Linked Life Data

11282022

Source:http://linkedlifedata.com/resource/pubmed/id/11282022

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 8
pubmed:dateCreated
2001-4-3
pubmed:abstractText
Our previous work has shown that long-term treatment of mucus-secreting HT-29 cells with 1-benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside (GalNAcalpha-O-bn), a competitive inhibitor of O-glycosylation, induced several phenotypic changes, in particular a blockade in the secretion of mucins, which are extensively O-glycosylated glycoproteins. Here, we have analyzed the effects of GalNAcalpha-O-bn upon the intracellular trafficking of basolateral and apical membrane glycoproteins at the cellular and biochemical levels in two types of cells, HT-29 G(-) and Caco-2, differentiated into an enterocyte-like phenotype. In HT-29 G(-) cells, but not in Caco-2 cells, DPP-IV and CD44 failed to be targeted to the apical or basolateral membrane, respectively, and accumulated inside intracytoplasmic vesicles together with GalNAcalpha-O-bn metabolites. We observed a strong inhibition of alpha2,3-sialylation of glycoproteins in HT-29 G(-) cells correlated to the high expression of alpha2,3-sialyltransferases ST3Gal I and ST3Gal IV. In these cells, DPP-IV and CD44 lost the sialic acid residue substituting the O-linked core 1 structure Galbeta1-3GalNAc (T-antigen). In contrast, sialylation was not modified in Caco-2 cells, but a decrease of alpha1,2-fucosylation was observed, in correlation with the high expression of alpha1,2-fucosyltransferases Fuc-TI and Fuc-TII. In conclusion, in HT-29 G(-) cells, GalNAcalpha-O-bn induces a specific cellular phenotype, which is morphologically characterized by the formation of numerous intracellular vesicles, in which are accumulated defectively sialylated O-glycosylproteins originally targeted to basolateral or apical membranes, and GalNAcalpha-O-bn metabolites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1455-71
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11282022-Antigens, CD44, pubmed-meshheading:11282022-Caco-2 Cells, pubmed-meshheading:11282022-Cell Differentiation, pubmed-meshheading:11282022-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, pubmed-meshheading:11282022-Enzyme Activation, pubmed-meshheading:11282022-Epitopes, pubmed-meshheading:11282022-Fucosyltransferases, pubmed-meshheading:11282022-Galactose, pubmed-meshheading:11282022-Gene Expression, pubmed-meshheading:11282022-Glycosylation, pubmed-meshheading:11282022-HT29 Cells, pubmed-meshheading:11282022-Humans, pubmed-meshheading:11282022-Membrane Glycoproteins, pubmed-meshheading:11282022-Monosaccharides, pubmed-meshheading:11282022-Polysaccharides, pubmed-meshheading:11282022-Protein Transport, pubmed-meshheading:11282022-Sialyltransferases, pubmed-meshheading:11282022-Tumor Cells, Cultured
pubmed:year
2001
pubmed:articleTitle
Differential effect of GalNAcalpha-O-bn on intracellular trafficking in enterocytic HT-29 and Caco-2 cells: correlation with the glycosyltransferase expression pattern.
pubmed:affiliation
Unité INSERM 377, place de Verdun, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't