Increase In Muscle Protein Synthesis Research Articles

Not Only Protein: Dietary Supplements to Optimize the Skeletal Muscle Growth Response to Resistance Training: The Current State of Knowledge

Regarding skeletal muscle hypertrophy, resistance training and nutrition, the most often discussed and proposed supplements include proteins. Although, the correct amount, quality, and daily distribution of proteins is of paramount importance for skeletal muscle hypertrophy, there are many other nutritional supplements that can help and support the physiological response of skeletal muscle to resistance training in terms of muscle hypertrophy. A healthy muscle environment and a correct whole muscle metabolism response to the stress of training is a prerequisite for the increase in muscle protein synthesis and, therefore, muscle hypertrophy. In this review, we discuss the role of different nutritional supplements such as carbohydrates, vitamins, minerals, creatine, omega-3, polyphenols, and probiotics as a support and complementary factors to the main supplement i.e., protein. The different mechanisms are discussed in the light of recent evidence.

Not Only Protein: Dietary Supplements to Optimize the Skeletal Muscle Growth Response to Resistance Training: The Current State of Knowledge.

Regarding skeletal muscle hypertrophy, resistance training and nutrition, the most often discussed and proposed supplements include proteins. Although, the correct amount, quality, and daily distribution of proteins is of paramount importance for skeletal muscle hypertrophy, there are many other nutritional supplements that can help and support the physiological response of skeletal muscle to resistance training in terms of muscle hypertrophy. A healthy muscle environment and a correct whole muscle metabolism response to the stress of training is a prerequisite for the increase in muscle protein synthesis and, therefore, muscle hypertrophy. In this review, we discuss the role of different nutritional supplements such as carbohydrates, vitamins, minerals, creatine, omega-3, polyphenols, and probiotics as a support and complementary factors to the main supplement i.e., protein. The different mechanisms are discussed in the light of recent evidence.

The muscle protein synthetic response following corn protein ingestion does not differ from milk protein in healthy, young adults

Plant-derived proteins are generally believed to possess lesser anabolic properties when compared with animal-derived proteins. This is, at least partly, attributed to the lower leucine content of most plant-derived proteins. Corn protein has a leucine content that is highest among most plant-derived proteins and it even exceeds the levels observed in animal-derived proteins such as whey protein. Therefore, this study aimed to compare muscle protein synthesis rates following the ingestion of 30 g corn protein and a 30 g blend of corn plus milk protein with 30 g milk protein. In a randomized, double blind, parallel-group design, 36 healthy young males (26 ± 4 y) received primed continuous L-[ring-13C6]-phenylalanine infusions and ingested 30 g corn protein (CORN), 30 g milk protein (MILK), or a 30 g proteinblend with 15 g corn plus 15 g milk protein (CORN + MILK). Blood and muscle biopsies were collected for 5 h following protein ingestion to assess post-prandial plasma amino acid profiles and myofibrillar protein synthesis rates. The results show that Ingestion of protein increased myofibrillar protein synthesis rates from basal post-absorptive values in all treatments(P < 0.001). Post-prandial myofibrillar protein synthesis rates did not differ between CORN vs MILK (0.053 ± 0.013 vs 0.053 ± 0.013%∙h−1, respectively; t-test P = 0.90), or between CORN + MILK vs MILK (0.052 ± 0.024 vs 0.053 ± 0.013%∙h−1, respectively; t-test P = 0.92). Ingestion of 30 g corn protein, 30 g milk protein, or a blend of 15 g corn plus 15 g milk protein robustly increases muscle protein synthesis rates in young males. The muscle protein synthetic response to the ingestion of 30 g corn-derived protein does not differ from the ingestion of an equivalent amount of milk protein in healthy, young males. Clinical Trial Registry number. NTR6548 (registration date: 27–06-2017) https://www.trialregister.nl/.

