Objective: To screen potential differentially expressed genes related to immune function in nasopharyngeal carcinoma through an online database, and to verify their mechanism of action, so as to provide a reference for the diagnosis and treatment of nasopharyngeal carcinoma in the future.
Methods: Differentially expressed genes were analyzed from the GSE227541 dataset, and functional enrichment analysis was conducted. With mucin 5B, oligomeric mucus/gel-forming as the focus, the correlation between its expression and immune indexes was analyzed by using the TIMER database. The expressions of mucin 5B, oligomeric mucus/gel-forming in clinical NPC tissues and adjacent tissue samples were detected Furthermore, mucin 5B, oligomeric mucus/gel-forming abnormal expression vectors were constructed and transfected into human NPC cell CNE-2Z to detect alterations in cell activity, ferroptosis and the immune microenvironment. In addition, the role of the Wnt/β-catenin signaling pathway in nasopharyngeal carcinoma was observed, and the influence of mucin 5B, oligomeric mucus/gel-forming on this pathway was discussed.
Results: A total of 42 differentially expressed genes were found in the GSE227541 dataset, among which mucin 5B, oligomeric mucus/gel-forming was obviously at the core of the entire network. In nasopharyngeal carcinoma tissues, the research team observed the upregulated expression of mucin 5B, oligomeric mucus/gel-forming (P < 0.05). In vitro, increased expression of elevated mucin 5B, oligomeric mucus/gel-forming activates nasopharyngeal carcinoma cell activity and immune escape and inhibits ferroptosis. In terms of pathways, upregulating mucin 5B, oligomeric mucus/gel-forming expression could activate the Wnt/β-catenin pathway.
Conclusions: Mucin 5B, oligomeric mucus/gel-forming regulates the immune escape of nasopharyngeal carcinoma cells and participates in tumor progression by mediating the Wnt/β-catenin signaling pathway.
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http://dx.doi.org/10.1007/s12672-025-01772-4 | DOI Listing |
Molecules
December 2024
Institute of Food Technology and Analysis, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, B. Stefanowskiego 2/22, 90-537 Łódź, Poland.
The purpose of this research was to investigate the prebiotic effects of different fractions of pectin-derived oligosaccharides (POSs) from apple pomace (AP) in relation to their molecular weight (MW), structure, and composition. Enzymatic treatment of the apple pomace resulted in high-molecular-weight arabinans and rhamnogalacturonans (MW 30-100 kDa, MW 10-30 kDa), as well as oligomeric fractions with molecular weights of less than 10 kDa, consisting mainly of homogalacturonan. The biological potential of the POSs against various lactobacilli and bifidobacteria was evaluated.
View Article and Find Full Text PDFDiscov Oncol
January 2025
Department of Ear, Nose and Throat (ENT), The First People's Hospital of Jiande, No. 599 Yanzhou Avenue, Xin'anjiang Street, Jiande, 311600, Zhejiang, China.
Objective: To screen potential differentially expressed genes related to immune function in nasopharyngeal carcinoma through an online database, and to verify their mechanism of action, so as to provide a reference for the diagnosis and treatment of nasopharyngeal carcinoma in the future.
Methods: Differentially expressed genes were analyzed from the GSE227541 dataset, and functional enrichment analysis was conducted. With mucin 5B, oligomeric mucus/gel-forming as the focus, the correlation between its expression and immune indexes was analyzed by using the TIMER database.
bioRxiv
December 2024
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Human lectins are critical carbohydrate-binding proteins that recognize diverse glycoconjugates from microorganisms and can play a key role in host-microbe interactions. Despite their importance in immune recognition and pathogen binding, the specific glycan ligands and functions of many human lectins remain poorly understood. Using previous proof-of-concept studies on selected lectins as the foundation for this work, we present ten additional glycan analysis probes (GAPs) from a diverse set of human soluble lectins, offering robust tools to investigate glycan-mediated interactions.
View Article and Find Full Text PDFMol Neurobiol
November 2024
Department of Neurology, The Second Medical Center and National Clinical Research Center for Geriatric Disease, Chinese PLA General Hospital, Beijing, China.
Eur J Clin Invest
December 2024
Division of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
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