scholarly journals Blood Essential Amino Acid Levels After Ingestion of High Quality Plant-Based Protein Blends Compared to Whey Protein: A Double Blind, Randomized, Cross-Over, Clinical Trial (P08-057-19)

2019 ◽  
Vol 3 (Supplement_1) ◽  
Author(s):  
Jessica Brennan ◽  
Maneephan Keerati-U-Rai ◽  
Huaixia Yin ◽  
Julie Daoust ◽  
Emilie Nonnotte ◽  
...  
Keyword(s):  
Amino Acid ◽  
Whey Protein ◽  
Repeated Measures ◽  
Essential Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Plant Protein ◽  
High Quality ◽  
Double Blind ◽  
The Impact

Abstract Objectives This study assessed the blood essential amino acid (eAA) response after consumption of high quality (PDCAAS = 1.0) plant-based protein blends versus whey protein (WPI, control) in healthy, resistance-trained adult men. Secondary Objectives assessed the blood leucine response (Cmax and Tmax). Methods The study was an acute, randomized, double-blind cross-over study. Participants consumed one of four study products: Blend 1 (34 grams of pea and pumpkin protein); Blend 2 (33 grams of pea, pumpkin, sunflower and coconut protein); Blend 3 (hydrolyzed version of Blend 1). Leucine was matched at 2.6 grams across test beverages equal to WPI (24 grams protein). Total eAA content was 12 grams across beverages. Fasting blood was collected and samples at 15 min, 30 min, 1 h, 2 h, 3 h and 4 h post consumption. Blood eAA were measured by UPLC. Repeated measures ANOVA assessed for equivalence of the total sum of blood eAA concentration. Primary endpoint was iAUC over 4 hours after consumption of the study blends. Cmax and Tmax of blood leucine response were secondary outcomes. Results Eighteen men (25.4 ± 4.64 y) with a BMI of 24.4 ±3.35 kg.m−2 completed the study. The eAA iAUC over 4 hours of plant-based protein blends were not equivalent to WPI, the three ratios [90% CI]: Blend #1: 0.66 [0.58–0.76]; Blend #2: 0.71 [0.62–0.82], Blend #3: 0.60 [0.52–0.69] fell below the pre-defined equivalence threshold [0.80–1.25], indicative of a 30 to 40% decrease compared to WPI. Leucine Cmax over 4-hours of plant-based protein blends were not equivalent to WPI Blend #1: 0.70 [0.67–0.73]; Blend #2: 0.72 [0.68–0.75], Blend #3: 0.65 [0.62–0.68], indicative of a 28 to 35% decrease compared to WPI. Leucine Tmax for Blend #1 and Blend #3 were close to WPI (Blend #1: 0.94 [0.73–1.18]; Blend #2: 1.56 [1.28–1.92]; Blend #3: 1.19 [0.95–1.48]). Conclusions This study represents the first human investigation in which blood eAA responses to high-quality, plant protein blends were compared to WPI. Although the eAA iAUC were not equivalent between plant protein blends and whey control, the leucine kinetic data across our plant protein blends showed an ∼2-fold increase from fasting. Further, similar Tmax data across two plant protein blends suggest a rapid hyperleucinemia. Future studies should assess the impact of high-quality plant proteins on muscle protein synthesis. Funding Sources Sequel Naturals, Danone Research.

scholarly journals Post-exercise whey protein hydrolysate supplementation induces a greater increase in muscle protein synthesis than its constituent amino acid content

2013 ◽  
Vol 110 (6) ◽  
pp. 981-987 ◽  
Author(s):  
Atsushi Kanda ◽  
Kyosuke Nakayama ◽  
Tomoyuki Fukasawa ◽  
Jinichiro Koga ◽  
Minoru Kanegae ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Whey Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Acid Mixture ◽  
Post Exercise ◽  
The Impact ◽  
Mtor Signalling