238 Leucine Supplementation Enhances Protein Synthesis in Lean Tissue Through a Sestrin2-GATOR2 and Raga-mTORC1 Signaling Pathway in a Preterm Piglet Model

Abstract Extrauterine growth restriction is common in preterm infants and is associated with reduced lean growth and long-term morbidities. We previously showed that leucine (Leu) acts as a nutrient signal to stimulate protein synthesis, and that in neonatal pigs born at term intermittent parenteral Leu pulses during continuous feeding increases skeletal muscle mTORC1 signaling and protein synthesis. The objective of this study was to determine the validity of the hypothesis that leu pulsing during continuous feeding enhances mTORC1 signaling via a Sestrin-mediated pathway to increase protein synthesis in lean tissue in the preterm piglet. Pigs delivered by cesarean section at 105 d gestation were continuously fed a protein and energy balanced milk-replacer diet [195 kcal ME and 13.5 g protein (kg body weight; BW)-1·d-1)]. Pigs (n = 11-12) were randomly assigned to Leu (LEU) or Alanine (ALA, isonitrogenous control) groups and treatments were administered as a pulse (1.6 mmol·kg BW-1·h-1) for 1 h every 4 h for 21 d. Indices of amino acid signaling and mTORC1 activation were determined postprandially, 60 min after initiation of the last pulse on day 24. Final body weight was greater (P &amp;lt; 0.05) and longissimus muscle weight was heavier in LEU than ALA pigs (P = 0.01). Upstream of mTORC1 activation, the abundance of the Sestrin2-GATOR2 complex was less and the RagA-mTORC1 complex was greater in longissimus muscle and gastrocnemius muscle of LEU compared with ALA pigs (P &amp;lt; 0.05). Downstream of mTORC1, the phosphorylation of S6K1 and 4EBP1 and abundance of the eIF4E-eIF4G complex were greater in longissimus muscle and gastrocnemius muscle of LEU compared with ALA pigs (P &amp;lt; 0.05). Fractional rates of protein synthesis in longissimus muscle and gastrocnemius muscle were greater in LEU compared with ALA pigs (P &amp;lt; 0.05). These results show that leucine supplementation enhances mTORC1-activated translation initiation in skeletal muscle of the preterm piglet via a Leu-sensing pathway mediated bySestrin2 and the Rag proteins. This leucine-mediated cascade promotes skeletal muscle and body weight gain by increasing muscle protein synthesis.

Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals.

Pea protein is an attractive nonanimal-derived protein source to support dietary protein requirements. However, although high in leucine, a low methionine content has been suggested to limit its anabolic potential. Mycoprotein has a complete amino acid profile which, at least in part, may explain its ability to robustly stimulate myofibrillar protein synthesis (MyoPS) rates. We hypothesized that an inferior postexercise MyoPS response would be seen following ingestion of pea protein compared with mycoprotein, which would be (partially) rescued by blending the two sources. Thirty-three healthy, young [age: 21 ± 1 yr, body mass index (BMI): 24 ± 1 kg·m-2] and resistance-trained participants received primed, continuous infusions of l-[ring-2H5]phenylalanine and completed a bout of whole body resistance exercise before ingesting 25 g of protein from mycoprotein (MYC, n = 11), pea protein (PEA, n = 11), or a blend (39% MYC, 61% PEA) of the two (BLEND, n = 11). Blood and muscle samples were taken pre-, 2 h, and 4 h postexercise/protein ingestion to assess postabsorptive and postprandial postexercise myofibrillar protein fractional synthetic rates (FSRs). Protein ingestion increased plasma essential amino acid and leucine concentrations (time effect; P < 0.0001), but more rapidly in BLEND and PEA compared with MYC (time × condition interaction; P < 0.0001). From similar postabsorptive values (MYC, 0.026 ± 0.008%·h-1; PEA, 0.028 ± 0.007%·h-1; BLEND, 0.026 ± 0.006%·h-1), resistance exercise and protein ingestion increased myofibrillar FSRs (time effect; P < 0.0001) over a 4-h postprandial period (MYC, 0.076 ± 0.004%·h-1; PEA, 0.087 ± 0.01%·h-1; BLEND, 0.085 ± 0.01%·h-1), with no differences between groups (all; P > 0.05). These data show that all three nonanimal-derived protein sources have utility in supporting postexercise muscle reconditioning.NEW & NOTEWORTHY This study provides evidence that pea protein (PEA), mycoprotein (MYC), and their blend (BLEND) can support postexercise myofibrillar protein synthesis rates following a bout of whole body resistance exercise. Furthermore, these data suggest that a methionine deficiency in pea may not limit its capacity to stimulate an acute increase in muscle protein synthesis (MPS).

