4.6 Article

Quantitative Label-Free Proteomic Analysis of Milk Fat Globule Membrane in Donkey and Human Milk

Journal

FRONTIERS IN NUTRITION
Volume 8, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fnut.2021.670099

Keywords

human; donkey; quantitative proteomic; comparison; milk fat globule membrane

Funding

  1. Open Project of Shandong Collaborative Innovation Center for Donkey Industry Technology [3193308]
  2. Agriculture Improved Varieties Project of Shandong Province, China [2017LZGC020]
  3. Beijing Agricultural Forestry Academy Youth Fund [QNJJ201930]

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Previous studies have suggested that donkey milk shares similar compositions with human milk and could be a hypoallergenic alternative for infants with cow's milk allergy. This study used label-free proteomics to compare differentially expressed milk fat globule membrane (MFGM) proteins in donkey milk and human milk, identifying differences in immune system regulation, membrane invagination, and lymphocyte activation. The findings contribute to understanding the biological functions and potentially valuable information for nutritional quality assessment.
Previous studies have found donkey milk (DM) has the similar compositions with human milk (HM) and could be used as a potential hypoallergenic replacement diet for babies suffering from cow's milk allergy. Milk fat globule membrane (MFGM) proteins are involved in many biological functions, behaving as important indicators of the nutritional quality of milk. In this study, we used label-free proteomics to quantify the differentially expressed MFGM proteins (DEP) between DM (in 4-5 months of lactation) and HM (in 6-8 months of lactation). In total, 293 DEP were found in these two groups. Gene Ontology (GO) enrichment analysis revealed that the majority of DEP participated in regulation of immune system process, membrane invagination and lymphocyte activation. Several significant Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways were determined for the DEP, such as lysosome, galactose metabolism and peroxisome proliferator-activated receptor (PPAR) signaling pathway. Our study may provide valuable information in the composition of MFGM proteins in DM and HM, and expand our knowledge of different biological functions between DM and HM.

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