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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1990-10-16
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pubmed:abstractText |
The human colon cancer cell line HT-29 remains totally undifferentiated when glucose is present in the culture medium (HT-29 Glc+), while the same cells may undergo typical enterocytic differentiation after reaching confluence when grown in glucose-deprived medium (HT-29 Glc-). Recently, we demonstrated a deficiency in the overall N-glycan processing in confluent undifferentiated cells, whereas differentiated cells follow a classical pattern of N-glycosylation. The main changes in N-glycosylation observed in confluent undifferentiated cells may be summarised as follows: 1) the conversion of high mannose into complex glycopeptides is greatly decreased; 2) this decreased conversion could be a consequence of an accumulation of Man9-8-GlcNAc2-Asn high mannose species. Whether these changes in N-glycan processing appear progressively during cell culture or are already present from the beginning of the culture was investigated in this study by comparing the actual status of N-glycan processing in exponentially growing HT-29 Glc- and HT-29 Glc+ cells. Under these conditions, HT-29 Glc- cells do not exhibit any characteristics of differentiation. The conversion of high mannose into complex glycoproteins is severely reduced in HT-29 Glc+ cells, regardless of the growth phase studied. In contrast, HT-29 Glc- cells display a normal pattern of N-glycan processing in both growth phases. We therefore conclude that N-glycan processing may be used as an early biochemical marker of the enterocytic differentiation process of HT-29 cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0926-5287
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
325-30
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2397029-Cell Differentiation,
pubmed-meshheading:2397029-Cell Division,
pubmed-meshheading:2397029-Colonic Neoplasms,
pubmed-meshheading:2397029-Glucose,
pubmed-meshheading:2397029-Glycosylation,
pubmed-meshheading:2397029-Humans,
pubmed-meshheading:2397029-Intestines,
pubmed-meshheading:2397029-Mannose,
pubmed-meshheading:2397029-Polysaccharides,
pubmed-meshheading:2397029-Proteins,
pubmed-meshheading:2397029-Tumor Cells, Cultured
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pubmed:year |
1990
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pubmed:articleTitle |
N-glycosylation modification of proteins is an early marker of the enterocytic differentiation process of HT-29 cells.
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pubmed:affiliation |
UFR Biomédicale des Saint-Péres, INSERM U180, Unité de Recherches sur la Biologie et Pathologie Moléculaires des Glycoprotéines, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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