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Comparative Analysis of Whey N-Glycoproteins in Human Colostrum and Mature Milk Using Quantitative Glycoproteomics
- Cao, Xueyan, Song, Dahe, Yang, Mei, Yang, Ning, Ye, Qing, Tao, Dongbing, Liu, Biao, Wu, Rina, Yue, Xiqing
- Journal of agricultural and food chemistry 2017 v.65 no.47 pp. 10360-10367
- amino acids, breast milk, coagulation, complement, gene expression regulation, gene ontology, glycoproteins, glycoproteomics, glycosylation, human colostrum, infant development, lactation, milk, whey
- Glycosylation is a ubiquitous post-translational protein modification that plays a substantial role in various processes. However, whey glycoproteins in human milk have not been completely profiled. Herein, we used quantitative glycoproteomics to quantify whey N-glycosylation sites and their alteration in human milk during lactation; 110 N-glycosylation sites on 63 proteins and 91 N-glycosylation sites on 53 proteins were quantified in colostrum and mature milk whey, respectively. Among these, 68 glycosylation sites on 38 proteins were differentially expressed in human colostrum and mature milk whey. These differentially expressed N-glycoproteins were highly enriched in “localization”, “extracellular region part”, and “modified amino acid binding” according to gene ontology annotation and mainly involved in complement and coagulation cascades pathway. These results shed light on the glycosylation sites, composition and biological functions of whey N-glycoproteins in human colostrum and mature milk, and provide substantial insight into the role of protein glycosylation during infant development.