Postprandial Muscle Protein Synthetic Response Research Articles

Underpinning the Food Matrix Regulation of Postexercise Myofibrillar Protein Synthesis by Comparing Salmon Ingestion With the Sum of Its Isolated Nutrients in Healthy Young Adults

BackgroundProtein is most commonly consumed as whole foods as opposed to single nutrients. However, the food matrix regulation of the postprandial muscle protein synthetic response has received little attention. ObjectivesThe purpose of this study was to assess the effects of eating salmon (SAL) and of ingesting the same nutrients as an isolated mixture of crystalline amino acids and fish oil (ISO) on the stimulation of postexercise myofibrillar protein synthesis (MPS) and whole-body leucine oxidation rates in healthy young adults. MethodsTen recreationally active adults (24 ± 4 y; 5 men, 5 women) performed an acute bout of resistance exercise, followed by the ingestion of SAL or ISO in a crossover fashion. Blood, breath, and muscle biopsies were collected at rest and after exercise during primed continuous infusions of L-[ring-2H5]phenylalanine and L-[1-13C]leucine. All data are presented as means ± SD and/or mean differences (95% CIs). ResultsPostprandial essential amino acid (EAA) concentrations peaked earlier (P = 0.024) in the ISO group than those in the SAL group. Postprandial leucine oxidation rates increased over time (P < 0.001) and peaked earlier in the ISO group (1.239 ± 0.321 nmol/kg/min; 63 ± 25 min) than those in the SAL group (1.230 ± 0.561 nmol/kg/min; 105 ± 20 min; P = 0.003). MPS rates for SAL (0.056 ± 0.022 %/h; P = 0.001) and ISO (0.046 ± 0.025 %/h; P = 0.025) were greater than the basal rates (0.020 ± 0.011 %/h) during the 0- to 5-h recovery period, with no differences between conditions (P = 0.308). ConclusionWe showed that the postexercise ingestion of SAL or ISO stimulate postexercise MPS rates with no differences between the conditions. Thus, our results indicate that ingesting protein from SAL as a whole-food matrix is similarly anabolic to ISO in healthy young adults. This trial was registered at www.clinicaltrials.gov as NCT03870165.

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.

Cheese Ingestion Increases Muscle Protein Synthesis Rates Both at Rest and During Recovery from Exercise in Healthy, Young Males: A Randomized Parallel-Group Trial

ABSTRACTBackgroundProtein ingestion increases muscle protein synthesis rates. The food matrix in which protein is provided can strongly modulate the postprandial muscle protein synthetic response. So far, the muscle protein synthetic response to the ingestion of whole foods remains largely unexplored.ObjectivesTo compare the impact of ingesting 30 g protein provided as milk protein or cheese on postprandial plasma amino acid concentrations and muscle protein synthesis rates at rest and during recovery from exercise in vivo in young males.MethodsIn this randomized, parallel-group intervention trial, 20 healthy males aged 18–35 y ingested 30 g protein provided as cheese or milk protein concentrate following a single-legged resistance-type exercise session consisting of 12 sets of leg press and leg extension exercises. 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 were analyzed using repeated measures Time × Group (× Leg) ANOVA.ResultsPlasma total amino acid concentrations increased after protein ingestion (Time: P < 0.001), with 38% higher peak concentrations following milk protein than cheese ingestion (Time × Group: P < 0.001). Muscle protein synthesis rates increased following both cheese and milk protein ingestion from 0.037 ± 0.014 to 0.055 ± 0.018%·h–1 and 0.034 ± 0.008 to 0.056 ± 0.010%·h–1 at rest and even more following exercise from 0.031 ± 0.010 to 0.067 ± 0.013%·h–1 and 0.030 ± 0.008 to 0.063 ± 0.010%·h–1, respectively (Time: all P < 0.05; Time × Leg: P = 0.002), with no differences between cheese and milk protein ingestion (Time × Group: both P > 0.05).ConclusionCheese ingestion increases muscle protein synthesis rates both at rest and during recovery from exercise. The postprandial muscle protein synthetic response to the ingestion of cheese or milk protein does not differ when 30 g protein is ingested at rest or during recovery from exercise in healthy, young males.

