Abstract
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. Mass spectrometry (MS) has become a powerful tool for glycoprotein analysis. 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
Glycoproteins consist of oligosaccharide chains covalently attached to polypeptide side-chains and play essential roles in a wide range of biological processes, as well as in disease genesis and progression [1,2,3]
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
Conclusions there is no universal method for comprehensive identification of glycoproteins, mass spectrometry has the great advantages in structural analysis of glycoproteins
Summary
Glycoproteins consist of oligosaccharide chains covalently attached to polypeptide side-chains and play essential roles in a wide range of biological processes, as well as in disease genesis and progression [1,2,3]. Combined with a linear ion trap, orbitrap has been already employed to identify glycoprotein with high resolution and mass accuracy [14], which provides rapid and accurate tandem MS analysis (CID, ETD, HCD) of complex compounds. At relatively low CID energies (typically 10−1–1 eV collisions in IT and FT-ICR analyzers and 10–102 eV collisions in tandem quadrupole (TQ) and Q-TOF) [9], glycosidic bonds of glycopeptides are often broken to produce B-/Y-type fragment ions in the positive mode for the analysis of the glycan structures [9]. The collision energy of HCD is higher than that of CID in the linear ion trap, and the resolution of fragment ions are very high [44] The cleavages of both peptide bonds and glycosidic bonds are observed, which could provide the information of peptide sequences and glycan structures [14,44,45]. The result was insufficient for a comprehensive MS study due to the volume (2 ml) of jacalin was too great to efficiently recover the glycopeptides from the lectin column for smaller scale analysis
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
