scholarly journals No differences in muscle protein synthesis rates following ingestion of wheat protein, milk protein, and their protein blend in healthy, young males

2021 ◽  
pp. 1-38
Author(s):  
Philippe J.M. Pinckaers ◽  
Imre W.K. Kouw ◽  
Floris K. Hendriks ◽  
Janneau M.X. van Kranenburg ◽  
Lisette C.P.G.M. de Groot ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Wheat Protein ◽  
Double Blind ◽  
Young Males ◽  
Protein Milk ◽  
Myofibrillar Protein Synthesis

ABSTRACT Plant-derived proteins have been suggested to have less anabolic properties when compared with animal-derived proteins. Whether blends of plant- and animal-derived proteins can compensate for their lesser anabolic potential has not been assessed. This study compares post-prandial muscle protein synthesis rates following the ingestion of milk protein with wheat protein or a blend of wheat plus milk protein in healthy, young males. In a randomized, double blind, parallel-group design, 36 males (23±3 y) received a primed continuous L-[ring-13C6]-phenylalanine infusion after which they ingested 30 g milk protein (MILK), 30 g wheat protein (WHEAT), or a 30 g blend combining 15 g wheat plus 15 g milk protein (WHEAT+MILK). Blood and muscle biopsies were collected frequently for 5 hours to assess post-prandial plasma amino acid profiles and subsequent myofibrillar protein synthesis rates. Ingestion of protein increased myofibrillar protein synthesis rates in all treatments (P<0.001). Post-prandial myofibrillar protein synthesis rates did not differ between MILK vs WHEAT (0.053±0.013 vs 0.056±0.012 %∙h-1, respectively; t-test P=0.56) or between MILK vs WHEAT+MILK (0.053±0.013 vs 0.059±0.025 %∙h-1, respectively; t-test P=0.46). In conclusion, ingestion of 30 g milk protein, 30 g wheat protein, or a blend of 15 g wheat plus 15 g milk protein increases muscle protein synthesis rates in young males. Furthermore, muscle protein synthesis rates following the ingestion of 30 g milk protein do not differ from rates observed after ingesting 30 g wheat protein or a blend with 15 g milk plus 15 g wheat protein in healthy, young males.

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

2021 ◽  
Vol 5 (Supplement_2) ◽  
pp. 517-517
Author(s):  
Philippe J.M. Pinckaers ◽  
Imre W.K. Kouw ◽  
Stefan H.M. Gorissen ◽  
Joan M. Senden ◽  
Lisette C.P.G.M. de Groot ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Essential Amino Acid ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Pea Protein ◽  
Young Males ◽  
Myofibrillar Protein Synthesis

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 &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 &lt; 0.05). Ingestion of both MILK and PLANT increased myofibrillar protein synthesis rates when compared to basal post-absorptive values (P &lt; 0.001), with no significant differences between treatments (0.053 ± 0.013 vs 0.064 ± 0.016%∙h−1,  respectively; P &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

scholarly journals The Muscle Protein Synthetic Response Following Ingestion of Corn Protein, Milk Protein and Their Protein Blend in Young Males

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 651-651
Author(s):  
Philippe J M Pinckaers ◽  
Michelle E G Weijzen ◽  
Lisanne H P Houben ◽  
Antoine H Zorenc ◽  
Imre W K Kouw ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Young Males ◽  
Corn Protein ◽  
Protein Ingestion ◽  
Myofibrillar Protein Synthesis

