and leucine, and caffeine resulted in improved high-intensity exercise performance ( Kackley et al., 2020 ). Unfortunately, the investigators used a water placebo, which is a limitation because caffeine is a well-established performance aid ( Grgic et al., 2020 ), even when consumed at low dosages
Manuel D. Quinones and Peter W.R. Lemon
Mark Messina, Heidi Lynch, Jared M. Dickinson, and Katharine E. Reed
of amino acids ( Devries & Phillips, 2015 ), that account for the greater effect of whey protein in comparison with soy protein on MPS. However, much of the difference between the two proteins is likely attributable to the higher leucine content of whey protein ( Norton et al., 2012 ; Tang et
Daniel L. Plotkin, Kenneth Delcastillo, Derrick W. Van Every, Kevin D. Tipton, Alan A. Aragon, and Brad J. Schoenfeld
Of the 20 amino acids recognized to compose the building blocks of human protein, only three possess a branched side chain: leucine, isoleucine, and valine. Numerous supplements are sold consisting of these three amino acids, collectively known as the branched-chain amino acids (BCAA), with claims
Adam D. Osmond, Dean J. Directo, Marcus L. Elam, Gabriela Juache, Vince C. Kreipke, Desiree E. Saralegui, Robert Wildman, Michael Wong, and Edward Jo
Of the 3 BCAA, leucine is evidently most contributory to this effect in muscle. Therefore, the speculation that supplementary leucine alone would likewise alleviate the symptoms of EIMD is within reason. 11 – 13 A limited amount of evidence demonstrates that supplementary leucine alone has only a
Jeferson L. Jacinto, João P. Nunes, Stefan H.M. Gorissen, Danila M.G. Capel, Andrea G. Bernardes, Alex S. Ribeiro, Edilson S. Cyrino, Stuart M. Phillips, and Andreo F. Aguiar
, 2018 ) and are crucial for muscle recovery and growth ( Hulmi et al., 2010 ; Shimomura & Kitaura, 2018 ; Shimomura et al., 2010 ). Moreover, the EAA leucine has been widely recognized as a direct stimulator of the mechanistic target of rapamycin (mTORC1; Blomstrand et al., 2006 ; Churchward
Louise M. Burke, Julie A Winter, David Cameron-Smith, Marc Enslen, Michelle Farnfield, and Jacques Decombaz
The authors undertook 2 crossover-designed studies to characterize plasma amino acid (AA) responses to the intake of 20 g of protein. In Study 1, 15 untrained and overnight-fasted subjects consumed 20 g protein from skim milk, soy milk, beefsteak, boiled egg, and a liquid meal supplement. In Study 2, 10 fasted endurance-trained subjects consumed 20 g protein from a protein-rich sports bar at rest and after a 60-min submaximal ride. Plasma AA concentrations were measured immediately before and for 180 min after food ingestion using a gas-chromatography flame-ionization detection technique. A pharmacokinetic analysis was undertaken for profiles of total AAs (TAA), essential AAs, branched-chain AAs (BCAA), and leucine. Although area-under-the-curve values for plasma TAA were similar across protein sources, the pattern of aminoacidemia showed robust differences between foods, with liquid forms of protein achieving peak concentrations twice as quickly after ingestion as solid protein-rich foods (e.g., ~50 min vs ~100 min) and skim milk achieving a significantly faster peak leucine concentration than all other foods (~25 min). Completing exercise before ingesting protein sources did not cause statistically significant changes in the pattern of delivery of key AAs, BCAAs, and leucine apart from a 20–40% increase in the rate of elimination. These results may be useful to plan the type and timing of intake of protein-rich foods to maximize the protein synthetic response to various stimuli such as exercise.
