ArticlePloS one2015
Redox proteomics of the inflammatory secretome identifies a common set of redoxins and other glutathionylated proteins released in inflammation, influenza virus infection and oxidative stress.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 73 citations in OpenAlex.
- Redox-Dependent Activation of Matrix Metalloproteinases Regulates Influenza A Virus Replication in Neuronal Cells.International journal of microbiology · 2026Article
- NRF2 Antioxidant Response and Interferon-Stimulated Genes Are Differentially Expressed in SARS-CoV-2-Positive Young Subjects.Immunity, inflammation and disease · 2025Article
- Strain-dependent glutathionylation of fibronectin fibers impacts mechano-chemical behavior and primes an integrin switch.Nature communications · 2024Article
- Global blood miRNA profiling unravels early signatures of immunogenicity of Ebola vaccine rVSVΔG-ZEBOV-GP.iScience · 2023Article
- Coordinated reprogramming of renal cancer transcriptome, metabolome and secretome associates with immune tumor infiltration.Cancer cell international · 2023Article
- Phytochemical Composition and Cytoprotective Properties of the EndemicPharmaceuticals (Basel, Switzerland) · 2022Article
- Changing Perspectives from Oxidative Stress to Redox Signaling-Extracellular Redox Control in Translational Medicine.Antioxidants (Basel, Switzerland) · 2022Review
- PRDX2 Knockdown Inhibits Extracellular Matrix Synthesis of Chondrocytes by Inhibiting Wnt5a/YAP1/CTGF and Activating IL-6/JAK2/STAT3 Pathways in Deer Antler.International journal of molecular sciences · 2022Article
- Preoperative circulating peroxiredoxin 1 levels as a predictor of non-alcoholic fatty liver disease remission after laparoscopic bariatric surgery.Frontiers in endocrinology · 2022Article
- Thiol Modifications in the Extracellular Space-Key Proteins in Inflammation and Viral Infection.Frontiers in immunology · 2022Review
- Time Course of Redox Biomarkers in COVID-19 Pneumonia: Relation with Inflammatory, Multiorgan Impairment Biomarkers and CT Findings.Antioxidants (Basel, Switzerland) · 2021Article
- Peroxiredoxins-The Underrated Actors during Virus-Induced Oxidative Stress.Antioxidants (Basel, Switzerland) · 2021Review
- Intracellular Redox-Modulated Pathways as Targets for Effective Approaches in the Treatment of Viral Infection.International journal of molecular sciences · 2021Review
- Susceptibility of the patients infected with Sars-Cov2 to oxidative stress and possible interplay with severity of the disease.Free radical biology & medicine · 2021Article
- Vimentin S-glutathionylation at Cys328 inhibits filament elongation and induces severing of mature filaments in vitro.The FEBS journal · 2020Article
- Redox control in the pathophysiology of influenza virus infection.BMC microbiology · 2020Review
- Paracrine regulation and improvement of β-cell function by thioredoxin.Redox biology · 2020Article
- Vimentin as a Multifaceted Player and Potential Therapeutic Target in Viral Infections.International journal of molecular sciences · 2020Review
- Redox-Modulating Agents in the Treatment of Viral Infections.International journal of molecular sciences · 2020Review
- Evolution, role in inflammation, and redox control of leaderless secretory proteins.The Journal of biological chemistry · 2020Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein cysteines can form transient disulfides with glutathione (GSH), resulting in the production of glutathionylated proteins, and this process is regarded as a mechanism by which the redox state of the cell can regulate protein function. Most studies on redox regulation of immunity have focused on intracellular proteins. In this study we have used redox proteomics to identify those proteins released in glutathionylated form by macrophages stimulated with lipopolysaccharide (LPS) after pre-loading the cells with biotinylated GSH. Of the several proteins identified in the redox secretome, we have selected a number for validation. Proteomic analysis indicated that LPS stimulated the release of peroxiredoxin (PRDX) 1, PRDX2, vimentin (VIM), profilin1 (PFN1) and thioredoxin 1 (TXN1). For PRDX1 and TXN1, we were able to confirm that the released protein is glutathionylated. PRDX1, PRDX2 and TXN1 were also released by the human pulmonary epithelial cell line, A549, infected with influenza virus. The release of the proteins identified was inhibited by the anti-inflammatory glucocorticoid, dexamethasone (DEX), which also inhibited tumor necrosis factor (TNF)-α release, and by thiol antioxidants (N-butanoyl GSH derivative, GSH-C4, and N-acetylcysteine (NAC), which did not affect TNF-α production. The proteins identified could be useful as biomarkers of oxidative stress associated with inflammation, and further studies will be required to investigate if the extracellular forms of these proteins has immunoregulatory functions.
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