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- Title
The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patients serum.
- Authors
Sarah J Storr; Louise Royle; Caroline J Chapman; Umi M Abd Hamid; John F Robertson; Andrea Murray; Raymond A Dwek; Pauline M Rudd
- 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.
- Subjects
GLYCOSYLATION; GLYCOPROTEINS; BREAST cancer patients; LIQUID chromatography
- Publication
Glycobiology, 2008, Vol 18, Issue 6, p456
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cwn022