Abstract Objectives The muscle protein synthetic response to the ingestion of animal based proteins has been reported to be superior to the ingestion of plant based proteins. The lesser anabolic properties of plant based compared with animal based proteins has been attributed to differences in essential amino acid (EAA) contents and amino acid composition. This study compares post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein with the ingestion of 30 g corn protein or a blend of 30 g corn and milk protein in vivo, in young males. Methods In a randomized, double blind, parallel-group design, 36 healthy young males (26 ± 4 y) received a primed continuous infusion of L-[ring-13C6]-phenylalanine and ingested 30 g milk protein (MILK), 30 g corn protein (CORN), or a blend of 15 g corn protein plus 15 g milk protein (CORN + MILK) (n = 12 per group). 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 were analyzed with 2-way repeated measures ANOVA and independent samples t-test. Data are expressed as mean ± SD. Results MILK increased plasma EAA concentrations more when compared to CORN (incremental area under curve (iAUC): 151 ± 31 vs 77 ± 19 mmol/L/300 min, respectively; P &lt; 0.001). Both milk and corn protein ingestion increased myofibrillar protein synthesis rates (P &lt; 0.001), with no differences between MILK and CORN (from 0.014 ± 0.014 to 0.053 ± 0.013 and from 0.017 ± 0.011 to 0.052 ± 0.013%/h, respectively; time*treatment P = 0.661). When MILK was compared to CORN + MILK, the iAUC for plasma EAA concentrations increased more in MILK when compared to CORN + MILK (151 ± 31 vs 126 ± 24 mmol/L/300 min, respectively; P = 0.036). Corn plus milk protein ingestion also increased myofibrillar protein synthesis rates (from 0.015 ± 0.015 to 0.052 ± 0.024%/h; P &lt; 0.001), with no differences between MILK and CORN + MILK (time*treatment P = 0.823). Conclusions Ingestion of 30 g milk protein, 30 g corn protein, or a blend of 15 g corn plus 15 g milk protein increases muscle protein synthesis rates in vivo in young males. Post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein do not differ from rates observed after ingesting 30 g corn protein or a blend providing 15 g milk plus 15 g corn protein in vivo, in young males. Funding Sources TiFN.

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

2019 ◽  
Vol 317 (3) ◽  
pp. E473-E482 ◽  
Author(s):  
Andrew M. Holwerda ◽  
Kevin J. M. Paulussen ◽  
Maarten Overkamp ◽  
Joy P. B. Goessens ◽  
Irene-Fleur Kramer ◽  
...  
Keyword(s):  
Older Adults ◽  
Protein Synthesis ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Older Men ◽  
Myofibrillar Protein ◽  
Whole Body ◽  
Younger Adults ◽  
Myofibrillar Protein Synthesis

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.

scholarly journals No independent or combined effects of vitamin D and conjugated linoleic acids on muscle protein synthesis in older adults: a randomized, double-blind, placebo-controlled clinical trial

2020 ◽  
Vol 112 (5) ◽  
pp. 1382-1389
Author(s):  
Stephan van Vliet ◽  
Alan Fappi ◽  
Dominic N Reeds ◽  
Bettina Mittendorfer
Keyword(s):  
Older Adults ◽  
Vitamin D ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Controlled Clinical Trial ◽  
Double Blind ◽  
Before And After ◽  
Myofibrillar Protein Synthesis

ABSTRACT Background Aging is associated with skeletal muscle anabolic resistance (i.e., reduced muscle protein synthesis during anabolic conditions such as hyperaminoacidemia). The results from studies conducted in cell culture systems and animals suggest that both vitamin D and conjugated linoleic acids (CLAs) stimulate muscle protein synthesis. Objectives To conduct a randomized, double-blind, placebo-controlled clinical trial to determine the independent and combined effects of dietary vitamin D and CLA supplementation on myofibrillar protein synthesis rates in sedentary older adults. Methods Thirty-two sedentary, older adults were randomized to receive either: 1) 2000 IU vitamin D-3 (Vit D) per day; 2) 4000 mg CLA per day; 3) both Vit D (2000 IU/d) and CLA (4000 mg/d); or 4) placebo for 8 wk. Myofibrillar protein synthesis rates were evaluated by using intravenous [ring-2H5]phenylalanine infusion in conjunction with muscle biopsies during basal, postabsorptive conditions and during combined amino acid and insulin infusion before and after the supplementation period. Results Before the intervention, basal myofibrillar protein synthesis rates were not different among groups (Placebo: 0.033 ± 0.003; Vit D: 0.034 ± 0.002; CLA: 0.029 ± 0.005; Vit D + CLA: 0.038 ± 0.005 %·h-1), and hyperinsulinemia–hyperaminoacidemia increased myofibrillar protein synthesis rates by ∼35%. Compared with placebo, neither Vit D nor CLA nor combined Vit D + CLA supplementation affected the basal myofibrillar protein synthesis rates (placebo: 0.040 ± 0.004%/h; Vit D: 0.044 ± 0.006%/h; CLA: 0.039 ± 0.006%/h; Vit D + CLA: 0.040 ± 0.007%/h) or the hyperinsulinemia–hyperaminoacidemia–induced increase in myofibrillar protein synthesis (percentage increase from basal before and after the interventions: placebo, 30 ± 11 and 36 ± 11; Vit D, 38 ± 8 and 34 ± 10; CLA, 50 ± 14 and 51 ± 16; Vit D + CLA, 29 ± 15 and 35 ± 8). Conclusions Vitamin D and/or CLA supplementation, at the doses provided in our study, does not have muscle anabolic effects in sedentary older adults. The study was registered at clinicaltrials.gov (NCT03115775).

