The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity.

@article{Ideo2003TheNC,
  title={The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity.},
  author={Hiroko Ideo and Akira Seko and Ineo Ishizuka and Katsuko Yamashita},
  journal={Glycobiology},
  year={2003},
  volume={13 10},
  pages={
          713-23
        }
}
Galectin-8 is a member of the galectin family and has two tandem repeated carbohydrate recognition domains (CRDs). We determined the binding specificities of galectin-8 and its two CRDs for oligosaccharides and glycosphingolipids using ELISA and surface plasmon resonance assays. Galectin-8 had much higher affinity for 3'-O-sulfated or 3'-O-sialylated lactose and a Lewis x-containing glycan than for oligosaccharides terminating in Galbeta1-->3/4GlcNAc. This specificity was mainly attributed to… Expand
Galectin-8-N-domain Recognition Mechanism for Sialylated and Sulfated Glycans*
TLDR
This study elucidated the crystal structures of the human galectin-8-N-domain (-8N) in the absence or presence of 4 ligands and found that Arg45, Gln47, Arg59, and the long loop region between the S3 and S4 β-strands are unique to galectIn-8N. Expand
Full-length galectin-8 and separate carbohydrate recognition domains: the whole is greater than the sum of its parts?
TLDR
Several aspects of the structure-function relationship of this protein including crystallographic structures, glycan specificity, cell function and biological roles are covered, with the ultimate goal of understanding the potential role of each CRD in predicting full-length Gal-8 involvement in relevant biological processes. Expand
Affinity of galectin-8 and its carbohydrate recognition domains for ligands in solution and at the cell surface.
TLDR
Galectin-8 binding and signaling at cell surfaces can be explained by combined binding of the two CRDs to low or medium affinity ligand, and their highest affinity ligands, such as sialylated galactosides, are not required. Expand
X-ray Structures of Human Galectin-9 C-terminal Domain in Complexes with a Biantennary Oligosaccharide and Sialyllactose*
TLDR
It is proposed that the wide entrance for ligand binding and the shallow binding site of hG9C are favorable for branched oligosaccharides and that Arg221 is responsible for recognizing sialylated oligosACcharides. Expand
Understanding the Specificity of Human Galectin-8C Domain Interactions with Its Glycan Ligands Based on Molecular Dynamics Simulations
TLDR
Molecular dynamics simulations are able to explain the glycan binding specificities of the Gal-8C-CRD in comparison to those of theGal-8N -CRD and show higher affinity than LacNAc and lactose. Expand
Structural characterisation of human galectin-4 N-terminal carbohydrate recognition domain in complex with glycerol, lactose, 3′-sulfo-lactose, and 2′-fucosyllactose
TLDR
The X-ray structures of human galectin-4 N-terminal CRD (galect in-4N) bound to different saccharide ligands are presented to help decipher its roles under specific conditions. Expand
Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.
TLDR
The comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals and indicates the distinct sets of functionality for these three members of the same subgroup of human gals. Expand
Crystal Structure of the Galectin-9 N-terminal Carbohydrate Recognition Domain from Mus musculus Reveals the Basic Mechanism of Carbohydrate Recognition*
TLDR
The crystal structures of mouse galectin-9 N-terminal CRD (NCRD) in the absence and the presence of four ligand complexes are reported, and the structure of the N-acetyllactosamine dimer shows a unique binding mode of galectIn-9. Expand
Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells.
TLDR
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 galectine-8, and also identified some fine differences in glycan recognition. Expand
Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cells
TLDR
The glycan-binding profile was shown to be influenced by glycocalix of the cell, where the galectin is anchored, and the involvement of cis-glycans in the interaction of cell-anchored galectins with external glycoconjugates is suppose to be involved. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 56 REFERENCES
High-affinity binding of recombinant human galectin-4 to SO3–→3Galβ1→3GalNAc pyranoside
Galectin-4 is a member of galectin family and has two carbohydrate recognition domains. Although galectin-4 has been thought to function in cell adhesion, its precise carbohydrate binding specificityExpand
High-affinity binding of recombinant human galectin-4 to SO(3)(-)-->3Galbeta1-->3GalNAc pyranoside.
TLDR
The results suggest that galectin-4 has a unique carbohydrate binding specificity and interacts with O-linked sulfoglycans. Expand
Structural basis for the recognition of carbohydrates by human galectin-7.
TLDR
This is the first structure of a galectin determined in both free and carbohydrate-bound forms, and shows a fold similar to that of the prototype galectins -1 and -2, but has greater similarity to a related galECTin molecule, Gal-10. Expand
X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution.
TLDR
Comparison with the published structures of galectins-1 and -2 provides an explanation for the differences in carbohydrate-binding specificity shown by galectin-3, and for the fact that it fails to form dimers by analogous CRD-CRD interactions. Expand
Oligosaccharide specificity of galectins: a search by frontal affinity chromatography.
Galectins are widely distributed sugar-binding proteins whose basic specificity for beta-galactosides is conserved by evolutionarily preserved carbohydrate-recognition domains (CRDs). Although theyExpand
Galectin-8
A protein of 35 kDa which has the characteristic properties of galectins (S-type lectins) was cloned from rat liver cDNA expression library. Since names for galectins 1-7 were already assigned, thisExpand
Selective Recognition of Mannose by the Human Eosinophil Charcot-Leyden Crystal Protein (Galectin-10): A Crystallographic Study at 1.8 Å Resolution.
TLDR
Structural studies on the carbohydrate binding properties of the CLC protein are described and the first structure of a carbohydrate in complex with the protein is reported, indicating no affinity for β-galactosides and binds mannose in a manner very different ... Expand
Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units.
TLDR
The N-linked carbohydrate chains of recombinant human erythropoietin expressed in CHO cells were quantitatively released with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F, and subsequently fractionated via FPLC on Mono Q, HPLC on Lichrosorb-NH2 and high-pH anion-exchange chromatography on CarboPac PA1. Expand
N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
TLDR
The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney. Expand
Galectin-1 Is a Major Receptor for Ganglioside GM1, a Product of the Growth-controlling Activity of a Cell Surface Ganglioside Sialidase, on Human Neuroblastoma Cells in Culture*
TLDR
The results open the possibility that the carbohydrate-dependent interaction between ganglioside GM1 and galectin-1 may relay sialidase-dependent alterations in this cell system. Expand
...
1
2
3
4
5
...