ArticlePloS one2012
Molecular interface of S100A8 with cytochrome b558 and NADPH oxidase activation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Defining the safety and efficacy of liver-directed AAV gene therapy using a human liver tissue-equivalent platform.Molecular therapy. Advances · 2026Article
- The S100A8/A9-NETosis feedback loop in sepsis: potential mechanisms, immune crosstalk, and therapeutic targeting.Frontiers in immunology · 2026Review
- Diagnostic immune-related markers for diabetic kidney disease: a bioinformatics and machine learning approach.Renal failure · 2025Article
- Cytosolic proliferating cell nuclear antigen (PCNA) orchestrates neutrophil hyperactivation in COVID-19.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- An exploratory study on the metagenomic and proteomic characterization of hypothyroidism in the first half of pregnancy and correlation with Th1/Th2 balance.Frontiers in immunology · 2025Article
- Generation of a novel monoclonal antibody against inflammatory biomarker S100A8 using hybridoma technology.Biotechnology letters · 2023Article
- Antimicrobial peptides: Defending the mucosal epithelial barrier.Frontiers in oral health · 2022Review
- Calprotectin and the Initiation and Progression of Head and Neck Cancer.Journal of dental research · 2018Review
- Article
- [Expression of S100A8 and A100A9 in giant cell tumor of bone and its relation with CT and MR imaging findings].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2015Article
- Lymphovascular invasion and histologic grade are associated with specific genomic profiles in invasive carcinomas of the breast.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Article
- S100 proteins in cancer.Nature reviews. Cancer · 2015Review
- Chronic granulomatous disease: why an inflammatory disease?Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2014Review
- Cell-based therapy for acute organ injury: preclinical evidence and ongoing clinical trials using mesenchymal stem cells.Anesthesiology · 2014Review
- Mg supplementation protects against ritonavir-mediated endothelial oxidative stress and hepatic eNOS downregulation.Free radical biology & medicine · 2014Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S100A8 and S100A9 are two calcium binding Myeloid Related Proteins, and important mediators of inflammatory diseases. They were recently introduced as partners for phagocyte NADPH oxidase regulation. However, the precise mechanism of their interaction remains elusive. We had for aim (i) to evaluate the impact of S100 proteins on NADPH oxidase activity; (ii) to characterize molecular interaction of either S100A8, S100A9, or S100A8/S100A9 heterocomplex with cytochrome b(558); and (iii) to determine the S100A8 consensus site involved in cytochrome b(558)/S100 interface. Recombinant full length or S100A9-A8 truncated chimera proteins and ExoS-S100 fusion proteins were expressed in E. coli and in P. aeruginosa respectively. Our results showed that S100A8 is the functional partner for NADPH oxidase activation contrary to S100A9, however, the loading with calcium and a combination with phosphorylated S100A9 are essential in vivo. Endogenous S100A9 and S100A8 colocalize in differentiated and PMA stimulated PLB985 cells, with Nox2/gp91(phox) and p22(phox). Recombinant S100A8, loaded with calcium and fused with the first 129 or 54 N-terminal amino acid residues of the P. aeruginosa ExoS toxin, induced a similar oxidase activation in vitro, to the one observed with S100A8 in the presence of S100A9 in vivo. This suggests that S100A8 is the essential component of the S100A9/S100A8 heterocomplex for oxidase activation. In this context, recombinant full-length rS100A9-A8 and rS100A9-A8 truncated 90 chimera proteins as opposed to rS100A9-A8 truncated 86 and rS100A9-A8 truncated 57 chimeras, activate the NADPH oxidase function of purified cytochrome b(558) suggesting that the C-terminal region of S100A8 is directly involved in the molecular interface with the hemoprotein. The data point to four strategic (87)HEES(90) amino acid residues of the S100A8 C-terminal sequence that are involved directly in the molecular interaction with cytochrome b(558) and then in the phagocyte NADPH oxidase activation.
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