scholarly journals A randomized controlled trial of the impact of protein supplementation on leg lean mass and integrated muscle protein synthesis during inactivity and energy restriction in older persons

2018 ◽  
Vol 108 (5) ◽  
pp. 1060-1068 ◽  
Author(s):  
Sara Y Oikawa ◽  
Chris McGlory ◽  
Lisa K D'Souza ◽  
Adrienne K Morgan ◽  
Nelson I Saddler ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Lean Mass ◽  
Older Persons ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Controlled Trial ◽  
Protein Supplementation ◽  
Energy Restriction ◽  
Habitual Activity ◽  
The Impact

ABSTRACT Background In older persons, muscle loss is accelerated during physical inactivity and hypoenergetic states, both of which are features of hospitalization. Protein supplementation may represent a strategy to offset the loss of muscle during inactivity, and enhance recovery on resumption of activity. Objective We aimed to determine if protein supplementation, with proteins of substantially different quality, would alleviate the loss of lean mass by augmenting muscle protein synthesis (MPS) while inactive during a hypoenergetic state. Design Participants (16 men, mean ± SD age: 69 ± 3 y; 15 women, mean ± SD age: 68 ± 4 y) consumed a diet containing 1.6 g protein · kg–1 · d–1, with 55% ± 9% of protein from foods and 45% ± 9% from supplements, namely, whey protein (WP) or collagen peptides (CP): 30 g each, consumed 2 times/d. Participants were in energy balance (EB) for 1 wk, then began a period of energy restriction (ER; –500 kcal/d) for 1 wk, followed by ER with step reduction (ER + SR; <750 steps/d) for 2 wk, before a return to habitual activity in recovery (RC) for 1 wk. Results There were significant reductions in leg lean mass (LLM) from EB to ER, and from ER to ER + SR in both groups (P < 0.001) with no differences between WP and CP or when comparing the change from phase to phase. During RC, LLM increased from ER + SR, but in the WP group only. Rates of integrated muscle protein synthesis decreased during ER and ER + SR in both groups (P < 0.01), but increased during RC only in the WP group (P = 0.05). Conclusions Protein supplementation did not confer a benefit in protecting LLM, but only supplemental WP augmented LLM and muscle protein synthesis during recovery from inactivity and a hypoenergetic state. This trial was registered at http://www.clinicaltrials.gov as NCT03285737.

scholarly journals Impact of dairy protein during limb immobilization and recovery on muscle size and protein synthesis; a randomized controlled trial

2018 ◽  
Vol 124 (3) ◽  
pp. 717-728 ◽  
Author(s):  
Cameron J. Mitchell ◽  
Randall F. D’Souza ◽  
Sarah M. Mitchell ◽  
Vandre C. Figueiredo ◽  
Benjamin F. Miller ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Controlled Trial ◽  
Protein Supplementation ◽  
Muscle Size ◽  
Thigh Muscle ◽  
Muscle Disuse ◽  
And Function ◽  
Dairy Protein

Muscle disuse results in the loss of muscular strength and size, due to an imbalance between protein synthesis (MPS) and breakdown (MPB). Protein ingestion stimulates MPS, although it is not established if protein is able to attenuate muscle loss with immobilization (IM) or influence the recovery consisting of ambulatory movement followed by resistance training (RT). Thirty men (49.9 ± 0.6 yr) underwent 14 days of unilateral leg IM, 14 days of ambulatory recovery (AR), and a further six RT sessions over 14 days. Participants were randomized to consume an additional 20 g of dairy protein or placebo with a meal during the intervention. Isometric knee extension strength was reduced following IM (−24.7 ± 2.7%), partially recovered with AR (−8.6 ± 2.6%), and fully recovered after RT (−0.6 ± 3.4%), with no effect of supplementation. Thigh muscle cross-sectional area decreased with IM (−4.1 ± 0.5%), partially recovered with AR (−2.1 ± 0.5%), and increased above baseline with RT (+2.2 ± 0.5%), with no treatment effect. Myofibrillar MPS, measured using deuterated water, was unaltered by IM, with no effect of protein. During AR, MPS was increased only with protein supplementation. Protein supplementation did not attenuate the loss of muscle size and function with disuse or potentiate recovery but enhanced myofibrillar MPS during AR. NEW & NOTEWORTHY Twenty grams of daily protein supplementation does not attenuate the loss of muscle size and function induced by 2 wk of muscle disuse or potentiate recovery in middle-age men. Average mitochondrial but not myofibrillar muscle protein synthesis was attenuated during immobilization with no effect of supplementation. Protein supplementation increased myofibrillar protein synthesis during a 2-wk period of ambulatory recovery following disuse but without group differences in phenotype recovery.

