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Does Exclusive Consumption of Plant-based Dietary Protein Impair Resistance Training-induced Muscle Adaptations?: 2873 Board #3 May 31 3:15 PM - 5:15 PM
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Maximizing the post-exercise increase in muscle protein synthesis, especially of the contractile myofibrillar protein fraction, is essential to facilitate effective muscle remodeling, and enhance hypertrophic gains with resistance training. MPS is the primary regulated variable influencing muscle net balance with dietary amino acid ingestion representing the single most important nutritional variable enhancing post-exercise rates of muscle protein synthesis. Dose-response studies in average (i.e., ~80 kg) males have reported an absolute 20 g dose of high quality, rapidly digested protein maximizes mixed, and myofibrillar protein synthetic rates. However, it is unclear if these absolute protein intakes can be viewed in a “one size fits all” solution. Re-analysis of published literature in young adults suggests a relative single meal intake of ~0.31 g/kg of rapidly digested, high quality protein (i.e., whey) should be considered as a nutritional guideline for individuals of average body composition aiming to maximize post-exercise myofibrillar protein synthesis while minimizing irreversible amino acid oxidative catabolism that occurs with excessive intakes of this macronutrient. This muscle-specific bolus intake is lower than that reported to maximize whole body anabolism (i.e., ≥0.5 g/kg). Review of the available literature suggests that potential confounders such as the co-ingestion of carbohydrate, sex, and amount of active muscle mass do not represent significant barriers to the translation of this objectively determined relative protein intake. Additional research is warranted to elucidate the effective dose for proteins with suboptimal amino acid compositions (e.g., plant-based), and/or slower digestion rates as well as whether recommendations are appreciably affected by other physiological conditions such endurance exercise, high habitual daily protein ingestion, aging, obesity, and/or periods of chronic negative energy balance.
Skeletal muscle is highly adaptable and has consistently been shown to morphologically respond to exercise training. Skeletal muscle growth during periods of resistance training has traditionally been referred to as skeletal muscle hypertrophy, and this manifests as increases in muscle mass, muscle thickness, muscle area, muscle volume, and muscle fiber cross-sectional area (fCSA). Delicate electron microscopy and biochemical techniques have also been used to demonstrate that resistance exercise promotes ultrastructural adaptations within muscle fibers. Decades of research in this area of exercise physiology have promulgated a widespread hypothetical model of training-induced skeletal muscle hypertrophy; specifically, fCSA increases are accompanied by proportional increases in myofibrillar protein, leading to an expansion in the number of sarcomeres in parallel and/or an increase in myofibril number. However, there is ample evidence to suggest that myofibrillar protein concentration may be diluted through sarcoplasmic expansion as fCSA increases occur. Furthermore, and perhaps more problematic, are numerous investigations reporting that pre-to-post training change scores in macroscopic, microscopic, and molecular variables supporting this model are often poorly associated with one another. The current review first provides a brief description of skeletal muscle composition and structure. We then provide a historical overview of muscle hypertrophy assessment. Next, current-day methods commonly used to assess skeletal muscle hypertrophy at the biochemical, ultramicroscopic, microscopic, macroscopic, and whole-body levels in response to training are examined. Data from our laboratory, and others, demonstrating correlations (or the lack thereof) between these variables are also presented, and reasons for comparative discrepancies are discussed with particular attention directed to studies reporting ultrastructural and muscle protein concentration alterations. Finally, we critically evaluate the biological construct of skeletal muscle hypertrophy, propose potential operational definitions, and provide suggestions for consideration in hopes of guiding future research in this area.
This study examined the effects of whey and pea protein supplementation on physiological adaptations following 8-weeks of high-intensity functional training (HIFT). Fifteen HIFT men (n = 8; 38.6 ± 12.7 y, 1.8 ± 0.1 m, 87.7 ± 15.8 kg) and women (n = 7; 38.9 ± 10.9 y, 1.7 ± 0.10 m, 73.3 ± 10.5 kg) participated in this study. Participants completed an 8-week HIFT program consisting of 4 training sessions per week. Participants consumed 24 g of either whey (n = 8) or pea (n = 7) protein before and after exercise on training days, and in-between meals on non-training days. Before and after training, participants underwent ultrasonography muscle thickness measurement, bioelectrical impedance analysis (BIA), two benchmark WODs (workout of the day), 1-Repetition Maximum (1RM) squat and deadlift testing, and Isometric Mid-thigh Pull (IMTP) performance. Separate analyses of covariance (ANCOVA) were performed on all measures collected at POST. Both groups experienced increased strength for 1RM back squat (p = 0.006) and deadlift (p = 0.008). No training effect (p > 0.05) was found for body composition, muscle thickness, IMTP peak force, IMTP rate of force development, or performance in either WOD. Using PRE values as the covariate, there were no group differences for any measured variable. We conclude that ingestion of whey and pea protein produce similar outcomes in measurements of body composition, muscle thickness, force production, WOD performance and strength following 8-weeks of HIFT.
The postprandial rise in essential amino acid (EAA) concentrations modulates the increase in muscle protein synthesis rates after protein ingestion. The EAA content and AA composition of the dietary protein source contribute to the differential muscle protein synthetic response to the ingestion of different proteins. Lower EAA contents and specific lack of sufficient leucine, lysine, and/or methionine may be responsible for the lower anabolic capacity of plant-based compared with animal-based proteins. We compared EAA contents and AA composition of a large selection of plant-based protein sources with animal-based proteins and human skeletal muscle protein. AA composition of oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, potato, milk, whey, caseinate, casein, egg, and human skeletal muscle protein were assessed using UPLC–MS/MS. EAA contents of plant-based protein isolates such as oat (21%), lupin (21%), and wheat (22%) were lower than animal-based proteins (whey 43%, milk 39%, casein 34%, and egg 32%) and muscle protein (38%). AA profiles largely differed among plant-based proteins with leucine contents ranging from 5.1% for hemp to 13.5% for corn protein, compared to 9.0% for milk, 7.0% for egg, and 7.6% for muscle protein. Methionine and lysine were typically lower in plant-based proteins (1.0 ± 0.3 and 3.6 ± 0.6%) compared with animal-based proteins (2.5 ± 0.1 and 7.0 ± 0.6%) and muscle protein (2.0 and 7.8%, respectively). In conclusion, there are large differences in EAA contents and AA composition between various plant-based protein isolates. Combinations of various plant-based protein isolates or blends of animal and plant-based proteins can provide protein characteristics that closely reflect the typical characteristics of animal-based proteins.
Much attention has been given to determining the influence of total protein intake and protein source on gains in lean body mass (LBM) and strength in response to resistance exercise training (RET). Acute studies indicate that whey protein, likely related to its higher leucine content, stimulates muscle protein synthesis (MPS) to a greater extent than proteins such as soy and casein. Less clear is the extent to which the type of protein supplemented impacts strength and LBM in longer term studies (≥6 weeks). Therefore, a meta-analysis was conducted to compare the effect of supplementation with soy protein to animal protein supplementation on strength and LBM in response to RET. Nine studies involving 266 participants suitable for inclusion in the meta-analysis were identified. Five studies compared whey with soy protein and four compared soy protein with other proteins (beef, milk or dairy protein). Meta-analysis showed that supplementing RET with whey or soy protein resulted in significant increases in strength but found no difference between groups (bench press Chi2 = 0.02, p=0.90; squat Chi2=0.22, p =0.64). There was no significant effect of whey or soy alone (n=5) on LBM change, and no differences between groups (Chi2=0.00, p=0.96). Strength and LBM both increased significantly in the 'other protein' and the soy groups (n=9), but there were no between group differences (bench Chi2=0.02, p=0.88; squat Chi2=0.78, p=0.38 and LBM Chi2=0.06, p=0.80). The results of this meta-analysis indicate that soy protein supplementation produces similar gains in strength and LBM in response to RET as whey protein.
We sought to identify biomarkers which delineated individual hypertrophic responses to resistance training. Untrained, college-aged males engaged in full-body resistance training (3 d/wk) for 12 weeks. Body composition via dual x-ray absorptiometry (DXA), vastus lateralis (VL) thickness via ultrasound, blood, VL muscle biopsies, and three-repetition maximum (3-RM) squat strength were obtained prior to (PRE) and following (POST) 12 weeks of training. K-means cluster analysis based on VL thickness changes identified LOW [n = 17; change (mean±SD) = +0.11±0.14 cm], modest (MOD; n = 29, +0.40±0.06 cm), and high (HI; n = 21, +0.69±0.14 cm) responders. Biomarkers related to histology, ribosome biogenesis, proteolysis, inflammation, and androgen signaling were analyzed between clusters. There were main effects of time (POST>PRE, p<0.05) but no cluster×time interactions for increases in DXA lean body mass, type I and II muscle fiber cross sectional area and myonuclear number, satellite cell number, and macronutrients consumed. Interestingly, PRE VL thickness was ~12% greater in LOW versus HI (p = 0.021), despite POST values being ~12% greater in HI versus LOW (p = 0.006). However there was only a weak correlation between PRE VL thickness scores and change in VL thickness (r² = 0.114, p = 0.005). Forced post hoc analysis indicated that muscle total RNA levels (i.e., ribosome density) did not significantly increase in the LOW cluster (351±70 ng/mg to 380±62, p = 0.253), but increased in the MOD (369±115 to 429±92, p = 0.009) and HI clusters (356±77 to 470±134, p<0.001; POST HI>POST LOW, p = 0.013). Nonetheless, there was only a weak association between change in muscle total RNA and VL thickness (r² = 0.079, p = 0.026). IL-1β mRNA levels decreased in the MOD and HI clusters following training (p<0.05), although associations between this marker and VL thickness changes were not significant (r² = 0.0002, p = 0.919). In conclusion, individuals with lower pre-training VL thickness values and greater increases muscle total RNA levels following 12 weeks of resistance training experienced greater VL muscle growth, although these biomarkers individually explained only ~8–11% of the variance in hypertrophy.
