Sialyl-LewisxSequence 6-O-Sulfated atN-Acetylglucosamine Rather Than at Galactose Is the Preferred Ligand forl-Selectin and De-N-acetylation of the Sialic Acid Enhances the Binding Strength

Galustian, Christine; Lawson, A. M.; Komba, Shiro; Ishida, Hideyuki; Kiso, Makoto; Feizi, Ten

doi:10.1006/bbrc.1997.7737

Cited by 79 publications

(69 citation statements)

References 11 publications

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“…Thus, 6-sulfation, but not 6Ј-sulfation, has a potentiating effect on human L-selectin binding not only to the 3Ј-sialyl-Le x , as shown previously (Ref. 10 and Fig. 1B), but also to the 3Ј-sulfo-Le x sequence.…”

Section: Binding Of Multivalent L-selectin To Mono-and Multisulfatedsupporting

confidence: 86%

“…Moreover, its presence partially hinders the recognition of the 3Ј-sialyl-or 3Ј-sulfo-Le x by the selectin. The enhancement of L-selectin binding in the presence of 6-sulfation was substantial for both the 3Ј-sulfoand the 3Ј-sialyl-Le x sequences, but the negative effect of 6Ј-sulfation was less pronounced with the 3Ј-sulfo-Le x than with the 3Ј-sialyl-Le x sequence investigated previously (10). Third, whereas the 6-sulfate on the subterminal N-acetylglucosamine of the Le x sequence is clearly a part of the recognition sequence for L-selectin, additional sulfates along the di-N-acetyllactosamine backbone are not recognized.…”

Section: Discussionmentioning

confidence: 62%

“…O-glycosidic oligosaccharides with other sulfation patterns have been isolated from one of the counter-receptors of L-selectin, Gly-CAM-1; these are heptasaccharides with 3Ј-sialyl-Le x capping groups containing 6-O-sulfate at the outer galactose (referred to as 6Ј-O-sulfation), at the penultimate N-acetylglucosamine (6-O-sulfation), or at both of these positions (6Ј,6-O-sulfation) (9). We have demonstrated that the 6-sulfo,3Ј-sialyl-Le x sequence constitutes a strong ligand for L-selectin, particularly where the N-acetylneuraminic acid is de-N-acetylated, whereas the 6Ј-sulfated analog is not bound (10,24). Indeed, the addition of 6Ј-O-sulfate to the 6-sulfo,3Ј-sialyl-Le x sequence impairs the L-selectin binding.…”

mentioning

confidence: 91%

“…The following were chemically synthesized glycosylceramides: the 3Ј-sialyl-Le ; and the 6Ј,6-sulfo,3Ј-sialyl-Le x (17) designated GSC64, GSC268, GSC269, and GSC270, respectively. These were purified by preparative TLC as described previously (10).…”

mentioning

confidence: 99%

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L-selectin Interactions with Novel Mono- and Multisulfated Lewisx Sequences in Comparison with the Potent Ligand 3′-Sulfated Lewisa

Galustian

Lubineau

Narvor

et al. 1999

Journal of Biological Chemistry

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Section: Binding Of Multivalent L-selectin To Mono-and Multisulfatedsupporting

confidence: 86%

Section: Discussionmentioning

confidence: 62%

mentioning

confidence: 91%

mentioning

confidence: 99%

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L-selectin Interactions with Novel Mono- and Multisulfated Lewisx Sequences in Comparison with the Potent Ligand 3′-Sulfated Lewisa

Galustian

Lubineau

Narvor

et al. 1999

Journal of Biological Chemistry

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“…The terminal Neu5Ac/Gc(␣2-3)Gal(␤1-4)[6-O-SO 3 H]GlcNAc structure is very uncommon and has been found only in N-glycans of the glycoprotein family (ZP3) from zona pellucida (55). The 6-O-sulfosialyl-Lewis X epitope has been identified as a potent inhibitor of the leukocyte adhesion molecule L-selectin (18), and its structure, function, and biosynthesis have been described by Kimura et al (56). It is intriguing that we found its presence on the very same molecule that carries the HNK-1 antigen that also binds to L-selectin (57,58).…”

Section: Characterization Of N-glycans Of Bovine Peripheral Myelin P0mentioning

confidence: 99%

Epitope Diversity of N-Glycans from Bovine Peripheral Myelin Glycoprotein P0 Revealed by Mass Spectrometry and Nano Probe Magic Angle Spinning 1H NMR Spectroscopy

