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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1991-5-1
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pubmed:abstractText |
Subclones of the HT29-18 clone, derived from a human adenocarcinoma, are able to acquire an enterocyte-like phenotype depending on the culture conditions. To investigate fluid-phase and receptor-mediated endocytosis in the polarized subclone HT29-18-C1, we established culture conditions that allowed cell growth on permeable supports. HT29-18-C1 monolayers had an electrical resistance of 43 ohms.cm2 and developed a transepithelial potential of about 2 mV. Transferrin receptors were uniformly distributed on the entire cell surface of undifferentiated HT29-18 cells but were located on the basolateral membrane of differentiated cells. Transferrin had a high affinity (Kd = 2.5 x 10(-9) M) for its receptor independent of the state of differentiation. The number of transferrin receptors and the mRNA amounts encoding them were comparable in the undifferentiated and differentiated HT29-18 cells. Transferrin was quickly internalized and recycled back to the cell surface of undifferentiated HT29-18 cells. The same phenomenon also occurred in differentiated HT29-18 cells, but the receptors were limited to the basolateral membrane. In the presence of ammonium chloride, the process was slower but remained polarized. Fluid-phase uptake was also investigated with horseradish peroxidase (HRP) in differentiated HT29-18 C1 cells. HRP that was internalized in 1 hour from a given membrane domain preferentially recycled back to the same membrane domain. No significant accumulation of the enzyme in the late endosomes and lysosomes of the differentiated HT29-18-C1 cells was observed.
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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/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Horseradish Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1043-4674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
875-86
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2078556-Adenocarcinoma,
pubmed-meshheading:2078556-Cell Differentiation,
pubmed-meshheading:2078556-Clone Cells,
pubmed-meshheading:2078556-Colonic Neoplasms,
pubmed-meshheading:2078556-Electric Conductivity,
pubmed-meshheading:2078556-Endocytosis,
pubmed-meshheading:2078556-Glucose,
pubmed-meshheading:2078556-Horseradish Peroxidase,
pubmed-meshheading:2078556-Humans,
pubmed-meshheading:2078556-Neoplasm Proteins,
pubmed-meshheading:2078556-Receptors, Transferrin,
pubmed-meshheading:2078556-Transferrin,
pubmed-meshheading:2078556-Tumor Cells, Cultured
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pubmed:year |
1990
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pubmed:articleTitle |
Establishment of polarized endocytosis in differentiable intestinal HT29-18 subclones.
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pubmed:affiliation |
Département de Biologie Moléculaire, URA CNRS 1149, Institut Pasteur, Paris, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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