Background: Resistance exercise leads to net muscle protein accretion through a synergistic interaction of exercise and feeding. Proteins from different sources may differ in their ability to support muscle protein accretion because of different patterns of postprandial hyperaminoacidemia.
Objective: We examined the effect of consuming isonitrogenous, isoenergetic, and macronutrient-matched soy or milk beverages (18 g protein, 750 kJ) on protein kinetics and net muscle protein balance after resistance exercise in healthy young men. Our hypothesis was that soy ingestion would result in larger but transient hyperaminoacidemia compared with milk and that milk would promote a greater net balance because of lower but prolonged hyperaminoacidemia.
Design: Arterial-venous amino acid balance and muscle fractional synthesis rates were measured in young men who consumed fluid milk or a soy-protein beverage in a crossover design after a bout of resistance exercise.
Results: Ingestion of both soy and milk resulted in a positive net protein balance. Analysis of area under the net balance curves indicated an overall greater net balance after milk ingestion (P < 0.05). The fractional synthesis rate in muscle was also greater after milk consumption (0.10 ± 0.01%/h) than after soy consumption (0.07 ± 0.01%/h; P = 0.05).
Conclusions: Milk-based proteins promote muscle protein accretion to a greater extent than do soy-based proteins when consumed after resistance exercise. The consumption of either milk or soy protein with resistance training promotes muscle mass maintenance and gains, but chronic consumption of milk proteins after resistance exercise likely supports a more rapid lean mass accrual.
Purpose of review:
Skeletal muscle mass with aging, during critical care, and following critical care is a determinant of quality of life and survival. In this review, we discuss the mechanisms that underpin skeletal muscle atrophy and recommendations to offset skeletal muscle atrophy with aging and during, as well as following, critical care.
Recent findings:
Anabolic resistance is responsible, in part, for skeletal muscle atrophy with aging, muscle disuse, and during disease states. Anabolic resistance describes the reduced stimulation of muscle protein synthesis to a given dose of protein/amino acids and contributes to declines in skeletal muscle mass. Physical inactivity induces: anabolic resistance (that is likely exacerbated with aging), insulin resistance, systemic inflammation, decreased satellite cell content, and decreased capillary density. Critical illness results in rapid skeletal muscle atrophy that is a result of both anabolic resistance and enhanced skeletal muscle breakdown.
Summary:
Insofar as atrophic loss of skeletal muscle mass is concerned, anabolic resistance is a principal determinant of age-induced losses and appears to be a contributor to critical illness-induced skeletal muscle atrophy. Older individuals should perform exercise using both heavy and light loads three times per week, ingest at least 1.2 g of protein/kg/day, evenly distribute their meals into protein boluses of 0.40 g/kg, and consume protein within 2 h of retiring for sleep. During critical care, early, frequent, and multimodal physical therapies in combination with early, enteral, hypocaloric energy (∼10-15 kcal/kg/day), and high-protein (>1.2 g/kg/day) provision is recommended.
Objective
We performed a systematic review, meta-analysis and meta-regression to determine if dietary protein supplementation augments resistance exercise training (RET)-induced gains in muscle mass and strength.
Data sources
A systematic search of Medline, Embase, CINAHL and SportDiscus.
Eligibility criteria
Only randomised controlled trials with RET ≥6 weeks in duration and dietary protein supplementation.
Design
Random-effects meta-analyses and meta-regressions with four a priori determined covariates. Two-phase break point analysis was used to determine the relationship between total protein intake and changes in fat-free mass (FFM).
Results
Data from 49 studies with 1863 participants showed that dietary protein supplementation significantly (all p<0.05) increased changes (means (95% CI)) in: strength—one-repetition-maximum (2.49 kg (0.64, 4.33)), FFM (0.30 kg (0.09, 0.52)) and muscle size—muscle fibre cross-sectional area (CSA; 310 µm² (51, 570)) and mid-femur CSA (7.2 mm² (0.20, 14.30)) during periods of prolonged RET. The impact of protein supplementation on gains in FFM was reduced with increasing age (−0.01 kg (−0.02,–0.00), p=0.002) and was more effective in resistance-trained individuals (0.75 kg (0.09, 1.40), p=0.03). Protein supplementation beyond total protein intakes of 1.62 g/kg/day resulted in no further RET-induced gains in FFM.
Summary/conclusion
Dietary protein supplementation significantly enhanced changes in muscle strength and size during prolonged RET in healthy adults. Increasing age reduces and training experience increases the efficacy of protein supplementation during RET. With protein supplementation, protein intakes at amounts greater than ~1.6 g/kg/day do not further contribute RET-induced gains in FFM.
Background:
Muscle mass maintenance is largely regulated by basal muscle protein synthesis and the capacity to stimulate muscle protein synthesis after food intake. The postprandial muscle protein synthetic response is modulated by the amount, source, and type of protein consumed. It has been suggested that plant-based proteins are less potent in stimulating postprandial muscle protein synthesis than animal-derived proteins. However, few data support this contention.
Objective:
We aimed to assess postprandial plasma amino acid concentrations and muscle protein synthesis rates after the ingestion of a substantial 35-g bolus of wheat protein hydrolysate compared with casein and whey protein.
Methods:
Sixty healthy older men [mean ± SEM age: 71 ± 1 y; body mass index (in kg/m(2)): 25.3 ± 0.3] received a primed continuous infusion of l-[ring-(13)C6]-phenylalanine and ingested 35 g wheat protein (n = 12), 35 g wheat protein hydrolysate (WPH-35; n = 12), 35 g micellar casein (MCas-35; n = 12), 35 g whey protein (Whey-35; n = 12), or 60 g wheat protein hydrolysate (WPH-60; n = 12). Plasma and muscle samples were collected at regular intervals.
Results:
The postprandial increase in plasma essential amino acid concentrations was greater after ingesting Whey-35 (2.23 ± 0.07 mM) than after MCas-35 (1.53 ± 0.08 mM) and WPH-35 (1.50 ± 0.04 mM) (P < 0.01). Myofibrillar protein synthesis rates increased after ingesting MCas-35 (P < 0.01) and were higher after ingesting MCas-35 (0.050% ± 0.005%/h) than after WPH-35 (0.032% ± 0.004%/h) (P = 0.03). The postprandial increase in plasma leucine concentrations was greater after ingesting Whey-35 than after WPH-60 (peak value: 580 ± 18 compared with 378 ± 10 μM, respectively; P < 0.01), despite similar leucine contents (4.4 g leucine). Nevertheless, the ingestion of WPH-60 increased myofibrillar protein synthesis rates above basal rates (0.049% ± 0.007%/h; P = 0.02).
Conclusions:
The myofibrillar protein synthetic response to the ingestion of 35 g casein is greater than after an equal amount of wheat protein. Ingesting a larger amount of wheat protein (i.e., 60 g) substantially increases myofibrillar protein synthesis rates in healthy older men. This trial was registered at clinicaltrials.gov as NCT01952639.
Physical activity recommendations for public health include typically muscle-strengthening activities for a minimum of 2 days a week. The range of inter-individual variation in responses to resistance training (RT) aiming to improve health and well-being requires to be investigated. The purpose of this study was to quantify high and low responders for RT-induced changes in muscle size and strength and to examine possible effects of age and sex on these responses. Previously collected data of untrained healthy men and women (age 19 to 78 years, n = 287 with 72 controls) were pooled for the present study. Muscle size and strength changed during RT are 4.8 ± 6.1 % (range from −11 to 30 %) and 21.1 ± 11.5 % (range from −8 to 60 %) compared to pre-RT, respectively. Age and sex did not affect to the RT responses. Fourteen percent and 12 % of the subjects were defined as high responders (>1 standard deviation (SD) from the group mean) for the RT-induced changes in muscle size and strength, respectively. When taking into account the results of non-training controls (upper 95 % CI), 29 and 7 % of the subjects were defined as low responders for the RT-induced changes in muscle size and strength, respectively. The muscle size and strength responses varied extensively between the subjects regardless of subject’s age and sex. Whether these changes are associated with, e.g., functional capacity and metabolic health improvements due to RT requires further studies.
