Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872294 | FEBS Letters | 2009 | 7 Pages |
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 ÎF508) 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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Authors
Kate J. Treharne, Diane Cassidy, Catharine Goddard, William H. Colledge, Andrew Cassidy, Anil Mehta,