The Best Whey Protein Powder Selection via VIKOR Based on Circular Intuitionistic Fuzzy Sets

People try very hard to have a symmetrical, strong, and beautiful body. The human body needs high amino acids for muscle protein synthesis. Whey protein is a good choice that contains all amino acids, which increases muscle protein synthesis and improves body shape with resistance exercise. For this reason, those who do sports, especially professionals, prefer to use these products frequently. A large number of commercial whey protein powders are sold on the market, and to achieve maximum purpose, individuals want to use the best one. Intuitionistic fuzzy sets are used in order to minimize the negative effects of the uncertainty environment and ambiguous information encountered in the decision-making process on the solution. In this study, VIKOR, based on the circular intuitionistic fuzzy set, has been used to determine the best whey protein supplement. In line with the comprehensive literature review and expert opinions, the evaluation criteria affecting the selection process have been determined, and the solution of the problem has been focused.

Effects of Whey Protein Combined with Amylopectin/Chromium on the Muscle Protein Synthesis and mTOR Phosphorylation in Exercised Rats.

This study aimed to examine the impact of varying doses of whey protein (WP) and amylopectin/chromium complex (ACr) supplementation on muscle protein synthesis (MPS), amino acid and insulin levels, and the rapamycin (mTOR) signaling pathways in exercised rats. A total of 72 rats were randomly divided into nine groups: (1) Exercise (Ex), (2) Ex + WPI to (5) Ex + WPIV with various oral doses of whey protein (0.465, 1.55, 2.33, and 3.1g/kg) and (6) Ex + WPI + ACr to (9) Ex + WPIV + ACr with various doses of whey protein combined with 0.155g/kg ACr. On the day of single-dose administration, the products were given by oral gavage after exercise. To measure the protein fractional synthesis rate (FSR), a bolus dose of deuterium-labeled phenylalanine was given, and its effects were evaluated 1h after supplementation. Rats that received 3.1g/kg of whey protein (WP) combined with ACr exhibited the most significant increase in muscle protein synthesis (MPS) compared to the Ex group (115.7%, p < 0.0001). In comparison to rats that received the same dose of WP alone, those given the combination of WP and ACr at the same dosage showed a 14.3% increase in MPS (p < 0.0001). Furthermore, the WP (3.1g/kg) + ACr group exhibited the highest elevation in serum insulin levels when compared to the Ex group (111.9%, p < 0.0001). Among the different groups, the WP (2.33g/kg) + ACr group demonstrated the greatest increase in mTOR levels (224.2%, p < 0.0001). Additionally, the combination of WP (2.33g/kg) and ACr resulted in a 169.8% increase in 4E-BP1 levels (p < 0.0001), while S6K1 levels rose by 141.2% in the WP (2.33g/kg) + ACr group (p < 0.0001). Overall, supplementation with various doses of WP combined with ACr increased MPS and enhanced the mTOR signaling pathway compared to WP alone and the Ex group.

Major nutrological approaches to macronutrients in the performance and body composition of highly trained athletes: a systematic review

Introduction: Findings around nutrient timing require appropriate context because factors such as age, gender, fitness level, previous fueling status, diet status, training volume, training intensity, program design, and time before upcoming training or competition can influence the extent to which timing can play a role in the adaptive response to exercise. Thus, nutrient timing is a feeding strategy that in almost all situations can be useful for promoting recovery and training adaptations. Objective: A systematic review was carried out to elucidate the importance of macronutrient consumption by highly trained athletes on performance and body composition. Methods: The present study followed a systematic review model (PRISMA). The search strategy was carried out in PubMed, Cochrane Library, Web of Science, Scopus, and Google Scholar databases, using scientific articles from 2009 to 2021. The low quality of evidence was attributed to case reports, editorials, and brief communications, according to the GRADE instrument. The risk of bias was analyzed according to the Cochrane instrument. Results and Conclusion: After the study eligibility process, a total of 42 scientifically favorable articles were found to compose the systematic review. Biases did not compromise the scientific basis of the studies. The amount depends on the mode and intensity of exercise, the quality of protein ingested, and the individual's energy and carbohydrate status. However, it should be noted that there is preliminary evidence that consuming much higher amounts of protein (&gt;3 g/kg/d) may confer a benefit concerning body composition. Concerns that protein intake within this range is unhealthy are unfounded in healthy, exercising individuals. One should try to consume whole foods that contain high-quality protein sources. Timing of protein intake in the period spanning the exercise session can provide several benefits, including improved recovery and greater gains in lean body mass. Essential amino acids and leucine supplements are beneficial for the exercising individual by increasing muscle protein synthesis rates, decreasing muscle protein breakdown, and possibly aiding exercise recovery.

