Author(s): Tian Y, Zhang H
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Abstract Glycosylation is the most structurally complicated and diverse type of protein modifications. Protein glycosylation has long been recognized to play fundamental roles in many biological processes, as well as in disease genesis and progression. Glycoproteomics focuses on characterization of proteins modified by carbohydrates. Glycoproteomic studies normally include strategies to enrich glycoproteins containing particular carbohydrate structures from protein mixtures followed by quantitative proteomic analysis. These glycoproteomic studies determine which proteins are glycosylated, the glycosylation sites, the carbohydrate structures, as well as the abundance and function of the glycoproteins in different biological and pathological processes. Here we review the recent development in methods used in glycoproteomic analysis. These techniques are essential in elucidation of the relationships between protein glycosylation and disease states. We also review the clinical applications of different glycoproteomic methods. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
This article was published in Proteomics Clin Appl
and referenced in Journal of Glycobiology