ArticleCell death and differentiation2018
Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts.
Article in Cell death and differentiation, 2018. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Sustainable development of novel zinc oxide nano flowers mediated red yeast rice for control of hepatocellular carcinoma.Scientific reports · 2026Article
- New Non-Saccharide Heparin Mimetics as Inhibitors of Cathepsin G.Chemical biology & drug design · 2026Article
- Targeting pyroptosis in periodontitis: mechanisms and therapeutic strategies.Frontiers in immunology · 2026Review
- Organelles and cancer cell pyroptosis: overview and perspectives.Cell death & disease · 2025Review
- From gum inflammation to oral cancers: pyroptosis as the molecular torchbearer in periodontitis-driven carcinogenesis.Discover oncology · 2025Review
- Trimming the fat: a brief review of lipids at the host-pathogen interface.Infection and immunity · 2025Review
- Pyroptosis of periodontal ligament stem cells aggravates periodontitis via Piezo1 channel.iScience · 2025Article
- An ATP-responsive metal-organic framework against periodontitis via synergistic ion-interference-mediated pyroptosis.National science review · 2024Article
- Dying for a cause: The pathogenic manipulation of cell death and efferocytic pathways.Molecular oral microbiology · 2024Review
- Inhibition of METTL3 Alleviates NLRP3 Inflammasome Activation via Increasing Ubiquitination of NEK7.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- High-Density Lipoproteins at the Interface between the NLRP3 Inflammasome and Myocardial Infarction.International journal of molecular sciences · 2024Review
- Extracellular vesicles from periodontal pathogens regulate hepatic steatosis via Toll-like receptor 2 and plasminogen activator inhibitor-1.Journal of extracellular vesicles · 2024Article
- The Role of Gingival Fibroblasts in the Pathogenesis of Periodontitis.Journal of dental research · 2023Review
- Homogeneous, Synthetic, Non-Saccharide Glycosaminoglycan Mimetics as Potent Inhibitors of Human Cathepsin G.Biomolecules · 2023Article
- Roles of Pyroptosis-Related Genes in the Diagnosis and Subtype Classification of Periodontitis.Journal of immunology research · 2023Article
- Characterization of Treponema denticola Major Surface Protein (Msp) by Deletion Analysis and Advanced Molecular Modeling.Journal of bacteriology · 2022Article
- Article
- Pyroptosis in periodontitis: From the intricate interaction with apoptosis, NETosis, and necroptosis to the therapeutic prospects.Frontiers in cellular and infection microbiology · 2022Review
- Pyroptosis-Mediated Periodontal Disease.International journal of molecular sciences · 2021Review
- Inflammasomes in Alveolar Bone Loss.Frontiers in immunology · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caspase-4 is an inflammatory caspase; however, its mechanism of activation is poorly understood. In this study, we demonstrate that Td92, a surface protein of the periodontal pathogen Treponema denticola and a homolog of the Treponema pallidum surface protein Tp92, activates caspase-4 and induces pyroptosis in primary cultured human gingival fibroblasts (HGFs) via cathepsin G activation. Cathepsin G inhibition or siRNA knockdown of cathepsin G inhibited Td92-induced caspase-4 activation and cell death. Td92-induced cell death was significantly inhibited by siRNA knockdown of gasdermin D. Td92 treatment resulted in the binding of cathepsin G to caspase-4 and the coaggregation of these two molecules. In addition, Td92 induced IL-1α expression and secretion, and this was inhibited by caspase-4 knockdown. Cytochalasin D did not block Td92-induced caspase-4 activation, suggesting that Td92 internalization is not required for caspase-4 activation. Our results demonstrate that cathepsin G is directly engaged in caspase-4 activation by a bacterial ligand, which is responsible for cell death and IL-1α secretion in HGFs.
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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.