Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking : Biological Chemistry Jump to ContentJump to Main Navigation
Show Summary Details

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

249,00 € / $374.00 / £187.00*

See all formats and pricing



Select Volume and Issue
Loading journal volume and issue information...

Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking

Willy Morelle1 / Laurence Stechly2, 3 / Sabine André4 / Isabelle Van Seuningen2 / Nicole Porchet2, 3 / Hans-Joachim Gabius4 / Jean-Claude Michalski1 / Guillemette Huet2, 3

1UMR CNRS 8576, Unité de Glycobiologie Structurale et Fonctionnelle, IFR 147, F-59655 Villeneuve d'Ascq, France

2Centre de Recherche Jean-Pierre Aubert, INSERM U837, CHRU, F-59045 Lille cedex, France

3Centre de Biologie Pathologie Pierre Degand, CHRU, F-59037 Lille cedex, France

4Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximililans University Munich, D-80539 Munich, Germany

Corresponding author

Citation Information: Biological Chemistry. Volume 390, Issue 7, Pages 529–544, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.075, May 2009

Publication History

Published Online:


We have previously reported that galectin-4, a tandem repeat-type galectin, regulates the raft-dependent delivery of glycoproteins to the apical brush border membrane of enterocyte-like HT-29 cells. N-Acetyllactos-amine-containing glycans, known as galectin ligands, were found enriched in detergent-resistant membranes. Here, we analyzed the potential contribution of N- and/or O-glycans in this mechanism. Structural studies were carried out on the brush border membrane-enriched fraction using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and nano-ESI-QTOF-MS/MS. The pattern of N-glycans was very heterogeneous, with the presence of high mannose- and hybrid-type glycans as well as a multitude of complex-type glycans. In contrast, the pattern of O-glycans was very simple with the presence of two major core type 1 O-glycans, sialylated and bisialylated T-antigen structures [Neu5Acα2–3Galβ1–3GalNAc-ol and Neu5Acα2– 3Galβ1–3(Neu5Acα2–6)GalNAc-ol]. Thus, N-glycans rather than O-glycans contain the N-acetyllactosamine recognition signals for the lipid raft-based galectin-4-dependent apical delivery. In the presence of 1-deoxymannojirimycin, a drug which inhibits the generation of hybrid-type or complex type N-glycans, the extensively O-glycosylated mucin-like MUC1 glycoprotein was not delivered to the apical brush border but accumulated inside the cells. Altogether, our data demonstrate the crucial role of complex N-glycans in the galectin-4-dependent delivery of glycoproteins to the apical brush border membrane of enterocytic HT-29 cells.

Keywords: brush border; detergent-resistant membrane (DRM); galectin-4; glycosphingolipids; N-glycans; O-glycans

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

Khuchtumur Bum-Erdene, Hakon Leffler, Ulf J. Nilsson, and Helen Blanchard
Scientific Reports, 2016, Volume 6, Page 20289
Hans-Joachim Gabius, Herbert Kaltner, Jürgen Kopitz, and Sabine André
Trends in Biochemical Sciences, 2015, Volume 40, Number 7, Page 360
José Abad-Rodríguez and Natalia Díez-Revuelta
Trends in Biochemical Sciences, 2015, Volume 40, Number 7, Page 385
H. Kaltner, A.-S. Raschta, J. C. Manning, and H.-J. Gabius
Glycobiology, 2013, Volume 23, Number 10, Page 1152
Silvia Velasco, Natalia Díez-Revuelta, Teresa Hernández-Iglesias, Herbert Kaltner, Sabine André, Hans-Joachim Gabius, and José Abad-Rodríguez
Journal of Neurochemistry, 2013, Volume 125, Number 1, Page 49
O. A. Vokhmyanina, E. M. Rapoport, S. Andre, V. V. Severov, I. Ryzhov, G. V. Pazynina, E. Korchagina, H.-J. Gabius, and N. V. Bovin
Glycobiology, 2012, Volume 22, Number 9, Page 1207
Johannes Gebert, Matthias Kloor, Jennifer Lee, Michaela Lohr, Sabine André, Rudolf Wagner, Juergen Kopitz, and Hans-Joachim Gabius
Histochemistry and Cell Biology, 2012, Volume 138, Number 2, Page 339
Robert W. Ledeen, Gusheng Wu, Sabine André, David Bleich, Guillemette Huet, Herbert Kaltner, Jürgen Kopitz, and Hans-Joachim Gabius
Annals of the New York Academy of Sciences, 2012, Volume 1253, Number 1, Page 206
Mirjana Stancic, Davor Slijepcevic, Anita Nomden, Michel J. Vos, Jenny C. de Jonge, Arend H. Sikkema, Hans-J. Gabius, Dick Hoekstra, and Wia Baron
Glia, 2012, Volume 60, Number 6, Page 919
C. Barres, L. Blanc, P. Bette-Bobillo, S. Andre, R. Mamoun, H.-J. Gabius, and M. Vidal
Blood, 2010, Volume 115, Number 3, Page 696
Sabine André, Dilip V. Jarikote, Dandan Yan, Lisa Vincenz, Guan-Nan Wang, Herbert Kaltner, Paul V. Murphy, and Hans-Joachim Gabius
Bioorganic & Medicinal Chemistry Letters, 2012, Volume 22, Number 1, Page 313
Bianca S. Batista, William S. Eng, Kanoelani T. Pilobello, Karen D. Hendricks-Muñoz, and Lara K. Mahal
Journal of Proteome Research, 2011, Volume 10, Number 10, Page 4624
Antonia Göhler, Sabine André, Herbert Kaltner, Markus Sauer, Hans-Joachim Gabius, and Sören Doose
Biophysical Journal, 2010, Volume 98, Number 12, Page 3044
Felix A. Habermann, Sabine André, Herbert Kaltner, Dieter Kübler, Fred Sinowatz, and Hans-Joachim Gabius
Histochemistry and Cell Biology, 2011, Volume 135, Number 6, Page 539
Carly Willenborg and Rytis Prekeris
Bioscience Reports, 2011, Volume 31, Number 4, Page 245
Biological Chemistry, 2009, Volume 390, Number 7

Comments (0)

Please log in or register to comment.