Source:http://linkedlifedata.com/resource/pubmed/id/20875079
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2011-1-7
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pubmed:abstractText |
The integrin ?E(CD103)?7 (?E?7) is expressed by intraepithelial lymphocytes, dendritic cells and regulatory T cells. It plays an important role in the mucosal immune system by retaining lymphocytes within the epithelium and is involved in graft rejection, immunity against tumours and the generation of gut-homing effector cells. In gut and breast, the ligand for ?E?7 is E-cadherin but in human oral mucosa and skin, there is evidence that lymphocytes use an alternative, unknown, ligand. In the present study, the I domain of the human ?E subunit, which contains the E-cadherin-binding site, was locked in a highly active, 'open' and an inactive, 'closed' conformation by the introduction of disulphide bonds and these domains were expressed as IgG Fc fusion proteins. ?E fusion proteins recognize E-cadherin, the only known ligand for ?E?7. This interaction was inhibited by an antibody that blocks the ?E-binding site on E-cadherin and by the omission of Mn(2+) , which is essential for integrin function in vitro. The locked 'open' conformation of ?E adhered to human oral and skin keratinocytes, including the E-cadherin-negative H376 cell line, and this was not inhibited by blocking antibody against the ?E?7-binding site on E-cadherin, providing further evidence for the existence of an alternative ligand for ?E?7 in skin and oral mucosa. The interaction with E-cadherin and the alternative ligand was Mn(2+) dependent and mediated by the metal ion-dependent coordination site (MIDAS) of the locked 'open'?E I domain, independently of the ?7 subunit.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin beta Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha E integrins,
http://linkedlifedata.com/resource/pubmed/chemical/integrin beta7
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1365-2567
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
132
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
188-96
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pubmed:dateRevised |
2011-3-11
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pubmed:meshHeading |
pubmed-meshheading:20875079-Antigens, CD,
pubmed-meshheading:20875079-Binding Sites,
pubmed-meshheading:20875079-Cadherins,
pubmed-meshheading:20875079-Cell Adhesion,
pubmed-meshheading:20875079-Cell Line, Tumor,
pubmed-meshheading:20875079-Humans,
pubmed-meshheading:20875079-Immunity, Mucosal,
pubmed-meshheading:20875079-Integrin alpha Chains,
pubmed-meshheading:20875079-Integrin beta Chains,
pubmed-meshheading:20875079-Keratinocytes,
pubmed-meshheading:20875079-Ligands,
pubmed-meshheading:20875079-Mouth Mucosa,
pubmed-meshheading:20875079-Protein Conformation,
pubmed-meshheading:20875079-Recombinant Fusion Proteins,
pubmed-meshheading:20875079-Skin,
pubmed-meshheading:20875079-T-Lymphocytes
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pubmed:year |
2011
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pubmed:articleTitle |
The ?E(CD103)?7 integrin interacts with oral and skin keratinocytes in an E-cadherin-independent manner*.
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pubmed:affiliation |
Unit of Oral and Maxillofacial Pathology, School of Clinical Dentistry, University of Sheffield, Sheffield Babraham Institute, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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