Ingestion of Free Amino Acids Compared with an Equivalent Amount of Intact Protein Results in More Rapid Amino Acid Absorption and Greater Postprandial Plasma Amino Acid Availability Without Affecting Muscle Protein Synthesis Rates in Young Adults in a Double-Blind Randomized Trial

BackgroundThe rate of protein digestion and amino acid absorption determines the postprandial rise in circulating amino acids and modulates postprandial muscle protein synthesis rates. ObjectiveWe sought to compare protein digestion, amino acid absorption kinetics, and the postprandial muscle protein synthetic response following ingestion of intact milk protein or an equivalent amount of free amino acids. MethodsTwenty-four healthy, young participants (mean ± SD age: 22 ± 3 y and BMI 23 ± 2 kg/m2; sex: 12 male and 12 female participants) received a primed continuous infusion of l-[ring-2H5]-phenylalanine and l-[ring-3,5–2H2]-tyrosine, after which they ingested either 30 g intrinsically l-[1–13C]-phenylalanine–labeled milk protein or an equivalent amount of free amino acids labeled with l-[1–13C]-phenylalanine. Blood samples and muscle biopsies were obtained to assess protein digestion and amino acid absorption kinetics (secondary outcome), whole-body protein net balance (secondary outcome), and mixed muscle protein synthesis rates (primary outcome) throughout the 6-h postprandial period. ResultsPostprandial plasma amino acid concentrations increased after ingestion of intact milk protein and free amino acids (both P < 0.001), with a greater increase following ingestion of the free amino acids than following ingestion of intact milk protein (P-time × treatment < 0.001). Exogenous phenylalanine release into plasma, assessed over the 6-h postprandial period, was greater with free amino acid ingestion (76 ± 9%) than with milk protein treatment (59 ± 10%; P < 0.001). Ingestion of free amino acids and intact milk protein increased mixed muscle protein synthesis rates (P-time < 0.001), with no differences between treatments (from 0.037 ± 0.015%/h to 0.053 ± 0.014%/h and 0.039 ± 0.016%/h to 0.051 ± 0.010%/h, respectively; P-time × treatment = 0.629). ConclusionsIngestion of a bolus of free amino acids leads to more rapid amino acid absorption and greater postprandial plasma amino acid availability than ingestion of an equivalent amount of intact milk protein. Ingestion of free amino acids may be preferred over ingestion of intact protein in conditions where protein digestion and amino acid absorption are compromised.

Ingestion of an ample amount of meat substitute based on a lysine-enriched, plant-based protein blend stimulates postprandial muscle protein synthesis to a similar extent as an isonitrogenous amount of chicken in healthy, young men.

Plant-based proteins are considered to be less effective in their capacity to stimulate muscle protein synthesis when compared with animal-based protein sources, likely due to differences in amino acid contents. We compared the postprandial muscle protein synthetic response following the ingestion of a lysine-enriched plant-based protein product with an isonitrogenous amount of chicken. Twenty-four men (age 24 ± 5 years; BMI 22·9 ± 2·6 kg·m-2) participated in this parallel, double-blind, randomised controlled trial and consumed 40 g of protein as a lysine-enriched wheat and chickpea protein product (Plant, n 12) or chicken breast fillet (Chicken, n 12). Primed, continuous intravenous l-(ring-13C6)-phenylalanine infusions were applied while repeated blood and muscle samples were collected over a 5-h postprandial period to assess plasma amino acid responses, muscle protein synthesis rates and muscle anabolic signalling responses. Postprandial plasma leucine and essential amino acid concentrations were higher following Chicken (P < 0·001), while plasma lysine concentrations were higher throughout in Plant (P < 0·001). Total plasma amino acid concentrations did not differ between interventions (P = 0·181). Ingestion of both Plant and Chicken increased muscle protein synthesis rates from post-absorptive: 0·031 ± 0·011 and 0·031 ± 0·013 to postprandial: 0·046 ± 0·010 and 0·055 ± 0·015 % h-1, respectively (P-time < 0·001), with no differences between Plant and Chicken (time x treatment P = 0·068). Ingestion of 40 g of protein in the form of a lysine-enriched plant-based protein product increases muscle protein synthesis rates to a similar extent as an isonitrogenous amount of chicken in healthy, young men. Plant-based protein products sold as meat replacers may be as effective as animal-based protein sources to stimulate postprandial muscle protein synthesis rates in healthy, young individuals.