Clinical and consumer market interest is increasingly directed toward the use of plant-based proteins as dietary components aimed at preserving or increasing skeletal muscle mass. However, recent evidence suggests that the ingestion of the plant-based proteins soy and wheat results in a lower muscle protein synthetic response when compared with several animal-based proteins. The possible lower anabolic properties of plant-based protein sources may be attributed to the lower digestibility of plant-based sources, in addition to greater splanchnic extraction and subsequent urea synthesis of plant protein-derived amino acids when compared with the ingestion of animal-based proteins. The latter may be related to the relative lack of specific essential amino acids in plant- as opposed to animal-based proteins. Furthermore, most plant proteins have a relatively low leucine content, which may further reduce their anabolic properties when compared with animal proteins. However, few studies have actually assessed the postprandial muscle protein synthetic response to the ingestion of plant proteins, with soy and wheat protein being the primary sources studied. Despite the proposed lower anabolic properties of plant vs. animal proteins, various strategies may be applied to augment the anabolic properties of plant proteins. These may include the following: 1) fortification of plant-based protein sources with the amino acids methionine, lysine, and/or leucine; 2) selective breeding of plant sources to improve amino acid profile; 3) consumption of greater amounts of plant-based protein sources; or 4) combining the ingestion of multiple protein sources to provide for a more balanced amino acid profile. However, the efficacy of such dietary strategies on postprandial muscle protein synthesis remains to be studied. Future research comparing the anabolic properties of a variety of plant-based proteins should define the preferred protein sources to be used in nutritional interventions to support skeletal muscle mass gain or maintenance in both healthy and clinical populations.
© 2015 American Society for Nutrition.
The present study aimed to determine the concurrent validity of ultrasound (US) measurement of the vastus lateralis muscle (VL) cross sectional area (CSA) having magnetic resonance imaging (MRI) as the gold-standard measurement, in a heterogeneous sample of participants. Thirty-one individuals (52.44 ± 16.37 yrs; 1.67 ± 0.11 m; 75.25 ± 13.82 kg) volunteered to participate in the study. All of the images were performed in the right leg. Imaging-fit technique (US) and computerized planimetry technique (US and MRI) were used to determine the VL CSA. The typical error of measurement (TE) was used to determine the concurrent validity of the US measurements. Our results demonstrated good validity of the US compared to the MRI measurements (TE = 0.37 cm²; CV = 1.75%). The Bland & Altman plot demonstrated bias of 0.07 ± 0.53 cm² and limits of agreement of 0.96 - 1.11 cm². Based on our TE, bias and limits of agreement, we concluded that the US image-fitting technique is valid to assess the VL CSA in a heterogeneous sample of participants. Thereby, the US can be used instead of the MRI to assess changes in skeletal muscle morphology.
To determine relationships between post-exercise changes in systemic [testosterone, growth hormone (GH), insulin like grow factor 1 (IGF-1) and interleukin 6 (IL-6)], or intramuscular [skeletal muscle androgen receptor (AR) protein content and p70S6K phosphorylation status] factors in a moderately-sized cohort of young men exhibiting divergent resistance training-mediated muscle hypertrophy.
Twenty three adult males completed 4 sessions•wk(-1) of resistance training for 16 wk. Muscle biopsies were obtained before and after the training period and acutely 1 and 5 h after the first training session. Serum hormones and cytokines were measured immediately, 15, 30 and 60 minutes following the first and last training sessions of the study.
Mean fiber area increased by 20% (range: -7 to 80%; P<0.001). Protein content of the AR was unchanged with training (fold change = 1.17 ± 0.61; P=0.19); however, there was a significant correlation between the changes in AR content and fiber area (r=0.60, P=0.023). Phosphorylation of p70S6K was elevated 5 hours following exercise, which was correlated with gains in mean fiber area (r=0.54, P=0.007). There was no relationship between the magnitude of the pre- or post-training exercise-induced changes in free testosterone, GH, or IGF-1 concentration and muscle fiber hypertrophy; however, the magnitude of the post exercise IL-6 response was correlated with muscle hypertrophy (r=0.48, P=0.019).
Post-exercise increases in circulating hormones are not related to hypertrophy following training. Exercise-induced changes in IL-6 correlated with hypertrophy, but the mechanism for the role of IL-6 in hypertrophy is not known. Acute increases, in p70S6K phosphorylation and changes in muscle AR protein content correlated with muscle hypertrophy implicating intramuscular rather than systemic processes in mediating hypertrophy.
Unlabelled:
Compared to soy, whey protein is higher in leucine, absorbed quicker and results in a more pronounced increase in muscle protein synthesis.
Objective:
To determine whether supplementation with whey promotes greater increases in muscle mass compared to soy or carbohydrate, we randomized non-resistance-trained men and women into groups who consumed daily isocaloric supplements containing carbohydrate (carb; n = 22), whey protein (whey; n = 19), or soy protein (soy; n = 22).
Methods:
All subjects completed a supervised, whole-body periodized resistance training program consisting of 96 workouts (~9 months). Body composition was determined at baseline and after 3, 6, and 9 months. Plasma amino acid responses to resistance exercise followed by supplement ingestion were determined at baseline and 9 months.
Results:
Daily protein intake (including the supplement) for carb, whey, and soy was 1.1, 1.4, and 1.4 g·kg body mass⁻¹, respectively. Lean body mass gains were significantly (p < 0.05) greater in whey (3.3 ± 1.5 kg) than carb (2.3 ± 1.7 kg) and soy (1.8 ± 1.6 kg). Fat mass decreased slightly but there were no differences between groups. Fasting concentrations of leucine were significantly elevated (20%) and postexercise plasma leucine increased more than 2-fold in whey. Fasting leucine concentrations were positively correlated with lean body mass responses.
Conclusions:
Despite consuming similar calories and protein during resistance training, daily supplementation with whey was more effective than soy protein or isocaloric carbohydrate control treatment conditions in promoting gains in lean body mass. These results highlight the importance of protein quality as an important determinant of lean body mass responses to resistance training.
Background
Consumption of moderate amounts of animal-derived protein has been shown to differently influence skeletal muscle hypertrophy during resistance training when compared with nitrogenous and isoenergetic amounts of plant-based protein administered in small to moderate doses. Therefore, the purpose of the study was to determine if the post-exercise consumption of rice protein isolate could increase recovery and elicit adequate changes in body composition compared to equally dosed whey protein isolate if given in large, isocaloric doses.
Methods
24 college-aged, resistance trained males were recruited for this study. Subjects were randomly and equally divided into two groups, either consuming 48 g of rice or whey protein isolate (isocaloric and isonitrogenous) on training days. Subjects trained 3 days per week for 8 weeks as a part of a daily undulating periodized resistance-training program. The rice and whey protein supplements were consumed immediately following exercise. Ratings of perceived recovery, soreness, and readiness to train were recorded prior to and following the first training session. Ultrasonography determined muscle thickness, dual emission x-ray absorptiometry determined body composition, and bench press and leg press for upper and lower body strength were recorded during weeks 0, 4, and 8. An ANOVA model was used to measure group, time, and group by time interactions. If any main effects were observed, a Tukey post-hoc was employed to locate where differences occurred.
Results
No detectable differences were present in psychometric scores of perceived recovery, soreness, or readiness to train (p > 0.05). Significant time effects were observed in which lean body mass, muscle mass, strength and power all increased and fat mass decreased; however, no condition by time interactions were observed (p > 0.05).
Conclusion
Both whey and rice protein isolate administration post resistance exercise improved indices of body composition and exercise performance; however, there were no differences between the two groups.
Key points
The branched‐chain amino acid (BCAA) leucine acts as both a ‘trigger’ for the initiation of protein synthesis, and as a substrate for newly synthesized protein.
As a BCAA, leucine can be metabolized within skeletal muscle, leaving open the possibility that leucine metabolites might possess anabolic properties.
One metabolite in particular, β‐hydroxy‐β‐methylbutyrate (HMB), has shown positive effects on lean body mass and strength following exercise, and in disease‐related muscle wasting, yet its impact on acute human muscle protein turnover is undefined.
We report here that HMB stimulates muscle protein synthesis to a similar extent to leucine. HMB was also found to decrease muscle protein breakdown.
Our observation that HMB enhances muscle protein anabolism may partly (or wholly) underlie its pre‐defined anabolic/anti‐catabolic supplemental efficacy in humans.
