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- Title
Monitoring Human Milk β-Casein Phosphorylation and O -Glycosylation Over Lactation Reveals Distinct Differences between the Proteome and Endogenous Peptidome.
- Authors
Dingess, Kelly A.; Gazi, Inge; van den Toorn, Henk W. P.; Mank, Marko; Stahl, Bernd; Reiding, Karli R.; Heck, Albert J. R.
- Abstract
Human milk is a vital biofluid containing a myriad of molecular components to ensure an infant's best start at a healthy life. One key component of human milk is β-casein, a protein which is not only a structural constituent of casein micelles but also a source of bioactive, often antimicrobial, peptides contributing to milk's endogenous peptidome. Importantly, post-translational modifications (PTMs) like phosphorylation and glycosylation typically affect the function of proteins and peptides; however, here our understanding of β-casein is critically limited. To uncover the scope of proteoforms and endogenous peptidoforms we utilized mass spectrometry (LC-MS/MS) to achieve in-depth longitudinal profiling of β-casein from human milk, studying two donors across 16 weeks of lactation. We not only observed changes in β-casein's known protein and endogenous peptide phosphorylation, but also in previously unexplored O-glycosylation. This newly discovered PTM of β-casein may be important as it resides on known β-casein-derived antimicrobial peptide sequences.
- Subjects
BREAST milk; COMPOSITION of breast milk; LACTATION; INFANTS' supplies; AMINO acid sequence; POST-translational modification; MASS spectrometry
- Publication
International Journal of Molecular Sciences, 2021, Vol 22, Issue 15, p8140
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms22158140