scholarly journals Effects of Salmon Ingestion on Post-Exercise Muscle Protein Synthesis: Exploration of Whole Protein Foods Versus Isolated Nutrients

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 650-650
Author(s):  
Kevin Paulussen ◽  
Amadeo Salvador ◽  
Colleen McKenna ◽  
Susannah Scaroni ◽  
Alexander Ulanov ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Post Exercise ◽  
Exercise Muscle ◽  
Amino Acid Concentrations ◽  
Myofibrillar Protein Synthesis ◽  
Stimulation Of

Abstract Objectives Healthy eating patterns consist of eating whole foods as opposed to single nutrients. The maintenance of skeletal muscle mass is of particular interest to overall health. As such, there is a need to underpin the role of eating nutrients within their natural whole-food matrix versus isolated nutrients on the regulation of postprandial muscle protein synthesis rates. This study assessed the effects of eating salmon, a potential food within a healthy Mediterranean style eating pattern, on the stimulation of post-exercise muscle protein synthesis rates versus eating these same nutrients in isolation in healthy young adults. Methods In a crossover design, 10 recreationally active adults (24 ± 4 y; 5 M, 5 F) performed an acute bout of resistance exercise followed by the ingestion of salmon (SAL) (20.5 g protein and 7.5 g fat) or its matched constituents in the form of crystalline amino acids and fish oil (ISO). Blood and muscle biopsies were collected at rest and after exercise at 2 and 5 h during primed continuous infusions of L-[ring-2H5]phenylalanine for the measurement of myofibrillar protein synthesis and plasma amino acid profiles. Data were analyzed by using a 2-factor (time × condition) repeated-measures ANOVA with Tukey's post hoc test. Results Plasma essential amino acid concentrations increased to a similar extent in both SAL and ISO during the postprandial period (P &gt; 0.05). Likewise, postprandial plasma leucine concentrations did not differ between nutrient condition (P &gt; 0.05). The post-exercise myofibrillar protein synthetic responses were similarly stimulated in both nutrition conditions early (0–2 h; 0.079 ± 0.039%/h (SAL) compared to 0.071 ± 0.078%/h (ISO); P = 0.64) and returned to baseline later (2–5 h; 0.046 ± 0.020%/h (SAL) compared to 0.038 ± 0.025%/h (ISO); P = 0.90). Similarly, there were no differences in the stimulation of myofibrillar protein synthesis rates between SAL and ISO during the entire 0–5 h recovery period (0.058 ± 0.024%/h compared to 0.045 ± 0.027%/h, respectively; P = 0.66). Conclusions We show that the ingestion of salmon or its isolated nutrients increases plasma amino acid concentrations and enhances the stimulation of post-exercise muscle protein synthesis rates with no differences in the temporal or cumulative responses in healthy young adults. Funding Sources USDA National Institute of Food and Agriculture Hatch project.

scholarly journals Branched-chain amino acid and branched-chain ketoacid ingestion increases muscle protein synthesis rates in vivo in older adults: a double-blind, randomized trial

2019 ◽  
Vol 110 (4) ◽  
pp. 862-872 ◽  
Author(s):  
Cas J Fuchs ◽  
Wesley J H Hermans ◽  
Andrew M Holwerda ◽  
Joey S J Smeets ◽  
Joan M Senden ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Postprandial Phase ◽  
Branched Chain ◽  
Myofibrillar Protein Synthesis ◽  
Older Males

