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The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum
- Source :
- Glycobiology. 18(6)
- Publication Year :
- 2008
-
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 (Galbeta1-3GalNAc) accounted for 14% of the total glycans. Interestingly, two core 1 type glycans were identified that had sialic acid alpha2-8 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 :
- CA15-3
Glycan
Glycosylation
Breast Neoplasms
Biochemistry
Cell Line
chemistry.chemical_compound
medicine
Carbohydrate Conformation
Humans
skin and connective tissue diseases
Glucans
MUC1
chemistry.chemical_classification
biology
Chemistry
Mucin-1
Cancer
medicine.disease
Molecular biology
Recombinant Proteins
Sialic acid
Neoplasm Proteins
carbohydrates (lipids)
Immunology
biology.protein
O-linked glycosylation
Female
Glycoprotein
Subjects
Details
- ISSN :
- 14602423
- Volume :
- 18
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Glycobiology
- Accession number :
- edsair.doi.dedup.....460358813eb86bb0fb134108a88aa0d3