It is well known that ingestion of a protein source is effective in stimulating muscle protein synthesis after exercise. In addition, there are numerous reports on the impact of leucine and leucine-rich whey protein on muscle protein synthesis and mammalian target of rapamycin (mTOR) signalling. However, there is only limited information on the effects of whey protein hydrolysates (WPH) on muscle protein synthesis and mTOR signalling. The aim of the present study was to compare the effects of WPH and amino acids on muscle protein synthesis and the initiation of translation in skeletal muscle during the post-exercise phase. Male Sprague–Dawley rats swam for 2 h to depress muscle protein synthesis. Immediately after exercise, the animals were administered either carbohydrate (CHO), CHO plus an amino acid mixture (AA) or CHO plus WPH. At 1 h after exercise, the supplements containing whey-based protein (AA and WPH) caused a significant increase in the fractional rate of protein synthesis (FSR) compared with CHO. WPH also caused a significant increase in FSR compared with AA. Post-exercise ingestion of WPH caused a significant increase in the phosphorylation of mTOR levels compared with AA or CHO. In addition, WPH caused greater phosphorylation of ribosomal protein S6 kinase and eukaryotic initiation factor 4E-binding protein 1 than AA and CHO. In contrast, there was no difference in plasma amino acid levels following supplementation with either AA or WPH. These results indicate that WPH may include active components that are superior to amino acids for stimulating muscle protein synthesis and initiating translation.

Minimal whey protein with carbohydrate stimulates muscle protein synthesis following resistance exercise in trained young men

2007 ◽  
Vol 32 (6) ◽  
pp. 1132-1138 ◽  
Author(s):  
Jason E. Tang ◽  
Joshua J. Manolakos ◽  
Greg W. Kujbida ◽  
Paul J. Lysecki ◽  
Daniel R. Moore ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Resistance Exercise ◽  
Whey Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Young Men ◽  
Skeletal Muscle Protein ◽  
Double Blind ◽  
Exercise Period ◽  
The Impact

Whey protein is a supplemental protein source often used by athletes, particularly those aiming to gain muscle mass; however, direct evidence for its efficacy in stimulating muscle protein synthesis (MPS) is lacking. We aimed to determine the impact of consuming whey protein on skeletal muscle protein turnover in the post-exercise period. Eight healthy resistance-trained young men (age = 21 ± 1 .0 years; BMI = 26.8 ± 0.9 kg/m2 (means ± SE)) participated in a double-blind randomized crossover trial in which they performed a unilateral leg resistance exercise workout (EX: 4 sets of knee extensions and 4 sets of leg press; 8–10 repetitions/set; 80% of maximal), such that one leg was not exercised and acted as a rested (RE) comparator. After exercise, subjects consumed either an isoenergetic whey protein plus carbohydrate beverage (WHEY: 10 g protein and 21 g fructose) or a carbohydrate-only beverage (CHO: 21 g fructose and 10 g maltodextran). Subjects received pulse-tracer injections of l-[ring-2H5]phenylalanine and l-[15N]phenylalanine to measure MPS. Exercise stimulated a rise in MPS in the WHEY-EX and CHO-EX legs, which were greater than MPS in the WHEY-RE leg and the CHO-RE leg (all p < 0.05), respectively. The rate of MPS in the WHEY-EX leg was greater than in the CHO-EX leg (p < 0.001). We conclude that a small dose (10 g) of whey protein with carbohydrate (21 g) can stimulate a rise in MPS after resistance exercise in trained young men that would be supportive of a positive net protein balance, which, over time, would lead to hypertrophy.

Muscle Protein Synthesis in the Elderly Following Ingestion of Whey Protein or its Corresponding Essential Amino Acid Content

2006 ◽  
Vol 38 (Supplement) ◽  
pp. S112
Author(s):  
Christos S. Katsanos ◽  
Douglas Paddon-Jones ◽  
Xiaojun Zhang ◽  
Asle Aarsland ◽  
Hisamine Kobayashi ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Whey Protein ◽  
Acid Content ◽  
Essential Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Amino Acid Content ◽  
The Elderly ◽  
Essential Amino Acid Content

scholarly journals Human Muscle Protein Synthesis Rates after Intake of Hydrolyzed Porcine-Derived and Cows’ Milk Whey Proteins—A Randomized Controlled Trial

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 989 ◽  
Author(s):  
Bendtsen ◽  
Thorning ◽  
Reitelseder ◽  
Ritz ◽  
Hansen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
G Protein ◽  
Whey Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Muscle Proteins ◽  
Mixed Meal ◽  
The Impact