ABSTRACTBackgroundProtein ingestion increases muscle protein synthesis rates. However, limited data are currently available on the effects of branched-chain amino acid (BCAA) and branched-chain ketoacid (BCKA) ingestion on postprandial muscle protein synthesis rates.ObjectiveThe aim of this study was to compare the impact of ingesting 6 g BCAA, 6 g BCKA, and 30 g milk protein (MILK) on the postprandial rise in circulating amino acid concentrations and subsequent myofibrillar protein synthesis rates in older males.MethodsIn a parallel design, 45 older males (age: 71 ± 1 y; BMI: 25.4 ± 0.8 kg/m2) were randomly assigned to ingest a drink containing 6 g BCAA, 6 g BCKA, or 30 g MILK. Basal and postprandial myofibrillar protein synthesis rates were assessed by primed continuous l-[ring-13C6]phenylalanine infusions with the collection of blood samples and muscle biopsies.ResultsPlasma BCAA concentrations increased following test drink ingestion in all groups, with greater increases in the BCAA and MILK groups compared with the BCKA group (P < 0.05). Plasma BCKA concentrations increased following test drink ingestion in all groups, with greater increases in the BCKA group compared with the BCAA and MILK groups (P < 0.05). Ingestion of MILK, BCAA, and BCKA significantly increased early myofibrillar protein synthesis rates (0–2 h) above basal rates (from 0.020 ± 0.002%/h to 0.042 ± 0.004%/h, 0.022 ± 0.002%/h to 0.044 ± 0.004%/h, and 0.023 ± 0.003%/h to 0.044 ± 0.004%/h, respectively; P < 0.001), with no differences between groups (P > 0.05). Myofibrillar protein synthesis rates during the late postprandial phase (2–5 h) remained elevated in the MILK group (0.039 ± 0.004%/h; P < 0.001), but returned to baseline values following BCAA and BCKA ingestion (0.024 ± 0.005%/h and 0.024 ± 0.005%/h, respectively; P > 0.05).ConclusionsIngestion of 6 g BCAA, 6 g BCKA, and 30 g MILK increases myofibrillar protein synthesis rates during the early postprandial phase (0–2 h) in vivo in healthy older males. The postprandial increase following the ingestion of 6 g BCAA and BCKA is short-lived, with higher myofibrillar protein synthesis rates only being maintained following the ingestion of an equivalent amount of intact milk protein. This trial was registered at Nederlands Trial Register (www.trialregister.nl) as NTR6047.

scholarly journals Time-dependent regulation of postprandial muscle protein synthesis rates after milk protein ingestion in young men

2019 ◽  
Vol 127 (6) ◽  
pp. 1792-1801 ◽  
Author(s):  
Stephan van Vliet ◽  
Joseph W. Beals ◽  
Andrew M. Holwerda ◽  
Russell S. Emmons ◽  
Joy P. Goessens ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Young Men ◽  
Myofibrillar Protein ◽  
Postprandial Period ◽  
Protein Ingestion ◽  
Stimulation Of