The Muscle Protein Synthetic Response to the Ingestion of a Plant-Based Protein Blend Is Not Different From Milk Protein in Healthy, Young Males

Abstract Objectives It has been reported that plant-based proteins are not as effective as animal-based proteins in their capacity to stimulate muscle protein synthesis rates. This has been attributed to the lower essential amino acid content and the selective deficiency in specific amino acids. It has been hypothesized that a blend of different plant-based proteins may complement each other and, as such, compensate for such deficits. This study compares post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein with the ingestion of a 30 g blend of wheat, corn, and pea protein in vivo, in healthy young males. Methods In a randomized, double blind, parallel-group design, 24 healthy young males (24 ± 4 y) received a primed continuous infusion of L-[ring-13C6]-phenylalanine and ingested 30 g milk protein (MILK), or a 30 g protein blend with 15 g wheat, 7.5 g corn, and 7.5 g pea protein (PLANT) in beverage form (n = 12 per group). Both interventional drinks were matched for leucine content. 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. Data are expressed as mean ± SD. Results MILK increased plasma essential amino acid concentrations ∼2 fold more than PLANT over the 5 h post-prandial period (incremental area under curve (iAUC): 151 ± 31 vs 79 ± 12 mmol∙5 h∙L−1 respectively; P &amp;lt; 0.001). Similarly, the leucine iAUC was ∼16% greater for MILK vs PLANT (36 ± 7 vs 31 ± 4 mmol∙5 h∙L−1 respectively; P &amp;lt; 0.05). Ingestion of both MILK and PLANT increased myofibrillar protein synthesis rates when compared to basal post-absorptive values (P &amp;lt; 0.001), with no significant differences between treatments (0.053 ± 0.013 vs 0.064 ± 0.016%∙h−1, respectively; P &amp;gt; 0.05). Conclusions Ingestion of 30 g of a wheat, corn, and pea protein blend increases muscle protein synthesis rates in healthy, young males. The post-prandial muscle protein synthetic response to the ingestion of 30 g of a wheat, corn and pea protein blend does not differ from the ingestion of an equivalent amount of milk protein in healthy, young males. Funding Sources TiFN

Basal and Postprandial Myofibrillar Protein Synthesis Rates Do Not Differ between Lean and Obese Middle-Aged Men

ABSTRACTBackgroundExcess lipid availability has been associated with the development of anabolic resistance. As such, obesity may be accompanied by impairments in muscle protein metabolism.ObjectiveWe hypothesized that basal and postprandial muscle protein synthesis rates are lower in obese than in lean men.MethodsTwelve obese men [mean ± SEM age: 48 ± 2 y; BMI (in kg/m2): 37.0 ± 1.5; body fat: 32 ± 2%] and 12 age-matched lean controls (age: 43 ± 3 y; BMI: 23.4 ± 0.4; body fat: 21 ± 1%) received primed continuous L-[ring-2H5]-phenylalanine and L-[ring-3,5-2H2]-tyrosine infusions and ingested 25 g intrinsically L-[1-13C]-phenylalanine labeled whey protein. Repeated blood and muscle samples were obtained to assess protein digestion and amino acid absorption kinetics, and basal and postprandial myofibrillar protein synthesis rates.ResultsExogenous phenylalanine appearance rates increased after protein ingestion in both groups (P < 0.001), with a total of 53 ± 1% and 53 ± 2% of dietary protein–derived phenylalanine appearing in the circulation over the 5-h postprandial period in lean and obese men, respectively (P = 0.82). After protein ingestion, whole-body protein synthesis and oxidation rates increased to a greater extent in lean men than in the obese (P-interaction < 0.05), resulting in a higher whole-body protein net balance in the lean than in the obese (7.1 ± 0.2 and 4.6 ± 0.4 µmol phenylalanine · h−1 · kg−1, respectively; P-interaction < 0.001). Myofibrillar protein synthesis rates increased from 0.030 ± 0.002 and 0.028 ± 0.003%/h in the postabsorptive period to 0.034 ± 0.002 and 0.035 ± 0.003%.h−1 in the 5-h postprandial period (P = 0.03) in lean and obese men, respectively, with no differences between groups (P-interaction = 0.58).ConclusionsBasal, postabsorptive myofibrillar protein synthesis rates do not differ between lean and obese middle-aged men. Postprandial protein handling, including protein digestion and amino acid absorption, and the postprandial muscle protein synthetic response after the ingestion of 25 g whey protein are not impaired in obese men. This trial was registered at www.trialregister.nl as NTR4060.

Leucine coingestion augments the muscle protein synthetic response to the ingestion of 15 g of protein following resistance exercise in older men.

