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Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens

Stowell, Sean R; Arthur, Connie M; Mehta, Padmaja; Slanina, Kristen A; Blixt, Ola; Leffler, Hakon LU ; Smith, David F and Cummings, Richard D (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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
283
issue
15
pages
10109 - 10123
publisher
ASBMB
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
2008-08-14 15:56:13
date last changed
2017-10-29 03:25:39
@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    = {ASBMB},
  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},
  volume       = {283},
  year         = {2008},
}