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

Kate J. Treharne, Diane Cassidy, Catharine Goddard, William H. Colledge, Andrew Cassidy, Anil Mehta

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    4 Citations (Scopus)

    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 Delta F508) 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. (c) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)2493-2499
    Number of pages7
    JournalFEBS Letters
    Volume583
    Issue number15
    DOIs
    Publication statusPublished - 6 Aug 2009

    Keywords

    • Smallpox
    • Antigen presentation/processing
    • Inflammation
    • Mucosa
    • Cell surface molecules
    • PROTEIN-KINASE
    • AIRWAY EPITHELIUM
    • BINDING PROTEIN
    • PHOSPHORYLATION
    • IDENTIFICATION
    • INFLAMMATION
    • MEMBRANES
    • DOMAIN

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