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Glycobiology, 2000, Vol. 10, No. 9 901-917
© 2000 Oxford University Press

Characterization of the carbohydrate chains of the secreted form of the human epidermal growth factor receptor

Corné J.M. Stroop, Wolfgang Weber2, Gerrit J. Gerwig, Manfred Nimtz3, Johannis P. Kamerling and Johannes F.G. Vliegenthart1

Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, P.O. Box 80075, 3508 TB Utrecht, The Netherlands, 2Institut für Physiologische Chemie, Universitätskrankenhaus Eppendorf, D-20246 Hamburg, Germany, and 3Gesellschaft für Biotechnologische Forschung mbH, Structure Research, Mascheroder Weg 1, D-38124 Braunschweig, Germany

The human epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein having 11 potential N-glycosylation sites in its extracellular domain. N-Glycosylation is needed for proper membrane insertion, EGF binding and receptor functioning. The human epidermoid carcinoma A431 cell line secretes a soluble 105 kDa glycoprotein (sEGFR) that represents the extracellular domain of the membrane-bound form, and its glycosylation pattern has been investigated. After liberation of the oligosaccharides from sEGFR with PNGase F, the glycans were fractionated along different routes, including Concanavalin A affinity chromatography, anion-exchange chromatography, HPLC and high-pH anion-exchange chromatography. The oligosaccharide fractions were characterized by 500- and 600-MHz 1H-NMR spectroscopy and mass spectrometry (FAB, ESI, and MALDI-TOF). The oligomannose-type glycans range from Man5GlcNAc2 to Man8GlcNAc2 and account for 17% of the total carbohydrate moiety. Furthermore, di-, tri'- and tetraantennary complex-type structures are present, both neutral and ({alpha}2–3)-sialylated (up to tetrasialo), comprising 24 and 59%, respectively, of the total carbohydrate moiety. In this study, 32 new complex-type glycans are characterized containing the Lex, Ley, and sialyl-Lex determinants, the bloodgroup A and H antigens, as well as the ALey determinant. This first comprehensive glycosylation study on a human nonrecombinant receptor shows the immense heterogeneity of the glycosylation of sEGFR.

1 To whom correspondence should be addressed


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