Abstract Maintenance of skeletal muscle mass is contingent upon the dynamic equilibrium (fasted losses–fed gains) in protein turnover. Of all nutrients, the single amino acid leucine (Leu) possesses the most marked anabolic characteristics in acting as a trigger element for the initiation of protein synthesis. While the mechanisms by which Leu is ‘sensed’ have been the subject of great scrutiny, as a branched‐chain amino acid, Leu can be catabolized within muscle, thus posing the possibility that metabolites of Leu could be involved in mediating the anabolic effect(s) of Leu. Our objective was to measure muscle protein anabolism in response to Leu and its metabolite HMB. Using [1,2‐ ¹³ C 2 ]Leu and [ ² H 5 ]phenylalanine tracers, and GC‐MS/GC‐C‐IRMS we studied the effect of HMB or Leu alone on MPS (by tracer incorporation into myofibrils), and for HMB we also measured muscle proteolysis (by arteriovenous (A–V) dilution). Orally consumed 3.42 g free‐acid (FA‐HMB) HMB (providing 2.42 g of pure HMB) exhibited rapid bioavailability in plasma and muscle and, similarly to 3.42 g Leu, stimulated muscle protein synthesis (MPS; HMB +70% vs . Leu +110%). While HMB and Leu both increased anabolic signalling (mechanistic target of rapamycin; mTOR), this was more pronounced with Leu (i.e. p70S6K1 signalling ≤90 min vs . ≤30 min for HMB). HMB consumption also attenuated muscle protein breakdown (MPB; −57%) in an insulin‐independent manner. We conclude that exogenous HMB induces acute muscle anabolism (increased MPS and reduced MPB) albeit perhaps via distinct, and/or additional mechanism(s) to Leu.
The content of this manuscript is intended to assist the reader in collecting valid and reliable data for quantifying muscular strength and power. Various drawbacks and pitfalls of specific tests, as well as recommendations for the practitioner are also provided. The content is divided into sections covering isometric, isotonic, field tests, and isokinetic modes of exercise. Inherent in these modes are both concentric and eccentric muscle actions as well as both open and closed kinetic chain activities. For Isometric testing, contractions should occur over a four to five seconds duration with a one second transition period at the start of the contraction. At least one minute of rest should be provided between contractions. For each muscle tested at each position, at least three contractions should be performed although more may be performed if deemed necessary by the tester. For isotonic testing, the 1-RM test should be performed. After the general warm-up, the subject should perform a specific warm-up set of 8 repetitions at approximately 50% of the estimated 1-RM followed by another set of 3 repetitions at 70% of the estimated 1-RM. Subsequent lifts are single repetitions of progressively heavier weights until failure. Repeat until the 1-RM is determined to the desired level of precision. The rest interval between sets should be not less than one and not more than five minutes. The optimal number of single repetitions ranges from three to five. Data and guidelines of the following field tests are also provided; vertical jump, bench press, Wingate anaerobic cycle test (WAT), and the Margaria stair-run test. For isokinetic testing, details are provided for testing peak torque, work, power, endurance, and estimation of fiber type percentages.
Sarcopenia seems to be attributed to a blunted muscle protein synthetic response to food intake and exercise. This blunted response could be the result of impaired protein digestion and absorption kinetics and lead to lower postprandial plasma amino acid availability.
The objective was to compare in vivo dietary protein digestion and absorption kinetics and subsequent postprandial muscle protein synthesis rates at rest and after exercise between young and elderly men.
Young and elderly men consumed a 20-g bolus of intrinsically L-[1-(13)C]phenylalanine-labeled protein at rest or after exercise. Continuous infusions with L-[ring-(2)H(5)]phenylalanine were applied, and blood and muscle samples were collected to assess in vivo protein digestion and absorption kinetics and subsequent postprandial muscle protein synthesis rates.
Exogenous phenylalanine appearance rates expressed over time did not differ between groups. No differences were observed in plasma phenylalanine availability between the young (51 ± 2%) and elderly (51 ± 1%) men or between the rest (52 ± 1%) and exercise (49 ± 1%) conditions. Muscle protein synthesis rates calculated from the oral tracer were 0.0620 ± 0.0065%/h and 0.0560 ± 0.0039%/h for the rest condition and 0.0719 ± 0.0057%/h and 0.0727 ± 0.0040%/h for the exercise condition in young and elderly men, respectively (age effect: P = 0.62; exercise effect: P < 0.05; interaction of age and exercise: P = 0.52).
Dietary protein digestion and absorption kinetics are not impaired after exercise or at an older age. Exercising before protein intake allows for a greater use of dietary protein-derived amino acids for de novo muscle protein synthesis in both young and elderly men. This trial was registered at clinicaltrials.gov as NCT00557388.
Vegetarians and vegans exclude certain food sources of vitamin D from their diet, but it is not clear to what extent this affects plasma concentrations of 25-hydroxyvitamin D (25(OH)D). The objective was to investigate differences in vitamin D intake and plasma concentrations of 25(OH)D among meat eaters, fish eaters, vegetarians and vegans.
A cross-sectional analysis.
United Kingdom.
Plasma 25(OH)D concentrations were measured in 2107 white men and women (1388 meat eaters, 210 fish eaters, 420 vegetarians and eighty-nine vegans) aged 20-76 years from the European Prospective Investigation into Cancer and Nutrition (EPIC)-Oxford cohort.
Plasma 25(OH)D concentrations reflected the degree of animal product exclusion and, hence, dietary intake of vitamin D; meat eaters had the highest mean intake of vitamin D (3·1 (95 % CI 3·0, 3·2) μg/d) and mean plasma 25(OH)D concentrations (77·0 (95 % CI 75·4, 78·8) nmol/l) and vegans the lowest (0·7 (95 % CI 0·6, 0·8) μg/d and 55·8 (95 % CI 51·0, 61·0) nmol/l, respectively). The magnitude of difference in 25(OH)D concentrations between meat eaters and vegans was smaller (20 %) among those participants who had a blood sample collected during the summer months (July-September) compared with the winter months (38 %; January-March). The prevalence of low plasma concentrations of 25(OH)D (<25 nmol/l) during the winter and spring ranged from <1 % to 8 % across the diet groups.
Plasma 25(OH)D concentrations were lower in vegetarians and vegans than in meat and fish eaters; diet is an important determinant of plasma 25(OH)D in this British population.
We previously showed that human muscle protein synthesis (MPS) increased during infusion of amino acids (AAs) and peaked at ≈120 min before returning to baseline rates, despite elevated plasma AA concentrations.
We tested whether a protein meal elicited a similar response and whether signaling responses that regulate messenger RNA translation matched MPS changes.
Eight postabsorptive healthy men (≈21 y of age) were studied during 8.5 h of primed continuous infusion of [1,2-¹³C₂]leucine with intermittent quadriceps biopsies for determination of MPS and anabolic signaling. After 2.5 h, subjects consumed 48 g whey protein.
At 45-90 min after oral protein bolus, mean (± SEM) myofibrillar protein synthesis increased from 0.03 ± 0.003% to 0.10 ± 0.01%/h; thereafter, myofibrillar protein synthesis returned to baseline rates even though plasma essential AA (EAA) concentrations remained elevated (+130% at 120 min, +80% at 180 min). The activity of protein kinase B (PKB) and phosphorylation of eukaryotic initiation factor 4G preceded the rise of MPS and increases in phosphorylation of ribosomal protein kinase S6 (S6K1), and 4E-binding protein 1 (4EBP1) was superimposable with MPS responses until 90 min. However, although MPS decreased thereafter, all signals, with the exception of PKB activity (which mirrored insulin responses), remained elevated, which echoed the slowly declining plasma EAA profile. The phosphorylation of eukaryotic initiation factor 2α increased only at 180 min. Thus, discordance existed between MPS and the mammalian target of rapamycin complex 1 (mTORC1) and signaling (ie, S6K1 and 4EBP1 phosphorylation).
We confirm our previous findings that MPS responses to AAs are transient, even with oral protein bolus. However, changes in MPS only reflect elevated mTORC1 signaling during the upswing in MPS.
Vegans, and to a lesser extent vegetarians, have low average circulating concentrations of vitamin B12; however, the relation between factors such as age or time on these diets and vitamin B12 concentrations is not clear. The objectives of this study were to investigate differences in serum vitamin B12 and folate concentrations between omnivores, vegetarians and vegans and to ascertain whether vitamin B12 concentrations differed by age and time on the diet.
A cross-sectional analysis involving 689 men (226 omnivores, 231 vegetarians and 232 vegans) from the European Prospective Investigation into Cancer and Nutrition Oxford cohort.
Mean serum vitamin B12 was highest among omnivores (281, 95% CI: 270-292 pmol/l), intermediate among vegetarians (182, 95% CI: 175-189 pmol/l) and lowest among vegans (122, 95% CI: 117-127 pmol/l). In all, 52% of vegans, 7% of vegetarians and one omnivore were classified as vitamin B12 deficient (defined as serum vitamin B12 <118 pmol/l). There was no significant association between age or duration of adherence to a vegetarian or a vegan diet and serum vitamin B12. In contrast, folate concentrations were highest among vegans, intermediate among vegetarians and lowest among omnivores, but only two men (both omnivores) were categorized as folate deficient (defined as serum folate <6.3 nmol/l).
Vegans have lower vitamin B12 concentrations, but higher folate concentrations, than vegetarians and omnivores. Half of the vegans were categorized as vitamin B12 deficient and would be expected to have a higher risk of developing clinical symptoms related to vitamin B12 deficiency.