Older adults have shown an attenuated postexercise increase in muscle protein synthesis rates following ingestion of smaller amounts of protein compared with younger adults. Consequently, it has been suggested that older adults require the ingestion of more protein to increase postexercise muscle protein synthesis rates compared with younger adults. We investigated whether coingestion of 1.5 g of free leucine with a single 15-g bolus of protein further augments the postprandial muscle protein synthetic response during recovery from resistance-type exercise in older men. Twenty-four healthy older men (67 ± 1 yr) were randomly assigned to ingest 15 g of milk protein concentrate (MPC80) with (15G+LEU; n = 12) or without (15G; n = 12) 1.5 g of free leucine after performing a single bout of resistance-type exercise. Postprandial protein digestion and amino acid absorption kinetics, whole body protein metabolism, and postprandial myofibrillar protein synthesis rates were assessed using primed, continuous infusions with l-[ring-2H5]phenylalanine, l-[ring-2H2]tyrosine, and l-[1-13C]leucine combined with ingestion of intrinsically l-[1-13C]phenylalanine-labeled milk protein. A total of 70 ± 1% (10.5 ±0.2 g) and 75 ± 2% (11.2 ± 0.3 g) of the protein-derived amino acids were released in the circulation during the 6-h postexercise recovery phase in 15G+LEU and 15G, respectively (P < 0.05). Postexercise myofibrillar protein synthesis rates were 16% (0.058 ± 0.003 vs. 0.049 ± 0.002%/h, P < 0.05; based on l-[ring-2H5]phenylalanine) and 19% (0.071 ± 0.003 vs. 0.060 ± 0.003%/h, P < 0.05; based on l-[1-13C]leucine) greater in 15G+LEU compared with 15G. Leucine coingestion further augments the postexercise muscle protein synthetic response to the ingestion of a single 15-g bolus of protein in older men.

Characterising the muscle anabolic potential of dairy, meat and plant-based protein sources in older adults.

The age-related loss of skeletal muscle mass and function is caused, at least in part, by a reduced muscle protein synthetic response to protein ingestion. The magnitude and duration of the postprandial muscle protein synthetic response to ingested protein is dependent on the quantity and quality of the protein consumed. This review characterises the anabolic properties of animal-derived and plant-based dietary protein sources in older adults. While approximately 60 % of dietary protein consumed worldwide is derived from plant sources, plant-based proteins generally exhibit lower digestibility, lower leucine content and deficiencies in certain essential amino acids such as lysine and methionine, which compromise the availability of a complete amino acid profile required for muscle protein synthesis. Based on currently available scientific evidence, animal-derived proteins may be considered more anabolic than plant-based protein sources. However, the production and consumption of animal-derived protein sources is associated with higher greenhouse gas emissions, while plant-based protein sources may be considered more environmentally sustainable. Theoretically, the lower anabolic capacity of plant-based proteins can be compensated for by ingesting a greater dose of protein or by combining various plant-based proteins to provide a more favourable amino acid profile. In addition, leucine co-ingestion can further augment the postprandial muscle protein synthetic response. Finally, prior exercise or n-3 fatty acid supplementation have been shown to sensitise skeletal muscle to the anabolic properties of dietary protein. Applying one or more of these strategies may support the maintenance of muscle mass with ageing when diets rich in plant-based protein are consumed.

Ingestion of Wheat Protein Increases In Vivo Muscle Protein Synthesis Rates in Healthy Older Men in a Randomized Trial

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/m2): 25.3 ± 0.3] received a primed continuous infusion of L-[ring-13C6]-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.

Diminished Postprandial Muscle Protein Synthetic Response To Protein Ingestion In Obese Adults

