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Journal of Histochemistry and Cytochemistry, Vol. 51, 349-361, March 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Induction of a Storage Phenotype and Abnormal Intracellular Localization of Apical Glycoproteins Are Two Independent Responses to GalNAc{alpha}-O-bn

Emmanuelle Leteurtrea,b, Valérie Gouyera, Delphine Delacoura, Brigitte Hémona, Alexandre Ponsc, Colette Richeta, Jean-Pierre Zanettac, and Guillemette Hueta
a Unité INSERM 560, Villeneuve d'Ascq, France
b Service d'Anatomie Pathologique, Villeneuve d'Ascq, France
c Lille, France, and Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS 8576, Laboratoire de Chimie Biologique, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France

Correspondence to: Guillemette Huet, Unité INSERM 560, Place de Verdun, 59045 Lille cedex, France. E-mail: huet@lille.inserm.fr

Our previous studies on an inhibitor of O-glycosylation of glycoproteins, GalNAc{alpha}-O-bn, in the model of enterocytic HT-29 cells, have shown at the cellular level an alteration of the normal localization of apical glycoproteins, and at the biochemical level an in situ synthesis and storage of sialylated GalNAc{alpha}-O-bn oligosaccharides. The purpose of this study was to examine if a relation existed between these two events, using different cell lines. Intracellular storage of GalNAc{alpha}-O-bn metabolites occurred in HT-29 and CAPAN-1 cells but not in Caco-2 cells. On the other hand, an accumulation of endosomal/lysosomal compartments was observed in HT-29 and CAPAN-1 cells but not in Caco-2 cells. These data focused on a GalNAc{alpha}-O-bn-derived storage phenotype in HT-29 and CAPAN-1 cells. The apical membrane glycoproteins MUC1 and CEA showed an abnormal localization inside intracytoplasmic vesicles in HT-29 cells, whereas they kept their normal localization in Caco-2 and CAPAN-1 cells. Studies on the glycosylation of these apical glycoproteins showed that GalNAc{alpha}-O-bn inhibited the glycosylation in a cell-specific manner. The alteration in the apical targeting of glycoproteins, and the appearance of a GalNAc{alpha}-O-bn-derived storage phenotype are two independent and cell type-specific events. The former depends on the inhibition pattern of the glycosylation of endogenous glycoproteins, whereas the latter is connected to the intracellular accumulation of GalNAc{alpha}-O-bn metabolites.

(J Histochem Cytochem 51:349–361, 2003)

Key Words: glycoproteins, inhibitor, GalNAc{alpha}-O-bn, apical membranes, glycosylation


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