Title: Glycoprotein expression in human milk during lactation.

Authors: Froehlich, John W; Dodds, Eric D; Barboza, Mariana; McJimpsey, Erica L; Seipert, Richard R; Francis, Jimi; An, Hyun Joo; Freeman, Samara; German, J Bruce; Lebrilla, Carlito B

Published In J Agric Food Chem, (2010 May 26)

Abstract: While milk proteins have been studied for decades, strikingly little effort has been applied to determining how the post-translational modifications (PTMs) of these proteins may change during the course of lactation. PTMs, particularly glycosylation, can greatly influence protein structure, function, and stability and can particularly influence the gut where their degradation products are potentially bioactive. In this work, previously undiscovered temporal variations in both expression and glycosylation of the glycoproteome of human milk are observed. Lactoferrin, one of the most abundant glycoproteins in human milk, is shown to be dynamically glycosylated during the first 10 days of lactation. Variations in expression or glycosylation levels are also demonstrated for several other abundant whey proteins, including tenascin, bile salt-stimulated lipase, xanthine dehydrogenase, and mannose receptor.

PubMed ID: 20415418

MeSH Terms: Electrophoresis, Polyacrylamide Gel; Female; Glycoproteins/analysis*; Glycoproteins/metabolism; Glycosylation; Humans; Lactation/metabolism*; Lactoferrin/analysis; Lactoferrin/metabolism; Milk Proteins/analysis*; Milk Proteins/metabolism; Milk, Human/chemistry*; Protein Processing, Post-Translational; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Time Factors