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Whey Protein Hydrolysate Increases Amino Acid Uptake, mTORC1 Signaling, and Protein Synthesis in Skeletal Muscle of Healthy Young Men in a Randomized Crossover Trial.

ABSTRACT: BACKGROUND:Muscle protein synthesis (MPS) can be stimulated by ingestion of protein sources, such as whey, casein, or soy. Protein supplementation can enhance muscle protein synthesis after exercise and may preserve skeletal muscle mass and function in aging adults. Therefore, identifying protein sources with higher anabolic potency is of high significance. OBJECTIVE:The aim of this study was to determine the anabolic potency and efficacy of a novel whey protein hydrolysate mixture (WPH) on mechanistic target of rapamycin complex 1 (mTORC1) signaling and skeletal MPS in healthy young subjects. METHODS:Ten young men (aged 28.7 ± 3.6 y, 25.2 ± 2.9 kg/m2 body mass index [BMI]) were recruited into a double-blind two-way crossover trial. Subjects were randomized to receive either 0.08 g/kg of body weight (BW) of WPH or an intact whey protein (WHEY) mixture during stable isotope infusion experiments. Fractional synthetic rate, leucine and phenylalanine kinetics, and markers of amino acid sensing were assessed as primary outcomes before and 1-3 h after protein ingestion using a repeated measures mixed model. RESULTS:Blood leucine concentration, delivery of leucine to muscle, transport of leucine from blood into muscle and intracellular muscle leucine concentration significantly increased to a similar extent 1 h after ingestion of both mixtures (P < 0.05). Phosphorylation of S6K1 (i.e. a marker of mTORC1 activation) increased equally by ?20% 1-h postingestion (P < 0.05). Ingestion of WPH and WHEY increased mixed MPS similarly in both groups by ?43% (P < 0.05); however, phenylalanine utilization for synthesis increased in both treatments 1-h postingestion but remained elevated 3-h postingestion only in the WPH group (P < 0.05). CONCLUSIONS:We conclude that a small dose of WPH effectively increases leucine transport into muscle, activating mTORC1 and stimulating MPS in young men. WPH anabolic potency and efficacy for promoting overall muscle protein anabolism is similar to WHEY, an intact protein source. This trial was registered at clinicaltrials.gov as NCT03313830.

SUBMITTER: Moro T

PROVIDER: S-EPMC7443767 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Whey Protein Hydrolysate Increases Amino Acid Uptake, mTORC1 Signaling, and Protein Synthesis in Skeletal Muscle of Healthy Young Men in a Randomized Crossover Trial.

Moro Tatiana T Brightwell Camille R CR Velarde Brenda B Fry Christopher S CS Nakayama Kyosuke K Sanbongi Chiaki C Volpi Elena E Rasmussen Blake B BB

The Journal of nutrition 20190701 7

<h4>Background</h4>Muscle protein synthesis (MPS) can be stimulated by ingestion of protein sources, such as whey, casein, or soy. Protein supplementation can enhance muscle protein synthesis after exercise and may preserve skeletal muscle mass and function in aging adults. Therefore, identifying protein sources with higher anabolic potency is of high significance.<h4>Objective</h4>The aim of this study was to determine the anabolic potency and efficacy of a novel whey protein hydrolysate mixtur ...[more]