Jordan D. Philpott, Chris Donnelly, Ian H. Walshe, Elizabeth E. MacKinley, James Dick, Stuart D.R. Galloway, Kevin D. Tipton, and Oliver C. Witard
study was to investigate the impact of adding fish oil–derived n-3PUFA to a whey protein, leucine, and carbohydrate containing supplement over a six-week period on acute recovery from eccentric muscle damage in competitive soccer players. Rationale for combining n-3PUFA with whey protein, leucine, and
Sharon L. Miller, P. Courtney Gaine, Carl M. Maresh, Lawrence E. Armstrong, Cara B. Ebbeling, Linda S. Lamont, and Nancy R. Rodriguez
This study determined the effect of nutritional supplementation throughout endurance exercise on whole-body leucine kinetics (leucine rate of appearance [Ra], oxidation [Ox], and nonoxidative leucine disposal [NOLD]) during recovery. Five trained men underwent a 2-h run at 65% VO2max, during which a carbohydrate (CHO), mixed protein-carbohydrate (milk), or placebo (PLA) drink was consumed. Leucine kinetics were assessed during recovery using a primed, continuous infusion of 1-13C leucine. Leucine Ra and NOLD were lower for milk than for PLA. Ox was higher after milk-supplemented exercise than after CHO or PLA. Although consuming milk during the run affected whole-body leucine kinetics, the benefits of such a practice for athletes remain unclear. Additional studies are needed to determine whether protein supplementation during exercise can optimize protein utilization during recovery.
Theocharis Ispoglou, Roderick F.G.J. King, Remco C.J. Polman, and Cathy Zanker
To investigate the effects of daily oral L-leucine ingestion on strength, bone mineral-free lean tissue mass (LTM) and fat mass (FM) of free living humans during a 12-wk resistance-training program.
Twenty-six initially untrained men (n = 13 per group) ingested either 4 g/d of L-leucine (leucine group: age 28.5 ± 8.2 y, body mass index 24.9 ± 4.2 kg/m2) or a corresponding amount of lactose (placebo group: age 28.2 ± 7.3 y, body mass index 24.9 ± 4.2 kg/m2). All participants trained under supervision twice per week following a prescribed resistance training program using eight standard exercise machines. Testing took place at baseline and at the end of the supplementation period. Strength on each exercise was assessed by fve repetition maximum (5-RM), and body composition was assessed by dual energy X-ray absorptiometry (DXA).
The leucine group demonstrated significantly higher gains in total 5-RM strength (sum of 5-RM in eight exercises) and 5-RM strength in five out of the eight exercises (P < .05). The percentage total 5-RM strength gains were 40.8% (± 7.8) and 31.0% (± 4.6) for the leucine and placebo groups respectively. Significant differences did not exist between groups in either total percentage LTM gains or total percentage FM losses (LTM: 2.9% ± 2.5 vs 2.0% ± 2.1, FM: 1.6% ± 15.6 vs 1.1% ± 7.6).
These results suggest that 4 g/d of L-leucine supplementation may be used as a nutritional supplement to enhance strength performance during a 12-week resistance training program of initially untrained male participants.
Thomas B. Walker, Jessica Smith, Monica Herrera, Breck Lebegue, Andrea Pinchak, and Joseph Fischer
The purpose of this study was to investigate the ability of whey-protein and leucine supplementation to enhance physical and cognitive performance and body composition. Thirty moderately fit participants completed a modified Air Force fitness test, a computer-based cognition test, and a dual-energy X-ray-absorptiometry scan for body composition before and after supplementing their daily diet for 8 wk with either 19.7 g of whey protein and 6.2 g leucine (WPL) or a calorie-equivalent placebo (P). Bench-press performance increased significantly from Week 1 to Week 8 in the WPL group, whereas the increase in the P group was not significant. Push-up performance increased significantly for WPL, and P showed a nonsignificant increase. Total mass, fat-free mass, and lean body mass all increased significantly in the WPL group but showed no change in the P group. No differences were observed within or between groups for crunches, chin-ups, 3-mile-run time, or cognition. The authors conclude that supplementing with whey protein and leucine may provide an advantage to people whose performance benefits from increased upper body strength and/or lean body mass.