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

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-Glycan...

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Bibliographic Details
Published in:Glycobiology (Oxford) 2008-06, Vol.18 (6), p.456-462
Main Authors: Storr, Sarah J, Royle, Louise, Chapman, Caroline J, Hamid, Umi M. Abd, Robertson, John F, Murray, Andrea, Dwek, Raymond A, Rudd, Pauline M
Format: Article
Language:English
Subjects:
breast cancer
Breast Neoplasms - chemistry
Breast Neoplasms - metabolism
Carbohydrate Conformation
Cell Line
Female
Glucans - biosynthesis
Glucans - chemistry
Glycosylation
Humans
MUC1/ O-linked glycosylation
Mucin-1 - biosynthesis
Mucin-1 - chemistry
Neoplasm Proteins - biosynthesis
Neoplasm Proteins - chemistry
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
α2-8 linked sialic acid
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Summary: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.
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/cwn022