PMID: 31095313

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Project description:We have previously showed that whey protein hydrolysate (WPH) causes a greater increase in muscle protein synthesis than an identical composition of amino acids mixture does. The present study was conducted to investigate a comparative effect of WPH on gene expression. Male Sprague-Dawley rats subjected to a 2-h swimming exercise were administered either a carbohydrate-amino acid diet or a carbohydrate-WPH diet immediately after exercise. One hour after exercise, epitrochlearis muscle mRNA was sampled and subjected to DNA microarray analysis. As a result, ingestion of WPH altered 189 genes in considering the false discovery rate. Among the upregulated genes, 8 Gene Ontology (GO) terms were enriched, which included key elements in muscle repair after exercise such as Cd24, Ccl2, Ccl7 and Cxcl1. On the other hand, 9 GO terms were enriched in the gene sets downregulated by ingestion of WPH and these GO terms fell into 2 clusters, 'regulation of ATPase activity' and 'immune response'. Furthermore, we found that WPH activate the 2 upstream proteins, extracellular signal-regulated kinase 1/2 (ERK1/2) and hypoxia-inducible factor-1a (HIF-1a), which may act as key factors for regulation of gene expression. These results suggest that ingestion of WPH, compared to an identical composition of amino acid mixture, induces greater changes in the after-exercise gene expression profile via activation of the proteins, ERK1/2 and HIF-1a. Male Sprague-Dawley rats (5-week-old) with body weights of approximately 150 g each (CLEA Japan, Inc., Tokyo, Japan) were used in this study. Rats were maintained at 23 +/- 2C, with lights on from 8:00 to 20:00 and off from 20:00 to 8:00. Rats had free access to food (protein 23.6%, fat 5.3%, carbohydrate 54.4%, ash 6.1%, fiber 2.9%, moisture 7.7%, MF, Oriental Yeast Co., Ltd., Osaka, Japan) and water. After 2- or 3-day acclimation, the rats were pre-trained to swimming exercise for 3 days. One day before the experiment, they were fed 5 g of a restricted diet (MF, Oriental Yeast Co., Ltd., Osaka, Japan). On the day of the experiment, rats swam for 2 hours, with 4 rats swimming simultaneously in a barrel filled with water to a depth of 50 cm, allowing an average surface area of 400 cm2 for each animal. The water temperature was maintained at a constant of 35C. Immediately following exercise, rats were given one of two isoenergetic test solutions by gavage. These solutions contained 44 kJ in a four-test dose that represented about 15% of daily energy needs and included either a mixed meal containing carbohydrate and amino acid mixture (AAM) or a mixed meal containing carbohydrate and whey protein hydrolysate (WPH; Meiji Co., Ltd., Japan). This study was approved by the Animal Committee of Food Science Research Lab., Meiji Co., Ltd., with the animals receiving care according to the guidelines laid down by this committee.

Project description:BackgroundProtein supplementation has been suggested to augment endurance training adaptations by increasing mixed muscle and myofibrillar protein synthesis and lean body mass. However, a potential beneficial effect on mitochondrial adaptations is yet to be clarified. The aim of the present study was to investigate the effect of consuming whey protein hydrolysate before and whey protein hydrolysate plus carbohydrate (PRO-CHO) after each exercise session during a six-week training period compared to similarly timed intake of isocaloric CHO supplements on biomarkers of mitochondrial biogenesis, VO2max and performance in trained runners.MethodsTwenty-four trained runners (VO2max 60.7 ± 3.7 ml O2 kg- 1 min1) completed a six-week block randomized controlled intervention period, consisting of progressive running training. Subjects were randomly assigned to either PRO-CHO or CHO and matched in pairs for gender, age, VO2max, training and performance status. The PRO-CHO group ingested a protein beverage (0.3 g kg- 1) before and protein-carbohydrate beverage (0.3 g protein kg- 1 and 1 g carbohydrate kg- 1) after each exercise session. The CHO group ingested an energy matched carbohydrate beverage. Resting muscle biopsies obtained pre and post intervention were analyzed for mitochondrial specific enzyme activity and mitochondrial protein content. Subjects completed a 6 K time trial (6 K TT) and a VO2max test pre, midway (only 6 K TT) and post intervention.ResultsFollowing six weeks of endurance training Cytochrome C (Cyt C) protein content was significantly higher in the PRO-CHO group compared to the CHO group (p < 0.05), with several other mitochondrial proteins (Succinate dehydrogenase (SDHA), Cytochrome C oxidase (COX-IV), Voltage-dependent anion channel (VDAC), Heat shock protein 60 (HSP60), and Prohibitin (PHB1)) following a similar, but non-significant pattern (p = 0.07-0.14). β-hydroxyacyl-CoA dehydrogenase (HAD) activity was significantly lower after training in the CHO group (p < 0.01), but not in the PRO-CHO group (p = 0.24). VO2max and 6 K TT was significantly improved after training with no significant difference between groups.ConclusionIntake of whey PRO hydrolysate before and whey PRO hydrolysate plus CHO after each exercise session during a six-week endurance training period may augment training effects on specific mitochondrial proteins compared to intake of iso-caloric CHO but does not alter VO2max or 6 K TT performance.Trial registrationclinicaltrials.gov , NCT03561337 . Registered 6 June 2018 - Retrospectively registered.