The US Department of Agriculture Automated Multiple-Pass Method (AMPM) is used for collecting 24-h dietary recalls in What We Eat In America, the dietary interview component of the National Health and Nutrition Examination Survey. Because the data have important program and policy applications, it is essential that the validity of the method be tested.
The accuracy of the AMPM was evaluated by comparing reported energy intake (EI) with total energy expenditure (TEE) by using the doubly labeled water (DLW) technique.
The 524 volunteers, aged 30-69 y, included an equal number of men and women recruited from the Washington, DC, area. Each subject was dosed with DLW on the first day of the 2-wk study period; three 24-h recalls were collected during the 2-wk period by using the AMPM. The first recall was conducted in person, and subsequent recalls were over the telephone.
Overall, the subjects underreported EI by 11% compared with TEE. Normal-weight subjects [body mass index (in kg/m(2)) < 25] underreported EI by <3%. By using a linear mixed model, 95% CIs were determined for the ratio of EI to TEE. Approximately 78% of men and 74% of women were classified as acceptable energy reporters (within 95% CI of EI:TEE). Both the percentage by which energy was underreported and the percentage of subjects classified as low energy reporters (<95% CI of EI:TEE) were highest for subjects classified as obese (body mass index > 30).
Although the AMPM accurately reported EIs in normal-weight subjects, research is warranted to enhance its accuracy in overweight and obese persons.
1. Measurements have been made of whole-body and skeletal muscle protein synthesis in fed and fasted adults with l-[1-13C]leucine.
2. The marked increase in whole-body synthesis on feeding largely reflects the changes in protein synthesis in muscle, which doubles on feeding, compared with a 40% increase in that of the rest of the body.
3. Skeletal muscle in fed man contributes more than half to total protein synthesis occurring in the whole body.
Muscle mass and function are improved in the elderly during resistance exercise training. These improvements must result from alterations in the rates of muscle protein synthesis and breakdown. We determined the rate of quadriceps muscle protein synthesis using the in vivo rate of incorporation of intravenously infused [13C]leucine into mixed-muscle protein in both young (24 yr) and elderly (63-66 yr) men and women before and at the end of 2 wk of resistance exercise training. Before training, the fractional rate of muscle protein synthesis was lower in the elderly than in the young (0.030 +/- 0.003 vs. 0.049 +/- 0.004%/h; P = 0.004) but increased (P < 0.03) to a comparable rate of muscle protein synthesis in both young (0.075 +/- 0.009%/h) and elderly subjects (0.076 +/- 0.011%/h) after 2 wk of exercise. In the elderly, muscle mass, 24-h urinary 3-methylhistidine and creatinine excretion, and whole body protein breakdown rate determined during the [13C]leucine infusion were not changed after 2 wk of exercise. These findings demonstrate that, during the initial phase of a resistance exercise training program, a marked increase in quadriceps muscle protein synthesis rate occurs in elderly and young adults without an increase in the rate of whole body protein breakdown. In the elderly, this was not accompanied by an increase in urinary 3-methylhistidine excretion, an index of myofibrillar protein breakdown.
We investigated the effects of the nature of the flooding amino acid on the rate of incorporation of tracer leucine into human skeletal muscle sampled by biopsy. Twenty-three healthy young men (24.5 +/- 5. 0 yr, 76.2 +/- 8.3 kg) were studied in groups of four or five. First, the effects of flooding with phenylalanine, threonine, or arginine (all at 0.05 g/kg body wt) on the incorporation of tracer [13C]leucine were studied. Then the effects of flooding with labeled [13C]glycine [0.1 g/kg body wt, 20 atoms percent excess (APE)] and [13C]serine (0.05 g/kg body wt, 15 APE) on the incorporation of simultaneously infused [13C]leucine were investigated. When a large dose of phenylalanine or threonine was administered, incorporation of the tracer leucine was significantly increased (from 0.036 to 0. 067 %/h and 0.037 to 0.070 %/h, respectively; each P < 0.01). However, when arginine, glycine, or serine was administered as a flooding dose, no stimulation of tracer leucine incorporation could be observed. These results, together with those previously obtained, suggest that large doses of individual essential, but not nonessential, amino acids are able to stimulate incorporation of constantly infused tracer amino acids into human muscle protein.
We used a previously developed compartmental model to assess the postprandial distribution and metabolism of dietary nitrogen (N) in the splanchnic and peripheral areas after the ingestion of a single mixed meal containing either (15)N-labeled milk or soy purified protein. Although the lower whole-body retention of dietary N from soy protein was measured experimentally, the splanchnic retention of dietary N was predicted by the model not to be affected by the protein source, and its incorporation into splanchnic proteins was predicted to reach approximately 35% of ingested N at 8 h after both meals. However, dietary N intestinal absorption and its appearance in splanchnic free amino acids were predicted to be more rapid from soy protein and were associated with a higher deamination, concomitant with a higher efficiency of incorporation of dietary N into proteins in the splanchnic bed. In contrast, soy protein was predicted to cause a reduction in peripheral dietary N uptake, as a consequence of both similar splanchnic retention and increased oxidation compared with milk protein. In addition, protein synthesis efficiency was reduced in the peripheral area after soy protein intake, leading to dietary N incorporation in peripheral proteins that fell from 26 to 19% of ingested N 8 h after milk and soy protein ingestion, respectively. Such a model thus enables a description of the processes involved in the differential metabolic utilization of dietary proteins and constitutes a valuable tool for further definition of the notion of protein quality during the period of protein gain.
Aging is associated with reductions in muscle mass and strength, but nutrition and exercise interventions can delay this progression and enhance the quality of life.
We examined whether the predominant source of protein consumed by older men influenced measures of muscle size and strength, body composition, resting energy expenditure, and skeletal muscle creatine concentrations in response to 12 wk of resistive training.
After consuming a lactoovovegetarian (LOV) diet for 2 wk, 21 men aged 65 +/- 5 y were randomly assigned to either consume a beef-containing (BC) diet (n = 10) or to continue the LOV diet (n = 11) throughout resistive training. The BC diet included 0.6 g protein. kg(-1). d(-1) from beef and the LOV diet included 0.6 g protein. kg(-1). d(-1) from textured vegetable protein (soy) sources. The remaining protein in the diets came from self-selected LOV sources.
The mean total protein intake for both groups ranged from 1.03 to 1.17 g. kg(-1). d(-1) during the intervention. Men in both groups had improvements (14-38%) in maximal dynamic strength of all the muscle groups trained with no significant difference between groups. With resistive training, cross-sectional muscle area of the vastus lateralis increased in both groups (4.2 +/- 3.0% and 6.0 +/- 2.6% for the LOV and BC groups, respectively) with no significant difference between groups. Body composition, resting energy expenditure, and concentrations of muscle creatine, phosphocreatine, and total creatine did not differ significantly between groups or change over time.
These data suggest that increases in muscle strength and size were not influenced by the predominant source of protein consumed by older men with adequate total protein intake.
Soy proteins have been shown to result in lower postprandial nitrogen retention than milk proteins, but the mechanisms underlying these differences have not been elucidated. To investigate this question, we measured the postprandial kinetics of the appearance of individual (15)N-amino acids in the serum of healthy adults after the ingestion of either (15)N-soy (n = 8) or (15)N-milk proteins (n = 8) in a mixed single meal (46 kJ/kg). The kinetics of total and dietary amino acids (AA) in the peripheral circulation were characterized by an earlier and higher peak after soy protein ingestion. Dietary AA levels peaked at 2.5 h in the soy group vs. 3.9 h in the milk group (P < 0.02). This time interval difference between groups was associated with a faster transfer of dietary N into urea in the soy group (peak at 3 vs. 4.75 h in the milk group, P < 0.005) and a higher level of incorporation into the serum protein pool from 3 to 8 h after the soy meal. The dietary AA pattern in the peripheral blood closely reflected the dietary protein AA pattern. Postprandial glucose, insulin, and glucagon levels and profiles did not differ between groups. Soy AA were digested more rapidly and were directed toward both deamination pathways and liver protein synthesis more than milk AA. We conclude that differences in the metabolic postprandial fates of soy and milk proteins are due mainly to differences in digestion kinetics; however, the AA composition of dietary proteins may also play a role.
Nutritional supplementation may be used to treat muscle loss with aging (sarcopenia). However, if physical activity does not increase, the elderly tend to compensate for the increased energy delivered by the supplements with reduced food intake, which results in a calorie substitution rather than supplementation. Thus, an effective supplement should stimulate muscle anabolism more efficiently than food or common protein supplements. We have shown that balanced amino acids stimulate muscle protein anabolism in the elderly, but it is unknown whether all amino acids are necessary to achieve this effect.
We assessed whether nonessential amino acids are required in a nutritional supplement to stimulate muscle protein anabolism in the elderly.
