ArticleMolecular & cellular proteomics : MCP2015
Global analysis of myocardial peptides containing cysteines with irreversible sulfinic and sulfonic acid post-translational modifications.
Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- A lysis-derived PMSF and orthovanadate oxidant defines a distinct cysteine-engagement profile.Cell chemical biology · 2026Article
- The Roles of Oxidative Stress and Red Blood Cells in the Pathology of the Varicose Vein.International journal of molecular sciences · 2024Review
- Proteomics of the heart.Physiological reviews · 2024Review
- Trioxidized cysteine in the aging proteome mimics the structural dynamics and interactome of phosphorylated serine.Aging cell · 2024Article
- ProtView: A Versatile Tool forJournal of proteome research · 2023Article
- Protein cysteine S-glycosylation: oxidative hydrolysis of protein S-glycosidic bonds in aqueous alkaline environments.Amino acids · 2023Article
- Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.Antioxidants (Basel, Switzerland) · 2021Review
- Characterization of cellular oxidative stress response by stoichiometric redox proteomics.American journal of physiology. Cell physiology · 2021Review
- Serum albumin cysteine trioxidation is a potential oxidative stress biomarker of type 2 diabetes mellitus.Scientific reports · 2020Observational
- Structural preferences of cysteine sulfinic acid: The sulfinate engages in multiple local interactions with the peptide backbone.Free radical biology & medicine · 2020Article
- Irreversible oxidative post-translational modifications in heart disease.Expert review of proteomics · 2019Review
- Protein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational Modifications.International journal of molecular sciences · 2019Review
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- Redox regulation of cell proliferation: Bioinformatics and redox proteomics approaches to identify redox-sensitive cell cycle regulators.Free radical biology & medicine · 2018Review
- Biochemistry of proinflammatory macrophage activation.Cellular and molecular life sciences : CMLS · 2018Review
- ROLE OF THIOLS IN OXIDATIVE STRESS.Current opinion in toxicology · 2018Article
- Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Molecular bioSystems · 2017Review
- Detection of ROS Induced Proteomic Signatures by Mass Spectrometry.Frontiers in physiology · 2017Review
- Glutathione and Glutathione Transferase Omega 1 as Key Posttranslational Regulators in Macrophages.Microbiology spectrum · 2017Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cysteine (Cys) oxidation is a crucial post-translational modification (PTM) associated with redox signaling and oxidative stress. As Cys is highly reactive to oxidants it forms a range of post-translational modifications, some that are biologically reversible (e.g. disulfides, Cys sulfenic acid) and others (Cys sulfinic [Cys-SO2H] and sulfonic [Cys-SO3H] acids) that are considered "irreversible." We developed an enrichment method to isolate Cys-SO2H/SO3H-containing peptides from complex tissue lysates that is compatible with tandem mass spectrometry (MS/MS). The acidity of these post-translational modification (pKa Cys-SO3H < 0) creates a unique charge distribution when localized on tryptic peptides at acidic pH that can be utilized for their purification. The method is based on electrostatic repulsion of Cys-SO2H/SO3H-containing peptides from cationic resins (i.e. "negative" selection) followed by "positive" selection using hydrophilic interaction liquid chromatography. Modification of strong cation exchange protocols decreased the complexity of initial flowthrough fractions by allowing for hydrophobic retention of neutral peptides. Coupling of strong cation exchange and hydrophilic interaction liquid chromatography allowed for increased enrichment of Cys-SO2H/SO3H (up to 80%) from other modified peptides. We identified 181 Cys-SO2H/SO3H sites from rat myocardial tissue subjected to physiologically relevant concentrations of H2O2 (<100 μm) or to ischemia/reperfusion (I/R) injury via Langendorff perfusion. I/R significantly increased Cys-SO2H/SO3H-modified peptides from proteins involved in energy utilization and contractility, as well as those involved in oxidative damage and repair.
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