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• W2020862910 abstract "Understanding the mechanisms underlying bacterial-driven inflammation and neutrophil recruitment is important to design better therapies for CF. CXCL8 is an important chemokine found elevated in the airways of CF patients that recruits neutrophil to sites of the inflammation.Airway epithelial cells (AECs) expressing wild-type CFTR or CFTR∆F508 were challenged with Pseudomonas aeruginosa diffusible material (PsaDM) and the synthesis of CXCL8 was measured by quantitative real-time PCR and ELISA in absence or presence of MAPK inhibitors, TLR antagonists, glutathione and a NADPH oxidase inhibitor.CFTR∆F508 AECs secrete more CXCL8 in response to PsaDM than their wild type counterpart, which can be reversed by addition of extracellular glutathione or incubating AECs at 27°C to favour folding and expression of CFTR at the cell membrane. Moreover, in CFTR∆F508 AECs, TLR2, TLR4 and TLR5 act redundantly to drive CXCL8 synthesis via the activation of NADPH oxidase.These results demonstrate that NADPH oxidase is necessary for CXCL8 synthesis in response to TLRs activation by P. aeruginosa." @default.
• W2020862910 created "2016-06-24" @default.
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• W2020862910 date "2011-03-01" @default.
• W2020862910 modified "2023-10-13" @default.
• W2020862910 title "P. aeruginosa drives CXCL8 synthesis via redundant toll-like receptors and NADPH oxidase in CFTR∆F508 airway epithelial cells" @default.
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• W2020862910 doi "https://doi.org/10.1016/j.jcf.2010.11.005" @default.
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