spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 22 January 2008
doi: 10.1242/jcs.020800

Journal of Cell Science 121, 458-465 (2008)
Published by The Company of Biologists 2008
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow All Versions of this Article:
jcs.020800v1
121/4/458    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Related articles in JCS
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Delacour, D.
Right arrow Articles by Jacob, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Delacour, D.
Right arrow Articles by Jacob, R.

Research Article

Loss of galectin-3 impairs membrane polarisation of mouse enterocytes in vivo

Delphine Delacour1,*, Annett Koch1,*, Waltraud Ackermann1, Isabelle Eude-Le Parco2, Hans-Peter Elsässer1, Francoise Poirier2 and Ralf Jacob1,{ddagger}

1 Department of Cell Biology and Cell Pathology, Philipps University, D-35037 Marburg, Germany
2 Department of Development, Institut Jacques Monod, CNRS UMR 7592, Universités Paris 6 and Paris 7, Cedex 05 Paris, France

{ddagger} Author for correspondence (e-mail: jacob{at}staff.uni-marburg.de)

Accepted 14 November 2007

Epithelial cells are characterised by distinct apical and basolateral membrane domains that are separated by tight junctions. Establishment and maintenance of this polarity depend on specific gene expression and protein targeting to their correct location. Our former studies, performed with renal epithelial MDCK cells, revealed a new function for galectin-3, a member of a conserved family of lectins. There, galectin-3 is required for intracellular sorting and correct targeting of non-raft-associated glycoproteins to the apical plasma membrane. In the present study, we found transport defects of the intestinal brush border hydrolases lactase-phlorizin hydrolase (LPH) and dipeptidylpeptidase IV (DPPIV) in galectin-3-null mutant mice. We could show that, in enterocytes of wild-type mice, both glycoproteins directly interact with galectin-3 and transit through non-raft-dependent apical transport platforms. Therefore, this genetic analysis provides definitive evidence for the involvement of galectin-3 in protein intracellular trafficking in vivo. Further investigations revealed that gal3-null enterocytes also exhibit striking cytoarchitecture defects, with the presence of numerous and regular protrusions located along basolateral membranes. Moreover, β-actin and villin, two characteristic markers of brush borders, become abnormally distributed along these atypical basolateral membranes in gal3–/– mice. Taken together, our results demonstrate that, in addition to a pivotal role in apical trafficking, galectin-3 also participates in epithelial morphogenesis in mouse enterocytes.

Key words: Apical sorting, Epithelial cells, Galectins, Intestinal hydrolases


Related articles in JCS:

Galectin-3 goes apical

JCS 2008 121: 403. [Full Text]  





© The Company of Biologists Ltd 2008