ArticleBMC biochemistry2009
Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function.
Article in BMC biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 119 citations in OpenAlex.
- 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
- S100A12 drives inflammatory and metabolic reprogramming in sepsis-associated acute kidney injury.Frontiers in molecular biosciences · 2026Review
- Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction.ACS chemical neuroscience · 2025Article
- Calprotectin-mediated survival ofmBio · 2025Article
- A review on clinical implications of S100 proteins in lung diseases.Frontiers in medicine · 2025Review
- Calcium mediated static and dynamic allostery in S100A12: Implications for target recognition by S100 proteins.Protein science : a publication of the Protein Society · 2024Article
- Systemic Markers of Lung Function and Forced Expiratory Volume in 1 Second Decline across Diverse Cohorts.Annals of the American Thoracic Society · 2023Article
- Zinc Binding Inhibits Cellular Uptake and Antifungal Activity of Histatin-5 inACS infectious diseases · 2022Article
- S100A12 promotes Mn(II) binding to pneumococcal PsaA and staphylococcal MntC by Zn(II) sequestration.Journal of inorganic biochemistry · 2022Article
- Metal sequestration by S100 proteins in chemically diverse environments.Trends in microbiology · 2022Review
- Regulation of zinc-dependent enzymes by metal carrier proteins.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Review
- A Structural Perspective on Calprotectin as a Ligand of Receptors Mediating Inflammation and Potential Drug Target.Biomolecules · 2022Review
- Discerning the promising binding sites of S100/calgranulins and their therapeutic potential in atherosclerosis.Expert opinion on therapeutic patents · 2021Review
- Nutritional immunity: targeting fungal zinc homeostasis.Heliyon · 2021Review
- Nutritional immunity: the impact of metals on lung immune cells and the airway microbiome during chronic respiratory disease.Respiratory research · 2021Review
- Zur: Zinc-Sensing Transcriptional Regulator in a Diverse Set of Bacterial Species.Pathogens (Basel, Switzerland) · 2021Review
- Zinc: Multidimensional Effects on Living Organisms.Biomedicines · 2021Review
- The Zinc Nutritional Immunity ofFrontiers in immunology · 2021Article
- Article
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
14 authors at 7 institutions in 4 countries.
Funding
Abstract
backgroundHuman S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins that are associated with many diseases including cancer, chronic inflammation and neurological disorders. S100A12 is an important factor in host/parasite defenses and in the inflammatory response. Like several other S100 proteins, it binds zinc and copper in addition to calcium. Mechanisms of zinc regulation have been proposed for a number of S100 proteins e.g. S100B, S100A2, S100A7, S100A8/9. The interaction of S100 proteins with their targets is strongly dependent on cellular microenvironment.
resultsThe aim of the study was to explore the factors that influence S100A12 oligomerization and target interaction. A comprehensive series of biochemical and biophysical experiments indicated that changes in the concentration of calcium and zinc led to changes in the oligomeric state of S100A12. Surface plasmon resonance confirmed that the presence of both calcium and zinc is essential for the interaction of S100A12 with one of its extracellular targets, RAGE--the Receptor for Advanced Glycation End products. By using a single-molecule approach we have shown that the presence of zinc in tissue culture medium favors both the oligomerization of exogenous S100A12 protein and its interaction with targets on the cell surface.
conclusionWe have shown that oligomerization and target recognition by S100A12 is regulated by both zinc and calcium. Our present work highlighted the potential role of calcium-binding S100 proteins in zinc metabolism and, in particular, the role of S100A12 in the cross talk between zinc and calcium in cell signaling.
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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.