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Open Access Review

The sweet and sour of serological glycoprotein tumor biomarker quantification

Uros Kuzmanov12, Hari Kosanam3 and Eleftherios P Diamandis123*

Author Affiliations

1 Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, 6th floor, 60 Murray Street, Box 32, Toronto, ON M5T 3L9, Canada

2 Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, 6th Floor, 60 Murray Street, Box 32, Toronto, ON M5T 3L9, Canada

3 Department of Clinical Biochemistry, University Health Network, 6th Floor, 60 Murray Street, Box 32, Toronto, ON M5T 3L9, Canada

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BMC Medicine 2013, 11:31  doi:10.1186/1741-7015-11-31

Published: 7 February 2013


Aberrant and dysregulated protein glycosylation is a well-established event in the process of oncogenesis and cancer progression. Years of study on the glycobiology of cancer have been focused on the development of clinically viable diagnostic applications of this knowledge. However, for a number of reasons, there has been only sparse and varied success. The causes of this range from technical to biological issues that arise when studying protein glycosylation and attempting to apply it to practical applications. This review focuses on the pitfalls, advances, and future directions to be taken in the development of clinically applicable quantitative assays using glycan moieties from serum-based proteins as analytes. Topics covered include the development and progress of applications of lectins, mass spectrometry, and other technologies towards this purpose. Slowly but surely, novel applications of established and development of new technologies will eventually provide us with the tools to reach the ultimate goal of quantification of the full scope of heterogeneity associated with the glycosylation of biomarker candidate glycoproteins in a clinically applicable fashion.

glycobiomarker; glycopeptide; lectin; lectin ELISA; mass spectrometry; N-glycosylation; ovarian cancer; sialic acid.