ArticleCancer cell international2023
The proteomics analysis of extracellular vesicles revealed the possible function of heat shock protein 60 in Helicobacter pylori infection.
Article in Cancer cell international, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 11 citations in OpenAlex.
- Chaperonin in health and disease.Molecular biomedicine · 2026Review
- Exosome-orchestrated network in gastric cancer: mechanisms, immune regulation, biomarkers and therapeutic vehicles.Frontiers in cell and developmental biology · 2026Review
- Bidirectional Interactions Between Nanomaterials and Extracellular Vesicles: Molecular Insights and Translational Implications.International journal of nanomedicine · 2026Review
- Hsp60-Bearing Exosomes inCells · 2025Review
- Gut microbiome and gastric cancer: microbial interactions and therapeutic potential.Gut pathogens · 2025Review
- The Role ofInternational journal of molecular sciences · 2025Review
- Environmental factors in gastric carcinogenesis and preventive intervention strategies.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2025Review
- Extracellular vesicles in Helicobacter pylori-mediated diseases: mechanisms and therapeutic potential.Cell communication and signaling : CCS · 2025Review
- Study of the relationships among known virulence genes, coccoid transformation and cytotoxicity ofVirulence · 2024Article
- Review
- Molecular Chaperonin HSP60: Current Understanding and Future Prospects.International journal of molecular sciences · 2024Review
- Interaction between intestinal flora and gastric cancer in tumor microenvironment.Frontiers in oncology · 2024Review
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
backgroundHelicobacter pylori (H. pylori) infection is a major risk factor for gastric diseases, including gastritis and gastric cancer. Heat shock protein 60 (HSP60) is a chaperone protein involved in various cellular processes and has been implicated in the immune response to bacterial infections. Extracellular vesicles (EVs) containing various protein components play important roles in cell communication. In the present study, a systematic proteomic analysis of EVs obtained from H. pylori infected cells was performed and the EV-derived HSP60 function was studied.
methodsEVs were evaluated by nanoparticle tracking analysis, transmission electron microscopy and western blotting. The recognized protein components were quantified by label-free proteomics and subjected to bioinformatics assays. The expression of HSP60 in EVs, host cells and gastric cancers infected by H. pylori was determined by western blotting and immunohistochemical, respectively. In addition, the apoptotic regulation mechanisms of HSP60 in H. pylori infection were analyzed by western blotting and flow cytometry.
resultsA total of 120 important differential proteins were identified in the EVs from H. pylori-infected cells and subjected to Gene Ontology analysis. Among them, CD63, HSP-70 and TSG101 were verified via western blotting. Moreover, HSP60 expression was significantly increased in the EVs from H. pylori-infected GES-1 cells. H. pylori infection promoted an abnormal increase in HSP60 expression in GES-1 cells, AGS cells, gastric mucosa and gastric cancer. In addition, knockdown of HSP60 suppressed the apoptosis of infected cells and the expression of Bcl2, and promoted the upregulation of Bax.
conclusionThis study provides a comprehensive proteomic profile of EVs from H. pylori-infected cells, shedding light on the potential role of HSP60 in H. pylori infection. The findings underscore the significance of EV-derived HSP60 in the pathophysiology of H. pylori-associated diseases.
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