The duration of glucocorticoid treatment alters the anabolic response to high-force muscle contractions.

Glucocorticoids induce a myopathy that includes loss of muscle mass and strength. Resistance exercise may reverse the muscle loss because it induces an anabolic response characterized by increases in muscle protein synthesis and potentially suppressing protein breakdown. Whether resistance exercise induces an anabolic response in glucocorticoid myopathic muscle is unknown, which is a problem because long-term glucocorticoid exposure alters the expression of genes that may prevent an anabolic response by limiting activation of pathways such as the mechanistic target of rapamycin in complex 1 (mTORC1). The purpose of this study was to assess whether high-force contractions initiate an anabolic response in glucocorticoid myopathic muscle. The anabolic response was analyzed by treating female mice with dexamethasone (DEX) for 7 days or 15 days. After treatment, the left tibialis anterior muscle of all mice was contracted via electrical stimulation of the sciatic nerve. Muscles were harvested 4 h after contractions. Rates of muscle protein synthesis were estimated using the SUnSET method. After 7 days of treatment, high-force contractions increased protein synthesis and mTORC1 signaling in both groups. After 15 days of treatment, high-force contractions activated mTORC1 signaling equally in both groups, but protein synthesis was only increased in control mice. The failure to increase protein synthesis may be because baseline synthetic rates were elevated in DEX-treated mice. The LC3 II/I ratio marker of autophagy was decreased by contractions regardless of treatment duration. These data show duration of glucocorticoid treatment alters the anabolic response to high-force contractions.NEW & NOTEWORTHY Glucocorticoid myopathy is the most common, toxic, noninflammatory myopathy. Our work shows that high-force contractions increase protein synthesis in skeletal muscle following short-term glucocorticoid treatment. However, longer duration glucocorticoid treatment results in anabolic resistance to high-force contractions despite activation of the mechanistic target of rapamycin in complex 1 (mTORC1) signaling pathway. This work defines potential limits for high-force contractions to activate the processes that would restore lost muscle mass in glucocorticoid myopathic patients.

Eggs: Healthy or Risky? A Review of Evidence from High Quality Studies on Hen's Eggs.

Hen's eggs (from Gallus gallus domesticus) provide choline, folate, vitamin D, iodine, B vitamins and high-quality protein and are no longer viewed by national bodies as a risk factor for hypercholesterolaemia and cardiovascular disease (CVD). Yet, questions remain about the benefits and risks of eating eggs regularly. This review evaluates recent high-quality evidence from randomised controlled trials (RCT) and meta-analyses of observational studies and considers new areas of interest, such as weight management, protein metabolism, allergy risk and sustainability. In several RCT, eggs increased muscle protein synthesis and lowered fat mass, which could support optimal body composition. Eggs within a meal improved satiety, which could translate into lower energy intakes, although more RCT are needed. In observational studies, higher egg consumption was associated with a null effect or a modest reduced risk of CVD. For type 2 diabetes (T2D) incidence and risk of CVD in people with T2D, there were inconsistencies between observational and RCT data, with the former noting positive associations and the latter seeing no effect of higher egg intake on markers of T2D and CVD. Sustainability metrics suggest that eggs have the lowest planetary impact amongst animal proteins. To lower allergy risk, earlier introduction of eggs into weaning diets is warranted. In conclusion, the balance of evidence points to eggs being a nutritious food suggesting there are broad health benefits from including eggs in the diet at intakes higher than that currently consumed by European populations.

