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Recombinant MUC1 mucin with a breast cancer-like O-glycosylation produced in large amounts in Chinese-hamster ovary cells.

Journal article
Authors Malin Bäckström
Thomas Link
Fredrik J. Olson
Hasse Karlsson
Rosalind Graham
Gianfranco Picco
Joy Burchell
Joyce Taylor-Papadimitriou
Thomas Noll
Gunnar C. Hansson
Published in The Biochemical journal
Volume 376
Issue Pt 3
Pages 677-86
ISSN 1470-8728
Publication year 2003
Published at Institute of Medical Biochemistry
Pages 677-86
Language en
Keywords Amino Acids, analysis, Animals, Antibodies, Monoclonal, immunology, Breast Neoplasms, metabolism, CHO Cells, Carbohydrate Sequence, Carcinoma, metabolism, Cell Line, Tumor, Cricetinae, Female, Glycosylation, Humans, Immunoglobulin G, genetics, Molecular Sequence Data, Mucin-1, chemistry, genetics, metabolism, Polysaccharides, chemistry, Recombinant Fusion Proteins, chemistry, isolation & purification, metabolism
Subject categories Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)


We have developed an expression system for the production of large quantities of recombinant MUC1 mucin in CHO-K1 (Chinese-hamster ovary K1) cells. The extracellular part of human MUC1, including 16 MUC1 tandem repeats, was produced as a fusion protein with murine IgG Fc, with an intervening enterokinase cleavage site for the removal of the Fc tail. Stable MUC1-IgG-producing CHO-K1 clones were generated and were found to secrete MUC1-IgG into the culture medium. After adaptation to suspension culture in protein-free medium in a bioreactor, the fusion protein was secreted in large quantities (100 mg/l per day) into the culture supernatant. From there, MUC1 could be purified to homogeneity using a two-step procedure including enterokinase cleavage and ion-exchange chromatography. Capillary liquid chromatography MS of released oligosaccharides from CHO-K1-produced MUC1 identified the main O-glycans as Galbeta1-3GalNAc (core 1) and mono- and di-sialylated core 1. The glycans occupied on average 4.3 of the five potential O-glycosylation sites in the tandem repeats, as determined by nano-liquid chromatography MS of partially deglycosylated Clostripain-digested protein. A very similar O-glycan profile and site occupancy was found in MUC1-IgG produced in the breast carcinoma cell line T47D, which has O-glycosylation typical for breast cancer. In contrast, MUC1-IgG produced in another breast cancer cell line, MCF-7, showed a more complex pattern with both core 1- and core 2-based O-glycans. This is the first reported production of large quantities of recombinant MUC1 with a breast cancer-like O-glycosylation that could be used for the immunotherapy of breast cancer.

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