Excess body fat blunts muscle protein synthesis rates under hyperinsulinemic, hyperaminoacidemic clamp conditions. However, the efficacy of the ingestion of single meal containing ample amounts of protein to augment postprandial muscle protein synthesis rates has not been studied in obese and overweight adults. PURPOSE: We aimed to compare myofibrillar protein synthesis after protein ingestion in healthy weight, overweight, and obese adults. METHODS: 10 healthy-weight (24±1 y, BMI 22.7±0.4 kg/m2, HOMA-IR 1.4±0.2), 10 overweight (26±2 y, BMI 27.1±0.5 kg/m2, HOMA-IR 1.25±0.11), and 10 obese (27±3 y, BMI 35.9±1.3 kg/m2, HOMA-IR 5.8±0.8) men and women underwent a primed continuous L-[ring-13C6]phenylalanine infusion. Blood and muscle biopsy samples were collected at rest and after ingestion of 36 g of protein to assess plasma amino acid and insulin concentrations and myofibrillar protein synthesis rates. RESULTS: Protein ingestion increased plasma essential amino acid concentrations similarly in all participants (time effect: P<0.05) with concentrations peaked at 2 h and returning to baseline values at 5 h. The obese participants had a greater peak postprandial plasma insulin response to protein ingestion than the overweight and healthy-weight participants (obese 56.7±8.0 compared to overweight 11.9±1.6 and healthy-weight 14.3±1.7 μIU/L, P<0.001). Protein ingestion increased myofibrillar protein synthesis in both the healthy-weight (rest: 0.057±0.006 %/h, fed: 0.084±0.014 %/h) and overweight groups (rest: 0.061±0.007, fed: 0.087±0.019 %/h) (P<0.05) with no increase in the obese group (rest: 0.055±0.005 %/h, fed: 0.067±0.005 %/h, P=0.45). CONCLUSIONS: Increased adiposity led to an impaired postprandial muscle protein synthetic response to protein ingestion in obese adults when compared to healthy-weight and overweight individuals. These data suggest that poor skeletal muscle remodeling may underlie early metabolic impairments in apparently “healthy” obese adults. Funding provided by the National Pork Board

MTOR Activation occurs Independent of Changes in Skeletal Muscle LAT1 Protein Content after Protein Ingestion

Activation of the mammalian target of rapamycin complex 1 (mTORC1) after protein ingestion has been shown to be obligatory to augment the postprandial muscle protein synthetic response. The delivery of dietary protein derived amino acids into skeletal muscle tissue is facilitated by amino acid transporters. In particular, the system L amino acid transporter (LAT1/solute-linked carrier (SLC)7A5) transports large neutral amino acids such as phenylalanine, tyrosine, and leucine across the muscle cell membrane and may also serve as an intracellular sensor for mTORC1 signaling. PURPOSE: We aimed to examine variations in skeletal muscle LAT1 (55 kDa) protein content and phosphorylation of mTORC1 (Ser2448) in relation to dietary protein digestion and absorption kinetics after ingestion of single meal containing ample amounts of protein. METHODS: Seven healthy, young men (24±1 y; BMI= 24.8±1.2 kg/m2) received a primed continuous infusion of L-[ring-2H5]phenylalanine, L-[ring-2H2]tyrosine, and L-[1-13C]leucine and ingested 38 g of intrinsically L-[1-13C]phenylalanine and L-[1-13C]leucine labeled milk protein. Blood samples were drawn every 0.5-1 h during the infusion protocol. Biopsies from the vastus lateralis were collected before and after protein ingestion at 1, 2, 3, and 5 h of the postprandial period. RESULTS: Postprandial release of dietary protein derived phenylalanine rapidly increased in circulation after protein ingestion and remained elevated throughout the 5 h postprandial period (Time effect: P<0.001). mTORC1 phosphorylation was increased (18±6%) throughout the postprandial phase (time effect: P<0.05). However, protein ingestion did not modulate LAT1 protein content during the postprandial period (P=0.53). CONCLUSIONS: We conclude that the increase in mTORC1 phosphorylation after protein ingestion occurs without modulations in overall skeletal muscle LAT1 protein content.

Body Position Modulates Gastric Emptying and Affects the Post-Prandial Rise in Plasma Amino Acid Concentrations Following Protein Ingestion in Humans.

Dietary protein digestion and amino acid absorption kinetics determine the post-prandial muscle protein synthetic response. Body position may affect gastrointestinal function and modulate the post-prandial rise in plasma amino acid availability. We aimed to assess the impact of body position on gastric emptying rate and the post-prandial rise in plasma amino acid concentrations following ingestion of a single, meal-like amount of protein. In a randomized, cross-over design, eight healthy males (25 ± 2 years, 23.9 ± 0.8 kg·m−2) ingested 22 g protein and 1.5 g paracetamol (acetaminophen) in an upright seated position (control) and in a −20° head-down tilted position (inversion). Blood samples were collected during a 240-min post-prandial period and analyzed for paracetamol and plasma amino acid concentrations to assess gastric emptying rate and post-prandial amino acid availability, respectively. Peak plasma leucine concentrations were lower in the inversion compared with the control treatment (177 ± 15 vs. 236 ± 15 mmol·L−1, p < 0.05), which was accompanied by a lower plasma essential amino acid (EAA) response over 240 min (31,956 ± 6441 vs. 50,351 ± 4015 AU; p < 0.05). Peak plasma paracetamol concentrations were lower in the inversion vs. control treatment (5.8 ± 1.1 vs. 10.0 ± 0.6 mg·L−1, p < 0.05). Gastric emptying rate and post-prandial plasma amino acid availability are significantly decreased after protein ingestion in a head-down tilted position. Therefore, upright body positioning should be considered when aiming to augment post-prandial muscle protein accretion in both health and disease.

