Expression of human α2, 6-Sialyltransferase in BHK-21A cells increases the sialylation of coexpressed human erythropoietin: NeuAc-transfer onto GalNAc(βl-4)GlcNAc-R motives View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1997

AUTHORS

Peter Schlenke , Eckart Grabenhorst , Roland Wagner , Manfred Nimtz , Harald S. Conradt

ABSTRACT

We have characterized two BHK cell lines (BHK-21B and BHK-21A) with different glycosylation properties. N-glycans synthesized by BHK-21B cells contain the typical N-acetyllactosamine motif (Gal(βl-4)GlcNAc-R) whereas BHK-21 A cells bear to a high amount nonsialylated terminal GalNAc(βl-4)GlcNAc-R moieties [1]. Due to the incapability of the endogenous oc2, 3-sialyltransferase to transfer NeuAc to the GalNAc(βl-4) GlcNAc-R structure recombinant glycoproteins produced by BHK-21 A cells are under-sialylated. Therefore we have transfected BHK-21 A cells harbouring a plasmid encoding human EPO with the human Golgi enzyme CMP-NeuAc:Gal(βl-4)GlcNAc-R a2,6-sialyltransferase (ST6N). Detailed structural analysis of Oligosaccharides from the affinity purified recombinant EPO (HPAEC-PAD-mapping and MALDI/TOF-MS) revealed a significant increased NeuAc content when compared to the parent BHK-21 A cells without ST6N activity. Methylation analysis corroborated these results. The newly introduced α2,6-sialyltransferase recognizes the terminal GlcNAc-R motif as a substrate. The cell line obtained thus exhibits a ‘human kidney-type’ glycosylation characteristic [2]. More... »

PAGES

475-480

Book

TITLE

Animal Cell Technology

ISBN

978-94-010-6273-2
978-94-011-5404-8

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-5404-8_76

DOI

http://dx.doi.org/10.1007/978-94-011-5404-8_76

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041422264


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