Abstract
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.
Highlights
Glycoproteomic analysis is complicated by the variety of types of carbohydrates, and by the complex linkage of the glycan to the protein
The current review focuses on the development of Mass spectrometry (MS) technologies and their application in the analysis of abnormal glycoproteins in biological samples to screen cancer biomarkers in recent years
Most proteomics and glycomics analyses are performed in a positive-ion mode, the glycan moieties composition is diverse, and if the particular moiety contains N-acetylation and acidic residues, such as sialic acid, ionization may be prevented
Summary
Glycoproteomic analysis is complicated by the variety of types of carbohydrates, and by the complex linkage of the glycan to the protein. Glycosylation can occur at several different amino acid residues in the protein sequence. The current review focuses on the development of MS technologies and their application in the analysis of abnormal glycoproteins in biological samples to screen cancer biomarkers in recent years.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
