Source:http://linkedlifedata.com/resource/pubmed/id/16204054
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
2005-10-5
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pubmed:abstractText |
The E-cadherin/catenin system acts as an invasion suppressor of epithelial malignancies. This invasion suppressive activity seems be mediated not only by the cell adhesive activity of E-cadherin but by other undetermined signaling pathways elicited by beta-catenin. In fact, cancer cells that have infiltrated the stroma reduce the expression of E-cadherin and accumulate beta-catenin. We attempted to identify the alternative partner proteins that make complexes with beta-catenin in the absence of E-cadherin. An approximately 100-kDa protein was constantly coimmunoprecipitated with beta-catenin from SW480 colorectal cancer cells, which lack the expression of E-cadherin, and was identified as actinin-4 by mass spectrometry. Transfection of E-cadherin cDNA suppressed the association between beta-catenin and actinin-4. Inhibition of E-cadherin by RNA interference transferred the beta-catenin and actinin-4 proteins into the membrane protrusions of DLD-1 cells. Immunofluorescence histochemistry of clinical colorectal cancer specimens showed that the beta-catenin and actinin-4 proteins were colocalized in colorectal cancer cells infiltrating the stroma. We reported previously that overexpression of actinin-4 induces cell motility and specifically promotes lymph node metastasis by colorectal cancer. The association between beta-catenin and actinin-4 and its regulation by E-cadherin may represent a novel molecular link connecting cell adhesion and motility. Shutting down the signals mediating this association may be worth considering as a therapeutic approach to cancer invasion and metastasis.
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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/ACTN4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Actinin,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0008-5472
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8836-45
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16204054-Actinin,
pubmed-meshheading:16204054-Actins,
pubmed-meshheading:16204054-Amino Acid Sequence,
pubmed-meshheading:16204054-Cadherins,
pubmed-meshheading:16204054-Cell Line, Tumor,
pubmed-meshheading:16204054-Cell Movement,
pubmed-meshheading:16204054-Cell Nucleus,
pubmed-meshheading:16204054-Colorectal Neoplasms,
pubmed-meshheading:16204054-Humans,
pubmed-meshheading:16204054-Laminin,
pubmed-meshheading:16204054-Microfilament Proteins,
pubmed-meshheading:16204054-Molecular Sequence Data,
pubmed-meshheading:16204054-Neoplasm Invasiveness,
pubmed-meshheading:16204054-Neoplasm Metastasis,
pubmed-meshheading:16204054-Pancreatic Neoplasms,
pubmed-meshheading:16204054-Stromal Cells,
pubmed-meshheading:16204054-Transfection,
pubmed-meshheading:16204054-beta Catenin
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pubmed:year |
2005
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pubmed:articleTitle |
E-cadherin regulates the association between beta-catenin and actinin-4.
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pubmed:affiliation |
Chemotherapy Division and Cancer Proteomics Project, National Cancer Center Research Institute, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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