Abstract: Background: Whey protein has been shown to be one of the best proteins to stimulate muscle protein synthesis rate (MPS), but other high quality proteins, e.g., animal/porcine-derived, could have similar effects. Objective: To investigate the effects of hydrolyzed porcine proteins from blood (HPB) and muscle (HPM), in comparison to hydrolyzed whey protein (HW), on MPS after intake of 15 g alone or 30 g protein as part of a mixed meal. We hypothesized that the postprandial MPS would be similar for porcine proteins and whey protein. Design: Eighteen men (mean ± SD age: 24 ± 1 year; BMI: 21.7 ± 0.4 kg/m2) participated in the randomized, double-blind, three-way cross-over study. Subjects consumed the three test products (HPB, HPM and HW) in a random order in two servings at each test day. Serving 1 consisted of a drink with 15 g protein and serving 2 of a drink with 30 g protein together with a mixed meal. A flood-primed continuous infusion of (ring-13C6) phenylalanine was performed and muscle biopsies, blood and urine samples were collected for determination of MPS, muscle free leucine, plasma amino acid concentrations and urea excretion. Results: There were no statistical differences between the MPS measured after consuming 15 g protein alone or 30 g with a mixed meal (p = 0.53) of HPB (0.048 ± 0.007 vs. 0.049 ± 0.008%/h, resp.), HPM (0.063 ± 0.011 vs. 0.062 ± 0.011 %/h, resp.) and HW (0.058 ± 0.007 vs. 0.071 ± 0.013%/h, resp.). However, the impact of protein type on MPS reached statistical tendency (HPB vs. HPM (p = 0.093) and HPB vs. HW (p = 0.067)) with no difference between HPM and HW (p = 0.88). Plasma leucine, branched-chain, essential and total amino acids were generally higher for HPB and HW than HPM (p < 0.01), which reflected their content in the proteins. Muscle-free leucine was higher for HPB than HW and HPM (p < 0.05). Conclusion: Hydrolyzed porcine proteins from blood and muscle resulted in an MPS similar to that of HW, although with a trend for porcine blood proteins to be inferior to muscle proteins and whey. Consequently, these porcine-derived muscle proteins can be used similarly to whey protein to support maintenance of skeletal muscle as part of supplements and ingredients in foods.

scholarly journals A cell-based evaluation of a non-essential amino acid formulation as a non-bioactive control for activation and stimulation of muscle protein synthesis using ex vivo human serum

PLoS ONE ◽  
2019 ◽  
Vol 14 (11) ◽  
pp. e0220757
Author(s):  
Bijal Patel ◽  
Martina Pauk ◽  
Miryam Amigo-Benavent ◽  
Alice B. Nongonierma ◽  
Richard J. Fitzgerald ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Human Serum ◽  
Essential Amino Acid ◽  
Ex Vivo ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Acid Formulation ◽  
A Cell ◽  
Stimulation Of

scholarly journals Whey protein ingestion in elderly persons results in greater muscle protein accrual than ingestion of its constituent essential amino acid content

2008 ◽  
Vol 28 (10) ◽  
pp. 651-658 ◽  
Author(s):  
Christos S. Katsanos ◽  
David L. Chinkes ◽  
Douglas Paddon-Jones ◽  
Xiao-jun Zhang ◽  
Asle Aarsland ◽  
...  
Keyword(s):  
Amino Acid ◽  
Whey Protein ◽  
Acid Content ◽  
Essential Amino Acid ◽  
Muscle Protein ◽  
Amino Acid Content ◽  
Elderly Persons ◽  
Protein Ingestion ◽  
Essential Amino Acid Content

scholarly journals Branched-Chain Amino Acid Fortification Does Not Restore Muscle Protein Synthesis Rates following Ingestion of Lower- Compared with Higher-Dose Mycoprotein

2020 ◽  
Vol 150 (11) ◽  
pp. 2931-2941 ◽  
Author(s):  
Alistair J Monteyne ◽  
Mariana O C Coelho ◽  
Craig Porter ◽  
Doaa R Abdelrahman ◽  
Thomas S O Jameson ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
G Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Young Men ◽  
Quadriceps Muscle ◽  
Double Blind ◽  
Protein Ingestion ◽  
Branched Chain

