scholarly journals Novel Essential Amino Acid Supplements Following Resistance Exercise Induce Aminoacidemia and Enhance Anabolic Signaling Irrespective of Age: A Proof-of-Concept Trial

Nutrients ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 2067
Author(s):  
Matthew J. Lees ◽  
Oliver J. Wilson ◽  
Erin K. Webb ◽  
Daniel A. Traylor ◽  
Todd Prior ◽  
...  

We investigated the effects of ingesting a leucine-enriched essential amino acid (EAA) gel alone or combined with resistance exercise (RE) versus RE alone (control) on plasma aminoacidemia and intramyocellular anabolic signaling in healthy younger (28 ± 4 years) and older (71 ± 3 years) adults. Blood samples were obtained throughout the three trials, while muscle biopsies were collected in the postabsorptive state and 2 h following RE, following the consumption of two 50 mL EAA gels (40% leucine, 15 g total EAA), and following RE with EAA (combination (COM)). Protein content and the phosphorylation status of key anabolic signaling proteins were determined via immunoblotting. Irrespective of age, during EAA and COM peak leucinemia (younger: 454 ± 32 µM and 537 ± 111 µM; older: 417 ± 99 µM and 553 ± 136 µM) occurred ~60–120 min post-ingestion (younger: 66 ± 6 min and 120 ± 60 min; older: 90 ± 13 min and 78 ± 12 min). In the pooled sample, the area under the curve for plasma leucine and the sum of branched-chain amino acids was significantly greater in EAA and COM compared with RE. For intramyocellular signaling, significant main effects were found for condition (mTOR (Ser2481), rpS6 (Ser235/236)) and age (S6K1 (Thr421/Ser424), 4E-BP1 (Thr37/46)) in age group analyses. The phosphorylation of rpS6 was of similar magnitude (~8-fold) in pooled and age group data 2 h following COM. Our findings suggest that a gel-based, leucine-enriched EAA supplement is associated with aminoacidemia and a muscle anabolic signaling response, thus representing an effective means of stimulating muscle protein anabolism in younger and older adults following EAA and COM.

2009 ◽  
Vol 106 (5) ◽  
pp. 1730-1739 ◽  
Author(s):  
Satoshi Fujita ◽  
Hans C. Dreyer ◽  
Micah J. Drummond ◽  
Erin L. Glynn ◽  
Elena Volpi ◽  
...  

Ingestion of an essential amino acid-carbohydrate (EAA + CHO) solution following resistance exercise enhances muscle protein synthesis during postexercise recovery. It is unclear whether EAA + CHO ingestion before resistance exercise can improve direct measures of postexercise muscle protein synthesis (fractional synthetic rate; FSR). We hypothesized that EAA + CHO ingestion before a bout of resistance exercise would prevent the exercise-induced decrease in muscle FSR and would result in an enhanced rate of muscle FSR during postexercise recovery. We studied 22 young healthy subjects before, during, and for 2 h following a bout of high-intensity leg resistance exercise. The fasting control group ( n = 11) did not ingest nutrients, and the EAA + CHO group ( n = 11) ingested a solution of EAA + CHO 1 h before beginning the exercise bout. Stable isotopic methods were used in combination with muscle biopsies to determine FSR. Immunoblotting procedures were utilized to assess cell signaling proteins associated with the regulation of FSR. We found that muscle FSR increased in the EAA + CHO group immediately following EAA + CHO ingestion ( P < 0.05), returned to basal values during exercise, and remained unchanged at 1 h postexercise. Muscle FSR decreased in the fasting group during exercise and increased at 1 h postexercise ( P < 0.05). However, the 2 h postexercise FSR increased by ∼50% in both groups with no differences between groups ( P > 0.05). Eukaryotic elongation factor 2 phosphorylation was reduced in both groups at 2 h postexercise (EAA + CHO: 39 ± 7%; fasting: 47 ± 9%; P < 0.05). We conclude that EAA + CHO ingestion before resistance exercise does not enhance postexercise FSR compared with exercise without nutrients.


