Time-dependent regulation of postprandial muscle protein synthesis rates after milk protein ingestion in young men

被引:20
作者
van Vliet, Stephan [1 ]
Reals, Joseph W. [2 ]
Holwerda, Andrew M. [3 ]
Emmons, Russell S. [2 ]
Goessens, Joy P. [3 ]
Paluska, Scott A. [4 ]
De Lisio, Michael [5 ,6 ]
van Loon, Luc J. C. [3 ]
Burd, Nicholas A. [1 ,2 ]
机构
[1] Univ Illinois, Dept Kinesiol & Community Hlth, 352 Louise Freer Hall,906 S Goodwin Ave, Urbana, IL 61801 USA
[2] Univ Illinois, Div Nutr Sci, Urbana, IL 61801 USA
[3] Maastricht Univ, NUTRIM Sch Nutr & Translat Res Metab, Maastricht, Netherlands
[4] Univ Illinois, Dept Family Med, Urbana, IL 61801 USA
[5] Univ Ottawa, Sch Human Kinet, Ottawa, ON, Canada
[6] Univ Ottawa, Dept Cellular & Mol Med, Ottawa, ON, Canada
关键词
anabolic signaling; leucine; mammalian target of rapamycin; muscle mass regulation; nutrition; INTRINSICALLY LABELED MILK; RESISTANCE EXERCISE; GREATER STIMULATION; IN-VIVO; REST; DIGESTION; MYOFIBRILLAR; HYDROLYSATE; ABSORPTION; PROVIDES;
D O I
10.1152/japplphysiol.00608.2019
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
The anabolic action of "fast" whey protein on the regulation of postprandial muscle protein synthesis has been established to be short-lived in healthy young adults. We assessed the time course of anabolic signaling activation and stimulation of myofibrillar protein synthesis rates (MPS) after ingestion of a food source that represents a more typical meal-induced pattern of aminoacidemia. Seven young men (age: 22 +/- 1 y) underwent repeated blood and biopsy sampling during primed, continuous L-[ring(2)H(5)]phenylalanine and L-[1-C-13]leucine tracer infusions and ingested 38 g of L-[1-C-13]phenylalanine- and L-[1-C-13]leucine-labeled milk protein concentrate. A total of similar to 27 +/- 4 (similar to 10 g) and similar to 31 +/- 1% (similar to 12 g) of dietary protein-derived amino acids were released in circulation between 0 and 120 min and 120-300 min, respectively, of the postprandial period. L-[ring-H-2(5)]phenylalanine-based MPS increased above basal (0.025 +/- 0.008%/h) by similar to 75% (0.043 +/- 0.009%/h; P = 0.05) between 0 and 120 min and by similar to 86% (0.046 +/- 0.004%/h; P = 0.02) between 120 and 300 min, respectively. L-[1-C-13]leucine-based MPS increased above basal (0.027 +/- 0.002%/h) by similar to 72% (0.051 +/- 0.016%/h; P = 0.10) between 0 and 120 min and by similar to 62% (0.047 +/- 0.004%/h; P = 0.001) between 120 and 300 min, respectively. Myofibrillar protein-bound L-[1-C-13]phenylalanine increased over time (P < 0.001) and equaled 0.004 +/- 0.001, 0.008 +/- 0.002, 0.017 +/- 0.004, and 0.020 +/- 0.003 mole percent excess at 60, 120, 180, and 300 min, respectively, of the postprandial period. Milk protein ingestion increased mTORC1 phosphorylation at 120, 180, and 300 min of the postprandial period (all P < 0.05). Our results show that ingestion of 38 g of milk protein results in sustained increases in MPS throughout a 5-h postprandial period in healthy young men. NEW & NOTEWORTHY The stimulation of muscle protein synthesis after whey protein ingestion is short-lived due to its transient systemic appearance of amino acids. Our study characterized the muscle anabolic response to a protein source that results in a more gradual release of amino acids into circulation. Our work demonstrates that a sustained increase in postprandial plasma amino acid availability after milk protein ingestion results in a prolonged stimulation of muscle protein synthesis rates in healthy young men.
引用
收藏
页码:1792 / 1801
页数:10
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