Journal
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
Volume 52, Issue -, Pages 47-57Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2014.04.001
Keywords
CFTR; Chloride ion channel; Cystic fibrosis mutations; F508del-CFTR; CFTR knockout pigs
Categories
Funding
- Cystic Fibrosis Foundation
- Cystic Fibrosis Trust
- Engineering and Physical Sciences Research Council [EP/J00961X/1]
- Beijing Sun-Hope Intellectual Property Ltd.
- Medical Research Council
- Engineering and Physical Sciences Research Council [EP/F03623X/1, EP/J00961X/1] Funding Source: researchfish
- Medical Research Council [1373338] Funding Source: researchfish
- EPSRC [EP/F03623X/1, EP/J00961X/1] Funding Source: UKRI
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Defective epithelial ion transport is the hallmark of the life-limiting genetic disease cystic fibrosis (CF). This abnormality is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), the ATP-binding cassette transporter that functions as a ligand-gated anion channel. Since the identification of the CFTR gene, almost 2000 disease-causing mutations associated with a spectrum of clinical phenotypes have been reported, but the majority remain poorly characterised. Studies of a small number of mutations including the most common, F508del-CFTR, have identified six general mechanisms of CFTR dysfunction. Here, we review selectively progress to understand how CF mutations disrupt CFTR processing, stability and function. We explore CFTR structure and function to explain the molecular mechanisms of CFTR dysfunction and highlight new knowledge of disease pathophysiology emerging from large animal models of CF. Understanding CFTR dysfunction is crucial to the development of transformational therapies for CF patients. (C) 2014 Elsevier Ltd. All rights reserved.
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