ArticleScientific reports2015
Development of 'Redox Arrays' for identifying novel glutathionylated proteins in the secretome.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Strain-dependent glutathionylation of fibronectin fibers impacts mechano-chemical behavior and primes an integrin switch.Nature communications · 2024Article
- Gbb glutathionylation promotes its proteasome-mediated degradation to inhibit synapse growth.The Journal of cell biology · 2023Article
- Redox Systems Biology: Harnessing the Sentinels of the Cysteine Redoxome.Antioxidants & redox signaling · 2020Review
- Targeting redox regulation to treat substance use disorder using N‐acetylcysteineThe European journal of neuroscience · 2019Review
- Positive Regulation of Interleukin-1β Bioactivity by Physiological ROS-Mediated Cysteine S-Glutathionylation.Cell reports · 2017Article
- Store-operated CaJCI insight · 2017Article
- Redox Regulation of Inflammatory Processes Is Enzymatically Controlled.Oxidative medicine and cellular longevity · 2017Review
- Glutathione Fine-Tunes the Innate Immune Response toward Antiviral Pathways in a Macrophage Cell Line Independently of Its Antioxidant Properties.Frontiers in immunology · 2017Article
- Protein Thiol Redox Signaling in Monocytes and Macrophages.Antioxidants & redox signaling · 2016Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteomics techniques for analysing the redox status of individual proteins in complex mixtures tend to identify the same proteins due to their high abundance. We describe here an array-based technique to identify proteins undergoing glutathionylation and apply it to the secretome and the proteome of human monocytic cells. The method is based on incorporation of biotinylated glutathione (GSH) into proteins, which can then be identified following binding to a 1000-protein antibody array. We thus identify 38 secreted and 55 intracellular glutathionylated proteins, most of which are novel candidates for glutathionylation. Two of the proteins identified in these experiments, IL-1 sRII and Lyn, were then confirmed to be susceptible to glutathionylation. Comparison of the redox array with conventional proteomic methods confirmed that the redox array is much more sensitive, and can be performed using more than 100-fold less protein than is required for methods based on mass spectrometry. The identification of novel targets of glutathionylation, particularly in the secretome where the protein concentration is much lower, shows that redox arrays can overcome some of the limitations of established redox proteomics techniques.
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