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

Storr, S. J; Royle, L.; Chapman, C. J; Hamid, U. M A.; Robertson, J. F; Murray, A.; Dwek, R. A; Rudd, P. M

Abstract

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 α2-8 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.

Citation

Storr, S. J., Royle, L., Chapman, C. J., Hamid, U. M. A., Robertson, J. F., Murray, A., …Rudd, P. M. (2008). The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum. Glycobiology, 18(6), 456-462. https://doi.org/10.1093/glycob/cwn022

• Journal Article Type: Article
• Acceptance Date: Mar 4, 2008
• Online Publication Date: Mar 10, 2008
• Publication Date: Jun 1, 2008
• Deposit Date: Oct 12, 2020
• Journal: Glycobiology
• Print ISSN: 0959-6658
• Electronic ISSN: 1460-2423
• Publisher: Oxford University Press
• Peer Reviewed: Peer Reviewed
• Volume: 18
• Issue: 6
• Pages: 456-462
• DOI: https://doi.org/10.1093/glycob/cwn022
• Keywords: Biochemistry
• Public URL: https://nottingham-repository.worktribe.com/output/4958825
• Publisher URL: https://academic.oup.com/glycob/article/18/6/456/1987721