of MetE has been described in Escherichia coli also leading to enzyme inactivation and methionine auxotrophy. In summary, our studies discover an important role of the BSH redox buffer in protection against hypochloric acid by S-bacillithiolation of the redox-sensing regulator OhrR and of four enzymes of the methionine biosynthesis pathway.

2011-07-04 | GSE27637 | GEO

Redox proteomics optimized protocol applyed to melanoma cells

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2018-03-05 | PXD007278 | Pride

effect of redox on gene expression

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Iodoacetyl tandem mass tag (iodoTMT)-based redox proteomics of Arabidopsis thaliana under fluctuating light

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Transcription profiling of Arabidopsis leaves reponse to DTT to examine the effect of redox on gene expression

Project description:In this study, we used GC-MS analysis in combination with flux analysis and the Affymetrix ATH1 GeneChip to survey the metabolome and transcriptome of Arabidopsis leaves in response to manipulation of the thiol-disulfide status. Feeding low concentrations of the sulfhydryl reagent dithiothreitol (DTT) for one hour at the end of the dark period led to post-translational redox-activation of ADP-glucose pyrophosphorylase and major alterations in leaf carbon partitioning, including an increased flux into major respiratory pathways, starch- cell-wall-, and amino-acid synthesis and a reduced flux to sucrose. This was accompanied by a decrease in the levels of hexose-phosphates, while metabolites in the second half of the TCA cycle and various amino acids increased, indicating a stimulation of anaplerotic fluxes reliant on Î±-ketoglutarate. There was also an increase in shikimate as a precursor of secondary plant products and marked changes in the levels of the minor sugars involved in ascorbate synthesis and cell wall metabolism. Transcript profiling revealed a relatively small number of changes in the levels of transcripts coding for components of redox-regulation, transport processes and cell wall, protein and amino acid metabolism, while there were no major alterations in transcript levels coding for enzymes involved in central metabolic pathways. These results provide a global picture of the effect of redox and reveal the utility of transcript and metabolite profiling as systemic strategies to uncover the occurrence of redox-modulation in vivo. Experiment Overall Design: Leaf discs were incubated with or without 5mM DTT for one hour to affect the redox status of the cells. The effect of this treatment on global gene expression was analysed using affymetrix ATH1 microarrays. The experiments contains one control (-DTT) and one treatment (+DTT) and is performed with 2 biological replicas.

2008-06-12 | E-GEOD-4021 | biostudies-arrayexpress

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