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rdf:type |
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lifeskim:mentions |
umls-concept:C0013081,
umls-concept:C0040649,
umls-concept:C0042172,
umls-concept:C0105770,
umls-concept:C0181586,
umls-concept:C0205217,
umls-concept:C0242275,
umls-concept:C0379710,
umls-concept:C0441655,
umls-concept:C0542341,
umls-concept:C1269955,
umls-concept:C1517945,
umls-concept:C2349975
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pubmed:issue |
6
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pubmed:dateCreated |
2004-1-6
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pubmed:abstractText |
EGF receptor (EGFR) overexpression correlates with metastasis in a variety of carcinomas, but the underlying mechanisms are poorly understood. We demonstrated that EGF disrupted cell-cell adhesion and caused epithelial-to-mesenchymal transition (EMT) in human tumor cells overexpressing EGFR, and also induced caveolin-dependent endocytosis of E-cadherin, a cell-cell adhesion protein. Chronic EGF treatment resulted in transcriptional downregulation of caveolin-1 and induction of the transcriptional repressor Snail, correlating with downregulation of E-cadherin expression. Caveolin-1 downregulation enhanced beta-catenin-TCF/LEF-1 transcriptional activity in a GSK-3beta-independent manner. Antisense RNA-mediated reduction of caveolin-1 expression in EGFR-overexpressing tumor cells recapitulated these EGF-induced effects and enhanced invasion into collagen gels. We propose that EGF-induced negative regulation of caveolin-1 plays a central role in the complex cellular changes leading to metastasis.
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pubmed:grant |
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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/CAV1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/glycogen synthase kinase 3 beta,
http://linkedlifedata.com/resource/pubmed/chemical/snail family transcription factors
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1535-6108
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
499-515
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:14706341-Cadherins,
pubmed-meshheading:14706341-Caveolae,
pubmed-meshheading:14706341-Caveolin 1,
pubmed-meshheading:14706341-Caveolins,
pubmed-meshheading:14706341-Cell Adhesion,
pubmed-meshheading:14706341-Cell Movement,
pubmed-meshheading:14706341-Cell Nucleus,
pubmed-meshheading:14706341-Cytoskeletal Proteins,
pubmed-meshheading:14706341-DNA-Binding Proteins,
pubmed-meshheading:14706341-Down-Regulation,
pubmed-meshheading:14706341-Endocytosis,
pubmed-meshheading:14706341-Epidermal Growth Factor,
pubmed-meshheading:14706341-Glycogen Synthase Kinase 3,
pubmed-meshheading:14706341-Humans,
pubmed-meshheading:14706341-Intercellular Junctions,
pubmed-meshheading:14706341-Neoplasm Metastasis,
pubmed-meshheading:14706341-RNA, Antisense,
pubmed-meshheading:14706341-Receptor, Epidermal Growth Factor,
pubmed-meshheading:14706341-Signal Transduction,
pubmed-meshheading:14706341-Trans-Activators,
pubmed-meshheading:14706341-Transcription Factors,
pubmed-meshheading:14706341-Transcriptional Activation,
pubmed-meshheading:14706341-Tumor Cells, Cultured,
pubmed-meshheading:14706341-beta Catenin
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pubmed:year |
2003
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pubmed:articleTitle |
Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of beta-catenin, and enhanced tumor cell invasion.
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pubmed:affiliation |
Molecular and Cell Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA. zhiminlu@mdanderson.org
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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