ArticleThe Journal of biological chemistry2013
Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 113 citations in OpenAlex.
- NLRP3 Inflammasome Activation in Oxidative Stress: A Key Mechanism Driving Neuroinflammation.Neuroimmunomodulation · 2026Review
- Thioredoxin system: mechanisms and therapeutic potential in mental disorders.Frontiers in pharmacology · 2026Review
- Molecular Mechanisms and Antioxidant Effects ofFoods (Basel, Switzerland) · 2025Article
- Nanomedicine-Driven Modulation of Reductive Stress for Cancer Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Article
- Unique features of KGN granulosa-like tumour cells in the regulation of steroidogenic and antioxidant genes.PloS one · 2024Article
- Distinct or Overlapping Areas of Mitochondrial Thioredoxin 2 May Be Used for Its Covalent and Strong Non-Covalent Interactions with Protein Ligands.Antioxidants (Basel, Switzerland) · 2023Article
- Nitric oxide and thioredoxin modulate the activity of caspase 9 in HepG2 cells.Biochimica et biophysica acta. General subjects · 2023Article
- Fluorescent Probes for Mammalian Thioredoxin Reductase: Mechanistic Analysis, Construction Strategies, and Future Perspectives.Biosensors · 2023Review
- Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility.Nature communications · 2023Article
- TXNIP: A key protein in the cellular stress response pathway and a potential therapeutic target.Experimental & molecular medicine · 2023Review
- S-Denitrosylation: A Crosstalk between Glutathione and Redoxin Systems.Antioxidants (Basel, Switzerland) · 2022Review
- The Thioredoxin System of Mammalian Cells and Its Modulators.Biomedicines · 2022Review
- The blood level of thioredoxin 1 as a supporting biomarker in the detection of breast cancer.BMC cancer · 2022Article
- Inhibition of Oxidative Stress: An Important Molecular Mechanism of Chinese Herbal Medicine (Astragalus membranaceus, Carthamus tinctorius L., Radix Salvia Miltiorrhizae, etc.) in the Treatment of Ischemic Stroke by Regulating the Antioxidant System.Oxidative medicine and cellular longevity · 2022Review
- Genetically Encoded Fluorescent Redox Indicators for Unveiling Redox Signaling and Oxidative Toxicity.Chemical research in toxicology · 2021Review
- Thioredoxin-1 Rescues MPPMolecular neurobiology · 2021Article
- Glutaredoxin: Discovery, redox defense and much more.Redox biology · 2021Review
- Proteomics characterization of mitochondrial-derived vesicles under oxidative stress.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian cytosolic thioredoxin system, comprising thioredoxin (Trx), Trx reductase, and NADPH, is the major protein-disulfide reductase of the cell and has numerous functions. Besides the active site thiols, human Trx1 contains three non-active site cysteine residues at positions 62, 69, and 73. A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. This could possibly provide a structural switch affecting Trx1 function during oxidative stress and redox signaling. We found that two-disulfide Trx1 was generated in A549 cells under oxidative stress. In vitro data showed that two-disulfide Trx1 was generated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2. The redox Western blot data indicated that the glutaredoxin system protected Trx1 in HeLa cells from oxidation caused by ebselen, a superfast oxidant for Trx1. Our results also showed that physiological concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulfide in vitro. This reaction was stimulated by glutaredoxin 1 via the so-called monothiol mechanism. In conclusion, reversible oxidation of the non-active site disulfide of Trx1 is suggested to play an important role in redox regulation and cell signaling via temporal inhibition of its protein-disulfide reductase activity for the transmission of oxidative signals under oxidative stress.
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