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 Daily resistance-type exercise stimulates muscle protein synthesis in vivo in young men

2018 ◽  
Vol 124 (1) ◽  
pp. 66-75 ◽  
Author(s):  
Andrew M. Holwerda ◽  
Kevin J. M. Paulussen ◽  
Maarten Overkamp ◽  
Joey S. J. Smeets ◽  
Annemie P. Gijsen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Exercise Training ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Living Conditions ◽  
Deuterated Water ◽  
Free Living ◽  
The Impact ◽  
Free Living Conditions

Resistance-type exercise increases muscle protein synthesis rates during acute postexercise recovery. The impact of resistance-type exercise training on (local) muscle protein synthesis rates under free-living conditions on a day-to-day basis remains unclear. We determined the impact of daily unilateral resistance-type exercise on local myofibrillar protein synthesis rates during a 3-day period. Twelve healthy young men (22 ± 1 yr) were recruited to participate in this study where they performed daily, unilateral resistance-type exercise during a 3-day intervention period. Two days before the exercise training subjects ingested 400 ml deuterated water (2H2O). Additional 50-ml doses of deuterated water were ingested daily during the training period. Saliva and blood samples were collected daily to assess body water and amino acid precursor deuterium enrichments, respectively. Muscle tissue biopsies were collected before and after the 3 days of unilateral resistance-type exercise training from both the exercised and the nonexercised, control leg for the assessment of muscle protein synthesis rates. Deuterated water dosing resulted in a steady-state body water enrichment of 0.70 ± 0.03%. Intramuscular free [2H]alanine enrichment increased up to 1.84 ± 0.06 mole percent excess (MPE) before the exercise training and did not change in both the exercised and control leg during the 3 subsequent exercise training days (2.11 ± 0.11 and 2.19 ± 0.12 MPE, respectively; P > 0.05). Muscle protein synthesis rates averaged 1.984 ± 0.118 and 1.642 ± 0.089%/day in the exercised vs. nonexercised, control leg when assessed over the entire 3-day period ( P < 0.05). Daily resistance-type exercise stimulates (local) muscle protein synthesis in vivo in humans. NEW & NOTEWORTHY This study demonstrates that daily resistance-type exercise stimulates muscle protein synthesis rates in vivo in humans over multiple days. Whereas acute studies have shown that resistance-type exercise increases muscle protein synthesis rates by 50–100%, we observed a lower impact of resistance-type exercise under free-living conditions. We also compared precursor tracer selection for the calculation of muscle protein synthesis rates and observed that saliva deuterium enrichment serves as an appropriate and practical choice of precursor.

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.

scholarly journals Downregulation of let-7 by Electrical Acupuncture Increases Protein Synthesis in Mice

2021 ◽  
Vol 12 ◽  
Author(s):  
Ying Huang ◽  
Manshu Yu ◽  
Akihiro Kuma ◽  
Janet D. Klein ◽  
Yanhua Wang ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Skeletal Muscles ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
High Sensitivity ◽  
Luciferase Reporter ◽  
C2c12 Myotubes ◽  
Electrical Acupuncture ◽  
The Impact ◽  
Serum Exosomes

BackgroundOur previous study found that acupuncture with low frequency electrical stimulation (Acu/LFES) prevents muscle atrophy by attenuation of protein degradation in mice. The current study examines the impact of Acu/LFES on protein synthesis.MethodC57/BL6 mice received Acu/LFES treatment on hindlimb for 30 min once. Acu/LFES points were selected by WHO Standard Acupuncture Nomenclature and electric stimulation applied using an SDZ-II Electronic acupuncture instrument. Muscle protein synthesis was measured by the surface-sensing of translation (SUnSET) assay. Exosomes were isolated using serial centrifugation and concentration and size of the collected exosomes were measured using a NanoSight instrument. The mature microRNA library in serum exosomes was validated using a High Sensitivity DNA chip.ResultsProtein synthesis was enhanced in the both hindlimb and forelimb muscles. Blocking exosome secretion with GW4869 decreased the Acu/LFES-induced increases in protein synthesis. MicroRNA-deep sequencing demonstrated that four members of the Let-7 miRNA family were significantly decreased in serum exosomes. Real time qPCR further verified Acu/LFES-mediated decreases of let-7c-5p in serum exosomes and skeletal muscles. In cultured C2C12 myotubes, inhibition of let-7c not only increased protein synthesis, but also enhanced protein abundance of Igf1 and Igf1 receptors. Using a luciferase reporter assay, we demonstrated that let-7 directly inhibits Igf1.ConclusionAcu/LFES on hindlimb decreases let-7-5p leading to upregulation of the Igf1 signaling and increasing protein synthesis in both hindlimb and forelimb skeletal muscles. This provides a new understanding of how the electrical acupuncture treatment can positively influence muscle health.

scholarly journals Dileucine ingestion is more effective than leucine in stimulating muscle protein turnover in young males: a double blind randomized controlled trial

