Brazilian Journal of Biological Sciences (ISSN 2358-2731)

Home Archive v. 4, No. 7 (2017) Shammala


Vol. 4, No. 7, p. 203-215 - Jun. 30, 2017


Mass spectrometry-based analysis of glycoproteins and its clinical applications in cancer biomarker discovery

Farid Abu Shammala

Most proteins are glycosylated, glycosylation is one of the most important posttranslational modifications of proteins and plays essential roles in various biological processes. Aberration in the glycan moieties of glycoproteins is associated with many diseases. It is especially critical to develop the rapid and sensitive methods for analysis of aberrant glycoproteins associated with diseases. With recent advances in proteomics, analytical and computational technologies, glycoproteomics, the global analysis of glycoproteins, is rapidly emerging as a subfield of proteomics with high biological and clinical relevance. Glycoproteomics integrates glycoprotein enrichment and proteomics technologies to support the systematic identification and quantification of glycoproteins in a complex sample. It is especially critical to develop the rapid and sensitive methods for analysis of aberrant glycoproteins associated with diseases. Mass spectrometry (MS) has become a powerful tool for mapping glycoprotein glycosylation and detailed glycan structural determination. Especially, tandem mass spectrometry can provide highly informative fragments for structural identification of glycoproteins. This review provides an overview of the development of MS technologies and their applications in identification of abnormal glycoproteins and glycans in human serum to screen cancer biomarkers in recent years.

Mass spectrometry; Glycoproteins; Cancer biomarker.


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