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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 |
1994-1-25
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pubmed:abstractText |
The aim of the present study was to elucidate the mechanism responsible for the high mannose glycoprotein instability in undifferentiated HT-29 cells (a human colon cancer cell line) reported previously. The results presented here are consistent with lysosomal degradation of these molecular species. In addition inhibitors of the autophagic-lysosomal degradative pathway (3-methyladenine, okadaic acid and asparagine) dramatically block the degradation of proteins and N-linked glycoproteins in undifferentiated HT-29 cells. The main conclusions of this work are: 1- the autophagic-lysosomal pathway is responsible for the high mannose glycoprotein degradation in undifferentiated HT-29 cells; 2- this degradative pathway exists in differentiated cells but is greatly reduced (3.5-4 fold); 3- the HT-29 cell line is a new model to investigate the molecular regulation of autophagy.
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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/3-methyladenine,
http://linkedlifedata.com/resource/pubmed/chemical/Adenine,
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Carcinogens,
http://linkedlifedata.com/resource/pubmed/chemical/Chloroquine,
http://linkedlifedata.com/resource/pubmed/chemical/Ethers, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
197
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
805-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8267619-Adenine,
pubmed-meshheading:8267619-Adenocarcinoma,
pubmed-meshheading:8267619-Asparagine,
pubmed-meshheading:8267619-Autophagy,
pubmed-meshheading:8267619-Carbon Radioisotopes,
pubmed-meshheading:8267619-Carcinogens,
pubmed-meshheading:8267619-Cell Differentiation,
pubmed-meshheading:8267619-Cell Line,
pubmed-meshheading:8267619-Chloroquine,
pubmed-meshheading:8267619-Colonic Neoplasms,
pubmed-meshheading:8267619-Ethers, Cyclic,
pubmed-meshheading:8267619-Glycoproteins,
pubmed-meshheading:8267619-Humans,
pubmed-meshheading:8267619-Kinetics,
pubmed-meshheading:8267619-Leucine,
pubmed-meshheading:8267619-Lysosomes,
pubmed-meshheading:8267619-Mannose,
pubmed-meshheading:8267619-Okadaic Acid,
pubmed-meshheading:8267619-Polysaccharides,
pubmed-meshheading:8267619-Tritium,
pubmed-meshheading:8267619-Tumor Cells, Cultured
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pubmed:year |
1993
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pubmed:articleTitle |
Autophagic degradation of N-linked glycoproteins is downregulated in differentiated human colon adenocarcinoma cells.
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pubmed:affiliation |
INSERM U239, Unité de Recherche sur la Biologie et la Physiopathologie des Cellules Digestives, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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