Vicia Faba Peptide Supplementation Does Not Differ From Milk Protein In Modulating Muscle Mass Loss During Immobilization And Recovery, But Increases Muscle Protein Synthesis Rates During Recovery

Vicia Faba Peptide Supplementation Does Not Differ From Milk Protein In Modulating Muscle Mass Loss During Immobilization And Recovery, But Increases Muscle Protein Synthesis Rates During Recovery

Relationship of Protein Synthesis to mRNA Levels in the Muscle of Chicks under Various Nutritional Conditions

The relationship between the rate of protein synthesis and the level of messenger RNA (mRNA) in the breast muscle (pectoralis major) was studied to examine the mechanisms regulating muscle protein synthesis in chicks under various nutritional conditions. The fractional synthesis rate (FSR) of protein was measured by a large-dose injection of L-[4-3H]phenylalanine. Poly(U)-Sepharose 4B affinity chromatography was used to extract Poly(A)+ RNA as mRNA. The first study examined the effect of dietary protein levels (0–60%) on protein synthesis rate and the contents of mRNA and total RNA. The fractional synthesis rate increased with increasing dietary protein levels from 0 to 20%. When chicks were fed high protein diets (40 and 60% of dietary protein), both the FSR and absolute synthesis rate (ASR) of protein were reduced compared with the 20% protein group. Multiple regression analysis indicated that for graded dietary protein levels below the dietary protein requirement, the response of muscle protein synthesis is largely regulated by variation in the ASR per unit RNA (the efficiency of RNA in synthesizing protein). At dietary protein levels above 20%, synthesis rates are also related to changes in the RNA:mRNA ratio (ribosome number relative to mRNA), the mRNA:DNA ratio (mRNA availability) and the DNA:protein ratio (DNA concentration). When chicks were food deprived for 2 d, FSR was reduced to about half that of well-fed controls. Upon refeeding of these chicks with the control diet, the FSR returned to the normal level within 0.5 h. When food-deprived chicks were refed with protein, carbohydrate or fat alone, the FSR returned to the control level within 0.5 h after consumption of each nutrient. The increase in muscle protein synthesis of unfed chicks following refeeding of various nutrients was explained by an increased ASR per unit RNA. Our results suggest that nutrient intake can change muscle protein synthesis rates in chicks largely by altering the ASR per unit RNA, in some cases associated also with changes in the levels of RNA, mRNA and DNA.

Gryllus bimaculatus-containing diets protect against dexamethasone-induced muscle atrophy, but not high-fat diet-induced obesity.

Sarcopenia and obesity are emerging as major social problems. In this study, we examined whether Gryllus bimaculatus (GB), an edible insect, prevents dexamethasone-induced muscle atrophy (sarcopenia) or high-fat diet (HFD)-induced obesity in mice. We generated a standard chow diet (SCD) + GB (85% SCD and 15% GB powder) and HFD + GB (85% HFD and 15% GB powder). SCD + GB feeding increased gains in body weight and white adipose tissue (WAT). Despite no difference in weight change between HFD + GB- and HFD-fed mice, HFD + GB feeding aggravated insulin resistance compared with HFD feeding. SCD + GB or HFD + GB feeding did not change most gene expressions in the liver and WAT but did increase MyHC1 expression in the muscle, meaning that GB increased muscle generation. Therefore, we fed SCD + GB with dexamethasone, which induces muscle degeneration. As a result, muscle fiber size increased, as did grip strength compared with dexamethasone-injected mice. In addition, SCD + GB reduced the expression of muscle degradation factors, such as atrogin1 and muscle RING-finger protein 1 (MuRF1). Furthermore, SCD + GB feeding increased Akt, mTOR, and p70S6K phosphorylation and MyHC1 expression, meaning that it may have increased protein synthesis. In conclusion, GB has great potential for inhibiting dexamethasone-induced muscle mass loss by increasing muscle protein synthesis and inhibiting muscle protein degradation.

Aging Is Associated With Impaired Postprandial Response of Skeletal Muscle Protein Synthesis to High-Intensity Muscle Contraction in Mice.

