Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0304-4165(98)00095-6
Title: Stable expression of human α-2,6-sialyltransferase in Chinese hamster ovary cells: Functional consequences for human erythropoietin expression and bioactivity
Authors: Zhang, X. 
Lok, S.H.L.
Kon, O.L. 
Keywords: α-2,6-Sialyltransferase
Bioactivity
CHO cell
Erythropoietin
Glycosylation
Issue Date: 1998
Source: Zhang, X., Lok, S.H.L., Kon, O.L. (1998). Stable expression of human α-2,6-sialyltransferase in Chinese hamster ovary cells: Functional consequences for human erythropoietin expression and bioactivity. Biochimica et Biophysica Acta - General Subjects 1425 (3) : 441-452. ScholarBank@NUS Repository. https://doi.org/10.1016/S0304-4165(98)00095-6
Abstract: Hamster cell lines are common hosts for recombinant protein production, e.g. erythropoietin (Epo). Terminal sialylation of native human proteins is characteristically in both α-2,3 and α-2,6 linkage to galactose at the termini of N-linked oligosaccharides but only in α-2,3 linkage in recombinant proteins expressed in hamster cells which do not express α-2,6-sialyltransferase (ST6GalI) (EC 2.4.99.1). This difference could alter the bioactivity of certain recombinant proteins. Chinese hamster ovary (CHO) cells stably transfected with human ST6GalI cDNA linked to the hamster metallothionein II promoter expressed highly inducible authentic ST6GalI activity. Untransfected CHO cells and CHO cells stably expressing ST6GalI cDNA when transfected with a human Epo cDNA expression cassette secreted immunoreactive Epo. Human Epo from singly transfected Pro-5 CHO cells induced significant reticulocytosis (7.00±1.58%; mean±S.D. % reticulocytes; control conditioned medium 3.04±1.29%; P<0.0024), whereas Epo from Pro-5 cells coexpressing ST6GalI elicited a more modest reticulocytosis (4.62±1.02%). Thus for recombinant human Epo, engineering CHO cells to express ST6GalI activity does not enhance Epo bioactivity in vivo in mice. The availability of CHO cells that express high levels of ST6GalI activity now enables systematic studies to determine the functional requirement for this form of sialylation in recombinant human proteins. Copyright (C) 1998 Elsevier Science B.V.
Source Title: Biochimica et Biophysica Acta - General Subjects
URI: http://scholarbank.nus.edu.sg/handle/10635/38273
ISSN: 03044165
DOI: 10.1016/S0304-4165(98)00095-6
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