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驴乳和人初乳及成熟乳中乳脂肪球膜蛋白组的特征分析及特异性 N-糖基化谱比较。

Characterization and comparison site-specific N-glycosylation profiling of milk fat globule membrane proteome in donkey and human colostrum and mature milk.

机构信息

College of Food Science, Shenyang Agricultural University, Shenyang 11086, China.

College of Science, Shenyang Agricultural University, Shenyang 11086, China.

出版信息

Food Chem. 2023 Sep 1;419:136081. doi: 10.1016/j.foodchem.2023.136081. Epub 2023 Mar 30.

DOI:10.1016/j.foodchem.2023.136081
PMID:37037133
Abstract

Milk fat globule membrane (MFGM) proteins are highly glycosylated and involved in various biological processes within the body. However, information on site-specific N-glycosylation of MFGM glycoproteins in donkey and human milk remains limited. This study aimed to map the most comprehensive site-specific N-glycosylation fingerprinting of donkey and human MFGM glycoproteins using a site-specific glycoproteomics strategy. We identified 1,360, 457, 2,617, and 986 site-specific N-glycans from 296, 77, 214, and 196 N-glycoproteins in donkey colostrum (DC), donkey mature milk (DM), human colostrum (HC), and human mature milk (HM), respectively. Bioinformatics was used to describe the structure-activity relationships of DC, DM, HC, and HM MFGM N-glycoproteins. The results revealed differences in the molecular composition of donkey and human MFGM N-glycoproteins and the dynamic changes to site-specific N-glycosylation of donkey and human MFGM glycoproteins during lactation, deepening our understanding of the composition of donkey and human MFGM N-glycoproteins and their potential physiological roles.

摘要

乳脂肪球膜(MFGM)蛋白高度糖基化,参与体内的各种生物学过程。然而,有关驴乳和人乳 MFGM 糖蛋白的特定部位 N-糖基化的信息仍然有限。本研究旨在使用特定部位糖蛋白质组学策略,绘制驴乳和人乳 MFGM 糖蛋白最全面的特定部位 N-糖基化指纹图谱。我们分别从驴初乳(DC)、驴成熟乳(DM)、人初乳(HC)和人成熟乳(HM)中鉴定出 296、77、214 和 196 个 N-糖蛋白中的 1360、457、2617 和 986 个特定部位 N-聚糖。使用生物信息学来描述 DC、DM、HC 和 HM MFGM N-糖蛋白的结构-活性关系。结果揭示了驴乳和人乳 MFGM N-糖蛋白的分子组成以及驴乳和人乳 MFGM 糖蛋白特定部位 N-糖基化在泌乳期间的动态变化存在差异,加深了我们对驴乳和人乳 MFGM N-糖蛋白的组成及其潜在生理作用的理解。

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引用本文的文献

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