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

doi:10.1016/j.febslet.2009.07.002

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

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	2493-2499
Number of pages	7
Journal	FEBS Letters
Volume	583
Issue number	15
DOIs	https://doi.org/10.1016/j.febslet.2009.07.002
Publication status	Published - 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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10.1016/j.febslet.2009.07.002

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@article{7fadee8228a4450bbf0c8f84539e71dc,

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

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.",

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

author = "Treharne, {Kate J.} and Diane Cassidy and Catharine Goddard and Colledge, {William H.} and Andrew Cassidy and Anil Mehta",

year = "2009",

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doi = "10.1016/j.febslet.2009.07.002",

language = "English",

volume = "583",

pages = "2493--2499",

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T1 - Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator

AU - Treharne, Kate J.

AU - Cassidy, Diane

AU - Goddard, Catharine

AU - Colledge, William H.

AU - Cassidy, Andrew

AU - Mehta, Anil

PY - 2009/8/6

Y1 - 2009/8/6

N2 - 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.

AB - 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.

KW - Smallpox

KW - Antigen presentation/processing

KW - Inflammation

KW - Mucosa

KW - Cell surface molecules

KW - PROTEIN-KINASE

KW - AIRWAY EPITHELIUM

KW - BINDING PROTEIN

KW - PHOSPHORYLATION

KW - IDENTIFICATION

KW - INFLAMMATION

KW - MEMBRANES

KW - DOMAIN

U2 - 10.1016/j.febslet.2009.07.002

DO - 10.1016/j.febslet.2009.07.002

M3 - Article

C2 - 19596328

SN - 0014-5793

VL - 583

SP - 2493

EP - 2499

JO - FEBS Letters

JF - FEBS Letters

IS - 15

ER -

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

Abstract

Keywords

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