| pubmed-article:19884339 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C0110116 | lld:lifeskim |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C1819995 | lld:lifeskim |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C0909826 | lld:lifeskim |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:19884339 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:19884339 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19884339 | pubmed:dateCreated | 2009-12-23 | lld:pubmed |
| pubmed-article:19884339 | pubmed:abstractText | The 24-member claudin protein family plays a key role in maintaining the normal structure and function of epithelial tight junctions. Previous studies with fibroblast transfectants and naturally sensitive Caco-2 cells have also implicated certain claudins (e.g., Claudin-4) as receptors for Clostridium perfringens enterotoxin (CPE). The present study first provided evidence that the second extracellular loop (ECL-2) of claudins is specifically important for mediating the host cell binding and cytotoxicity of native CPE. Rat fibroblast transfectants expressing a Claudin-4 chimera, where the natural ECL-2 was replaced by ECL-2 from Claudin-2, exhibited no CPE-induced cytotoxicity. Conversely, CPE bound to, and killed, CPE-treated transfectants expressing a Claudin-2 chimera with a substituted ECL-2 from Claudin-4. Site-directed mutagenesis was then used to alter an ECL-2 residue that invariably aligns as N in claudins known to bind native CPE but as D or S in claudins that cannot bind CPE. Transfectants expressing a Claudin-4(N149D) mutant lost the ability to bind or respond to CPE, while transfectants expressing a Claudin-1 mutant with the corresponding ECL-2 residue changed from D to N acquired CPE binding and sensitivity. Identifying carriage of this N residue in ECL-2 as being important for native CPE binding helps to explain why only certain claudins can serve as CPE receptors. Finally, preincubating CPE with soluble recombinant Claudin-4, or Claudin-4 fragments containing ECL-2 specifically blocked the cytotoxicity on Caco-2 cells. This result opens the possibility of using receptor claudins as therapeutic decoys to ameliorate CPE-mediated intestinal disease. | lld:pubmed |
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| pubmed-article:19884339 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19884339 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19884339 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19884339 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19884339 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19884339 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19884339 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19884339 | pubmed:issn | 1098-5522 | lld:pubmed |
| pubmed-article:19884339 | pubmed:author | pubmed-author:McClaneBruce... | lld:pubmed |
| pubmed-article:19884339 | pubmed:author | pubmed-author:SmedleyJames... | lld:pubmed |
| pubmed-article:19884339 | pubmed:author | pubmed-author:RobertsonSusa... | lld:pubmed |
| pubmed-article:19884339 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19884339 | pubmed:volume | 78 | lld:pubmed |
| pubmed-article:19884339 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19884339 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19884339 | pubmed:pagination | 505-17 | lld:pubmed |
| pubmed-article:19884339 | pubmed:dateRevised | 2011-2-7 | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:meshHeading | pubmed-meshheading:19884339... | lld:pubmed |
| pubmed-article:19884339 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19884339 | pubmed:articleTitle | Identification of a claudin-4 residue important for mediating the host cell binding and action of Clostridium perfringens enterotoxin. | lld:pubmed |
| pubmed-article:19884339 | pubmed:affiliation | University of Pittsburgh School of Medicine, E1240 BSTWR, Pittsburgh, PA 15261, USA. | lld:pubmed |
| pubmed-article:19884339 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19884339 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:1364 | entrezgene:pubmed | pubmed-article:19884339 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19884339 | lld:entrezgene |
