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Glycobiology Advance Access published online on March 10, 2008
Glycobiology, doi:10.1093/glycob/cwn022
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

The O-linked glycosylation of secretory/shed MUC1 from advanced breast cancer patient serum

Sarah J. Storr1,2, Louise Royle3,4, Caroline J. Chapman1, Umi M. Abd Hamid3,5, John F. Robertson1,6,, Andrea Murray6, Raymond A. Dwek3 and Pauline M. Rudd3,5

1 Tumour Immunology Group, University of Nottingham, Division of Breast Surgery, Nottingham City Hospital, Hucknall Road, Nottingham NG5 1PB, UK
3 Oxford Glycobiology Institute, Department of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK
6 Oncimmune Ltd., Clinical Sciences Building, Nottingham City Hospital, Hucknall Road, Nottingham NG5 1PB, UK

Correspondence Address: Tumour Immunology Group, University of Nottingham, Division of Breast Surgery, Nottingham City Hospital, Hucknall Road, Nottingham NG5 1PB, UK. Phone: 011582 31825. Email Address: sarah.storr{at}nottingham.ac.uk

Received on November 26, 2007; accepted on March 4, 2008

MUC1 is a high molecular weight glycoprotein that is over-expressed in breast cancer. Aberrant O-linked glycosylation of MUC1 in cancer has been implicated in disease progression. We investigated the O-linked glycosylation of MUC1 purified from the serum of an advanced breast cancer patient. O-glycans were released by hydrazinolysis and analyzed by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) and by high performance liquid chromatography (HPLC) coupled with sequential exoglycosidase digestions. Core 1 type glycans (83%) dominated the profile which also confirmed high levels of sialylation: 80% of the glycans were mono-, di- or tri-sialylated. Core 2 type structures contributed approximately 17% of the assigned glycans and the oncofoetal Thomsen-Friedenreich (TF) antigen (Gal1–3GalNAc) accounted for 14% of the total glycans. Interestingly, two core 1 type glycans were identified that had sialic acid 2--8 linked to sialylated core 1 type structures (9% of the total glycan pool). This is the first O-glycan analysis of MUC1 from the serum of a breast cancer patient; the results suggest that amongst the cell lines commonly used to express recombinant MUC1 the T47D cell line processes glycans that are most similar to patient derived material.

Key words: Breast cancer / MUC1 / O-linked glycosylation / 2--8 linked sialic acid

2Current address; Oncimmune Ltd., Clinical Sciences Building, Nottingham City Hospital, Hucknall Road, Nottingham NG5 1PB, UK

4Current address; Ludger Ltd, Culham Science Centre, Abingdon, Oxfordshire OX14 3EB, UK

5Current address; Dublin-Oxford Glycobiology Laboratory, NIBRT, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland


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