Co-ingesting milk fat with micellar casein does not affect postprandial protein handling in healthy older men

Dietary protein digestion and absorption plays an important role in modulating postprandial muscle protein synthesis. The impact of co-ingesting other macronutrients with dietary protein on protein digestion and absorption and the subsequent muscle protein synthetic response remains largely unexplored. This study investigated the impact of co-ingesting milk fat with micellar casein on dietary protein-derived amino acid appearance in the circulation and the subsequent postprandial muscle protein synthetic response in healthy older men. Twenty-four healthy, older males (age: 65±1y, BMI: 25.7±0.5kg/m2) received a primed continuous infusion of L-[ring-2H5]-phenylalanine and L-[1-13C]-leucine and ingested 20g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine-labeled casein with (PRO+FAT; n=12) or without (PRO; n=12) 26.7g milk fat. Plasma samples and muscle biopsies were collected in both the postabsorptive and postprandial state. Release of dietary protein-derived phenylalanine into the circulation increased following protein ingestion (P<0.001) and tended to be higher in PRO compared with PRO+FAT (Time×Treatment P=0.076). No differences were observed in dietary protein-derived plasma phenylalanine availability (52±2 vs 52±3% in PRO vs PRO+FAT, respectively; P=0.868). Myofibrillar protein synthesis rates did not differ between treatments, calculated using either the L-[ring-2H5]-phenylalanine (0.036±0.003 vs 0.036±0.004 %/h after PRO vs PRO+FAT, respectively; P=0.933) or L-[1-13C]-leucine (0.051±0.004 vs 0.046±0.004 %/h, respectively; P=0.480) tracer. In accordance, no differences were observed in myofibrillar protein-bound L-[1-13C]-phenylalanine enrichments between treatments (0.018±0.002 vs 0.014±0.001 MPE, respectively; P=0.173). Co-ingesting milk fat with micellar casein does not impair protein-derived phenylalanine appearance in the circulation and does not modulate postprandial myofibrillar protein synthesis rates. NCT01680146 (http://www.clinicaltrials.gov/).

Impact of the Macronutrient Composition of a Nutritional Supplement on Muscle Protein Synthesis Rates in Older Men: A Randomized, Double Blind, Controlled Trial.

An impaired muscle protein synthetic response to feeding likely contributes to muscle loss with aging. There are few data available on the effect of the macronutrient composition of clinical supplements on the postprandial muscle protein synthetic response in older subjects. The objective of the study was to determine the impact of the macronutrient composition of a nutritional supplement on the postprandial muscle protein synthetic response in older men. A total of 45 nonsarcopenic older men (aged 69 ± 1 y; body mass index 25.7 ± 0.3 kg/m(2)) were randomly assigned to ingest 21 g of leucine-enriched whey protein with carbohydrate (9 g) and fat (3 g) (Pro-En), an isonitrogenous amount of 21 g of leucine-enriched whey protein without carbohydrate and fat (Pro), or an isocaloric mixture (628 kJ) containing carbohydrate and fat only (En). Stable isotope tracer methodology was applied to assess the basal as well as the postprandial muscle protein synthesis rates in the three groups. Ingestion of protein in the Pro-En and Pro groups significantly increased muscle protein synthesis rates when compared with the basal rates (from 0.032 ± 0.003%/h to 0.05%/h 3 ± 0.004%/h and 0.040%/h ± 0.003%/h to 0.049%/h ± 0.003%/h, respectively; P < .05), whereas ingestion of carbohydrate and fat did not increase muscle protein synthesis rates in the En group (from 0.039%/h ± 0.004%/h to 0.040%/h ± 0.003%/h; P = .60). Despite the greater postprandial rise in circulating insulin concentration in the Pro-En group, no significant differences were observed in postprandial muscle protein synthesis rates between the Pro-En and Pro groups (P = .32). Postprandial muscle protein synthesis rates were higher in the Pro-En vs En group (P = .01). The ingestion of a nutritional supplement containing 21 g of leucine-enriched whey protein significantly raises muscle protein synthesis rates in nonsarcopenic older men, but coingestion of carbohydrate and fat does not modulate the postprandial muscle protein synthetic response to protein ingestion in older men.

