ArticleThe Journal of biological chemistry2010
S-glutathionylation regulates inflammatory activities of S100A9.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
- Sputum Glutaredoxin 1 and Protein S-Glutathionylation in COPD.Antioxidants (Basel, Switzerland) · 2026Article
- S100A9: The Unusual Suspect Connecting Viral Infection and Inflammation.Journal of immunology (Baltimore, Md. : 1950) · 2024Review
- The Post-Translational Modifications of Human Salivary Peptides and Proteins Evidenced by Top-Down Platforms.International journal of molecular sciences · 2023Review
- Psoriatic Dermal-Derived Mesenchymal Stem Cells Induced C3 Expression in Keratinocytes.Clinical, cosmetic and investigational dermatology · 2022Article
- S100a9 Protects Male Lupus-Prone NZBWF1 Mice From Disease Development.Frontiers in immunology · 2021Article
- Gingival Crevicular Fluid Peptidome Profiling in Healthy and in Periodontal Diseases.International journal of molecular sciences · 2020Review
- Dysregulation of the glutaredoxin/American journal of physiology. Cell physiology · 2020Article
- miRNAs Regulate Cytokine Secretion Induced by Phosphorylated S100A8/A9 in Neutrophils.International journal of molecular sciences · 2019Article
- Oxidative cross-linking of calprotectin occurs in vivo, altering its structure and susceptibility to proteolysis.Redox biology · 2019Article
- Article
- Role of glutathione metabolism in host defense againstProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanistic understanding of nanoparticles' interactions with extracellular matrix: the cell and immune system.Particle and fibre toxicology · 2017Review
- Article
- Comprehensive Proteomic and Metabolomic Signatures of Nontypeable Haemophilus influenzae-Induced Acute Otitis Media Reveal Bacterial Aerobic Respiration in an Immunosuppressed Environment.Molecular & cellular proteomics : MCP · 2016Article
- Transition from identity to bioactivity-guided proteomics for biomarker discovery with focus on the PF2D platform.Proteomics. Clinical applications · 2016Review
- Myeloperoxidase-dependent lipid peroxidation promotes the oxidative modification of cytosolic proteins in phagocytic neutrophils.The Journal of biological chemistry · 2015Article
- Regulation of neovascularization by S-glutathionylation via the Wnt5a/sFlt-1 pathway.Biochemical Society transactions · 2014Review
- Binding of glutathione to enterovirus capsids is essential for virion morphogenesis.PLoS pathogens · 2014Article
- Cell death-associated molecular-pattern molecules: inflammatory signaling and control.Mediators of inflammation · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reactive oxygen species generated by activated neutrophils can cause oxidative stress and tissue damage. S100A8 (A8) and S100A9 (A9), abundant in neutrophil cytoplasm, are exquisitely sensitive to oxidation, which may alter their functions. Murine A8 is a neutrophil chemoattractant, but it suppresses leukocyte transmigration in the microcirculation when S-nitrosylated. Glutathione (GSH) modulates intracellular redox, and S-glutathionylation can protect susceptible proteins from oxidative damage and regulate function. We characterized S-glutathionylation of A9; GSSG and GSNO generated S-glutathionylated A8 (A8-SSG) and A9 (A9-SSG) in vitro, whereas only A9-SSG was detected in cytosol of neutrophils activated with phorbol myristate acetate (PMA) but not with fMLP or opsonized zymosan. S-Glutathionylation exposed more hydrophobic regions in Zn(2+)-bound A9 but did not alter Zn(2+) binding affinity. A9-SSG had reduced capacity to form heterocomplexes with A8, but the arachidonic acid binding capacities of A8/A9 and A8/A9-SSG were similar. A9 and A8/A9 bind endothelial cells; S-glutathionylation reduced binding. We found little effect of A9 or A9-SSG on neutrophil CD11b/CD18 expression or neutrophil adhesion to endothelial cells. However, A9, A9-SSG and A8/A9 promoted neutrophil adhesion to fibronectin but, in the presence of A8, A9-mediated adhesion was abrogated by glutathionylation. S-Glutathionylation of A9 may protect its oxidation to higher oligomers and reduce neutrophil binding to the extracellular matrix. This may regulate the magnitude of neutrophil migration in the extravasculature, and together with the functional changes we reported for S-nitrosylated A8, particular oxidative modifications of these proteins may limit tissue damage in acute inflammation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.