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Int. J. Mol. Sci. 2013, 14(8), 15636-15654; doi:10.3390/ijms140815636

Exploring the Glycosylation of Serum CA125

NIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Dublin 4, Ireland
The Mass Spectrometry Resource, Conway Institute, University College Dublin, Dublin 4, Ireland
UCD School of Medicine and Medical Science, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Dublin 4, Ireland
Department of Pathology and Laboratory Medicine, St Vincent's University Hospital, Dublin 4, Ireland
Author to whom correspondence should be addressed.
Received: 22 April 2013 / Revised: 15 July 2013 / Accepted: 16 July 2013 / Published: 26 July 2013
(This article belongs to the Special Issue Advances in Cancer Diagnosis)


Ovarian cancer is the most lethal gynaecologic cancer affecting women. The most widely used biomarker for ovarian cancer, CA125, lacks sensitivity and specificity. Here, we explored differences in glycosylation of CA125 between serum from patients with ovarian cancer and healthy controls. We found differences between CA125 N-glycans from patient sera compared to controls. These include increases in core-fucosylated bi-antennary monosialylated glycans, as well as decreases in mostly bisecting bi-antennary and non-fucosylated glycans in patients compared to controls. Measurement of the glycosylated state of CA125 may therefore provide a more specific biomarker for patients with ovarian cancer.
Keywords: CA125; N-glycosylation; biomarker; ovarian cancer CA125; N-glycosylation; biomarker; ovarian cancer

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Saldova, R.; Struwe, W.B.; Wynne, K.; Elia, G.; Duffy, M.J.; Rudd, P.M. Exploring the Glycosylation of Serum CA125. Int. J. Mol. Sci. 2013, 14, 15636-15654.

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