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Glycoprotein expression in human milk during lactation
John W Froehlich1, Eric D Dodds, Mariana Barboza
1Department of Chemistry, University of California, Davis, California 95616, USA.
Journal of Agricultural and Food Chemistry
|April 27, 2010
Summary
This study reveals new temporal changes in human milk protein glycosylation during early lactation. These findings highlight dynamic shifts in milk glycoproteome, impacting protein function and bioactive potential.
Area of Science:
- Biochemistry
- Proteomics
- Human Milk Studies
Background:
- Milk proteins are extensively studied, but their post-translational modifications (PTMs) during lactation remain under-explored.
- PTMs, especially glycosylation, significantly affect protein properties and the bioactivity of their degradation products in the infant gut.
Purpose of the Study:
- To investigate temporal variations in the expression and glycosylation of human milk proteins throughout lactation.
- To identify changes in the human milk glycoproteome during the early stages of lactation.
Main Methods:
- Analysis of human milk samples collected during the first 10 days of lactation.
- Proteomic techniques to assess protein expression levels.
- Glycosylation analysis to determine modifications on milk glycoproteins.
Main Results:
- Discovery of previously unknown temporal variations in both expression and glycosylation of the human milk glycoproteome.
- Demonstration of dynamic glycosylation changes in lactoferrin within the first 10 days of lactation.
- Observed variations in expression or glycosylation for other key whey proteins like tenascin and bile salt-stimulated lipase.
Conclusions:
- Human milk protein expression and glycosylation exhibit significant temporal dynamics during early lactation.
- These dynamic changes in the glycoproteome may influence the functional properties and bioactivity of milk proteins.
- Further research into lactation-induced PTM variations is warranted to understand their full impact.
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