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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Veröffentlicht in: | FEBS letters 2009-08, Vol.583 (15), p.2493-2499 |
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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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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. 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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. 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Cassidy, Diane ; Goddard, Catharine ; Colledge, William H. ; Cassidy, Andrew ; Mehta, Anil</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5924-614234fc8c5da4ab56375afa5cc7459be69979632a694810404d56acdd74cb883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigen presentation/processing</topic><topic>Cell surface molecules</topic><topic>Cystic Fibrosis - immunology</topic><topic>Cystic Fibrosis - pathology</topic><topic>Cystic Fibrosis Transmembrane Conductance Regulator - genetics</topic><topic>Cystic Fibrosis Transmembrane Conductance Regulator - metabolism</topic><topic>Epithelial Cells - cytology</topic><topic>Epithelial Cells - immunology</topic><topic>Epithelial Cells - physiology</topic><topic>Humans</topic><topic>Immunoglobulin G - metabolism</topic><topic>Inflammation</topic><topic>Mice</topic><topic>Mice, Transgenic</topic><topic>Molecular Sequence Data</topic><topic>Mucosa</topic><topic>Mutation</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Phenylalanine - metabolism</topic><topic>Poxviridae - genetics</topic><topic>Poxviridae - metabolism</topic><topic>Respiratory Mucosa - cytology</topic><topic>Respiratory Mucosa - immunology</topic><topic>Respiratory Mucosa - pathology</topic><topic>Sequence Alignment</topic><topic>Sheep</topic><topic>Smallpox</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Treharne, Kate J.</creatorcontrib><creatorcontrib>Cassidy, Diane</creatorcontrib><creatorcontrib>Goddard, Catharine</creatorcontrib><creatorcontrib>Colledge, William H.</creatorcontrib><creatorcontrib>Cassidy, Andrew</creatorcontrib><creatorcontrib>Mehta, Anil</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Wiley Online Library Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Treharne, Kate J.</au><au>Cassidy, Diane</au><au>Goddard, Catharine</au><au>Colledge, William H.</au><au>Cassidy, Andrew</au><au>Mehta, Anil</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2009-08-06</date><risdate>2009</risdate><volume>583</volume><issue>15</issue><spage>2493</spage><epage>2499</epage><pages>2493-2499</pages><issn>0014-5793</issn><issn>1873-3468</issn><eissn>1873-3468</eissn><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.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>19596328</pmid><doi>10.1016/j.febslet.2009.07.002</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Antigen presentation/processing Cell surface molecules Cystic Fibrosis - immunology Cystic Fibrosis - pathology Cystic Fibrosis Transmembrane Conductance Regulator - genetics Cystic Fibrosis Transmembrane Conductance Regulator - metabolism Epithelial Cells - cytology Epithelial Cells - immunology Epithelial Cells - physiology Humans Immunoglobulin G - metabolism Inflammation Mice Mice, Transgenic Molecular Sequence Data Mucosa Mutation Peptides - genetics Peptides - metabolism Phenylalanine - metabolism Poxviridae - genetics Poxviridae - metabolism Respiratory Mucosa - cytology Respiratory Mucosa - immunology Respiratory Mucosa - pathology Sequence Alignment Sheep Smallpox |
title | 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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