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Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator |
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| Authors: | Kate J. Treharne Catharine Goddard Andrew Cassidy |
| Affiliation: | a Division of Medical Sciences, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, UK b Physiology, Development and Neuroscience Department, University of Cambridge, Cambridge, UK c DNA Analysis Facility, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, UK |
| Abstract: | The most debilitating feature of cystic fibrosis (CF) disease is uncontrolled inflammation of respiratory epithelium. The relationship between the commonest mutated form of CFTR (F508del or ΔF508) and inflammation has not yet been elucidated. Here, we present a new paradigm suggesting that CFTR can interact with intra-epithelial IgG, establishing a direct link between normal CFTR and the immune system. Further, our data show that the amino-acid sequence local to F508 can bind IgG with high affinity, dependent on F508, such that loss of F508 abolishes this link both in vitro and in the intact cell. |
| Keywords: | Smallpox Antigen presentation/processing Inflammation Mucosa Cell surface molecules |
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