Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator

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...

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Autores principales: Treharne, Kate J., Cassidy, Diane, Goddard, Catharine, Colledge, William H., Cassidy, Andrew, Mehta, Anil
Formato: Texto
Lenguaje:English
Publicado: Elsevier Science B.V 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2741568/
https://www.ncbi.nlm.nih.gov/pubmed/19596328
http://dx.doi.org/10.1016/j.febslet.2009.07.002
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author Treharne, Kate J.
Cassidy, Diane
Goddard, Catharine
Colledge, William H.
Cassidy, Andrew
Mehta, Anil
author_facet Treharne, Kate J.
Cassidy, Diane
Goddard, Catharine
Colledge, William H.
Cassidy, Andrew
Mehta, Anil
author_sort Treharne, Kate J.
collection PubMed
description 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.
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spelling pubmed-27415682009-09-17 Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator Treharne, Kate J. Cassidy, Diane Goddard, Catharine Colledge, William H. Cassidy, Andrew Mehta, Anil FEBS Lett Article 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. Elsevier Science B.V 2009-08-06 /pmc/articles/PMC2741568/ /pubmed/19596328 http://dx.doi.org/10.1016/j.febslet.2009.07.002 Text en © 2009 Elsevier B.V. https://creativecommons.org/licenses/by-nc-nd/3.0/ Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license
spellingShingle Article
Treharne, Kate J.
Cassidy, Diane
Goddard, Catharine
Colledge, William H.
Cassidy, Andrew
Mehta, Anil
Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
title Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
title_full Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
title_fullStr Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
title_full_unstemmed Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
title_short Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
title_sort epithelial igg and its relationship to the loss of f508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2741568/
https://www.ncbi.nlm.nih.gov/pubmed/19596328
http://dx.doi.org/10.1016/j.febslet.2009.07.002
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