2021 ◽  
Author(s):  
Kevin J. M. Paulussen ◽  
Rafael A. Alamilla ◽  
Amadeo F. Salvador ◽  
Colleen F. McKenna ◽  
Andrew T. Askow ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Controlled Trial ◽  
Young Men ◽  
Double Blind ◽  
Muscle Protein Turnover ◽  
Breakdown Rates ◽  
Over Time

Leucine is regarded as an anabolic trigger for the mTORC1 pathway and the stimulation muscle protein synthesis rates. More recently, there has been an interest in underpinning the relevance of BCAA-containing dipeptides and their intact absorption into circulation to regulate muscle anabolic responses. We investigated the effects of dileucine and leucine ingestion on postprandial muscle protein turnover. Ten healthy young men (age: 23±3 y) consumed either 2 g of leucine (LEU) or 2 g of dileucine (DILEU) in a randomized crossover design. The participants underwent repeated blood and muscle biopsy sampling during primed continuous infusions of L-[ring-13C6]phenylalanine and L-[15N]phenylalanine to determine myofibrillar protein synthesis (MPS) and mixed muscle protein breakdown rates (MPB), respectively. LEU and DILEU similarly increased plasma leucine net area under the curve (AUC; P = 0.396). DILEU increased plasma dileucine AUC to a greater extent than LEU (P = 0.013). Phosphorylation of Akt (P = 0.002), rpS6 (P <0.001) and p70S6K (P < 0.001) increased over time in both LEU and DILEU conditions. Phosphorylation of 4E-BP1 (P = 0.229) and eEF2 (P = 0.999) did not change over time irrespective of condition. Cumulative (0-180 min) MPS increased in DILEU (0.075±0.032 %⋅hour-1), but not in LEU (0.047±0.029 %⋅hour-1; P=0.023). MPB did not differ between LEU (0.043±0.030 %⋅h-1) and DILEU conditions (0.051±0.027 %⋅hour-1; P = 0.659). Our results showed that dileucine ingestion elevated plasma dileucine concentrations and muscle protein turnover by stimulating MPS in young men.

scholarly journals Effects of Testosterone on Mixed Muscle Protein Synthesis and Proteome Dynamics During Energy Deficit

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 649-649 ◽  
Author(s):  
Stefan Pasiakos ◽  
Mahalakshmi Shankaran ◽  
Claire Berryman ◽  
Lee Margolis ◽  
Harris Lieberman ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Dynamics ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Controlled Trial ◽  
Weight Maintenance ◽  
Energy Deficit ◽  
Deuterated Water ◽  
Short Term ◽  
Double Blind

Abstract Objectives Short-term energy deficit reduces acute measures of mixed muscle protein synthesis (MPS) and suppresses the hypothalamic-pituitary axis and endogenous testosterone synthesis. We hypothesized that testosterone supplementation could mitigate the effects of energy deficit on MPS. We conducted a randomized, double-blind, placebo-controlled trial to determine the effects of 28 days of tightly-controlled severe energy deficit (deficit 55% of total energy requirements) on measures of mixed-MPS and proteome-wide protein dynamics in non-obese men either given 200 mg testosterone enanthate (Testosterone, n = 24) or placebo (Placebo, n = 26) injections per week. Methods Participants received daily aliquots of deuterated water (2H2O) for 42 consecutive days (14-d weight maintenance period followed by 28-d energy deficit). Muscle biopsies were collected at rest in a fasted state at the end of the weight maintenance phase (PRE) and at the middle (MID) and end (POST) of the 28-d energy deficit. Mixed-MPS and proteome-wide protein fractional synthesis rates (FSR) were quantified. Changes over time and differences between Testosterone and Placebo were determined for mixed-MPS, and cross-sectional comparisons between Testosterone and Placebo were performed at MID and POST for proteome dynamics. Results In both Testosterone and Placebo, mixed-MPS were 40% and 33% lower (P &lt; 0.0005) at MID and POST energy deficit, respectively, compared to PRE, with no differences between groups or between MID and POST. Proteome-wide FSR of individual muscle proteins did not differ between Testosterone and Placebo at any time point. However, at POST, the number of individual proteins with higher FSR in Testosterone than Placebo was significant by 2-tailed binomial test (P &lt; 0.05), with values ranging from 20–32% higher FSR for myofibrillar, mitochondrial and cytosolic proteins. Conclusions Findings confirm the pronounced effect of short-term severe energy deficit on mixed-MPS and suggest the anabolic suppression occurs largely independent of testosterone. However, proteome-wide protein dynamics may reveal a novel time sensitive signal by which supplemental testosterone triggers a delayed increase in MPS, providing a synthetic mechanism for muscle mass preservation or accrual. Funding Sources Supported by DHP JPC-5/MOMRP; authors’ views not official U.S. Army or DoD policy.

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