1989 ◽  
Vol 77 (3) ◽  
pp. 329-336 ◽  
Author(s):  
Peter J. Garlick ◽  
Jan Wernerman ◽  
Margaret A. McNurlan ◽  
Pia Essen ◽  
Gerald E. Lobley ◽  
...  

1. The ‘flooding dose’ technique for measuring the rate of protein synthesis in tissues in vivo involves the injection of a large amount of unlabelled amino acid together with the tracer to minimize differences in isotopic enrichment of the free amino acid in plasma and tissue compartments. This approach has been investigated in human muscle by taking biopsies from postabsorptive male volunteers given [1-13C]leucine. 2. Intravenous injection of 4 g of unlabelled leucine resulted in a rapid rise in free leucine concentration of seven- to eleven-fold in plasma and five-fold in muscle. Values were still elevated by two-fold after 2 h. 3. Five minutes after injection of [1-13C]leucine (0.05 g/kg) the isotopic enrichment of plasma leucine was 82% that of the injected material, falling to 44% at 120 min. The enrichment of free leucine in sequential muscle biopsies was close to that in plasma and almost identical to that for plasma α-ketoisocaproate. 4. The rate of protein synthesis was determined from the increase in leucine enrichment in protein of muscle biopsies taken before and 90 min after injection of [1-13C]leucine (0.05 g/kg; 19 or 39 atom% excess) and the average plasma α-ketoisocaproate enrichment over this period (taken to represent muscle free leucine). The mean rate of muscle protein synthesis in 10 subjects was 1.95 (sem 0.12)%/day. Rates of protein synthesis calculated from plasma leucine as precursor enrichment were only 5% lower than those calculated from plasma α-ketoisocaproate. 5. It is concluded that a ‘flooding dose’ of 13C-labelled amino acid is a useful and convenient technique for determining the rate of protein synthesis in tissues of human volunteers and patients.


2019 ◽  
Vol 44 (11) ◽  
pp. 1141-1149 ◽  
Author(s):  
Mathew Butterworth ◽  
Matthew Lees ◽  
Paul Harlow ◽  
Karen Hind ◽  
Lauren Duckworth ◽  
...  

Deficiencies in protein and energy intakes are partly responsible for age-related sarcopenia. We investigated the effects of supplements matched in essential amino acid (EAA) content (7.5 g) on energy intake and appetite. Ten women aged 69.2 ± 2.7 years completed 3 trials in a randomised, crossover design. Composite appetite scores, peptide-YY (PYY), and insulin responses to a 200-mL whey protein (WP) isolate (275 kJ), a 50-mL EAA gel (GEL, 478 kJ), or nothing as the control (CON) condition were investigated over 1 h, followed by an ad libitum breakfast. Energy intake at breakfast (CON, 1957 ± 713; WP, 1413 ± 623; GEL, 1963 ± 611 kJ) was higher in CON and GEL than in WP (both P = 0.006). After accounting for supplement energy content, energy intake in GEL was higher than in CON (P = 0.0006) and WP (P = 0.0008). Time-averaged area under the curve for composite appetite scores (CON, 74 ± 20; WP, 50 ± 22; GEL, 60 ± 16 mm) was higher in CON than WP (P = 0.015). Time-averaged area under the curve for PYY (CON, 87 ± 13; WP, 119 ± 27; GEL, 97 ± 22 pg·mL−1) was higher in WP than CON (P = 0.009) and GEL (P = 0.012). In conclusion, supplementation with WP facilitated an increase in protein intake, whereas supplementation with GEL increases in both energy and protein intakes, when consumed before an ad libitum breakfast. Such findings highlight potential gel-based EAA supplementation intake for addressing age-related sarcopenia.