ABSTRACT Background We have shown that ingesting a large bolus (70 g) of the fungal-derived, whole food mycoprotein robustly stimulates muscle protein synthesis (MPS) rates. Objective The aim of this study was to determine if a lower dose (35 g) of mycoprotein enriched with branched-chain amino acids (BCAAs) stimulates MPS to the same extent as 70 g of mycoprotein in resistance-trained young men. Methods Nineteen men [aged 22 ± 1 y, BMI (kg/m2): 25 ± 1] took part in a randomized, double-blind, parallel-group study. Participants received primed, continuous infusions of l-[ring-2H5]phenylalanine and ingested either 70 g mycoprotein (31.5 g protein; MYCO; n = 10) or 35 g BCAA-enriched mycoprotein (18.7 g protein: matched on BCAA content; ENR; n = 9) following a bout of unilateral resistance exercise. Blood and bilateral quadriceps muscle samples were obtained before exercise and protein ingestion and during a 4-h postprandial period to assess MPS in rested and exercised muscle. Two- and 3-factor ANOVAs were used to detect differences in plasma amino acid kinetics and mixed muscle fractional synthetic rates, respectively. Results Postprandial plasma BCAA concentrations increased more rapidly and to a larger degree in ENR compared with MYCO. MPS increased with protein ingestion (P ≤ 0.05) but to a greater extent following MYCO (from 0.025% ± 0.006% to 0.057% ± 0.004% · h−1 in rested muscle, and from 0.024% ± 0.007% to 0.072% ± 0.005% · h−1 in exercised muscle; P &lt; 0.0001) compared with ENR (from 0.031% ± 0.003% to 0.043% ± 0.005% · h−1 in rested muscle, and 0.027% ± 0.005% to 0.052% ± 0.005% · h−1 in exercised muscle; P &lt; 0.01) ingestion. Postprandial MPS rates were greater in MYCO compared with ENR (P &lt; 0.01). Conclusions The ingestion of lower-dose BCAA-enriched mycoprotein stimulates resting and postexercise MPS rates, but to a lesser extent compared with the ingestion of a BCAA-matched 70-g mycoprotein bolus in healthy young men. This trial was registered at clinicaltrials.gov as 660065600.

scholarly journals Short-term prednisone use antagonizes insulin's anabolic effect on muscle protein and glucose metabolism in young healthy people

2009 ◽  
Vol 297 (6) ◽  
pp. E1260-E1268 ◽  
Author(s):  
Kevin R. Short ◽  
Maureen L. Bigelow ◽  
K. Sreekumaran Nair
Keyword(s):  
Amino Acid ◽  
Muscle Atrophy ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Interactive Effect ◽  
Amino Acid Replacement ◽  
Healthy People ◽  
Whole Body ◽  
Short Term ◽  
Double Blind

Glucocorticoids cause muscle atrophy and weakness, but the mechanisms for these effects are unclear. The purpose of this study was to test a hypothesis that prednisone (Pred) counteracts insulin's anabolic effects on muscle. A randomized, double-blind cross-over design was used to test the effects of 6 days either Pred (0.8 mg·kg−1·day−1) or placebo use in seven healthy young volunteers. Protein dynamics were measured across the leg using stable isotope tracers of leucine (Leu) and phenylalanine (Phe) after overnight fast and during a hyperinsulinemic (1.5 μU·min−1·kg FFM−1) euglycemic clamp with amino acid replacement. Fasting glucose, amino acids, insulin, and glucagon were higher ( P < 0.01) on Pred vs. placebo, whereas leg blood flow was 18% lower. However, basal whole body and leg kinetics of Leu and Phe were unaltered by Pred. Insulin infusion increased leg glucose uptake in both trials but was 65% lower with Pred than with placebo. Insulin in both trials similarly suppressed whole body flux of Leu and Phe. Importantly, insulin increased net Leu and Phe balance across the leg and the balance between muscle protein synthesis and breakdown, but these changes were 45–140% lower ( P < 0.03) in Pred than in placebo. The present study demonstrates that short-term Pred use in healthy people does not alter whole body or leg muscle protein metabolism during the postaborptive state but causes muscle insulin resistance for both glucose and amino acid metabolism, with a blunted protein anabolism. This interactive effect may lead to muscle atrophy with continued use of glucocorticoids.

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