Related Experiment Video
Updated: Jun 14, 2025

Skeletal Muscle Gender Dimorphism from Proteomics
Published on: December 14, 2011
Milk Protein Glycation Compromises Postprandial Lysine Bioavailability but does not Modulate Postprandial Muscle
Glenn Aa van Lieshout1, Jorn Trommelen2, Floris K Hendriks2
1Department of Human Biology, NUTRIM Institute of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre+, Maastricht, the Netherlands; FrieslandCampina, Amersfoort, the Netherlands.
Background:
Industrial processing and storage of milk products can strongly increase protein glycation level. Previously, we have reported that a high protein glycation level impairs protein digestion, thereby compromising lysine bioavailability. The lower postprandial lysine availability may restrict the anabolic properties of a high glycated protein.
Objectives:
The objective of this study was to assess the impact of milk protein glycation on postprandial plasma amino acid availability and subsequent postprandial muscle protein synthesis rates during recovery from a single bout of resistance-type exercise.
Methods:
Forty-five recreationally active, healthy young males participated in this double-blinded, randomized parallel study. After performing a single bout of whole-body resistance-type exercise, subjects ingested 20 g milk protein with either a low (4%; LOW-GLYC) or high (47%; HIGH-GLYC) glycation level or a noncaloric placebo (PLA). Continuous intravenous infusion of L-[ring-13C6]-phenylalanine was combined with the collection of blood and muscle tissue samples during a 6-h postprandial period to assess plasma amino acid concentrations and muscle protein synthesis rates.
Results:
Protein ingestion increased plasma total and essential amino acid concentrations compared with placebo (time × treatment interaction: P < 0.001), with no differences between the low and high glycated milk protein. Plasma lysine availability, assessed over the full 6 h postprandial period, was substantially lower following ingestion of the protein with the high versus low glycation level (-5 ± 7 compared with 10 ± 9 mmol · L-1 · 360 min, respectively, P < 0.001). Postprandial muscle protein synthesis rates did not differ between treatments (0.059 ± 0.016, 0.061 ± 0.012, and 0.061 ± 0.018 % · h-1, in LOW-GLYC, HIGH-GLYC and PLA, respectively, P = 0.939).
Conclusions:
Ingestion of protein with a higher glycation level attenuates postprandial plasma lysine availability. Milk protein glycation does not modulate postprandial muscle protein synthesis rates during recovery from resistance exercise in healthy, young males. This trial was registered at the Dutch Trial Register as NL8690; https://onderzoekmetmensen.nl/nl/trial/49398.
More Related Videos
08:01Measurement of Insulin- and Contraction-Stimulated Glucose Uptake in Isolated and Incubated Mature Skeletal Muscle from Mice
Published on: May 16, 2021
08:04Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
Published on: October 23, 2018
Related Concept Videos
Overview of Protein Metabolism
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Protein Glycosylation
Glycosylation occurs in...
Proteins: Dietary Sources and Requirements
Muscle Recovery and Fatigue
Proteoglycans
Metabolic States of the Body: The Absorptive State