Changes in glycosylated proteins in colostrum and mature milk and their implication

文献类型： 外文期刊

第一作者： Lu, Jing

作者： Lu, Jing;Dai, Ying;Zhu, Tong;Liu, Jinqi;Xing, Lina;Zhang, Wenyuan;Pang, Xiaoyang;Zhang, Shuwen;Lv, Jiaping;Ma, Changlu

作者机构：

关键词： glycoproteins; colostrum; mature milk; host defense; IgA

期刊名称：FRONTIERS IN NUTRITION （ 影响因子：5.0； 五年影响因子：5.7 ）

ISSN： 2296-861X

年卷期： 2023 年 10 卷

页码：

收录情况： SCI

摘要： IntroductionGlycosylation is one of the essential post-translational modifications that influences the function of milk proteins. MethodsIn the present study, 998 proteins and 764 glycosylated sites from 402 glycoproteins were identified in human milk by TMT labeling proteomics. Compared to human milk proteins, the glycoproteins were mainly enriched in cell adhesion, proteolysis, and defense/immune process. ResultsThe abundance of 353 glycosylated sites and their 179 parent proteins was quantified. After normalization to their parent protein's abundance, 78 glycosylated sites in 56 glycoproteins and 10 glycosylated sites in 10 glycoproteins were significantly higher in colostrum and mature milk, respectively. These changed glycoproteins were mainly related to host defense. Intriguingly, one glycosylated site (Asp144) in IgA and two glycosylated sites (Asp38 and Asp1079) in tenascin are significantly upregulated even though their protein abundance was downregulated during lactation. DiscussionThis study helps us figure out the critical glycosylated sites in proteins that might influence their biological function in an unbiased way.

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