The purpose of this study was to investigate whether aging alters the effect of nutritional status on contraction-induced muscle protein metabolism. In an overnight fasted or fed states, the right gastrocnemius muscle of young (3 months) and aged (24 months) male C57BL/6J mice was isometrically contracted via percutaneous electrical stimulation. The left gastrocnemius muscle served as a control. In the fasted state, there were no differences in basal or contraction-induced muscle protein synthesis between young and old mice. However, in the fed state, basal muscle protein synthesis was greater in young mice, and contraction increased muscle protein synthesis only in young mice. In the fed state, although phosphorylation of 4E-BP1 was similarly increased by contraction in both ages, the increase in phosphorylation of p70S6K was greater in young mice. Our results indicate that aging impairs the ability to integrate signals from muscle contraction and nutrition, leading to aging-induced anabolic resistance to muscle contraction in the postprandial state.

Vicia faba Peptide Network Supplementation Does Not Differ From Milk Protein in Modulating Changes in Muscle Size During Short-Term Immobilization and Subsequent Remobilization, but Increases Muscle Protein Synthesis Rates During Remobilization in Healthy Young Men

BackgroundMuscle mass and strength decrease during short periods of immobilization and slowly recover during remobilization. Recent artificial intelligence applications have identified peptides that appear to possess anabolic properties in in vitro assays and murine models. ObjectivesThis study aimed to compare the impact of Vicia faba peptide network compared with milk protein supplementation on muscle mass and strength loss during limb immobilization and regain during remobilization. MethodsThirty young (24 ± 5 y) men were subjected to 7 d of one-legged knee immobilization followed by 14 d of ambulant recovery. Participants were randomly allocated to ingest either 10 g of the Vicia faba peptide network (NPN_1; n = 15) or an isonitrogenous control (milk protein concentrate; MPC; n = 15) twice daily throughout the study. Single-slice computed tomography scans were performed to assess quadriceps cross-sectional area (CSA). Deuterium oxide ingestion and muscle biopsy sampling were applied to measure myofibrillar protein synthesis rates. ResultsLeg immobilization decreased quadriceps CSA (primary outcome) from 81.9 ± 10.6 to 76.5 ± 9.2 cm2 and from 74.8 ± 10.6 to 71.5 ± 9.8 cm2 in the NPN_1 and MPC groups, respectively (P < 0.001). Remobilization partially recovered quadriceps CSA (77.3 ± 9.3 and 72.6 ± 10.0 cm2, respectively; P = 0.009), with no differences between the groups (P > 0.05). During immobilization, myofibrillar protein synthesis rates (secondary outcome) were lower in the immobilized leg (1.07% ± 0.24% and 1.10% ± 0.24%/d, respectively) than in the non-immobilized leg (1.55% ± 0.27% and 1.52% ± 0.20%/d, respectively; P < 0.001), with no differences between the groups (P > 0.05). During remobilization, myofibrillar protein synthesis rates in the immobilized leg were greater with NPN_1 than those with MPC (1.53% ± 0.38% vs. 1.23% ± 0.36%/d, respectively; P = 0.027). ConclusionNPN_1 supplementation does not differ from milk protein in modulating the loss of muscle size during short-term immobilization and the regain during remobilization in young men. NPN_1 supplementation does not differ from milk protein supplementation in modulating the myofibrillar protein synthesis rates during immobilization but further increases myofibrillar protein synthesis rates during remobilization.

Potential mechanisms involved in regulating muscle protein turnover after acute exercise: A brief review.

It is well established that resistance training increases muscle mass. Indeed, there is evidence to suggest that a single session of resistance training is associated with an increase in muscle protein synthesis in young adults. However, the fundamental mechanisms that are involved in regulating muscle protein turnover rates after an acute bout of physical exercise are unclear. Therefore, this review will briefly focus on summarizing the potential mechanisms behind the growth of skeletal muscle after physical exercise. We also present mechanistic differences that may exist between young and older individuals during muscle protein synthesis and breakdown after physical exercise. Pathways leading to the activation of AKT/mTOR signals after resistance exercise and the activation of AMPK signaling pathway following a HIIT (High intensity interval training) are discussed.

