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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2004-9-7
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pubmed:abstractText |
We have characterized the modulation of cell-cell adhesion and the structure of adherens junctions in the human colon adenocarcinoma HT-29 cell line that differentiates into enterocytes after glucose substitution for galactose in the medium. We demonstrate that differentiated cells (HT-29 Gal) rapidly established E-cadherin-mediated interactions in aggregation assays. This effect is not due to an increase in E-cadherin expression during this early stage of cell differentiation, but rather results from the maturation of preexisting adherens junctions. These junctions are characterized by the redistribution of E-cadherin to the basolateral membrane and its co-localization with the actin cytoskeleton. Subcellular fractionation studies indicate that actin-associated E-cadherins bind beta-catenin and p120ctn. Furthermore, the p120ctn/E-cadherin association is upregulated. These data reveal a cooperative interaction between p120ctn and E-cadherin that corresponds to mature functional adherens junctions able to initiate tight cell-cell adhesion required for epithelium architecture and further affirm the gatekeeper role of p120ctn.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Catenins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/delta catenin
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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 |
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pubmed:copyrightInfo |
Copyright 2004 Elsevier Inc.
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
299
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
498-510
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15350547-Actins,
pubmed-meshheading:15350547-Adherens Junctions,
pubmed-meshheading:15350547-Cadherins,
pubmed-meshheading:15350547-Catenins,
pubmed-meshheading:15350547-Cell Adhesion,
pubmed-meshheading:15350547-Cell Adhesion Molecules,
pubmed-meshheading:15350547-Cell Communication,
pubmed-meshheading:15350547-Cell Differentiation,
pubmed-meshheading:15350547-Cell Division,
pubmed-meshheading:15350547-Cell Polarity,
pubmed-meshheading:15350547-Cytoskeletal Proteins,
pubmed-meshheading:15350547-Cytoskeleton,
pubmed-meshheading:15350547-Enterocytes,
pubmed-meshheading:15350547-Glucose,
pubmed-meshheading:15350547-HT29 Cells,
pubmed-meshheading:15350547-Humans,
pubmed-meshheading:15350547-Intercellular Junctions,
pubmed-meshheading:15350547-Phosphoproteins,
pubmed-meshheading:15350547-Subcellular Fractions,
pubmed-meshheading:15350547-Trans-Activators,
pubmed-meshheading:15350547-Tumor Cells, Cultured,
pubmed-meshheading:15350547-beta Catenin
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pubmed:year |
2004
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pubmed:articleTitle |
Early enterocytic differentiation of HT-29 cells: biochemical changes and strength increases of adherens junctions.
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pubmed:affiliation |
Laboratoire d'Etude de la Différenciation et de l'Adhérence Cellulaires, UMR UJF/CNRS 5538, Institut Albert Bonniot, Faculté de Médecine de Grenoble, 38706 La Tronche Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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