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

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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; Smith, David F; Cummings, Richard D.

In: Journal of Biological Chemistry, Vol. 283, No. 15, 2008, p. 10109-10123.

Research output: Contribution to journalArticle

Harvard

Stowell, SR, Arthur, CM, Mehta, P, Slanina, KA, Blixt, O, Leffler, H, Smith, DF & Cummings, RD 2008, 'Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens', Journal of Biological Chemistry, vol. 283, no. 15, pp. 10109-10123. https://doi.org/10.1074/jbc.M709545200

APA

Stowell, S. R., Arthur, C. M., Mehta, P., Slanina, K. A., Blixt, O., Leffler, H., Smith, D. F., & Cummings, R. D. (2008). Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens. Journal of Biological Chemistry, 283(15), 10109-10123. https://doi.org/10.1074/jbc.M709545200

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MLA

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Author

Stowell, Sean R ; Arthur, Connie M ; Mehta, Padmaja ; Slanina, Kristen A ; Blixt, Ola ; Leffler, Hakon ; Smith, David F ; Cummings, Richard D. / Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens. In: Journal of Biological Chemistry. 2008 ; Vol. 283, No. 15. pp. 10109-10123.

RIS

TY - JOUR

T1 - Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens

AU - Stowell, Sean R

AU - Arthur, Connie M

AU - Mehta, Padmaja

AU - Slanina, Kristen A

AU - Blixt, Ola

AU - Leffler, Hakon

AU - Smith, David F

AU - Cummings, Richard D

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M709545200

DO - 10.1074/jbc.M709545200

M3 - Article

VL - 283

SP - 10109

EP - 10123

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 15

ER -