Acute Quark Ingestion Increases Muscle Protein Synthesis Rates at Rest with a Further Increase after Exercise in Young and Older Adult Males in a Parallel-Group Intervention Trial

BackgroundIngestion of protein concentrates or isolates increases muscle protein synthesis rates in young and older adults. There is far less information available on the anabolic response following the ingestion of dairy wholefoods, which are commonly consumed in a normal diet. ObjectivesThis study investigates whether ingestion of 30 g protein provided as quark increases muscle protein synthesis rates at rest and whether muscle protein synthesis rates are further increased after resistance exercise in young and older adult males. MethodsIn this parallel-group intervention trial, 14 young (18–35 y) and 15 older (65–85 y) adult males ingested 30 g protein provided as quark after a single-legged bout of resistance exercise on leg press and leg extension machines. Primed, continuous intravenous L-[ring-13C6]-phenylalanine infusions were combined with the collection of blood and muscle tissue samples to assess postabsorptive and 4-h postprandial muscle protein synthesis rates at rest and during recovery from exercise. Data represent means ± SDs; η2 was used to measure the effect size. ResultsPlasma total amino acid and leucine concentrations increased after quark ingestion in both groups (both time: P < 0.001; η2 > 0.8), with no differences between groups (time × group: P = 0.127 and P = 0.172, respectively; η2<0.1). Muscle protein synthesis rates increased following quark ingestion at rest in both young (from 0.030 ± 0.011 to 0.051 ± 0.011 %·h−1) and older adult males (from 0.036 ± 0.011 to 0.062 ± 0.013 %·h−1), with a further increase in the exercised leg (to 0.071 ± 0.023 %·h−1 and to 0.078 ± 0.019 %·h−1, respectively; condition: P < 0.001; η2 = 0.716), with no differences between groups (condition × group: P = 0.747; η2 = 0.011). ConclusionsQuark ingestion increases muscle protein synthesis rates at rest with a further increase following exercise in both young and older adult males. The postprandial muscle protein synthetic response following quark ingestion does not differ between healthy young and older adult males when an ample amount of protein is ingested.This trial was registered at the Dutch Trial register, which is accessible via trialsearch.who.int www.trialregister.nl as NL8403.

The Muscle Protein Synthetic Response to the Ingestion of a Plant-Derived Protein Blend Does Not Differ from an Equivalent Amount of Milk Protein in Healthy Young Males

Plant-derived proteins are considered to have lesser anabolic properties when compared with animal-derived proteins. The attenuated rise in muscle protein synthesis rates following ingestion of plant-derived compared with animal-derived protein has been, at least partly, attributed to deficiencies in specific amino acids such as leucine, lysine, and/or methionine. Combining different plant-derived proteins could provide plant-derived protein blends with a more balanced amino acid profile. This study aimed to compare postprandial muscle protein synthesis rates following the ingestion of 30 g milk protein with a 30 g blend combining wheat, corn, and pea protein in healthy young men. In a randomized, double-blind, parallel-group design, 24 young males (aged 24 ± 4 y) received a primed continuous l-[ring-13C6]-phenylalanine infusion after which they ingested 30 g milk protein (MILK) or a 30 g plant-derived protein blend combining 15 g wheat, 7.5 g corn, and 7.5 g pea protein (PLANT-BLEND). Blood and muscle biopsies were collected frequently for 5 h to assess postprandial plasma amino acid profiles (secondary outcome) and subsequent muscle protein synthesis rates (primary outcome). Data were analyzed by 2-factor repeated measures ANOVA and 2-samples t tests. MILK increased plasma essential amino acid concentrations more than PLANT-BLEND over the 5 h postprandial period (incremental AUC = 151 ± 31 compared with 79 ± 12 mmol·300 min·L-1, respectively; P < 0.001). Ingestion of both MILK and PLANT-BLEND increased myofibrillar protein synthesis rates (P < 0.001), with no significant differences between treatments (0.053 ± 0.013%/h and 0.064 ± 0.016%/h, respectively; P = 0.08). Ingestion of 30 g plant-derived protein blend combining wheat-, corn-, and pea-derived protein increases muscle protein synthesis rates in healthy young males. The muscle protein synthetic response to the ingestion of 30 g of this plant-derived protein blend does not differ from the ingestion of an equivalent amount of a high-quality animal-derived protein. Clinical trial registry number for Nederlands Trial Register: NTR6548 (https://trialsearch.who.int/Trial2.aspx?TrialID=NTR6548).

