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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2011-6-20
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pubmed:abstractText |
The lung's epithelial surface is at the same time vitally exchanging gas with the environment and acting as a barrier that protects the organism from the environment. We hypothesized that activation of epithelial-cell G-protein-coupled receptors for immune-defense molecules would temporarily interrupt cadherin-dependent cell-cell adhesion of epithelial cells and thereby focally and temporarily compromise the epithelial barrier to facilitate delivery of other immune molecules and cells to challenged sites. Activation of type 1 histamine or type 2 PAR receptors on the basolateral surface of primary airway epithelial cells or L-cells expressing E-cadherin interrupted cadherin adhesion and caused approximately a 50% decrease in the epithelial barrier for 2-3 minutes. Given basic biochemical observations of others, we further hypothesized that activation of the receptors altered the barrier by phosphorylating tyrosines on an essential cadherin-complex component, beta-catenin. Y-F mutations in beta-catenin completely blocked the effects of activating the same receptors on cadherin-dependent adhesion and on the epithelial barrier. Hence, G-protein-coupled receptors responding to immune-defense molecules temporarily and focally interrupt the lung epithelial barrier by compromising cadherin-based adhesion.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-10593980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-11121423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-11279024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-11348595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-11847339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-12794099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-15166221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-16714334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-17087658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-17322282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-17618275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-18083766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-19515834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-6370707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21686228-6976838
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDH1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, PAR-2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Histamine H1,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/seryl-leucyl-isoleucyl-glycyl-arginy...
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pubmed:status |
MEDLINE
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pubmed:issn |
0065-7778
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
122
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
217-28
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pubmed:meshHeading |
pubmed-meshheading:21686228-Animals,
pubmed-meshheading:21686228-Cadherins,
pubmed-meshheading:21686228-Cell Adhesion,
pubmed-meshheading:21686228-Cell Line,
pubmed-meshheading:21686228-Dogs,
pubmed-meshheading:21686228-Electric Impedance,
pubmed-meshheading:21686228-Epithelial Cells,
pubmed-meshheading:21686228-Humans,
pubmed-meshheading:21686228-Immunity, Mucosal,
pubmed-meshheading:21686228-Kidney,
pubmed-meshheading:21686228-Mutation,
pubmed-meshheading:21686228-Oligopeptides,
pubmed-meshheading:21686228-Permeability,
pubmed-meshheading:21686228-Phosphorylation,
pubmed-meshheading:21686228-Receptor, PAR-2,
pubmed-meshheading:21686228-Receptors, Histamine H1,
pubmed-meshheading:21686228-Respiratory Mucosa,
pubmed-meshheading:21686228-Signal Transduction,
pubmed-meshheading:21686228-Time Factors,
pubmed-meshheading:21686228-Transfection,
pubmed-meshheading:21686228-Tyrosine,
pubmed-meshheading:21686228-beta Catenin
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pubmed:year |
2011
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pubmed:articleTitle |
H1 and PAR2 receptors enhance delivery of immune-competent cells and molecules by interrupting E-cadherin adhesion in epithelia.
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pubmed:affiliation |
Department of Internal Medicine, University of Iowa Carver College of Medicine, Newton Rd., Iowa City, IA 52242, USA. michael-shasby@uiowa.edu
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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