ArticleChemical science2016
Calcium-induced Tetramerization and Zinc Chelation Shield Human Calprotectin from Degradation by Host and Bacterial Extracellular Proteases.
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 51 citations in OpenAlex.
- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
- Multi-target litholytic strategy toward calcium oxalate stone therapy: a fundamental study.Frontiers in pharmacology · 2026Article
- Design and characterization of calprotectin tetramerization variants for probing the role of oligomerization in receptor activation.Protein science : a publication of the Protein Society · 2026Article
- Calprotectin elicits aberrant iron starvation responses inJournal of bacteriology · 2025Article
- Review
- Development of Luminescent Biosensors for Calprotectin.ACS chemical biology · 2024Article
- Iron Sequestration by Murine Calprotectin Induces Starvation Responses inACS infectious diseases · 2024Article
- Spectroscopic and computational investigations of Cobalt(II) binding to the innate immune protein human calprotectin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- A Serological Neoepitope Biomarker of Neutrophil Elastase-Degraded Calprotectin, Associated with Neutrophil Activity, Identifies Idiopathic Pulmonary Fibrosis and Chronic Obstructive Pulmonary Disease More Effectively Than Total Calprotectin.Journal of clinical medicine · 2023Article
- 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
- Steric Effects on the Chelation of MnChemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- A Specific Calprotectin Neo-epitope [CPa9-HNE] in Serum from Inflammatory Bowel Disease Patients Is Associated with Neutrophil Activity and Endoscopic Severity.Journal of Crohn's & colitis · 2022Article
- Metal sequestration by S100 proteins in chemically diverse environments.Trends in microbiology · 2022Review
- A Structural Perspective on Calprotectin as a Ligand of Receptors Mediating Inflammation and Potential Drug Target.Biomolecules · 2022Review
- Zinc sequestration by human calprotectin facilitates manganese binding to the bacterial solute-binding proteins PsaA and MntC.Metallomics : integrated biometal science · 2022Article
- Bacterial Responses to Iron Withholding by Calprotectin.Biochemistry · 2021Review
- Molecular Basis of Ca(II)-Induced Tetramerization and Transition-Metal Sequestration in Human Calprotectin.Journal of the American Chemical Society · 2021Article
- Review
- Calprotectin (S100A8/A9) Is an Innate Immune Effector in Experimental Periodontitis.Infection and immunity · 2021Article
- Calprotectin-Mediated Zinc Chelation Inhibits Pseudomonas aeruginosa Protease Activity in Cystic Fibrosis Sputum.Journal of bacteriology · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Calprotectin (CP, S100A8/S100A9 oligomer, MRP-8/14 oligomer, calgranulins A and B) is a protein component of the innate immune system that contributes to the metal-withholding response by sequestering bioavailable transition metal ions at sites of infection. Human CP employs Ca(II) ions to modulate its quaternary structure, transition metal binding properties, and antimicrobial activity. In this work, we report the discovery that Ca(II)-induced self-association of human CP to afford heterotetramers protects the protein scaffold from degradation by host serine proteases. We present the design and characterization of two new human CP-Ser variants, S100A8(C42S)(I60E)/S100A9(C3S) and S100A8(C42S)(I60K)/S100A9(C3S), that exhibit defective tetramerization properties. Analytical size exclusion chromatography and analytical ultracentrifugation reveal that both variants, hereafter I60E and I60K, persist as heterodimers in the presence of Ca(II) only, and form heterotetramers in the presence of Mn(II) only and both Ca(II) and Mn(II). Coordination to Fe(II) also causes I60E and I60K to form heterotetramers in both the absence and presence of Ca(II). The Ca(II)-bound I60E and I60K heterodimers are readily degraded by trypsin, chymotrypsin and human neutrophil elastase, whereas the Ca(II)-bound CP-Ser heterotetramers and the Ca(II)- and Mn(II)-bound I60E and I60K heterotetramers are resistant to degradation by these host proteases. The staphylococcal extracellular protease GluC cuts the S100A8 subunit of CP-Ser at the C-terminal end of residue 89 to afford a ΔSKHE variant. The GluC cleavage site is in close proximity to the His
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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.