Plasma omega-3 fatty acids are positively associated with appendicular muscle mass index only in adults with low protein intake: Results from NHANES 2011–2012

Omega-3 (ω-3) fatty acids may indirectly increase muscle protein synthesis making the muscle more sensitive to amino acids uptake; therefore, ω-3 could promote benefits on muscle mass mainly when protein intake is low. However, no study has evaluated the association between ω-3 fatty acids and muscle mass according to protein intake. To evaluate the association between plasma ω-3 fatty acids and appendicular muscle mass index (AMMI) in adults according to the protein intake. A cross-sectional study was performed evaluating 1037 individuals aged 20-59 years from a sub-sample of the National Health and Nutrition Examination Survey (NHANES) 2011-2012. Gas chromatography-mass spectrometry method was used to assess plasma ω-3 fatty acids. The lean mass was evaluated by dual-energy x-ray absorptiometry (DXA) and AMMI (kg/m2) was calculated by appendicular lean mass (kg) divided by height squared. The evaluation of protein intake was performed using two 24-h dietary recalls. Linear regression analysis was performed to assess the association of total plasma ω-3, docosahexaenoic acid (DHA), eicosapentaenoic acid (EPA), alpha-linolenic acid (ALA), and EPA plus DHA with AMMI according to protein intake (<0.8; ≥0.8; ≥0.8 -<1.2; ≥1.2 -<1.6; and ≥1.6g/kg/d). Total plasma ω-3 (β=0.0030; CI=0.0013-0.0046; p=0.002), ALA (β=0.0063; CI=0.0020-0.0107; p=0.008), EPA (β=0.0073; CI=0.0005-0.0142, p=0.037), DHA (β=0.0057; CI=0.0022-0.0093; p=0.004) and EPA+DHA (β=0.0040; CI=0.0010-0.0071; p=0.013) were positively associated with AMMI in individuals with low protein intake (<0.8g/kg). However, no association was observed in individuals with protein intake higher than 0.8g/kg. Plasma ω-3 fatty acids were positively associated with AMMI only in individuals with low protein intake.

Regulation of skeletal muscle protein synthesis in the preterm pig by intermittent leucine pulses during continuous parenteral feeding.

Extrauterine growth restriction is a common complication of preterm birth. Leucine (Leu) is an agonist for the mechanistic target of rapamycin (mTOR) complex 1 (mTORC1) signaling pathway that regulates translation initiation and protein synthesis in skeletal muscle. Previously, we showed that intermittent intravenous pulses of Leu to neonatal pigs born at term receiving continuous enteral nutrition increases muscle protein synthesis and lean mass accretion. Our objective was to determine the impact of intermittent intravenous pulses of Leu on muscle protein anabolism in preterm neonatal pigs administered continuous parenteral nutrition. Following preterm delivery (on day 105 of 115 gestation), pigs were fitted with umbilical artery and jugular vein catheters and provided continuous parenteral nutrition. Four days after birth, pigs were assigned to receive intermittent Leu (1600 µmol kg-1  h-1 ; n = 8) or alanine (1600 µmol kg-1  h-1 ; n = 8) parenteral pulses every 4 h for 28 h. Anabolic signaling and fractional protein synthesis were determined in skeletal muscle. Leu concentration in the longissimus dorsi and gastrocnemius muscles increased in the leucine (LEU) group compared with the alanine (ALA) group (P < 0.0001). Despite the Leu-induced disruption of the Sestrin2·GATOR2 complex, which inhibits mTORC1 activation, in these muscles (P < 0.01), the abundance of mTOR·RagA and mTOR·RagC was not different. Accordingly, mTORC1-dependent activation of 4EBP1, S6K1, eIF4E·eIF4G, and protein synthesis were not different in any muscle between the LEU and ALA groups. Intermittent pulses of Leu do not enhance muscle protein anabolism in preterm pigs supplied continuous parenteral nutrition.