Protein blend ingestion following resistance exercise promotes human muscle protein synthesis.
High-quality proteins such as soy, whey, and casein are all capable of promoting muscle protein synthesis postexercise by activating the mammalian target of rapamycin (mTORC1) signaling pathway. We hypothesized that a protein blend of soy and dairy proteins would capitalize on the unique properties of each individual protein and allow for optimal delivery of amino acids to prolong the fractional synthetic rate (FSR) following resistance exercise (RE). In this double-blind, randomized, clinical trial, 19 young adults were studied before and after ingestion of ∼19 g of protein blend (PB) or ∼18 g whey protein (WP) consumed 1 h after high-intensity leg RE. We examined mixed-muscle protein FSR by stable isotopic methods and mTORC1 signaling with western blotting. Muscle biopsies from the vastus lateralis were collected at rest (before RE) and at 3 postexercise time points during an early (0-2 h) and late (2-4 h) postingestion period. WP ingestion resulted in higher and earlier amplitude of blood branched-chain amino acid (BCAA) concentrations. PB ingestion created a lower initial rise in blood BCAA but sustained elevated levels of blood amino acids later into recovery (P < 0.05). Postexercise FSR increased equivalently in both groups during the early period (WP, 0.078 ± 0.009%; PB, 0.088 ± 0.007%); however, FSR remained elevated only in the PB group during the late period (WP, 0.074 ± 0.010%; PB, 0.087 ± 0.003%) (P < 0.05). mTORC1 signaling similarly increased between groups, except for no increase in S6K1 phosphorylation in the WP group at 5 h postexercise (P < 0.05). We conclude that a soy-dairy PB ingested following exercise is capable of prolonging blood aminoacidemia, mTORC1 signaling, and protein synthesis in human skeletal muscle and is an effective postexercise nutritional supplement.
Division of Rehabilitation Sciences, University of Texas Medical Branch, Galveston, TX, USA.
Paul T
PT
Reidy
Dillon K
DK
Walker
Jared M
JM
Dickinson
David M
DM
Gundermann
Micah J
MJ
Drummond
Kyle L
KL
Timmerman
Christopher S
CS
Fry
Michael S
MS
Borack
Mark B
MB
Cope
Ratna
R
Mukherjea
Kristofer
K
Jennings
Elena
E
Volpi
Blake B
BB
Rasmussen
D000293:Adolescent; D000328:Adult; D000597:Amino Acids, Branched-Chain / Q000097:blood; D002364:Caseins / Q000008:administration & dosage; D004044:Dietary Proteins / Q000008:administration & dosage*; D019587:Dietary Supplements; D004311:Double-Blind Method; D015444:Exercise / Q000502:physiology*; D005260:Female; D006801:Humans; D007553:Isotope Labeling; D007700:Kinetics; D008297:Male; D000076222:Mechanistic Target of Rapamycin Complex 1; D008894:Milk Proteins / Q000008:administration & dosage; D046912:Multiprotein Complexes / Q000378:metabolism; D009124:Muscle Proteins / Q000096:biosynthesis*; D055070:Resistance Training; D015398:Signal Transduction; D030262:Soybean Proteins / Q000008:administration & dosage; D058570:TOR Serine-Threonine Kinases / Q000378:metabolism; D000067816:Whey Proteins; D055815:Young Adult
D000597:Amino Acids, Branched-Chain; D002364:Caseins; D004044:Dietary Proteins; D008894:Milk Proteins; D046912:Multiprotein Complexes; D009124:Muscle Proteins; D030262:Soybean Proteins; D000067816:Whey Proteins; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases