Construction of novel BHK-21 cell lines coexpressing Golgi resident or soluble forms of human α2,6-sialyltransferase and α1,3/4-fucosyltransferases together with secretory ... View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1997

AUTHORS

Eckart Grabenhorst , Júlia Costa , Harald S. Conradt

ABSTRACT

The most frequently used mammalian host cell lines (BHK-21, CHO) for the production of recombinant therapeutic glycoproteins are incapable of producing α2,6-sialylated or sialyl Lewis X containing Oligosaccharide structures. Therefore, we have constructed novel stable BHK-21 cell lines by cotransfection of cells with plasmids encoding human secretory glycoproteins (β-trace protein, erythropoietin, antithrombin III) and the membrane-bound or soluble forms of human glycosyltransferases α2,6-sialyltransferase (ST6Gal), α1,3-fucosyltransferase III (FT3) or VI (FT6). The secreted recombinant glycoproteins were purified from culture supernatants and were analyzed in detail using HPAE-PAD, mass spectrometry and NMR-analysis of their Oligosaccharide chains. The soluble forms of the recombinant glycosyltransferases showed in vitro activity with Oligosaccharides, glycolipids as well as glycoproteins. However, no modification of coexpressed secretory glycoproteins was detected. Thus a proper targeting/localization of the glycosyltransferases into the appropriate Golgi compartments is required for their in vivo activity on secreted recombinant glycoproteins. Such cell lines can be successfully used for the production of recombinant proteins with novel/tailored glycosylation characteristics that might alter and improve their biological in vivo properties (e.g. stability, tissue addressing). More... »

PAGES

481-487

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-5404-8_77

DOI

http://dx.doi.org/10.1007/978-94-011-5404-8_77

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037624999


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