Ingestion of Casein in a Milk Matrix Modulates Dietary Protein Digestion and Absorption Kinetics but Does Not Modulate Postprandial Muscle Protein Synthesis in Older Men1–3

Background: The slow digestion and amino acid absorption kinetics of isolated micellar casein have been held responsible for its relatively lower postprandial muscle protein synthetic response compared with rapidly digested proteins such as isolated whey. However, casein is normally consumed within a milk matrix. We hypothesized that protein digestion and absorption kinetics and the subsequent muscle protein synthetic response after micellar casein ingestion are modulated by the milk matrix.Objective: The aim of this study was to determine the impact of a milk matrix on casein protein digestion and absorption kinetics and postprandial muscle protein synthesis in older men.Methods: In a parallel-group design, 32 healthy older men (aged 71 ± 1 y) received a primed continuous infusion of L-[ring-2H5]-phenylalanine, L-[ring-3,5-2H2]-tyrosine, and L-[1-13C]-leucine, and ingested 25 g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine labeled casein dissolved in bovine milk serum (Cas+Serum) or water (Cas). Plasma samples and muscle biopsies were collected in the postabsorptive state and for 300 min in the postprandial period to examine whole-body and skeletal muscle protein metabolism.Results: Casein ingestion increased plasma leucine and phenylalanine concentrations and L-[1-13C]-phenylalanine enrichments, with a more rapid rise after Cas vs. Cas+Serum. Nonetheless, dietary protein–derived phenylalanine availability did not differ between Cas+Serum (47 ± 2%, mean ± SEM) and Cas (46 ± 3%) when assessed over the 300-min postprandial period (P = 0.80). The milk matrix did not modulate postprandial myofibrillar protein synthesis rates from 0 to 120 min (0.038 ± 0.005 vs. 0.031 ± 0.007%/h) or from 120 to 300 min (0.052 ± 0.004 vs. 0.067 ± 0.005%/h) after Cas+Serum vs. Cas. Similarly, no treatment differences in muscle protein–bound L-[1-13C]-phenylalanine enrichments were observed at 120 min (0.003 ± 0.001 vs. 0.002 ± 0.001) or 300 min (0.015 ± 0.002 vs. 0.016 ± 0.002 mole percent excess) after Cas+Serum vs. Cas.Conclusions: Casein ingestion in a milk matrix delays protein digestion and absorption but does not modulate postprandial muscle protein synthesis when compared to the ingestion of micellar casein only in healthy older men. This trial was registered at Nederlands Trial Register as NTR4429.

Towards a Sustainable Dairy Sector: The underappreciated role of dairy protein in the preservation of lean tissue mass in the elderly

Sarcopenia has been attributed to a diminished postprandial muscle protein synthetic response. Differences in digestion and absorption kinetics of dietary protein and/or its amino acid composition have been suggested to modulate postprandial muscle protein accretion. The amino acid composition of dairy protein, especially whey, has the potential to confer advantages above other nondairy protein sources in prevention of lean tissue mass loss. This may be attributable to its relative high concentration of the essential amino acid leucine.

Leucine co-ingestion improves post-prandial muscle protein accretion in elderly men

It has been speculated that the amount of leucine in a meal largely determines the post-prandial muscle protein synthetic response to food intake. The present study investigates the impact of leucine co-ingestion on subsequent post-prandial muscle protein accretion following the ingestion of a single bolus of dietary protein in elderly males. Twenty-four elderly men (74.3±1.0 y) were randomly assigned to ingest 20 g intrinsically L-[1-(13)C]phenylalanine-labeled casein protein with (PRO+LEU) or without (PRO) 2.5 g crystalline leucine. Ingestion of specifically produced intrinsically labeled protein allowed us to create a plasma phenylalanine enrichment pattern similar to the absorption pattern of phenylalanine from the ingested protein and assess the subsequent post-prandial incorporation of L-[1-(13)C] phenylalanine into muscle protein. Plasma amino acid concentrations increased rapidly following protein ingestion in both groups, with higher leucine concentrations observed in the PRO+LEU compared with the PRO group (P<0.01). Plasma L-[1-(13)C]phenylalanine enrichments increased rapidly and to a similar extent in both groups following protein ingestion. Muscle protein-bound L-[1-(13)C]phenylalanine enrichments were significantly greater after PRO+LEU when compared with PRO at 2 h (72%; 0.0078±0.0010 vs. 0.0046±0.00100 MPE, respectively; P<0.05) and 6 h (25%; 0.0232±0.0015 vs. 0.0185±0.0010 MPE, respectively; P<0.05) following protein ingestion. The latter translated into a greater muscle protein synthetic rate following PRO+LEU compared with PRO over the entire 6 h post-prandial period (22%; 0.049±0.003 vs. 0.040±0.003% h(-1), respectively; P<0.05). Leucine co-ingestion with a bolus of pure dietary protein further stimulates post-prandial muscle protein synthesis rates in elderly men.

