Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens
(2008) In Journal of Biological Chemistry 283(15). p.10109-10123- Abstract
- Human galectins have functionally divergent roles, although most of the members of the galectin family bind weakly to the simple disaccharide lactose (Galss1-4Glc). To assess galectin-glycan interactions in more detail, we explored the binding of several important galectins (Gal-1, Gal-2, and Gal-3) on a glycan microarray containing hundreds of structurally diverse glycans. All three galectins exhibited unique glycan binding characteristics. Only Gal-1 and Gal-2 bound complex-type N-glycans and extended core 1 O-glycans with high affinity, while Gal-2 and Gal-3, but not Gal-1, bound A and B blood group antigens. Gal-2 failed to recognize any sialylated glycans regardless of linkage, whereas Gal-1 and Gal-3 bound a2-3, but not a2-6... (More)
- Human galectins have functionally divergent roles, although most of the members of the galectin family bind weakly to the simple disaccharide lactose (Galss1-4Glc). To assess galectin-glycan interactions in more detail, we explored the binding of several important galectins (Gal-1, Gal-2, and Gal-3) on a glycan microarray containing hundreds of structurally diverse glycans. All three galectins exhibited unique glycan binding characteristics. Only Gal-1 and Gal-2 bound complex-type N-glycans and extended core 1 O-glycans with high affinity, while Gal-2 and Gal-3, but not Gal-1, bound A and B blood group antigens. Gal-2 failed to recognize any sialylated glycans regardless of linkage, whereas Gal-1 and Gal-3 bound a2-3, but not a2-6 sialylated glycans. All galectins showed higher binding to sulfated glycans relative to unsulfated ones. Each galectin exhibited higher binding for glycans with poly-N-acetyllactosamine (PL) sequences (Galss1-4GlcNAc)n when compared to N-acetyllactosamine (Galss1-4GlcNAc) in the microarray. However, only Gal-3 preferred PL when assessed by solution-based surface plasmon resonance. Removal of the terminal galactose residue in PL abrogated its recognition by Gal-1 and Gal-2 while having no substantial effect on Gal-3 recognition, demonstrating that Gal-3 recognizes internal N-acetyllactosamine units. These results provide novel insights into the functional constraints of glycan recognition by each galectin and underscore the basis for differences in biological activity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1144522
- author
- Stowell, Sean R ; Arthur, Connie M ; Mehta, Padmaja ; Slanina, Kristen A ; Blixt, Ola ; Leffler, Hakon LU ; Smith, David F and Cummings, Richard D
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 283
- issue
- 15
- pages
- 10109 - 10123
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:18216021
- wos:000254671600065
- scopus:44049104824
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M709545200
- language
- English
- LU publication?
- yes
- id
- 53d47594-1513-422a-a0c8-a17c06728c0f (old id 1144522)
- date added to LUP
- 2016-04-01 11:38:54
- date last changed
- 2022-04-28 17:55:14
@article{53d47594-1513-422a-a0c8-a17c06728c0f,
abstract = {{Human galectins have functionally divergent roles, although most of the members of the galectin family bind weakly to the simple disaccharide lactose (Galss1-4Glc). To assess galectin-glycan interactions in more detail, we explored the binding of several important galectins (Gal-1, Gal-2, and Gal-3) on a glycan microarray containing hundreds of structurally diverse glycans. All three galectins exhibited unique glycan binding characteristics. Only Gal-1 and Gal-2 bound complex-type N-glycans and extended core 1 O-glycans with high affinity, while Gal-2 and Gal-3, but not Gal-1, bound A and B blood group antigens. Gal-2 failed to recognize any sialylated glycans regardless of linkage, whereas Gal-1 and Gal-3 bound a2-3, but not a2-6 sialylated glycans. All galectins showed higher binding to sulfated glycans relative to unsulfated ones. Each galectin exhibited higher binding for glycans with poly-N-acetyllactosamine (PL) sequences (Galss1-4GlcNAc)n when compared to N-acetyllactosamine (Galss1-4GlcNAc) in the microarray. However, only Gal-3 preferred PL when assessed by solution-based surface plasmon resonance. Removal of the terminal galactose residue in PL abrogated its recognition by Gal-1 and Gal-2 while having no substantial effect on Gal-3 recognition, demonstrating that Gal-3 recognizes internal N-acetyllactosamine units. These results provide novel insights into the functional constraints of glycan recognition by each galectin and underscore the basis for differences in biological activity.}},
author = {{Stowell, Sean R and Arthur, Connie M and Mehta, Padmaja and Slanina, Kristen A and Blixt, Ola and Leffler, Hakon and Smith, David F and Cummings, Richard D}},
issn = {{1083-351X}},
language = {{eng}},
number = {{15}},
pages = {{10109--10123}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens}},
url = {{http://dx.doi.org/10.1074/jbc.M709545200}},
doi = {{10.1074/jbc.M709545200}},
volume = {{283}},
year = {{2008}},
}