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Glycobiology Advance Access originally published online on March 10, 2008
Glycobiology 2008 18(6):456-462; 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 an advanced breast cancer patient's serum

Sarah J Storr1,2,5, Louise Royle3,6, Caroline J Chapman5, Umi M Abd Hamid4,6, John F Robertson5,7, Andrea Murray7, Raymond A Dwek6 and Pauline M Rudd4,6

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

1 To whom correspondence should be addressed: Tel: +44-11582-31871; e-mail: sarah.storr{at}nottingham.ac.uk

Received on November 26, 2007; revised on February 11, 2008; accepted on March 4, 2008

MUC1 is a high molecular weight glycoprotein that is overexpressed 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 and by high performance liquid chromatography 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 trisialylated. Core 2 type structures contributed approximately 17% of the assigned glycans and the oncofoetal Thomsen–Friedenreich (TF) antigen (Galβ1-3GalNAc) accounted for 14% of the total glycans. Interestingly, two core 1 type glycans were identified that had sialic acid {alpha}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: {alpha}2-8 linked sialic acid / breast cancer / MUC1/ O-linked glycosylation

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

3 Present address: Ludger Ltd, Culham Science Centre, Abingdon, Oxfordshire OX14 3EB, UK.

4 Present address: Dublin-Oxford Glycobiology Laboratory, NIBRT, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland.


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