We compared the response of muscle protein metabolism to either 18 g essential amino acids (EAA group: n = 6, age 69 +/- 2 y; +/- SD) or 40 g balanced amino acids (18 g essential amino acids + 22 g nonessential amino acids, BAA group; n = 8, age 71 +/- 2 y) given orally in small boluses every 10 min for 3 h to healthy elderly volunteers. Muscle protein metabolism was measured in the basal state and during amino acid administration via L-[ring-(2)H(5)]phenylalanine infusion, femoral arterial and venous catheterization, and muscle biopsies.
Phenylalanine net balance (in nmol x min(-1). 100 mL leg volume(-1)) increased from the basal state (P < 0.01), with no differences between groups (BAA: from -16 +/- 5 to 16 +/- 4; EAA: from -18 +/- 5 to 14 +/- 13) because of an increase (P < 0.01) in muscle protein synthesis and no change in breakdown.
Essential amino acids are primarily responsible for the amino acid-induced stimulation of muscle protein anabolism in the elderly.
Physical inactivity is a global concern, but diverse physical activity measures in use prevent international comparisons. The International Physical Activity Questionnaire (IPAQ) was developed as an instrument for cross-national monitoring of physical activity and inactivity.
Between 1997 and 1998, an International Consensus Group developed four long and four short forms of the IPAQ instruments (administered by telephone interview or self-administration, with two alternate reference periods, either the "last 7 d" or a "usual week" of recalled physical activity). During 2000, 14 centers from 12 countries collected reliability and/or validity data on at least two of the eight IPAQ instruments. Test-retest repeatability was assessed within the same week. Concurrent (inter-method) validity was assessed at the same administration, and criterion IPAQ validity was assessed against the CSA (now MTI) accelerometer. Spearman's correlation coefficients are reported, based on the total reported physical activity.
Overall, the IPAQ questionnaires produced repeatable data (Spearman's rho clustered around 0.8), with comparable data from short and long forms. Criterion validity had a median rho of about 0.30, which was comparable to most other self-report validation studies. The "usual week" and "last 7 d" reference periods performed similarly, and the reliability of telephone administration was similar to the self-administered mode.
The IPAQ instruments have acceptable measurement properties, at least as good as other established self-reports. Considering the diverse samples in this study, IPAQ has reasonable measurement properties for monitoring population levels of physical activity among 18- to 65-yr-old adults in diverse settings. The short IPAQ form "last 7 d recall" is recommended for national monitoring and the long form for research requiring more detailed assessment.
The effects of the presence of some of the important antinutritional factors on protein and amino digestibilities of food and feed products was presented. Antinutritional factors may occur naturally, such as glucosinolates in mustard and rapeseed protein products, trypsin inhibitors and hemagglutinins in legumes, tannins in legumes and cereals, phytates in cereals and oilseeds, and gossypol in cottonseed protein products. It was observed that presence of high levels of dietry trypsin inhibitors from grain legumes caused reductions in protein and amino acid digestibilities of upto 50% in living systems. It was also observed that high levels of tannins in cereals resulted in reduced protein and amino acid digestibilities of upto 23% in living systems.
The popularity of resistance training has grown immensely over the past 25 years, with extensive research demonstrating that not only is resistance training an effective method to improve neuromuscular function, it can also be equally effective in maintaining or improving individual health status. However, designing a resistance training programme is a complex process that incorporates several acute programme variables and key training principles. The effectiveness of a resistance training programme to achieve a specific training outcome (i.e. muscular endurance, hypertrophy, maximal strength, or power) depends on manipulation of the acute programme variables, these include: (i) muscle action; (ii) loading and volume; (iii) exercise selection and order; (iv) rest periods; (v) repetition velocity; and (vi) frequency. Ultimately, it is the acute programme variables, all of which affect the degree of the resistance training stimuli, that determine the magnitude to which the neuromuscular, neuroendocrine and musculoskeletal systems adapt to both acute and chronic resistance exercise. This article reviews the available research that has examined the application of the acute programme variables and their influence on exercise performance and training adaptations. The concepts presented in this article represent an important approach to effective programme design. Therefore, it is essential for those involved with the prescription of resistance exercise (i.e. strength coaches, rehabilitation specialists, exercise physiologists) to acquire a fundamental understanding of the acute programme variables and the importance of their practical application in programme design.
Skeletal muscle has indispensable roles in regulating whole body health (e.g. glycemic control, energy consumption) and, in being central in locomotion, is crucial in maintaining quality-of-life. Therefore, understanding the regulation of muscle mass is of significant importance. Resistance exercise training (RET) combined with supportive nutrition is an effective strategy to achieve muscle hypertrophy by driving chronic elevations in muscle protein synthesis (MPS). The regulation of muscle protein synthesis is a coordinated process, in requiring ribosomes to translate mRNA and sufficient myonuclei density to provide the platform for ribosome and mRNA transcription; as such MPS is determined by both translational efficiency (ribosome activity) and translational capacity (ribosome number). Moreover, as the muscle protein pool expands during hypertrophy, translation capacity (i.e. ribosomes and myonuclei content) could theoretically become rate-limiting such that an inability to expand these pools through ribosomal biogenesis and satellite cell (SC) mediated myonuclear addition could limit growth potential. Simple measures of RNA (ribosome content) and DNA (SC/Myonuclei number) concentrations reveal that these pools do increase with hypertrophy; yet whether these adaptations are a pre-requisite or a limiting factor for hypertrophy is unresolved and highly debated. This is primarily due to methodological limitations and many assumptions being made on static measures or correlative associations. However recent advances within the field using stable isotope tracers shows promise in resolving these questions in muscle adaptation.
Background
Vegetarian diets exclude meat, seafood, and products containing these foods. Although the vegetarian lifestyle could lead to a better health status in adults, it may also bear risks for certain nutritional deficiencies. Cross-sectional studies and narrative reviews have shown that the iron status of vegetarians is compromised by the absence of highly bioavailable haem-iron in meatless diets and the inhibiting effect of certain components present in plant foods on non-haem iron bioavailability.
Methods
The databases Pubmed, Scopus, Embase, and Cochrane Central Register of Controlled Trials were searched for studies comparing serum ferritin, as the major laboratory parameter for iron status of adult vegetarians with non-vegetarian control groups. A qualitative review was conducted as well as an inverse-variance random-effects meta-analysis to pool available data. In addition the effect of vegetarian diets according to gender was investigated with a subgroup analysis. The results were validated using a sensitivity analysis.
Results
A total of 27 cross-sectional studies and 3 interventional studies were selected for the systematic review. The meta-analysis which combined data of 24 cross-sectional studies showed that adult vegetarians have significantly lower serum ferritin levels than their non-vegetarian controls (−29.71 µg/l, 95% CI [−39.69, −19.73], p<0.01). Inclusion of semi-vegetarian diets did not change the results considerably (−23.27 µg/l, 95% CI [−29.77, −16.76], p<0.01). The effects were more pronounced in men (−61.88 µg/l, 95% CI [−85.59, −38.17], p<0.01) than in both premenopausal women (−17.70 μg/l, 95% CI [−29.80, −5.60], p<0.01) and all women (−13.50 μg/l, 95% CI [−22.96, −4.04], p<0.01), respectively.
Conclusions
In conclusion our results showed that vegetarians are more likely to have lower iron stores compared with non-vegetarians. However, since high iron stores are also a risk factor for certain non-communicable diseases, such as type II diabetes, it is recommended that not only vegetarians but also non-vegetarians should regularly control their iron status and improve their diet regarding the content and bioavailability of iron by consuming more plants and less meat.
The intake of whey, compared with casein and soy protein intakes, stimulates a greater acute response of muscle protein synthesis (MPS) to protein ingestion in rested and exercised muscle.
We characterized the dose-response relation of postabsorptive rates of myofibrillar MPS to increasing amounts of whey protein at rest and after exercise in resistance-trained, young men.
Volunteers (n = 48) consumed a standardized, high-protein (0.54 g/kg body mass) breakfast. Three hours later, a bout of unilateral exercise (8 × 10 leg presses and leg extensions; 80% one-repetition maximum) was performed. Volunteers ingested 0, 10, 20, or 40 g whey protein isolate immediately (∼10 min) after exercise. Postabsorptive rates of myofibrillar MPS and whole-body rates of phenylalanine oxidation and urea production were measured over a 4-h postdrink period by continuous tracer infusion of labeled [(13)C6] phenylalanine and [(15)N2] urea.
Myofibrillar MPS (±SD) increased (P < 0.05) above 0 g whey protein (0.041 ± 0.015%/h) by 49% and 56% with the ingestion of 20 and 40 g whey protein, respectively, whereas no additional stimulation was observed with 10 g whey protein (P > 0.05). Rates of phenylalanine oxidation and urea production increased with the ingestion of 40 g whey protein.
A 20-g dose of whey protein is sufficient for the maximal stimulation of postabsorptive rates of myofibrillar MPS in rested and exercised muscle of ∼80-kg resistance-trained, young men. A dose of whey protein >20 g stimulates amino acid oxidation and ureagenesis. This trial was registered at http://www.isrctn.org/ as ISRCTN92528122.
