Post-Prandial Protein Handling: You Are What You

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Nov 10, 2015 - nine enrichment in the muscle free and muscle protein bound amino acid ... nylalanine hydroxylation (first step of phenylalanine conversion to tyrosine) ...... Epub. 2012/02/15. PMID: 22330017. Post-Prandial Stimulation of ...
RESEARCH ARTICLE

Post-Prandial Protein Handling: You Are What You Just Ate Bart B. L. Groen1,2, Astrid M. Horstman1,2, Henrike M. Hamer1,2, Michiel de Haan3, Janneau van Kranenburg2, Jörgen Bierau4, Martijn Poeze5, Will K. W. H. Wodzig6, Blake B. Rasmussen7, Luc J. C. van Loon1,2* 1 Top Institute Food and Nutrition, Wageningen, The Netherlands, 2 Department of Human Movement Sciences, Maastricht University Medical Centre, Maastricht, The Netherlands, 3 Department of Radiology, Maastricht University Medical Centre, Maastricht, The Netherlands, 4 Laboratory Biochemical Genetics, Department of Clinical Genetics, Maastricht University Medical Centre, Maastricht, The Netherlands, 5 Department of Surgery, Maastricht University Medical Centre, Maastricht, The Netherlands, 6 Central Diagnostic Laboratory, Maastricht University Medical Centre, Maastricht, The Netherlands, 7 Department of Nutrition and Metabolism, University of Texas Medical Branch, Galveston, Texas, United States of America * [email protected]

OPEN ACCESS Citation: Groen BBL, Horstman AM, Hamer HM, de Haan M, van Kranenburg J, Bierau J, et al. (2015) Post-Prandial Protein Handling: You Are What You Just Ate. PLoS ONE 10(11): e0141582. doi:10.1371/ journal.pone.0141582 Editor: Dylan Thompson, University of Bath, UNITED KINGDOM Received: April 16, 2015 Accepted: October 8, 2015 Published: November 10, 2015 Copyright: This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. Data Availability Statement: All relevant data are within the paper. Funding: This work was funded by TI Food and Nutrition, a public-private partnership on precompetitive research in food and nutrition. The researchers are responsible for the study design, data collection and analysis, decision to publish, and preparation of the manuscript. The industrial partners have contributed to the project through regular discussion. Funding was realized by TI Food and Nutrition: (http://www.tifn.nl/). The funders had no role in data collection and analysis, decision to publish, or preparation of the manuscript. The sponsors Danone,

Abstract Background Protein turnover in skeletal muscle tissue is highly responsive to nutrient intake in healthy adults.

Objective To provide a comprehensive overview of post-prandial protein handling, ranging from dietary protein digestion and amino acid absorption, the uptake of dietary protein derived amino acids over the leg, the post-prandial stimulation of muscle protein synthesis rates, to the incorporation of dietary protein derived amino acids in de novo muscle protein.

Design 12 healthy young males ingested 20 g intrinsically [1-13C]-phenylalanine labeled protein. In addition, primed continuous L-[ring-2H5]-phenylalanine, L-[ring-2H2]-tyrosine, and L-[1-13C]leucine infusions were applied, with frequent collection of arterial and venous blood samples, and muscle biopsies throughout a 5 h post-prandial period. Dietary protein digestion, amino acid absorption, splanchnic amino acid extraction, amino acid uptake over the leg, and subsequent muscle protein synthesis were measured within a single in vivo human experiment.

Results 55.3±2.7% of the protein-derived phenylalanine was released in the circulation during the 5 h post-prandial period. The post-prandial rise in plasma essential amino acid availability improved leg muscle protein balance (from -291±72 to 103±66 μMmin-1100 mL leg volume-1; P