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Glycobiology Advance Access published online on November 29, 2005
Glycobiology, doi:10.1093/glycob/cwj063
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org.
Received August 18, 2005
Revised November 10, 2005
Accepted November 15, 2005

Article

Complex N-glycans are the Major Ligands for Galectin-1, Galectin-3 and Galectin-8 on Chinese Hamster Ovary Cells

Santosh Kumar Patnaik 1, Barry Potvin 1, Susanne Carlsson 2, David Sturm 1, Hakon Leffler 2, and Pamela Stanley 1 *

1 Department of Cell Biology, Albert Einstein College of Medicine, New York, NY 10461, USA
2 Section MIG (Microbiology, Immunology, Glycobiology), Institute of Laboratory Medicine, Lund University, POB 124, SE-221 00, Lund, Sweden

* To whom correspondence should be addressed.
Pamela Stanley, E-mail: stanley{at}aecom.yu.edu


  Abstract

Galectins are implicated in a large variety of biological functions, many of which depend on their carbohydrate binding ability. Fifteen members of the family have been identified in verteberates based on binding to galactose that is mediated by one or two, evolutionarily conserved, carbohydrate recognition domains (CRD). Variations in glycan structures expressed on glycoconjugates at the cell surface may therefore affect galectin binding and functions. In order to identify roles for different glycans in the binding of the three types of mammalian galectins to cells, we performed fluorescence cytometry at 4 °C with recombinant rat galectin-1, human galectin-3, and three forms of human galectin-8, to Chinese hamster ovary (CHO) cells and twelve different CHO glycosylation mutants. All galectin species bound to parent CHO cells and binding was inhibited >90% by 0.2 M lactose. Galectin-8 isoforms with either a long or a short inter-CRD linker bound similarly to CHO cells. However, a truncated form of galectin-8 containing only the N-terminal CRD bound only weakly to CHO cells and the C-terminal galectin-8 CRD exhibited extremely low binding. Binding of the galectins to the different CHO glycosylation mutants revealed that complex N-glycans are the major ligands for each galectin except the N-terminal CRD of galectins-8, and also identified some fine differences in glycan recognition. Interestingly, increased binding of galectin-1 at 4 °C correlated with increased propidium iodide uptake, while galectin-3 or galectin-8 binding did not induce permeability to propidium iodide. The CHO glycosylation mutants with various repertoires of cell surface glycans are a useful tool for investigating galectin-cell interactions as they present complex and simple glycans in a natural mixture of multivalent protein and lipid glycoconjugates anchored in a cell membrane.

Keywords: Glycan recognition/CHO/Galectin/Glycosylation mutants/Lectin.
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