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Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney


Morelle, W; Haslam, S M; Ziak, M; Roth, J; Morris, H R; Dell, A (2000). Characterization of the N-linked oligosaccharides of megalin (gp330) from rat kidney. Glycobiology, 10(3):295-304.

Abstract

Megalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galβ1-4GlcNAc (LacNAc), NeuAcα2-6Galβ1-4GlcNAc (sialylated LacNAc), GalNAcβ1-4[NeuAcα2-3]Galβ1-4GlcNAc (Sda) and Galα1-3Galβ1-4GlcNAc. Most complex structures are characterized by the presence of (α1,6)-core fucosylation and the presence of a bisecting GlcNAc residue

Abstract

Megalin (gp 330) is a large cell surface receptor expressed on the apical surfaces of epithelial tissues, that mediates the binding and internalization of a number of structurally and functionally distinct ligands. In this paper we report the first detailed structural characterization of megalin-derived oligosaccharides. Using strategies based on mass spectrometric analysis, we have defined the structures of the N-glycans of megalin. The results reveal that megalin glycoprotein is heterogeneously glycosylated. The major N-glycans identified belong to the following two classes: high mannose structures and complex type structures, with complex structures being more abundant than high mannose structures. The major nonreducing epitopes in the complex-type glycans are: GlcNAc, Galβ1-4GlcNAc (LacNAc), NeuAcα2-6Galβ1-4GlcNAc (sialylated LacNAc), GalNAcβ1-4[NeuAcα2-3]Galβ1-4GlcNAc (Sda) and Galα1-3Galβ1-4GlcNAc. Most complex structures are characterized by the presence of (α1,6)-core fucosylation and the presence of a bisecting GlcNAc residue

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Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:610 Medicine & health
Scopus Subject Areas:Life Sciences > Biochemistry
Language:English
Date:1 March 2000
Deposited On:25 Sep 2018 14:14
Last Modified:15 Apr 2021 14:50
Publisher:Oxford University Press
ISSN:0959-6658
OA Status:Hybrid
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1093/glycob/10.3.295

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