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:BackgroundA combination of resistance training and whey protein supplementation is a common practice among athletes and recreational exercisers to enhance muscle growth and strength. Although their safety as food additives is controversial, artificial sweeteners are present in whey protein supplements. Thus, natural sweeteners extracted from the leaves of Stevia rebaudiana are a potential alternative, due to their safety and health benefits. Here, we investigated the effects of whey protein sweetened with S. rebaudiana on physical performance and mitochondrial biogenesis markers in the skeletal muscle of resistance-trained rats.MethodsForty male Wistar rats were distributed into four groups: sedentary rats, trained rats, trained rats receiving whey protein and trained rats receiving whey protein sweetened with S. rebaudiana leaf extracts. Resistance training was performed by climbing a ladder 5 days per week, during 8-weeks. The training sessions consisted of four climbs carrying a load of 50, 75, 90, and 100% of the maximum load-carrying capacity which we determined before by performing a maximum load-carrying test for each animal. After this period, we collected plasma and tissues samples to evaluate biochemical, histological and molecular (western blot) parameters in these rats.ResultsDietary supplementation with whey protein sweetened with S. rebaudiana significantly enhanced the maximum load-carrying capacity of resistance-trained rats, compared with non-sweetened whey protein supplementation. This enhanced physical performance was accompanied by an increase in the weight of the gastrocnemius and soleus muscle pads. Although the muscle pad of the biceps brachii was not altered, we observed a significant increase in PGC-1α expression, which was followed by a similar pattern in TFAM protein expression, two important mitochondrial biogenesis markers. In addition, a higher level of AMPK phosphorylation was observed in these resistance-trained rats. Finally, supplementation with whey protein sweetened with S. rebaudiana also induced a significant decrease in retroperitoneal adipocyte diameter and an increase in the weight of brown adipose tissue pads in resistance-trained rats.ConclusionThe addition of Stevia rebaudiana leaf extracts to whey protein appears to be a potential strategy for those who want to increase muscular mass and strength and also improve mitochondrial function. This strategy may be useful for both athletes and patients with metabolic disorders, such as obesity and type 2 diabetes.

Project description:BACKGROUND:We have determined the acute response of protein kinetics to one or two servings (6.3 g and 12.6 g) of a proprietary composition containing free-form essential amino acids (EAA) (3.2 g EAA per serving) and whey protein (2.4 g per serving), as well as the response to consumption of a popular whey-based protein supplement (Gatorade Recover) (17 g; 12.6 g protein). METHODS:Whole-body rates of protein synthesis, breakdown and net balance (taken to be the anabolic response) were determined using primed-constant infusions of 2H5-phenylalnine and 2H2-tyrosine. Muscle protein fractional synthetic rate (FSR) was also determined with the 2H5-phenylalanine tracer. RESULTS:Plasma EAA levels increased following consumption of all beverages, with the greatest response in the high-dose EAA/protein composition. Similarly, the increase in net balance between whole-body protein synthesis and breakdown was greatest following consumption of the high-dose EAA/protein composition, while the low-dose EAA/protein composition and Gatorade Recover induced similar increases in net balance. When the net balance response was normalized for the total amount of product given, the high- and low-dose EAA/protein beverages were approximately 6- and 3-fold more anabolic than the Gatorade Recover, respectively. The greater anabolic response to the EAA/protein composition was due to greater increases in whole-body protein synthesis with both doses, and a markedly greater suppression of whole-body protein breakdown in the high-dose group. Muscle protein FSR after beverage consumption reflected changes in whole-body protein synthesis, with the larger EAA/protein dose significantly increasing FSR. CONCLUSION:We conclude that a composition of a balanced EAA formulation combined with whey protein is highly anabolic as compared to a whey protein-based recovery product, and that the response is dose-dependent. TRIAL REGISTRATION:ClinicalTrials.gov Identifier: NCT03502941. This trial was registered on April 19, 2018.

Dataset Information

Whey Protein Hydrolysate Increases Amino Acid Uptake, mTORC1 Signaling, and Protein Synthesis in Skeletal Muscle of Healthy Young Men in a Randomized Crossover Trial.

Publications

Whey Protein Hydrolysate Increases Amino Acid Uptake, mTORC1 Signaling, and Protein Synthesis in Skeletal Muscle of Healthy Young Men in a Randomized Crossover Trial.

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