Dietary Protein Digestion and Absorption Rates and the Subsequent Postprandial Muscle Protein Synthetic Response Do Not Differ between Young and Elderly Men ,

Impaired digestion and/or absorption of dietary protein lowers postprandial plasma amino acid availability and, as such, could reduce the postprandial muscle protein synthetic response in the elderly. We aimed to compare in vivo dietary protein digestion and absorption and the subsequent postprandial muscle protein synthetic response between young and elderly men. Ten elderly (64 ± 1 y) and 10 young (23 ± 1 y) healthy males consumed a single bolus of 35 g specifically produced, intrinsically l-[1-13C]phenylalanine-labeled micellar casein (CAS) protein. Furthermore, primed continuous infusions with l-[ring-2H5]phenylalanine, l-[1-13C]leucine, and l-[ring-2H2]tyrosine were applied and blood and muscle tissue samples were collected to assess the appearance rate of dietary protein-derived phenylalanine in the circulation and the subsequent muscle protein fractional synthetic rate over a 6-h postprandial period. Protein ingestion resulted in a rapid increase in exogenous phenylalanine appearance in both the young and elderly men. Total exogenous phenylalanine appearance rates (expressed as area under the curve) were 39 ± 3 μmol·6 h·kg−1 in the young men and 38 ± 2 μmol·6 h·kg−1 in the elderly men (P = 0.73). In accordance, splanchnic amino acid extraction did not differ between young (72 ± 2%) and elderly (73 ± 1%) volunteers (P = 0.74). Muscle protein synthesis rates, calculated from the oral tracer, were 0.063 ± 0.006 and 0.054 ± 0.004%/h in the young and elderly men, respectively, and did not differ between groups (P = 0.27). We conclude that protein digestion and absorption kinetics and the subsequent muscle protein synthetic response following the ingestion of a large bolus of intact CAS are not substantially impaired in healthy, elderly men.

0078 STUDIES ON TH 1, TH 2 AND TH 3 IMMUNE REACTIVITY IN PATIENTS WITH FIRST EPISODE PSYCHOSIS

It has been speculated that the amount of leucine in a meal largely determines the post-prandial muscle protein synthetic response to food intake. The present study investigates the impact of leucine co-ingestion on subsequent post-prandial muscle protein accretion following the ingestion of a single bolus of dietary protein in elderly males.Twenty-four elderly men (74.3 ± 1.0 y) were randomly assigned to ingest 20 g intrinsically l-[1-13C]phenylalanine-labeled casein protein with (PRO + LEU) or without (PRO) 2.5 g crystalline leucine. Ingestion of specifically produced intrinsically labeled protein allowed us to create a plasma phenylalanine enrichment pattern similar to the absorption pattern of phenylalanine from the ingested protein and assess the subsequent post-prandial incorporation of l-[1-13C] phenylalanine into muscle protein.Plasma amino acid concentrations increased rapidly following protein ingestion in both groups, with higher leucine concentrations observed in the PRO + LEU compared with the PRO group (P < 0.01). Plasma l-[1-13C]phenylalanine enrichments increased rapidly and to a similar extent in both groups following protein ingestion. Muscle protein-bound l-[1-13C]phenylalanine enrichments were significantly greater after PRO + LEU when compared with PRO at 2 h (72%; 0.0078 ± 0.0010 vs. 0.0046 ± 0.00100 MPE, respectively; P < 0.05) and 6 h (25%; 0.0232 ± 0.0015 vs. 0.0185 ± 0.0010 MPE, respectively; P < 0.05) following protein ingestion. The latter translated into a greater muscle protein synthetic rate following PRO + LEU compared with PRO over the entire 6 h post-prandial period (22%; 0.049 ± 0.003 vs. 0.040 ± 0.003% h−1, respectively; P < 0.05).Leucine co-ingestion with a bolus of pure dietary protein further stimulates post-prandial muscle protein synthesis rates in elderly men.