Whey and casein labeled withl-[1-13C]leucine and muscle protein synthesis: effect of resistance exercise and protein ingestion

Author:

Reitelseder Søren1,Agergaard Jakob1,Doessing Simon1,Helmark Ida C.1,Lund Peter2,Kristensen Niels B.2,Frystyk Jan3,Flyvbjerg Allan3,Schjerling Peter1,van Hall Gerrit4,Kjaer Michael1,Holm Lars1

Affiliation:

1. Institute of Sports Medicine Copenhagen, Department of Orthopedic Surgery M, Bispebjerg Hospital and Center for Healthy Aging, Faculty of Health Sciences, University of Copenhagen, Copenhagen;

2. Department of Animal Health and Bioscience, Faculty of Agricultural Sciences, Aarhus University, Tjele;

3. The Medical Research Laboratories, Clinical Institute and Department of Endocrinology and Internal Medicine, Aarhus University Hospital, Aarhus; and

4. Department of Biomedical Sciences, Faculty of Health Sciences, University of Copenhagen and Metabolic Mass Spectrometry Facility, Rigshospitalet, Copenhagen, Denmark

Abstract

Muscle protein turnover following resistance exercise and amino acid availability are relatively well described. By contrast, the beneficial effects of different sources of intact proteins in relation to exercise need further investigation. Our objective was to compare muscle anabolic responses to a single bolus intake of whey or casein after performance of heavy resistance exercise. Young male individuals were randomly assigned to participate in two protein trials ( n = 9) or one control trial ( n = 8). Infusion of l-[1-13C]leucine was carried out, and either whey, casein (0.3 g/kg lean body mass), or a noncaloric control drink was ingested immediately after exercise. l-[1-13C]leucine-labeled whey and casein were used while muscle protein synthesis (MPS) was assessed. Blood and muscle tissue samples were collected to measure systemic hormone and amino acid concentrations, tracer enrichments, and myofibrillar protein synthesis. Western blots were used to investigate the Akt signaling pathway. Plasma insulin and branched-chain amino acid concentrations increased to a greater extent after ingestion of whey compared with casein. Myofibrillar protein synthesis was equally increased 1–6 h postexercise after whey and casein intake, both of which were higher compared with control ( P < 0.05). Phosphorylation of Akt and p70S6Kwas increased after exercise and protein intake ( P < 0.05), but no differences were observed between the types of protein except for total 4E-BP1, which was higher after whey intake than after casein intake ( P < 0.05). In conclusion, whey and casein intake immediately after resistance exercise results in an overall equal MPS response despite temporal differences in insulin and amino acid concentrations and 4E-BP1.

Publisher

American Physiological Society

Subject

Physiology (medical),Physiology,Endocrinology, Diabetes and Metabolism

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