Gallego¹,

Blanco²,

Zuylen³

et al. 2001

Journal of Biological Chemistry

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The carbohydrate structures present on the glycoproteins in the central and peripheral nerve systems are essential in many cell adhesion processes. The P0 glycoprotein, expressed by myelinating Schwann cells, plays an important role during the formation and maintenance of myelin, and it is the most abundant constituent of myelin. Using monoclonal antibodies, the homophilic binding of the P0 glycoprotein was shown to be mediated via the human natural keller cell (HNK)-1 epitope (3-O-SO 3 H-GlcUA(␤1-3)Gal(␤1-4)GlcNAc) present on the N-glycans. We recently described the structure of the N-glycan carrying the HNK-1 epitope, present on bovine peripheral myelin P0 (Voshol, H., van Zuylen, C. W. E. M., Orberger, G., Vliegenthart, J. F. G., and Schachner, M. (1996) J. Biol. Chem. 271, 22957-22960). In this study, we report on the structural characterization of the detectable glycoforms, present on the single N-glycosylation site, using state-of-the-art NMR and mass spectrometry techniques. Even though all structures belong to the hybrid-or biantennary complex-type structures, the variety of epitopes is remarkable. In addition to the 3-Osulfate present on the HNK-1-carrying structures, most of the glycans contain a 6-O-sulfated N-acetylglucosamine residue. This indicates the activity of a 6-Osulfo-GlcNAc-transferase, which has not been described before in peripheral nervous tissue. The presence of the disialo-, galactosyl-, and 6-O-sulfosialyl-Lewis X epitopes provides evidence for glycosyltransferase activities not detected until now. The finding of such an epitope diversity triggers questions related to their function and whether events, previously attributed merely to the HNK-1 epitope, could be mediated by the structures described here.The P0 glycoprotein consists of a single immunoglobulin-like domain in its extracellular part, a transmembranous domain, and a cytoplasmic tail. It is the most abundant protein constituent of peripheral myelin. P0 contains a single N-glycosylation site and heterogeneity in its glycosylation pattern that originates from variable contents of fucose, galactose, and sialic acid residues; sulfate; and the HNK-1 carbohydrate epitope (1-4). P0 appears at the initial stage of myelination and contributes to the formation and maintenance of myelin compaction as an adhesion molecule (5). The essential functional role of P0 in the processes of myelination has been demonstrated by creating P0 knockout mice, which show severe hypomyelination and myelin degeneration (5, 6). In humans, several neurological disorders such as Charcot-Marie-Tooth disease, Dejerine-Sottas disease, and congenital hypomyelination have been associated with mutations in the P0 gene (7).It has been reported that the glycan moiety of P0 plays an important role in cell-cell adhesion via homophilic binding. This homophilic binding has been mapped to the SDNGT sequence composing amino acids 91-95, which harbors the single N-glycosylation site on P0 (8). Thus, it was observed that this glycopeptide fragment inhibits cell adhesion t...

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Die erste Totalsynthese des 6-Sulfo-de-N-acetylsialyl-Lewisx-Gangliosids: ein hervorragender Ligand für menschliches L-Selectin

et al. 1999

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Ursprünglich als unbedeutendes Nebenprodukt von 6‐Sulfo‐N‐acetylsialyl‐Lewisx angesehen wurde dessen N‐Desacetyl‐Form 1, bis sich zeigte, daß dieses „Nebenprodukt”︁ der N‐Acetyl‐Form als L‐Selectin‐Ligand überlegen ist. Um die außergewöhnliche Reaktivität von 1 zu untermauern, wurde es nun erstmals gezielt synthetisiert und seine Bindung an L‐Selectin untersucht. 1 und verwandte Strukturen könnten an der Wechselwirkung zwischen Leukocyten und dem Gefäßendothel als hochaffine endogene Liganden für L‐Selectin beteiligt sein.

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Sialyl-LewisxSequence 6-O-Sulfated atN-Acetylglucosamine Rather Than at Galactose Is the Preferred Ligand forl-Selectin and De-N-acetylation of the Sialic Acid Enhances the Binding Strength

Cited by 79 publications

References 11 publications

L-selectin Interactions with Novel Mono- and Multisulfated Lewisx Sequences in Comparison with the Potent Ligand 3′-Sulfated Lewisa

L-selectin Interactions with Novel Mono- and Multisulfated Lewisx Sequences in Comparison with the Potent Ligand 3′-Sulfated Lewisa

Epitope Diversity of N-Glycans from Bovine Peripheral Myelin Glycoprotein P0 Revealed by Mass Spectrometry and Nano Probe Magic Angle Spinning 1H NMR Spectroscopy

Die erste Totalsynthese des 6-Sulfo-de-N-acetylsialyl-Lewisx-Gangliosids: ein hervorragender Ligand für menschliches L-Selectin

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