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J. Biol. Chem., Vol. 278, Issue 39, 37799-37809, September 26, 2003

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1-Benzyl-2-acetamido-2-deoxy--D-galactopyranoside Blocks the Apical Biosynthetic Pathway in Polarized HT-29 Cells^*

Delphine Delacour  , Valérie Gouyer  , Emmanuelle Leteurtre , Tounsia Ait-Slimane ¶, Hervé Drobecq ||, Christelle Lenoir ¶, Odile Moreau-Hannedouche , Germain Trugnan ¶ and Guillemette Huet  **

From the Unité INSERM 560, Place de Verdun, 59045 Lille cedex, ^¶Unité INSERM 538, 75571, Paris, and ^||CNRS UMR 8525, Institut de Biologie de Lille, 59019 Lille cedex, France

In previous work we reported that long term treatment of polarized HT-29 cells by 1-benzyl-2-acetamido-2-deoxy--D-galactopyranoside (GalNAc-O-bn) induced undersialylation and intracellular distribution of apical glycoproteins such as dipeptidyl peptidase IV (DPP-IV), and we suggested therefore that sialylation could act as an apical targeting signal. In this work, the apical direct biosynthetic route was studied after transfection of polarized enterocyte-like HT-29 5M12 cloned cells with a murine cDNA coding for a soluble form of DPP-IV, which was secreted into the apical medium. A 24-h treatment of transfected cells by GalNAc-O-bn markedly inhibited the apical secretion and the sialylation of this soluble murine DPP-IV, which became blocked inside the cell. A similar short GalNAc-O-bn treatment also induced an intracellular distribution of both endogenous transmembrane DPP-IV and proteins involved in the regulation of the apical trafficking such as the apical t-SNARE syntaxin-3 and the raft-associated protein annexin XIIIb, whereas the basolateral t-SNARE syntaxin-4 kept its normal localization. These apical membrane proteins moved efficiently from trans-Golgi network to apical carrier vesicles but failed to be transported from carrier vesicles to the apical plasma membrane. Isolation of membrane microdomains showed that GalNAc-O-bn induced the formation of abnormal lipid-rich microdomains in comparison to normal rafts, as shown by their lower buoyant density and their depletion in annexin XIIIb. In conclusion, GalNAc-O-bn blocks the anterograde traffic to the apical surface of polarized HT-29 cells at the transport level or docking/fusion level of carrier vesicles.

Received for publication, June 2, 2003 , and in revised form, July 8, 2003.

^* This work was supported by Association pour la Recherche sur le Cancer Grant 5687. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

^** To whom correspondence should be addressed: Unité INSERM 560, Place de Verdun, 59045 Lille cedex, France. Tel.: 33-3-20-29-88-60; Fax: 33-3-20-53-85-62; E-mail: huet{at}lille.inserm.fr.

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