ArticleMediators of inflammation2005
Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity.
Article in Mediators of inflammation, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 66 citations in OpenAlex.
- The C-terminal extension of calprotectin mediates zinc chelation and modulates Staphylococcus aureus biomass accumulation.Protein science : a publication of the Protein Society · 2025Article
- Characterization and Physiological Differences of Two Primary Cultures of Human Normal and Hypertrophic Scar Dermal Fibroblasts: A Pilot Study.Biomedicines · 2024Article
- Unraveling the Mechanisms of S100A8/A9 in Myocardial Injury and Dysfunction.Current issues in molecular biology · 2024Review
- Article
- S100A9 plays a key role in Clostridium perfringens beta2 toxin-induced inflammatory damage in porcine IPEC-J2 intestinal epithelial cells.BMC genomics · 2023Article
- Review
- Zinc is an important inter-kingdom signal between the host and microbe.Veterinary research · 2021Review
- GLI3: a mediator of genetic diseases, development and cancer.Cell communication and signaling : CCS · 2020Review
- Intracellular calprotectin (S100A8/A9) controls epithelial differentiation and caspase-mediated cleavage of EGFR in head and neck squamous cell carcinoma.Oral oncology · 2019Article
- Clinical Value of Serum S100A8/A9 and CA15-3 in the Diagnosis of Breast Cancer.Iranian journal of pathology · 2019Article
- S100A8/A9 in Inflammation.Frontiers in immunology · 2018Review
- Article
- Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells.PloS one · 2017Article
- Identification of proteins from 4200-year-old skin and muscle tissue biopsies from ancient Egyptian mummies of the first intermediate period shows evidence of acute inflammation and severe immune response.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Article
- The Hexahistidine Motif of Host-Defense Protein Human Calprotectin Contributes to Zinc Withholding and Its Functional Versatility.Journal of the American Chemical Society · 2016Article
- Nutritional Immunity: S100 Proteins at the Host-Pathogen Interface.The Journal of biological chemistry · 2015Review
- Article
- S100A8 and S100A9 Positive Cells in Colorectal Carcinoma: Clinicopathological Analysis.Gastroenterology research and practice · 2014Article
- The landscape of protein biomarkers proposed for periodontal disease: markers with functional meaning.BioMed research international · 2014Review
- Contributions of the S100A9 C-terminal tail to high-affinity Mn(II) chelation by the host-defense protein human calprotectin.Journal of the American Chemical Society · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S100A8/A9 (calprotectin), which is released by neutrophils under inflammatory conditions, has the capacity to induce apoptosis in various cells. We previously reported that S100A8/A9 induces apoptosis of EL-4 lymphoma cells via the uptake of extracellular zinc in a manner similar to DTPA, a membrane-impermeable zinc chelator. In this study, S100A8/A9-induced apoptosis was examined in several cell lines that are weakly sensitive to DTPA, suggesting S100A8/A9 is directly responsible for apoptosis in these cells. Since zinc inhibits apoptosis of MM46, one of these cells, the regulation by zinc of the capacity of S100A8/A9 to bind MM46 cells was studied. When MM46 cells were incubated with S100A8/A9 in standard or zinc-depleted medium, the amounts of S100A8/A9 bound to cells was markedly lower at 3 h than at 1 h. In contrast, when MM46 cells were incubated with S100A8/A9 in the presence of high levels of zinc, binding to cells was the same at 1 and 3 h. When the cells were permeabilized with saponin prior to analysis, a larger amount of cell-associated S100A8/A9 was detected at 3 h. The amount was further increased in cells treated with chloroquine, suggesting that S100A8/A9 was internalized and degraded in lysosomes. Although it has been reported that S100A8/A9 binds to heparan sulfate on cell membranes, the amount of S100A8/A9 bound to MM46 cells was not reduced by heparinase treatment, but was reduced by trypsin treatment. These results suggest that S100A8/A9 induces apoptosis by direct binding to MM46 cells, and that this activity is regulated by zinc.
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