Aging has been associated with a reduced muscle protein synthetic response to protein intake, termed anabolic resistance. Physical activity performed prior to protein intake increases the use of protein derived amino acids for postprandial muscle protein accretion in senescent muscle. Thus, the level of habitual physical activity may be fundamental to maintain the anabolic responsiveness to protein intake with aging.
Increased amino acid availability stimulates muscle protein synthesis, however, aged muscle appears less responsive to the anabolic effects of amino acids when compared to the young. We aimed to compare changes in myofibrillar protein synthesis (MPS) in elderly men at rest and after resistance exercise following ingestion of different doses of soy protein and compare the responses to those we previously observed with ingestion of whey protein isolate.
Thirty elderly men (age 71 ± 5 y) completed a bout of unilateral knee-extensor resistance exercise prior to ingesting no protein (0 g), or either 20 g or 40 g of soy protein isolate (0, S20, and S40 respectively). We compared these responses to previous responses from similar aged men who had ingested 20 g and 40 g of whey protein isolate (W20 and W40). A primed constant infusion of L-[1-13 C]leucine and L-[ring-13 C6]phenylalanine and skeletal muscle biopsies were used to measure whole-body leucine oxidation and MPS over 4 h post-protein consumption in both exercised and non-exercised legs.
Whole-body leucine oxidation increased with protein ingestion and was significantly greater for S20 vs. W20 (P = 0.003). Rates of MPS for S20 were less than W20 (P = 0.02) and not different from 0 g (P = 0.41) in both exercised and non-exercised leg muscles. For S40, MPS was also reduced compared with W40 under both rested and post-exercise conditions (both P < 0.005); however S40 increased MPS greater than 0 g under post-exercise conditions (P = 0.04).
The relationship between protein intake and MPS is both dose and protein source-dependent, with isolated soy showing a reduced ability, as compared to isolated whey protein, to stimulate MPS under both rested and post-exercise conditions. These differences may relate to the lower postprandial leucinemia and greater rates of amino acid oxidation following ingestion of soy versus whey protein.
This study was designed to compare the acute response of mixed muscle protein synthesis (MPS) to rapidly (i.e., whey hydrolysate and soy) and slowly (i.e., micellar casein) digested proteins both at rest and after resistance exercise. Three groups of healthy young men (n = 6 per group) performed a bout of unilateral leg resistance exercise followed by the consumption of a drink containing an equivalent content of essential amino acids (10 g) as either whey hydrolysate, micellar casein, or soy protein isolate. Mixed MPS was determined by a primed constant infusion of l-[ring-(13)C(6)]phenylalanine. Ingestion of whey protein resulted in a larger increase in blood essential amino acid, branched-chain amino acid, and leucine concentrations than either casein or soy (P < 0.05). Mixed MPS at rest (determined in the nonexercised leg) was higher with ingestion of faster proteins (whey = 0.091 +/- 0.015, soy = 0.078 +/- 0.014, casein = 0.047 +/- 0.008%/h); MPS after consumption of whey was approximately 93% greater than casein (P < 0.01) and approximately 18% greater than soy (P = 0.067). A similar result was observed after exercise (whey > soy > casein); MPS following whey consumption was approximately 122% greater than casein (P < 0.01) and 31% greater than soy (P < 0.05). MPS was also greater with soy consumption at rest (64%) and following resistance exercise (69%) compared with casein (both P < 0.01). We conclude that the feeding-induced simulation of MPS in young men is greater after whey hydrolysate or soy protein consumption than casein both at rest and after resistance exercise; moreover, despite both being fast proteins, whey hydrolysate stimulated MPS to a greater degree than soy after resistance exercise. These differences may be related to how quickly the proteins are digested (i.e., fast vs. slow) or possibly to small differences in leucine content of each protein.
Muscle protein synthesis (MPS) and muscle protein breakdown are simultaneous ongoing processes. Here, we examine evidence for how protein quality can affect exercise-induced muscle protein anabolism or protein balance (MPS minus muscle protein breakdown). Evidence is highlighted showing differences in the responses of MPS, and muscle protein accretion, with ingestion of milk-based and soy-based proteins in young and elderly persons.
Protein consumption, and the accompanying hyperaminoacidemia, stimulates an increase in MPS and a small suppression of muscle protein breakdown. Beyond the feeding-induced rise in MPS, small incremental addition of new muscle protein mass occurs following intense resistance exercise which over time (i.e. resistance training) leads to muscle hypertrophy. Athletes make use of the paradigm of resistance training and eating to maximize the gains in their skeletal muscle mass. Importantly, however, metabolically active skeletal muscle can offset the morbidities associated with the sarcopenia of aging such as type II diabetes, decline in aerobic fitness and the reduction in metabolic rate that can lead to fat mass accumulation.
Recent evidence suggests that consumption of different proteins can affect the amplitude and possibly duration of MPS increases after feeding and this effect interacts and is possibly accentuated with resistance exercise.
The anabolic effect of resistance exercise is enhanced by the provision of dietary protein.
We aimed to determine the ingested protein dose response of muscle (MPS) and albumin protein synthesis (APS) after resistance exercise. In addition, we measured the phosphorylation of candidate signaling proteins thought to regulate acute changes in MPS.
Six healthy young men reported to the laboratory on 5 separate occasions to perform an intense bout of leg-based resistance exercise. After exercise, participants consumed, in a randomized order, drinks containing 0, 5, 10, 20, or 40 g whole egg protein. Protein synthesis and whole-body leucine oxidation were measured over 4 h after exercise by a primed constant infusion of [1-(13)C]leucine.
MPS displayed a dose response to dietary protein ingestion and was maximally stimulated at 20 g. The phosphorylation of ribosomal protein S6 kinase (Thr(389)), ribosomal protein S6 (Ser(240/244)), and the epsilon-subunit of eukaryotic initiation factor 2B (Ser(539)) were unaffected by protein ingestion. APS increased in a dose-dependent manner and also reached a plateau at 20 g ingested protein. Leucine oxidation was significantly increased after 20 and 40 g protein were ingested.
Ingestion of 20 g intact protein is sufficient to maximally stimulate MPS and APS after resistance exercise. Phosphorylation of candidate signaling proteins was not enhanced with any dose of protein ingested, which suggested that the stimulation of MPS after resistance exercise may be related to amino acid availability. Finally, dietary protein consumed after exercise in excess of the rate at which it can be incorporated into tissue protein stimulates irreversible oxidation.
1. Anterior tibial muscle protein synthesis in seven healthy postabsorptive men was determined from increases in muscle protein bound leucine enrichment during a primed continuous infusion of l-[1−13C]leucine. Biopsies were taken 30 min after the beginning of leucine infusion (when plasma 13C enrichment was steady), 240 min later during continued fasting and again after 240 min of infusion of a mixed amino acid solution which increased plasma total amino acid concentrations by 37%. The mean enrichment of 13C in plasma α-ketoisocaproate was used as an index of the enrichment of the precursor pool for leucine metabolism.
2. Anterior tibial muscle mixed protein synthetic rate during fasting was 0.055 (sd 0.008) %/h and this increased by an average of 35% during infusion of mixed amino acid to 0.074 (sd 0.021) %/h (P < 0.05).
3. Whole-body protein breakdown (expressed as the rate of endogenous leucine appearance in plasma) was 121 (sd 8) μmol h−1 kg−1 during fasting and decreased (P < 0.01) by an average of 12% during amino acid infusion. Leucine oxidation was 18 (sd 3) μmol h−1 kg−1 during fasting and increased (P < 0.001) by 89% during amino acid infusion. Whole-body protein synthesis (non-oxidative leucine disappearance) was 104 (sd 6) μmol h−1 kg−1 during fasting and rose by 13% (P < 0.001) during mixed amino acid infusion.
4. 13C enrichment of muscle free leucine was only 61 (sd 19) % of that in plasma α-ketoisocaproate and this increased to 74 (sd 16) % (P < 0.02) during mixed amino acid infusion.
5. The results suggest that increased availability of amino acids reverses whole-body protein balance from negative to positive and a major component of this is the increase in muscle protein synthesis.
The rates of protein synthesis and degradation and of amino acid transport were determined in the leg muscle of untrained postabsorptive normal volunteers at rest and approximately 3 h after a resistance exercise routine. The methodology involved use of stable isotopic tracers of amino acids, arteriovenous catheterization of the femoral vessels, and biopsy of the vastus lateralis muscle. During postexercise recovery, the rate of intramuscular phenylalanine utilization for protein synthesis increased above the basal value by 108 +/- 18%, whereas the rate of release from proteolysis increased by 51 +/- 17%. Muscle protein balance improved (P < 0.05) after exercise but did not become positive (from -15 +/- 12 to -6 +/- 3 nmol phenylalanine.min-1.100 ml leg volume-1). After exercise, rates of inward transport of leucine, lysine, and alanine increased (P < 0.05) above the basal state from 132 +/- 16 to 208 +/- 29, from 122 +/- 8 to 260 +/- 8, and from 384 +/- 71 to 602 +/- 89 nmol.min-1.100 ml leg-1, respectively. Transport of phenylalanine did not change significantly. These results indicate that, during recovery after resistance exercise, muscle protein turnover is increased because of an acceleration of synthesis and degradation. A postexercise acceleration of amino acid transport may contribute to the relatively greater stimulation of protein synthesis.
