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Essential amino acid-enriched meal replacement promotes superior net protein balance in older, overweight adults.

ABSTRACT: BACKGROUND & AIMS:Older individuals are susceptible to the loss of muscle and accumulation of fat. To address this problem, we have compared protein kinetics following consumption of an essential amino acid (EAA)-enriched meal replacement (EMR) to consumption of a high-protein meal replacement beverage (Bariatric Advantage, BA) using stable isotope methodology. METHODS:Eight older (67 ± 2), obese (35 ± 2 kg/m²) female and male participants completed two studies using a randomized, crossover design in which they ingested each meal replacement. The isotopic tracers L-[²H₅]phenylalanine & L-[²H₂]tyrosine were delivered via primed, continuous intravenous infusion throughout a basal period and following consumption of EMR or BA. We determined changes in whole body protein synthesis (PS), protein breakdown (PB), and net protein balance (NB) from fasted states via analysis of plasma samples by LC-ESI-MS. RESULTS:PS was higher (P = 0.03) and PB was less (P = 0.005) with EMR in comparison to BA. As a result, NB was much greater (P = 0.00003) following the ingestion of EMR as compared to BA. CONCLUSIONS:In comparison with BA, which has a higher amount of intact protein that any other meal replacement, EMR promoted a greater increment in NB. These data support the potential efficacy of EMR as a meal replacement for the preservation of lean tissue mass during weight loss in older, overweight individuals.

SUBMITTER: Coker RH

PROVIDER: S-EPMC6588419 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Essential amino acid-enriched meal replacement promotes superior net protein balance in older, overweight adults.

Coker Robert H RH Shin Kenneth K Scholten Kristen K Johannsen Michelle M Tsigonis Jean J Kim Il-Young IY Schutzler Scott E SE Wolfe Robert R RR

Clinical nutrition (Edinburgh, Scotland) 20181219 6

<h4>Background & aims</h4>Older individuals are susceptible to the loss of muscle and accumulation of fat. To address this problem, we have compared protein kinetics following consumption of an essential amino acid (EAA)-enriched meal replacement (EMR) to consumption of a high-protein meal replacement beverage (Bariatric Advantage, BA) using stable isotope methodology.<h4>Methods</h4>Eight older (67 ± 2), obese (35 ± 2 kg/m<sup>2</sup>) female and male participants completed two studies using a ...[more]

PMID: 30638738

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Project description:BackgroundThe effects of ingesting varying essential amino acid (EAA)/protein-containing food formats on protein kinetics during energy deficit are undetermined. Therefore, recommendations for EAA/protein food formats necessary to optimize both whole-body protein balance and muscle protein synthesis (MPS) during energy deficit are unknown. We measured protein kinetics after consuming iso-nitrogenous amounts of free-form essential amino acid-enriched whey (EAA?+?W; 34.7?g protein, 24?g EAA sourced from whey and free-form EAA), whey (WHEY; 34.7?g protein, 18.7?g EAA), or a mixed-macronutrient meal (MEAL; 34.7?g protein, 11.4?g EAA) after exercise during short-term energy deficit.MethodsTen adults (mean?±?SD; 21?±?4 y; 25.7?±?1.7?kg/m2) completed a randomized, double-blind crossover study consisting of three, 5 d energy-deficit periods (-?30?±?3% of total energy requirements), separated by 14 d. Whole-body protein synthesis (PS), breakdown (PB), and net balance (NET) were determined at rest and in response to combination exercise consisting of load carriage treadmill walking, deadlifts, and box step-ups at the end of each energy deficit using L-[2H5]-phenylalanine and L-[2H2]-tyrosine infusions. Treatments were ingested immediately post-exercise. Mixed-muscle protein synthesis (mixed-MPS) was measured during exercise through recovery.ResultsChange (? postabsorptive + exercise to postprandial + recovery [mean treatment difference (95%CI)]) in whole-body (g/180?min) PS was 15.8 (9.8, 21.9; P?=?0.001) and 19.4 (14.8, 24.0; P?=?0.001) greater for EAA?+?W than WHEY and MEAL, respectively, with no difference between WHEY and MEAL. ?PB was -?6.3 (-?11.5, -?1.18; P?=?0.02) greater for EAA?+?W than WHEY and?-?7.7 (-?11.9, -?3.6; P?=?0.002) greater for MEAL than WHEY, with no difference between EAA?+?W and MEAL. ?NET was 22.1 (20.5, 23.8; P?=?0.001) and 18.0 (16.5, 19.5; P?=?0.00) greater for EAA?+?W than WHEY and MEAL, respectively, while ?NET was 4.2 (2.7, 5.6; P?=?0.001) greater for MEAL than WHEY. Mixed-MPS did not differ between treatments.ConclusionsWhile mixed-MPS was similar across treatments, combining free-form EAA with whey promotes greater whole-body net protein balance during energy deficit compared to iso-nitrogenous amounts of whey or a mixed-macronutrient meal.Trial registrationClinicalTrials.gov, Identifier no. NCT04004715 . Retrospectively registered 28 June 2019, first enrollment 6 June 2019.

