Skip Navigation



Glycobiology Advance Access published online on March 15, 2006
Glycobiology, doi:10.1093/glycob/cwj102
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow Supplemental Data
Right arrow All Versions of this Article:
16/6/524    most recent
cwj102v1
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 Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Wu, A. M.
Right arrow Articles by Gabius, H.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wu, A. M.
Right arrow Articles by Gabius, H.-J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received December 25, 2005
Revised March 10, 2006
Accepted March 12, 2006

Article

Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine-specificity and the effect of naturally clustered ligand presentation

Albert M. Wu 1 *, Tanuja Singh 1, June H. Wu 2, Martin Lensch 3, Sabine André 3, and Hans-Joachim Gabius 3

1 Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, Chang-Gung University, Kwei-san, Tao-yuan, 333, Taiwan
2 Department of Microbiology and Immunology, Chang-Gung University, Kwei-san, Tao-yuan, 333, Taiwan
3 Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstrasse 13, D-80539 Munich, Germany

* To whom correspondence should be addressed.
Albert M. Wu, E-mail: amwu{at}mail.cgu.edu.tw


  Abstract

Cell surface glycans are functional docking sites for tissue lectins such as the members of the galectin family. This interaction triggers a wide variety of responses; hence, there is a keen interest in defining its structural features. Toward this aim, we have used enzyme-linked lectinosorbent and inhibition assays with the proto-type rat galectin-5 and panels of free saccharides and glycoconjugates. Among 45 natural glycans tested for lectin binding, galectin-5 reacted best with glycoproteins (gps) presenting a high density of Gal{beta}1-3/4GlcNAc (I/II) and multi-antennary N-glycans with II termini. Their reactivities, on a nanogram basis, were up to 4.3x102, 3.2x102, 2.5x102 and 1.7x104 times higher than monomeric Gal{beta}1-3/4GlcNAc (I/II), triantennary-II (Tri-II) and Gal, respectively. Galectin-5 also bound well to several blood-group type B (Gal{alpha}1-3Gal)- and A (GalNAc{alpha}1-3Gal)-containing gps. It reacted weakly or not at all with tumor-associated Tn (GalNAc{alpha}1-Ser/Thr) and sialylated gps. Among the mono-, di- and oligosaccharides and mammalian glycoconjugates tested, blood group B-active II (Gal{alpha}1-3Gal{beta}1-4GlcNAc), B-active II{beta}1-3L (Gal{alpha}1-3Gal{beta}1-4GlcNAc {beta}1-3Gal{beta}1-4Glc) and Tri-II were the best. It is concluded that: (a) Gal{beta}1-3/4GlcNAc and other Gal{beta}1-related oligosaccharides with {alpha}1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (b) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted {beta}-galactoside, especially with {alpha}-anomeric extension at the non-reducing end, e. g. human blood group B-active II and B-active II{beta}1-3L; (c) the preference within {beta}-anomeric positioning is Gal{beta}1-4 ≥ Gal{beta}1-3 > Gal{beta}1-6; (d) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding. These results are an important step in the systematic comparison of ligand selection in this family of adhesion/growth-regulatory effectors with potential for medical applications.

Keywords: blood group/glycoprotein/lectin/N-glycans/O-glycans/sialylation.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Rheumatology (Oxford)Home page
A. Alavi and J. S. Axford
Sweet and sour: the impact of sugars on disease
Rheumatology, June 1, 2008; 47(6): 760 - 770.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
E. M Rapoport, S. Andre, O. V Kurmyshkina, T. V Pochechueva, V. V Severov, G. V Pazynina, H.-J Gabius, and N. V Bovin
Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: A case study on galectins-1 and -3 and the impact of assay setting
Glycobiology, April 1, 2008; 18(4): 315 - 324.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
A. M. Wu, T. Singh, J.-H. Liu, M. Krzeminski, R. Russwurm, H.-C. Siebert, A. M.J.J. Bonvin, S. Andre, and H.-J. Gabius
Activity-structure correlations in divergent lectin evolution: fine specificity of chicken galectin CG-14 and computational analysis of flexible ligand docking for CG-14 and the closely related CG-16
Glycobiology, February 1, 2007; 17(2): 165 - 184.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.