ArticleRedox biology2019
Oxidative cross-linking of calprotectin occurs in vivo, altering its structure and susceptibility to proteolysis.
Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- The persulfidome of alveolar epithelial cells reveals persulfidation of calprotectin as critical to preserve its antifungal activity.iScience · 2026Article
- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
- A first structural model for covalent dimerization of S100 proteins.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Myeloperoxidase Luminol Reaction - A Novel Faecal Assay for Predicting Colonoscopy Findings in Patients with Ulcerative Colitis: A Pilot Cross-Sectional Clinical Study.Advanced healthcare materials · 2026Article
- Fecal Myeloperoxidase Levels Reflect Disease Activity in Children With Crohn's Disease.Inflammatory bowel diseases · 2025Observational
- Comparison of machine learning methods for Predicting 3-Year survival in elderly esophageal squamous cancer patients based on oxidative stress.BMC cancer · 2024Article
- Biomarkers in inflammatory bowel disease: a practical guide.Therapeutic advances in gastroenterology · 2024Review
- How S100B crosses brain barriers and why it is considered a peripheral marker of brain injury.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- The Post-Translational Modifications of Human Salivary Peptides and Proteins Evidenced by Top-Down Platforms.International journal of molecular sciences · 2023Review
- Post-translational modifications on the metal-sequestering protein calprotectin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- Myeloperoxidase in Health and Disease.International journal of molecular sciences · 2023Article
- Hypochlorous Acid and Chloramines Induce Specific Fragmentation and Cross-Linking of the G1-IGD-G2 Domains of Recombinant Human Aggrecan, and Inhibit ADAMTS1 Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Faecal Myeloperoxidase as a Biomarker of Endoscopic Activity in Inflammatory Bowel Disease.Journal of Crohn's & colitis · 2022Article
- New Faecal Calprotectin Assay by IDS: Validation and Comparison to DiaSorin Method.Diagnostics (Basel, Switzerland) · 2022Article
- Metal sequestration by S100 proteins in chemically diverse environments.Trends in microbiology · 2022Review
- Review
- Serum Calprotectin Level as an Inflammatory Marker in Newly Diagnosed Hypertensive Patients.International journal of hypertension · 2022Article
- Antimicrobial peptides: Defending the mucosal epithelial barrier.Frontiers in oral health · 2022Review
- Role of inflammation and oxidative stress in tissue damage associated with cystic fibrosis: CAPE as a future therapeutic strategy.Molecular and cellular biochemistry · 2022Review
- Upregulation of oxidative stress gene markers during SARS-COV-2 viral infection.Free radical biology & medicine · 2021Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calprotectin, the major neutrophil protein, is a critical alarmin that modulates inflammation and plays a role in host immunity by strongly binding trace metals essential for bacterial growth. It has two cysteine residues favourably positioned to act as a redox switch. Whether their oxidation occurs in vivo and affects the function of calprotectin has received little attention. Here we show that in saliva from healthy adults, and in lavage fluid from the lungs of patients with respiratory diseases, a substantial proportion of calprotectin was cross-linked via disulfide bonds between the cysteine residues on its S100A8 and S100A9 subunits. Stimulated human neutrophils released calprotectin and subsequently cross-linked it by myeloperoxidase-dependent production of hypochlorous acid. The myeloperoxidase-derived oxidants hypochlorous acid, taurine chloramine, hypobromous acid, and hypothiocyanous acid, all at 10 μM, cross-linked calprotectin (5 μM) via reversible disulfide bonds. Hypochlorous acid generated A9-A9 and A8-A9 cross links. Hydrogen peroxide (10 μM) did not cross-link the protein. Purified neutrophil calprotectin existed as a non-covalent heterodimer of A8/A9 which was converted to a heterotetramer - (A8/A9)
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