Site-Specific Analysis of Core and Antenna Fucosylation on Serum Glycoproteins

• Published in: Analytical chemistry (Washington) Vol. 96; no. 15; pp. 5741 - 5745
• Main Authors: Li, Jun, Liu, Didi, Zhang, Yingjie, Shen, Jiechen, Dan, Wei, Chen, Zexuan, Sun, Shisheng
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 16.04.2024
• Subjects: Antennas; Biological activity; Blood coagulation; Cell adhesion; Coagulation; Complement activation; Glycopeptides; Glycoproteins; N-glycans; Polysaccharides; Serum; Signal transduction
• ISSN: 0003-2700; 1520-6882; 1520-6882
• DOI: 10.1021/acs.analchem.4c00445

Fucosylation is an important structural feature of glycans and plays an essential role in the regulation of glycoprotein functions. Fucosylation can be classified into core- (CF) and antenna-fucosylation (AF, also known as (sialyl-) Lewis) based on the location on N-glycans, and they perform distinct biological functions. In this study, core- and antenna-fucosylated N-glycans on human serum glycoproteins that hold great clinical application values were systematically characterized at the site-specific level using StrucGP combined with the recently developed fucosylation assignment method. The results showed that fucosylation was widely distributed on serum glycoproteins, with 50% of fucosylated glycopeptides modified by AF N-glycans, 37% by CF N-glycans, and 13% by dual-fucosylated N-glycans. Interestingly, CF and AF N-glycans preferred to modify different groups of serum glycoproteins with different tissue origins and were involved in distinctive biological processes. Specifically, AF N-glycoproteins are mainly from the liver and participated in complement activation, blood coagulation, and endopeptidase activities, while CF N-glycoproteins originate from diverse tissues and are mainly involved in cell adhesion and signaling transduction. These data further enhanced our understanding of fucosylation on circulation glycoproteins.