Expression of Human Interleukin-2 in Recombinant Baby Hamster Kidney, Ltk−, and Chinese Hamster Ovary Cells
In: Journal of Biological Chemistry, Jg. 264 (1989-10-01), S. 17368-17373
Online
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Zugriff:
The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model. Human interleukin-2 was constitutively expressed in several mammalian cell lines in high amounts. The recombinant proteins were purified to homogeneity and their carbohydrate structures were analyzed. Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines. The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2. The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions. Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
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Expression of Human Interleukin-2 in Recombinant Baby Hamster Kidney, Ltk−, and Chinese Hamster Ovary Cells
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Autor/in / Beteiligte Person: | Hoppe, J ; Dittmar, K.E.J. ; Nimtz, Manfred ; Lindenmaier, W. ; Hauser, Hansjörg ; Conradt, Harald S. |
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Zeitschrift: | Journal of Biological Chemistry, Jg. 264 (1989-10-01), S. 17368-17373 |
Veröffentlichung: | Elsevier BV, 1989 |
Medientyp: | unknown |
ISSN: | 0021-9258 (print) |
DOI: | 10.1016/s0021-9258(18)71502-0 |
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