Quantitative label-free site-specific glycoproteomic analysis of the milk fat globule membrane protein in human colostrum and mature milk
Human milk fat globule membrane (MFGM) proteins, which are N-glycosylated, play essential roles in neonatal development and physiological health. However, the profiles and landscape changes in the site-specific N-glycosylation of human MFGM proteins during lactation remain unclear. Therefore, in thi...
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| Published in | Carbohydrate polymers Vol. 306; p. 120588 |
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| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier Ltd
15.04.2023
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| Abstract | Human milk fat globule membrane (MFGM) proteins, which are N-glycosylated, play essential roles in neonatal development and physiological health. However, the profiles and landscape changes in the site-specific N-glycosylation of human MFGM proteins during lactation remain unclear. Therefore, in this study, based on an intact glycopeptide-centred strategy, 2617 unique site-specific N-glycans of 221 MFGM glycoproteins in human colostrum and 986 unique site-specific N-glycans of 200 MFGM glycoproteins in mature milk were characterised and quantified using label-free glycoproteomics. With milk maturation, 33 site-specific N-glycans on 10 N-glycoproteins increased significantly, and 113 site-specific N-glycans on 25 N-glycoproteins decreased significantly. Moreover, human MFGM glycoproteins with core-α1,6-fucosylated structures and Lewis and sialylated branching structures play a role in the biological processes of antigen processing and presentation. This study reveals the dynamic changes in human MFGM protein N-glycosylation patterns during lactation. Meanwhile, the study deepens our understanding of site-specific N-glycosylation of human MFGM glycoproteins. The results of the study provide a background reference for the development of infant formulas.
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| AbstractList | Human milk fat globule membrane (MFGM) proteins, which are N-glycosylated, play essential roles in neonatal development and physiological health. However, the profiles and landscape changes in the site-specific N-glycosylation of human MFGM proteins during lactation remain unclear. Therefore, in this study, based on an intact glycopeptide-centred strategy, 2617 unique site-specific N-glycans of 221 MFGM glycoproteins in human colostrum and 986 unique site-specific N-glycans of 200 MFGM glycoproteins in mature milk were characterised and quantified using label-free glycoproteomics. With milk maturation, 33 site-specific N-glycans on 10 N-glycoproteins increased significantly, and 113 site-specific N-glycans on 25 N-glycoproteins decreased significantly. Moreover, human MFGM glycoproteins with core-α1,6-fucosylated structures and Lewis and sialylated branching structures play a role in the biological processes of antigen processing and presentation. This study reveals the dynamic changes in human MFGM protein N-glycosylation patterns during lactation. Meanwhile, the study deepens our understanding of site-specific N-glycosylation of human MFGM glycoproteins. The results of the study provide a background reference for the development of infant formulas. Human milk fat globule membrane (MFGM) proteins, which are N-glycosylated, play essential roles in neonatal development and physiological health. However, the profiles and landscape changes in the site-specific N-glycosylation of human MFGM proteins during lactation remain unclear. Therefore, in this study, based on an intact glycopeptide-centred strategy, 2617 unique site-specific N-glycans of 221 MFGM glycoproteins in human colostrum and 986 unique site-specific N-glycans of 200 MFGM glycoproteins in mature milk were characterised and quantified using label-free glycoproteomics. With milk maturation, 33 site-specific N-glycans on 10 N-glycoproteins increased significantly, and 113 site-specific N-glycans on 25 N-glycoproteins decreased significantly. Moreover, human MFGM glycoproteins with core-α1,6-fucosylated structures and Lewis and sialylated branching structures play a role in the biological processes of antigen processing and presentation. This study reveals the dynamic changes in human MFGM protein N-glycosylation patterns during lactation. Meanwhile, the study deepens our understanding of site-specific N-glycosylation of human MFGM glycoproteins. The results of the study provide a background reference for the development of infant formulas. [Display omitted] |
| ArticleNumber | 120588 |
| Author | Feng, Daguang Liu, Xiaoyu Guan, Boyuan Cao, Xueyan Luo, Xue Zhang, Zhenghan Bai, Xue Zhao, Shanshan Yang, Liu Yue, Xiqing |
| Author_xml | – sequence: 1 givenname: Boyuan surname: Guan fullname: Guan, Boyuan organization: College of Food Science, Shenyang Agricultural University, Shenyang 11086, China – sequence: 2 givenname: Zhenghan surname: Zhang fullname: Zhang, Zhenghan organization: College of Food Science, Shenyang Agricultural University, Shenyang 11086, China – sequence: 3 givenname: Xiaoyu surname: Liu fullname: Liu, Xiaoyu organization: Department of Obstetrics and Gynaecology, General Hospital of Northern Theater Command, Shenyang 110003, China – sequence: 4 givenname: Shanshan surname: Zhao fullname: Zhao, Shanshan organization: College of Food Science, Shenyang Agricultural University, Shenyang 11086, China – sequence: 5 givenname: Xue surname: Bai fullname: Bai, Xue organization: College of Food Science, Shenyang Agricultural University, Shenyang 11086, China – sequence: 6 givenname: Xue surname: Luo fullname: Luo, Xue organization: College of Food Science, Shenyang Agricultural University, Shenyang 11086, China – sequence: 7 givenname: Daguang surname: Feng fullname: Feng, Daguang organization: College of Science, Shenyang Agricultural University, Shenyang 11086, China – sequence: 8 givenname: Liu surname: Yang fullname: Yang, Liu organization: Foreign Language Teaching Department, Shenyang Agricultural University, Shenyang 11086, China – sequence: 9 givenname: Xueyan surname: Cao fullname: Cao, Xueyan email: 526287162@qq.com organization: College of Food Science, Shenyang Agricultural University, Shenyang 11086, China – sequence: 10 givenname: Xiqing surname: Yue fullname: Yue, Xiqing email: yxqsyau@126.com organization: College of Food Science, Shenyang Agricultural University, Shenyang 11086, China |
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| CitedBy_id | crossref_primary_10_1021_acs_jafc_3c07805 crossref_primary_10_1016_j_foodchem_2023_136447 crossref_primary_10_1016_j_lwt_2023_115648 crossref_primary_10_1002_pmic_202300281 crossref_primary_10_3390_nu16050587 crossref_primary_10_1016_j_foodchem_2024_138651 crossref_primary_10_1021_acs_jafc_3c07405 crossref_primary_10_1021_acs_jafc_3c04534 |
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| Keywords | Human milk Site-specific glycoproteomics Colostrum Milk fat globule membrane protein Mature milk |
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| SubjectTerms | Colostrum Colostrum - chemistry Colostrum - metabolism Female Glycoproteins - chemistry Human milk Humans Infant, Newborn Mature milk Membrane Proteins - metabolism Milk fat globule membrane protein Milk Proteins - chemistry Milk, Human - chemistry Pregnancy Site-specific glycoproteomics Tandem Mass Spectrometry |
| Title | Quantitative label-free site-specific glycoproteomic analysis of the milk fat globule membrane protein in human colostrum and mature milk |
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