ArticleMolecular & cellular proteomics : MCP2013
Selective targeting of the cysteine proteome by thioredoxin and glutathione redox systems.
Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 93 citations in OpenAlex.
- Role of Antioxidant Systems and Heat Shock Response in Aquatic Animals Under Multistress Conditions.Antioxidants (Basel, Switzerland) · 2026Review
- Thioredoxin system: mechanisms and therapeutic potential in mental disorders.Frontiers in pharmacology · 2026Review
- Modulating the microbiome as an approach to anticancer drug development.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Data-Independent Acquisition (DIA)-Based Label-Free Redox Proteomics (DIALRP) Identifies Prominent Cysteine Oxidations in Translation Machinery in Prostate Cancer Cells Under Oxidative Stress.Journal of proteome research · 2025Article
- Two Amino Acid Substitutions Improve the Pharmacological Profile of the Snake Venom Peptide Mambalgin.Toxins · 2025Article
- Mechanistic role for mTORC1 signaling in profibrotic toxicity of low-dose cadmium.Toxicology and applied pharmacology · 2025Article
- Functional utility of gold complexes with phosphorus donor ligands in biological systems.Coordination chemistry reviews · 2025Article
- Thioredoxin (Trx): A redox target and modulator of cellular senescence and aging-related diseases.Redox biology · 2024Review
- Protein S-palmitoylation enhances profibrotic signaling in response to cadmium.Toxicology and applied pharmacology · 2024Article
- Harnessing redox proteomics to study metabolic regulation and stress response in lignin-fed Rhodococci.Biotechnology for biofuels and bioproducts · 2023Article
- 50 shades of oxidative stress: A state-specific cysteine redox pattern hypothesis.Redox biology · 2023Article
- Proximity-labeling chemoproteomics defines the subcellular cysteinome and inflammation-responsive mitochondrial redoxome.Cell chemical biology · 2023Article
- Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs.Redox biology · 2023Article
- Proximity-labeling chemoproteomics defines the subcellular cysteinome and inflammation-responsive mitochondrial redoxome.bioRxiv : the preprint server for biology · 2023Article
- Antioxidant Defense and Pseudoexfoliation Syndrome: An Updated Review.Medical sciences (Basel, Switzerland) · 2022Review
- Speciation Analysis Highlights the Interactions of Auranofin with the Cytoskeleton Proteins of Lung Cancer Cells.Pharmaceuticals (Basel, Switzerland) · 2022Article
- MITF Is Regulated by Redox Signals Controlled by the Selenoprotein Thioredoxin Reductase 1.Cancers · 2022Article
- Novel Insights into Redox-Based Mechanisms for Auranofin-Induced Rapid Cancer Cell Death.Cancers · 2022Article
- Organometallic gold(I) and gold(III) complexes for lung cancer treatment.Frontiers in pharmacology · 2022Review
- Can thiol-based redox systems be utilized as parts for synthetic biology applications?Redox report : communications in free radical research · 2021Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Thioredoxin (Trx) and GSH are the major thiol antioxidants protecting cells from oxidative stress-induced cytotoxicity. Redox states of Trx and GSH have been used as indicators of oxidative stress. Accumulating studies suggest that Trx and GSH redox systems regulate cell signaling and metabolic pathways differently and independently during diverse stressful conditions. In the current study, we used a mass spectrometry-based redox proteomics approach to test responses of the cysteine (Cys) proteome to selective disruption of the Trx- and GSH-dependent systems. Auranofin (ARF) was used to inhibit Trx reductase without detectable oxidation of the GSH/GSSG couple, and buthionine sulfoximine (BSO) was used to deplete GSH without detectable oxidation of Trx1. Results for 606 Cys-containing peptides (peptidyl Cys) showed that 36% were oxidized more than 1.3-fold by ARF, whereas BSO-induced oxidation of peptidyl Cys was only 10%. Mean fold oxidation of these peptides was also higher by ARF than BSO treatment. Analysis of potential functional pathways showed that ARF oxidized peptides associated with glycolysis, cytoskeleton remodeling, translation and cell adhesion. Of 60 peptidyl Cys oxidized due to depletion of GSH, 41 were also oxidized by ARF and included proteins of translation and cell adhesion but not glycolysis or cytoskeletal remodeling. Studies to test functional correlates showed that pyruvate kinase activity and lactate levels were decreased with ARF but not BSO, confirming the effects on glycolysis-associated proteins are sensitive to oxidation by ARF. These data show that the Trx system regulates a broader range of proteins than the GSH system, support distinct function of Trx and GSH in cellular redox control, and show for the first time in mammalian cells selective targeting peptidyl Cys and biological pathways due to deficient function of the Trx system.
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