Oligosaccharide specificity of galectins: a search by frontal affinity chromatography

Hirabayashi, Jun; Hashidate, Tomomi; Arata, Yoichiro; Nishi, Nozomu; Nakamura, Takanori; Hirashima, Mitsuomi; Urashima, Tadasu; Oka, Toshihiko; Futai, Masamitsu; Müller, Werner; Yagi, Fumio; Kasai, Ken‐ichi

doi:10.1016/s0304-4165(02)00311-2

Cited by 849 publications

(801 citation statements)

References 112 publications

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“…Previous in-depth studies of GAL8 showed that its N-CRD is a really unique domain for recognizing sulphated and sialylated sugars 19,28,29 . In our structure, the diphosphate moiety attached to the pentose ring in NAD binds to the sugar-binding site of N-CRD specifically.…”

Section: Discussionmentioning

confidence: 99%

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

et al. 2013

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Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the detailed molecular basis of the interaction between these two receptors remains to be elucidated. Here, we report the biochemical characterization of both NDP52 and galectin-8 as well as the crystal structure of galectin-8 complexed with an NDP52 peptide. The unexpected observation of nicotinamide adenine dinucleotide located at the carbohydrate-binding site expands our knowledge of the sugar-binding specificity of galectin-8. The NDP52-galectin-8 complex structure explains the key determinants for recognition on both receptors and defines a special orientation of N-and C-terminal carbohydrate recognition domains of galectin-8. Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules. These results lay the groundwork for understanding how host cells target bacterial pathogens for autophagy.

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Section: Discussionmentioning

confidence: 99%

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

et al. 2013

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“…Lectin-monosaccharide interactions are relatively weak (dissociation constants ~10 −4 M), with two to five hydrogen bonds complemented by hydrophobic and van der Waals interactions [4,5,7]. Galectins preferentially bind β-galactoside-containing glycans comprised of repeating units of N-acetyllactosamine (Galβ1,4GlcNAc; LacNAc), either as disaccharide units at the termini of complex N-glycans, or as repeating units in a poly-N-acetyllactosamine chain on N-or O-glycans [5,7,8].…”

Section: Biochemical Aspects Of Galectin-glycoprotein Lattices Formationmentioning

confidence: 99%

“…Galectins preferentially bind β-galactoside-containing glycans comprised of repeating units of N-acetyllactosamine (Galβ1,4GlcNAc; LacNAc), either as disaccharide units at the termini of complex N-glycans, or as repeating units in a poly-N-acetyllactosamine chain on N-or O-glycans [5,7,8]. Galectin binding affinities to complex N-glycans are proportional to their LacNAc content and to their GlcNAc branching [5,[7][8][9][10][11].…”

Section: Biochemical Aspects Of Galectin-glycoprotein Lattices Formationmentioning

confidence: 99%

Functions of cell surface galectin-glycoprotein lattices

Rabinovich

Toscano

Jackson

et al. 2007

Current Opinion in Structural Biology

358

318

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Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases, can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for β-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions and immune cell activation and homeostasis.

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“…These findings suggest that the expression level of GnT-Va indeed played a role in regulating expression of other proteins. In addition, it is believed that the galectin binding increases if galactose is attached to an N-acetylglucosamine of glycoproteins on the cell surface forming N-acetyllactosamine [32]. A recent paper shows that galectins cross-link glycoproteins on the cell surface with avidities dependent on N-glycan structure and number [30].…”

Section: Discussionmentioning

confidence: 99%

Loss of expression of N‐acetylglucosaminyltransferase Va results in altered gene expression of glycosyltransferases and galectins

et al. 2008

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We isolated mouse embryo fibroblasts (MEFs) from N-acetylglucosaminyltransferase Va (GnT-Va) knockout mice and studied the effects of loss of expression of GnT-Va on asparagine-linked glycans (N-glycan) synthesis and the gene expression of groups of glycosyltransferases and galectins. Loss of GnT-Va expression caused aberrant expression of several N-glycan structures, including N-linked b(1,6) branching, poly-N-lactosamine, bisecting N-acetylglucosamine (GlcNAc) and sialic acid. Using quantitative reverse transcriptase-PCR (qRT-PCR), altered gene expression of several groups of glycosyltransferases and galectins was observed in GnT-Va null MEFs, supporting the observed changes in N-glycan structures. These results suggest that genetic disruption of GnT-Va ultimately resulted in altered MEFs gene expression and decreased tumor progression associated with loss of GnT-Va observed may result in part from a combination of effects from these altered gene expressions.

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Oligosaccharide specificity of galectins: a search by frontal affinity chromatography

Cited by 849 publications

References 112 publications

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

Functions of cell surface galectin-glycoprotein lattices

Loss of expression of N‐acetylglucosaminyltransferase Va results in altered gene expression of glycosyltransferases and galectins

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