SARAH STORR sarah.storr@nottingham.ac.uk
Assistant Professor
SARAH STORR sarah.storr@nottingham.ac.uk
Assistant Professor
L. Royle
C. J Chapman
U. M A. Hamid
J. F Robertson
A. Murray
R. A Dwek
P. M Rudd
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.
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 |
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