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Glycobiology Advance Access originally published online on July 14, 2004
Glycobiology 2004 14(11):979-986; doi:10.1093/glycob/cwh127
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Glycobiology vol. 14 no. 11 © Oxford University Press 2004; all rights reserved.

Influence of lactation parameters on the N-glycosylation of recombinant human C1 inhibitor isolated from the milk of transgenic rabbits

Kate Koles1,4, Patrick H.C. van Berkel2,5, Maurice L.M. Mannesse5, Raimon Zoetemelk5, Johannes F.G. Vliegenthart4 and Johannis P. Kamerling3,4

4 Bijvoet Center for Biomolecular Research, Department of Bio-Organic Chemistry, Section of Glycoscience and Biocatalysis, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, The Netherlands; and 5 Pharming Technologies BV, Archimedesweg 4, P.O. Box 451, NL-2300 AL Leiden, The Netherlands

Received on April 1, 2004; revised on July 5, 2004; accepted on July 6, 2004

The large-scale production of recombinant biopharmaceutical glycoproteins in the milk of transgenic animals is becoming more widespread. However, in comparison with bacterial, plant cell, or cell culture production systems, little is known about the glycosylation machinery of the mammary gland, and hence on the glycosylation of recombinant glycoproteins produced in transgenic animals. Here the influence is presented of several lactation parameters on the N-glycosylation of recombinant C1 inhibitor (rhC1INH), a human serum glycoprotein, expressed in the milk of transgenic rabbits. Enzymatically released N-glycans of series of rhC1INH samples were fluorescently labeled and fractionated by HPLC. The major N-glycan structures on rhC1INH of pooled rabbit milk were similar to those on native human C1 inhibitor and recombinant human C1 inhibitor produced in transgenic mouse milk, with only the degree of sialylation and core fucosylation being lower. Analyses of individual animals furthermore showed slight interindividual differences; a decrease in the extent of sialylation, core fucosylation, and oligomannose-type glycosylation with the progress of lactation; and a positive correlation between expression level and oligomannose-type N-glycan content. However, when large quantities of rhC1INH were isolated for preclinical and clinical studies, highly consistent N-linked glycan profiles and monosaccharide compositions were found.

1 Present address: Department of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, TX 77843-2128

2 Present address: GenMab BV, Jenalaan 18d, NL-3584 CK Utrecht, The Netherlands

3 To whom correspondence should be addressed; e-mail: j.p.kamerling{at}chem.uu.nl


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