Six normal untrained men were studied during the intravenous infusion of a balanced amino acid mixture (approximately 0.15 g.kg-1.h-1 for 3 h) at rest and after a leg resistance exercise routine to test the influence of exercise on the regulation of muscle protein kinetics by hyperaminoacidemia. Leg muscle protein kinetics and transport of selected amino acids (alanine, phenylalanine, leucine, and lysine) were isotopically determined using a model based on arteriovenous blood samples and muscle biopsy. The intravenous amino acid infusion resulted in comparable increases in arterial amino acid concentrations at rest and after exercise, whereas leg blood flow was 64 +/- 5% greater after exercise than at rest. During hyperaminoacidemia, the increases in amino acid transport above basal were 30-100% greater after exercise than at rest. Increases in muscle protein synthesis were also greater after exercise than at rest (291 +/- 42% vs. 141 +/- 45%). Muscle protein breakdown was not significantly affected by hyperminoacidemia either at rest or after exercise. We conclude that the stimulatory effect of exogenous amino acids on muscle protein synthesis is enhanced by prior exercise, perhaps in part because of enhanced blood flow. Our results imply that protein intake immediately after exercise may be more anabolic than when ingested at some later time.
Very limited data suggest that meat consumption by older people may promote skeletal muscle hypertrophy in response to resistance training (RT).
The objective of this study was to assess whether the consumption of an omnivorous (meat-containing) diet would influence RT-induced changes in whole-body composition and skeletal muscle size in older men compared with a lactoovovegetarian (LOV) (meat-free) diet.
Nineteen men aged 51-69 y participated in the study. During a 12-wk period of RT, 9 men consumed their habitual omnivorous diets, which provided approximately 50% of total dietary protein from meat sources (beef, poultry, pork, and fish) (mixed-diet group). Another 10 men were counseled to self-select an LOV diet (LOV-diet group).
Maximal strength of the upper- and lower-body muscle groups that were exercised during RT increased by 10-38% (P < 0.001), independent of diet. The RT-induced changes in whole-body composition and skeletal muscle size differed significantly between the mixed- and LOV-diet groups (time-by-group interactions, P < 0. 05). With RT, whole-body density, fat-free mass, and whole-body muscle mass increased in the mixed diet group but decreased in the LOV- diet group. Type II muscle fiber area of the vastus lateralis muscle increased with RT for all men combined (P < 0.01), and the increase tended to be greater in the mixed-diet group (16.2 +/- 4.4 %) than in the LOV diet group (7.3 +/- 5.1%). Type I fiber area was unchanged with RT in both diet groups.
Consumption of a meat-containing diet contributed to greater gains in fat-free mass and skeletal muscle mass with RT in older men than did an LOV diet.
The protein digestibility-corrected amino acid score (PDCAAS) has been adopted by FAO/WHO as the preferred method for the measurement of the protein value in human nutrition. The method is based on comparison of the concentration of the first limiting essential amino acid in the test protein with the concentration of that amino acid in a reference (scoring) pattern. This scoring pattern is derived from the essential amino acid requirements of the preschool-age child. The chemical score obtained in this way is corrected for true fecal digestibility of the test protein. PDCAAS values higher than 100% are not accepted as such but are truncated to 100%. Although the principle of the PDCAAS method has been widely accepted, critical questions have been raised in the scientific community about a number of issues. These questions relate to 1) the validity of the preschool-age child amino acid requirement values, 2) the validity of correction for fecal instead of ileal digestibility and 3) the truncation of PDCAAS values to 100%. At the time of the adoption of the PDCAAS method, only a few studies had been performed on the amino acid requirements of the preschool-age child, and there is still a need for validation of the scoring pattern. Also, the scoring pattern does not include conditionally indispensable amino acids. These amino acids also contribute to the nutrition value of a protein. There is strong evidence that ileal, and not fecal, digestibility is the right parameter for correction of the amino acid score. The use of fecal digestibility overestimates the nutritional value of a protein, because amino acid nitrogen entering the colon is lost for protein synthesis in the body and is, at least in part, excreted in urine as ammonia. The truncation of PDCAAS values to 100% can be defended only for the limited number of situations in which the protein is to be used as the sole source of protein in the diet. For evaluation of the nutritional significance of proteins as part of mixed diets, the truncated value should not be used. In those cases, a more detailed evaluation of the contribution of the protein to the amino acid composition of the mixed diet is required. From such an evaluation, it appears that milk proteins are superior to plant proteins in cereal-based diets.
Daily requirements for protein are set by the amount of amino acids that is irreversibly lost in a given day. Different agencies have set requirement levels for daily protein intakes for the general population; however, the question of whether strength-trained athletes require more protein than the general population is one that is difficult to answer. At a cellular level, an increased requirement for protein in strength-trained athletes might arise due to the extra protein required to support muscle protein accretion through elevated protein synthesis. Alternatively, an increased requirement for protein may come about in this group of athletes due to increased catabolic loss of amino acids associated with strength-training activities. A review of studies that have examined the protein requirements of strength-trained athletes, using nitrogen balance methodology, has shown a modest increase in requirements in this group. At the same time, several studies have shown that strength training, consistent with the anabolic stimulus for protein synthesis it provides, actually increases the efficiency of use of protein, which reduces dietary protein requirements. Various studies have shown that strength-trained athletes habitually consume protein intakes higher than required. A positive energy balance is required for anabolism, so a requirement for "extra" protein over and above normal values also appears not to be a critical issue for competitive athletes because most would have to be in positive energy balance to compete effectively. At present there is no evidence to suggest that supplements are required for optimal muscle growth or strength gain. Strength-trained athletes should consume protein consistent with general population guidelines, or 12% to 15% of energy from protein.
The purpose was to compare changes in lean tissue mass, strength, and myofibrillar protein catabolism resulting from combining whey protein or soy protein with resistance training. Twenty-seven untrained healthy subjects (18 female, 9 male) age 18 to 35 y were randomly assigned (double blind) to supplement with whey protein (W; 1.2 g/kg body mass whey protein + 0.3 g/kg body mass sucrose power, N = 9: 6 female, 3 male), soy protein (S; 1.2 g/kg body mass soy protein + 0.3 g/kg body mass sucrose powder, N= 9: 6 female, 3 male) or placebo (P; 1.2 g/kg body mass maltodextrine + 0.3 g/kg body mass sucrose powder, N = 9: 6 female, 3 male) for 6 wk. Before and after training, measurements were taken for lean tissue mass (dual energy X-ray absorptiometry), strength (1-RM for bench press and hack squat), and an indicator of myofibrillar protein catabolism (urinary 3-methylhistidine). Results showed that protein supplementation during resistance training, independent of source, increased lean tissue mass and strength over isocaloric placebo and resistance training (P < 0.05). We conclude that young adults who supplement with protein during a structured resistance training program experience minimal beneficial effects in lean tissue mass and strength.
The mammalian target of rapamycin (mTOR) and AMP‐activated protein kinase (AMPK) are important nutrient‐ and energy‐sensing and signalling proteins in skeletal muscle. AMPK activation decreases muscle protein synthesis by inhibiting mTOR signalling to regulatory proteins associated with translation initiation and elongation. On the other hand, essential amino acids (leucine in particular) and insulin stimulate mTOR signalling and protein synthesis. We hypothesized that anabolic nutrients would be sensed by both AMPK and mTOR, resulting in an acute and potent stimulation of human skeletal muscle protein synthesis via enhanced translation initiation and elongation.
We measured muscle protein synthesis and mTOR‐associated upstream and downstream signalling proteins in young male subjects ( n = 14) using stable isotopic and immunoblotting techniques. Following a first muscle biopsy, subjects in the ‘Nutrition’ group ingested a leucine‐enriched essential amino acid–carbohydrate mixture (EAC). Subjects in the Control group did not consume nutrients. A second biopsy was obtained 1 h later. Ingestion of EAC significantly increased muscle protein synthesis, modestly reduced AMPK phosphorylation, and increased Akt/PKB (protein kinase B) and mTOR phosphorylation ( P < 0.05). mTOR signalling to its downstream effectors (S6 kinase 1 (S6K1) and 4E‐binding protein 1 (4E‐BP1) phosphorylation status) was also increased ( P < 0.05). In addition, eukaryotic elongation factor 2 (eEF2) phosphorylation was significantly reduced ( P < 0.05). Protein synthesis and cell signalling (phosphorylation status) was unchanged in the control group ( P > 0.05).
We conclude that anabolic nutrients alter the phosphorylation status of both AMPK‐ and mTOR‐associated signalling proteins in human muscle, in association with an increase in protein synthesis not only via enhanced translation initiation but also through signalling promoting translation elongation.