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Journal of Cell Science, Vol 114, Issue 8 1455-1471, Copyright © 2001 by Company of Biologists

JOURNAL ARTICLES

Differential effect of GalNAc(&agr;)-O-bn on intracellular trafficking in enterocytic HT-29 and Caco-2 cells: correlation with the glycosyltransferase expression pattern

V Gouyer, E Leteurtre, P Delmotte, WF Steelant, MA Krzewinski-Recchi, JP Zanetta, T Lesuffleur, G Trugnan, P Delannoy and G Huet
Unite INSERM 377, place de Verdun, France. huet@lille.inserm.fr

Our previous work has shown that long-term treatment of mucus-secreting HT-29 cells with 1-benzyl-2-acetamido-2-deoxy-(&agr;)-D-galactopyranoside (GalNAc(&agr;)-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 GalNAc(&agr;)-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 GalNAc(&agr;)-O-bn metabolites. We observed a strong inhibition of (&agr;)2,3-sialylation of glycoproteins in HT-29 G(-) cells correlated to the high expression of (&agr;)2,3-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 Gal(&bgr;)1-3GalNAc (T-antigen). In contrast, sialylation was not modified in Caco-2 cells, but a decrease of (&agr;)1,2-fucosylation was observed, in correlation with the high expression of (&agr;)1,2-fucosyltransferases Fuc-TI and Fuc-TII. In conclusion, in HT-29 G(-) cells, GalNAc(&agr;)-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 GalNAc(&agr;)-O-bn metabolites.


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