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• W2065160977 abstract "Rationale: Cystic fibrosis transmembrane conductance regulator (CFTR) protein is a chloride channel regulating fluid homeostasis at epithelial surfaces. Its loss of function induces hypohydration, mucus accumulation, and bacterial infections in CF and potentially other lung chronic diseases.Objectives: To test whether neutrophil elastase (NE) and neutrophil-mediated inflammation negatively impact CFTR structure and function, in vitro and in vivo.Methods: Using an adenovirus-CFTR overexpression approach, we showed that NE degrades wild-type (WT)- and ΔF508-CFTR in vitro and WT-CFTR in mice through a new pathway involving the activation of intracellular calpains.Measurements and Main Results: CFTR degradation triggered a loss of function, as measured in vitro by channel patch-clamp and in vivo by nasal potential recording in mice. Importantly, this mechanism was also shown to be operative in a Pseudomonas aeruginosa lung infection murine model, and was NE-dependent, because CFTR integrity was significantly protected in NE−/− mice compared with WT mice.Conclusions: These data provide a new mechanism and show for the first time a link between NE-calpains activation and CFTR loss of function in bacterial lung infections relevant to CF and to other chronic inflammatory lung conditions." @default.
• W2065160977 created "2016-06-24" @default.
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• W2065160977 date "2013-01-15" @default.
• W2065160977 modified "2023-10-06" @default.
• W2065160977 title "Neutrophil Elastase Degrades Cystic Fibrosis Transmembrane Conductance Regulator via Calpains and Disables Channel Function<i>In Vitro</i>and<i>In Vivo</i>" @default.
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• W2065160977 doi "https://doi.org/10.1164/rccm.201205-0875oc" @default.
• W2065160977 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23220915" @default.
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