Project description:BackgroundThe development of effective nutritional strategies in support of muscle growth for patients with chronic obstructive pulmonary disease (COPD) remains challenging. Dietary essential amino acids (EAAs) are the main driver of postprandial net protein anabolism. In agreement, EAA supplements in healthy older adults are more effective than supplements with the composition of complete proteins. In patients with COPD it is still unknown whether complete protein supplements can be substituted with only EAAs, and whether they are as effective as in healthy older adults.MethodsAccording to a double-blind randomized crossover design, we examined in 23 patients with moderate to very severe COPD (age: 65±2 years, FEV1: 40±2% of predicted) and 19 healthy age-matched subjects (age: 64±2 years), whether a free EAA mixture with a high proportion (40%) of leucine (EAA mixture) stimulated whole body net protein gain more than a similar mixture of balanced free EAAs and non-EAAs as present in whey protein (TAA mixture). Whole body net protein gain and splanchnic extraction of phenylalanine (PHE) were assessed by continuous IV infusion of L-[ring-2H5]-PHE and L-[ring-2H2]-tyrosine, and enteral intake of L-[15N]-PHE (added to the mixtures).ResultsBesides an excellent positive linear relationship between PHE intake and net protein gain in both groups (r=0.84-0.91, P<0.001), net protein gain was 42% higher in healthy controls and 49% higher in COPD patients after intake of the EAA mixture compared to the TAA mixture (P<0.0001). These findings could not be attributed to the high LEU content, as in both groups net protein gain per gram EAA intake was lower for the EAA mixture (P<0.0001). Net protein gain was higher in COPD patients for both mixtures due to a 40% lower splanchnic extraction (P<0.0001), but was similarly related to dietary PHE (i.e. EAA) plasma appearance.ConclusionsIn COPD patients, similarly to healthy older adults, free EAA supplements stimulate whole body protein anabolism more than free amino acid supplements with the composition of complete proteins. Therefore, free EAA supplements may aid in the prevention and treatment of muscle wasting in this patient population.

Project description:BACKGROUND:Age-related decline in skeletal muscle mass is at least partly attributed to anabolic resistance to food intake. Resistance exercise sensitizes skeletal muscle tissue to the anabolic properties of amino acids. OBJECTIVE:The present study assessed protein digestion and amino acid absorption kinetics, whole-body protein balance, and the myofibrillar protein synthetic response to ingestion of different amounts of protein during recovery from resistance exercise in older men. METHODS:Forty-eight healthy older men [mean ± SEM age: 66 ± 1 y; body mass index (kg/m2): 25.4 ± 0.3] were randomly assigned to ingest 0, 15, 30, or 45 g milk protein concentrate after a single bout of resistance exercise consisting of 4 sets of 10 repetitions of leg press and leg extension and 2 sets of 10 repetitions of lateral pulldown and chest press performed at 75-80% 1-repetition maximum. Postprandial protein digestion and amino acid absorption kinetics, whole-body protein metabolism, and myofibrillar protein synthesis rates were assessed using primed, continuous infusions of l-[ring-2H5]-phenylalanine, l-[ring-2H2]-tyrosine, and l-[1-13C]-leucine combined with ingestion of intrinsically l-[1-13C]-phenylalanine and l-[1-13C]-leucine labeled protein. RESULTS:Whole-body net protein balance showed a dose-dependent increase after ingestion of 0, 15, 30, or 45 g of protein (0.015 ± 0.002, 0.108 ± 0.004, 0.162 ± 0.008, and 0.215 ± 0.009 μmol Phe · kg-1 · min-1, respectively; P < 0.001). Myofibrillar protein synthesis rates were higher after ingesting 30 (0.0951% ± 0.0062%/h, P = 0.07) or 45 g of protein (0.0970% ± 0.0062%/h, P < 0.05) than after 0 g (0.0746% ± 0.0051%/h). Incorporation of dietary protein-derived amino acids (l-[1-13C]-phenylalanine) into de novo myofibrillar protein showed a dose-dependent increase after ingestion of 15, 30, or 45 g protein (0.0171 ± 0.0017, 0.0296 ± 0.0030, and 0.0397 ± 0.0026 mole percentage excess, respectively; P < 0.05). CONCLUSIONS:Dietary protein ingested during recovery from resistance exercise is rapidly digested and absorbed. Whole-body net protein balance and dietary protein-derived amino acid incorporation into myofibrillar protein show dose-dependent increases. Ingestion of ≥30 g protein increases postexercise myofibrillar protein synthesis rates in older men. This trial was registered at Nederlands Trial Register as NTR4492.

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Essential amino acid-enriched meal replacement promotes superior net protein balance in older, overweight adults.

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Essential amino acid-enriched meal replacement promotes superior net protein balance in older, overweight adults.

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