2007 ◽  
Vol 17 (6) ◽  
pp. 608-623 ◽  
Author(s):  
Nicholas A. Ratamess ◽  
Jay R. Hoffman ◽  
Ryan Ross ◽  
Miles Shanklin ◽  
Avery D. Faigenbaum ◽  
...  

The authors aimed to examine the acute hormonal and performance responses to resistance exercise with and without prior consumption of an amino acid/creatine/energy supplement. Eight men performed a resistance-exercise protocol at baseline (BL), 20 min after consuming a supplement (S) consisting of essential amino acids, creatine, taurine, caffeine, and glucuronolactone or a maltodextrin placebo (P). Venous blood samples were obtained before and immediately after (IP), 15 min (15P), and 30 min (30P) after each protocol. Area under the curve of resistance-exercise volume revealed that BL was significantly less than S (10%) and P (8.6%). For fatigue rate, only S (18.4% ± 12.0%) was significantly lower than BL (32.9% ± 8.4%). Total testosterone (TT) and growth hormone (GH) were significantly elevated at IP and 15P in all conditions. The GH response was significantly lower, however, in S and P than in BL. The TT and GH responses did not differ between S and P. These results indicated that a supplement consisting of amino acids, creatine, taurine, caffeine, and glucuronolactone can modestly improve high-intensity endurance; however, the anabolic-hormonal response was not augmented.


1988 ◽  
Vol 254 (2) ◽  
pp. 579-584 ◽  
Author(s):  
P J Garlick ◽  
I Grant

Rates of muscle protein synthesis were measured in vivo in tissues of post-absorptive young rats that were given intravenous infusions of various combinations of insulin and amino acids. In the absence of amino acid infusion, there was a steady rise in muscle protein synthesis with plasma insulin concentration up to 158 mu units/ml, but when a complete amino acids mixtures was included maximal rates were obtained at 20 mu units/ml. The effect of the complete mixture could be reproduced by a mixture of essential amino acids or of branched-chain amino acids, but not by a non-essential mixture, alanine, methionine or glutamine. It is concluded that amino acids, particularly the branched-chain ones, increase the sensitivity of muscle protein synthesis to insulin.


2005 ◽  
Vol 288 (5) ◽  
pp. E914-E921 ◽  
Author(s):  
Jeffery Escobar ◽  
Jason W. Frank ◽  
Agus Suryawan ◽  
Hanh V. Nguyen ◽  
Scot R. Kimball ◽  
...  

Protein synthesis in skeletal muscle of adult rats increases in response to oral gavage of supraphysiological doses of leucine. However, the effect on protein synthesis of a physiological rise in plasma leucine has not been investigated in neonates, an anabolic population highly sensitive to amino acids and insulin. Therefore, in the current study, fasted pigs were infused intra-arterially with leucine (0, 200, or 400 μmol·kg−1·h−1), and protein synthesis was measured after 60 or 120 min. Protein synthesis was increased in muscle, but not in liver, at 60 min. At 120 min, however, protein synthesis returned to baseline levels in muscle but was reduced below baseline values in liver. The increase in protein synthesis in muscle was associated with increased plasma leucine of 1.5- to 3-fold and no change in plasma insulin. Leucine infusion for 120 min reduced plasma essential amino acid levels. Phosphorylation of eukaryotic initiation factor (eIF)-4E-binding protein-1 (4E-BP1), ribosomal protein (rp) S6 kinase, and rpS6 was increased, and the amount of eIF4E associated with its repressor 4E-BP1 was reduced after 60 and 120 min of leucine infusion. No change in these biomarkers of mRNA translation was observed in liver. Thus a physiological increase in plasma leucine stimulates protein synthesis in skeletal muscle of neonatal pigs in association with increased eIF4E availability for eIF4F assembly. This response appears to be insulin independent, substrate dependent, and tissue specific. The results suggest that the branched-chain amino acid leucine can act as a nutrient signal to stimulate protein synthesis in skeletal muscle of neonates.


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