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Glycobiology, 2000, Vol. 10, No. 3 295-304
© 2000 Oxford University Press

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

Willy Morelle, Stuart M. Haslam, Martin Ziak2, Jürgen Roth2, Howard R. Morris and Anne Dell1

Department of Biochemistry, Imperial College, London, SW7 2AY, UK and 2Department of Pathology, Division of Cell and Molecular Pathology, University of Zurich, CH-8091 Zurich, Switzerland

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, Galß1–4GlcNAc (LacNAc), NeuAc{alpha}2–6Galß1–4GlcNAc (sialylated LacNAc), GalNAcß1–4[NeuAc{alpha}2–3]Galß1–4GlcNAc (Sda) and Gal{alpha}1–3Galß1–4GlcNAc. Most complex structures are characterized by the presence of ({alpha}1,6)-core fucosylation and the presence of a bisecting GlcNAc residue.

1 To whom correspondence should be addressed


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