Source:http://linkedlifedata.com/resource/pubmed/id/16054130
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-9-19
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pubmed:abstractText |
We recently described that in the metastasizing rat pancreatic carcinoma line BSp73ASML the cell-cell adhesion molecule EpCAM, CD44 variant isoforms and the tetraspanins D6.1A and CD9 form a complex that is located in glycolipid-enriched membrane microdomains. This complex contains, in addition, an undefined 20 kDa protein. As such complex formation influenced cell-cell adhesion and apoptosis resistance, it became of interest to identify the 20 kDa polypeptide. This 20 kDa protein, which co-precipitated with EpCAM in BSp73ASML lysates, was identified as the tight junction protein claudin-7. Correspondingly, an association between EpCAM and claudin-7 was noted in rat and human tumors and in non-transformed tissues of the gastrointestinal tract. Co-localization of the two molecules was most pronounced at basolateral membranes, but was also observed in tight junctions. Evidence for direct protein-protein interactions between EpCAM and claudin-7 was obtained by co-immunoprecipitation after treatment of tumor cells with a membrane-permeable chemical cross-linker. The complex, which is located in glycolipid-enriched membrane microdomains, is not disrupted by partial cholesterol depletion, but claudin-7 phosphorylation is restricted to the localization in glycolipid-enriched membrane microdomains. This is the first report on an association between EpCAM and claudins in both non-transformed tissues and metastasizing tumor cell lines.
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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, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/CD44v6 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/CLDN7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/EPCAM protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/tumor-associated antigen GA733
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
309
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
345-57
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pubmed:dateRevised |
2011-10-28
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pubmed:meshHeading |
pubmed-meshheading:16054130-Animals,
pubmed-meshheading:16054130-Antigens, CD44,
pubmed-meshheading:16054130-Antigens, Neoplasm,
pubmed-meshheading:16054130-Cell Adhesion,
pubmed-meshheading:16054130-Cell Adhesion Molecules,
pubmed-meshheading:16054130-Cell Line, Tumor,
pubmed-meshheading:16054130-Duodenum,
pubmed-meshheading:16054130-Glycoproteins,
pubmed-meshheading:16054130-Humans,
pubmed-meshheading:16054130-Intestinal Mucosa,
pubmed-meshheading:16054130-Membrane Proteins,
pubmed-meshheading:16054130-Microscopy, Electron,
pubmed-meshheading:16054130-Phosphorylation,
pubmed-meshheading:16054130-Protein Structure, Tertiary,
pubmed-meshheading:16054130-Rats,
pubmed-meshheading:16054130-Tight Junctions
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pubmed:year |
2005
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pubmed:articleTitle |
The cell-cell adhesion molecule EpCAM interacts directly with the tight junction protein claudin-7.
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pubmed:affiliation |
Department of Tumor Progression and Tumor Defense, German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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