The anabolic action of “fast” whey protein on the regulation of postprandial muscle protein synthesis has been established to be short-lived in healthy young adults. We assessed the time course of anabolic signaling activation and stimulation of myofibrillar protein synthesis rates (MPS) after ingestion of a food source that represents a more typical meal-induced pattern of aminoacidemia. Seven young men (age: 22 ± 1 y) underwent repeated blood and biopsy sampling during primed, continuous l-[ ring-2H5]phenylalanine and l-[1-13C]leucine tracer infusions and ingested 38 g of l-[1-13C]phenylalanine- and l-[1-13C]leucine-labeled milk protein concentrate. A total of ∼27 ± 4 (∼10 g) and ∼31 ± 1% (∼12 g) of dietary protein-derived amino acids were released in circulation between 0 and 120 min and 120–300 min, respectively, of the postprandial period. l-[ ring-2H5]phenylalanine-based MPS increased above basal (0.025 ± 0.008%/h) by ∼75% (0.043 ± 0.009%/h; P = 0.05) between 0 and 120 min and by ∼86% (0.046 ± 0.004%/h; P = 0.02) between 120 and 300 min, respectively. l-[1-13C]leucine-based MPS increased above basal (0.027 ± 0.002%/h) by ∼72% (0.051 ± 0.016%/h; P = 0.10) between 0 and 120 min and by ∼62% (0.047 ± 0.004%/h; P = 0.001) between 120 and 300 min, respectively. Myofibrillar protein-bound l-[1-13C]phenylalanine increased over time ( P < 0.001) and equaled 0.004 ± 0.001, 0.008 ± 0.002, 0.017 ± 0.004, and 0.020 ± 0.003 mole percent excess at 60, 120, 180, and 300 min, respectively, of the postprandial period. Milk protein ingestion increased mTORC1 phosphorylation at 120, 180, and 300 min of the postprandial period (all P < 0.05). Our results show that ingestion of 38 g of milk protein results in sustained increases in MPS throughout a 5-h postprandial period in healthy young men. NEW & NOTEWORTHY The stimulation of muscle protein synthesis after whey protein ingestion is short-lived due to its transient systemic appearance of amino acids. Our study characterized the muscle anabolic response to a protein source that results in a more gradual release of amino acids into circulation. Our work demonstrates that a sustained increase in postprandial plasma amino acid availability after milk protein ingestion results in a prolonged stimulation of muscle protein synthesis rates in healthy young men.

Whey and casein labeled with l-[1-13C]leucine and muscle protein synthesis: effect of resistance exercise and protein ingestion

2011 ◽  
Vol 300 (1) ◽  
pp. E231-E242 ◽  
Author(s):  
Søren Reitelseder ◽  
Jakob Agergaard ◽  
Simon Doessing ◽  
Ida C. Helmark ◽  
Peter Lund ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Western Blots ◽  
Amino Acid Availability ◽  
Amino Acid Concentrations ◽  
Myofibrillar Protein Synthesis

Muscle protein turnover following resistance exercise and amino acid availability are relatively well described. By contrast, the beneficial effects of different sources of intact proteins in relation to exercise need further investigation. Our objective was to compare muscle anabolic responses to a single bolus intake of whey or casein after performance of heavy resistance exercise. Young male individuals were randomly assigned to participate in two protein trials ( n = 9) or one control trial ( n = 8). Infusion of l-[1-13C]leucine was carried out, and either whey, casein (0.3 g/kg lean body mass), or a noncaloric control drink was ingested immediately after exercise. l-[1-13C]leucine-labeled whey and casein were used while muscle protein synthesis (MPS) was assessed. Blood and muscle tissue samples were collected to measure systemic hormone and amino acid concentrations, tracer enrichments, and myofibrillar protein synthesis. Western blots were used to investigate the Akt signaling pathway. Plasma insulin and branched-chain amino acid concentrations increased to a greater extent after ingestion of whey compared with casein. Myofibrillar protein synthesis was equally increased 1–6 h postexercise after whey and casein intake, both of which were higher compared with control ( P < 0.05). Phosphorylation of Akt and p70S6K was increased after exercise and protein intake ( P < 0.05), but no differences were observed between the types of protein except for total 4E-BP1, which was higher after whey intake than after casein intake ( P < 0.05). In conclusion, whey and casein intake immediately after resistance exercise results in an overall equal MPS response despite temporal differences in insulin and amino acid concentrations and 4E-BP1.

scholarly journals Presleep protein ingestion does not compromise the muscle protein synthetic response to protein ingested the following morning

2016 ◽  
Vol 311 (6) ◽  
pp. E964-E973 ◽  
Author(s):  
Benjamin T. Wall ◽  
Nicholas A. Burd ◽  
Rinske Franssen ◽  
Stefan H. M. Gorissen ◽  
Tim Snijders ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Protein Supplementation ◽  
Protein Consumption ◽  
Nutrient Timing ◽  
Protein Ingestion ◽  
Postexercise Recovery ◽  
Myofibrillar Protein Synthesis

Protein ingestion before sleep augments postexercise muscle protein synthesis during overnight recovery. It is unknown whether postexercise and presleep protein consumption modulates postprandial protein handling and myofibrillar protein synthetic responses the following morning. Sixteen healthy young (24 ± 1 yr) men performed unilateral resistance-type exercise (contralateral leg acting as a resting control) at 2000. Participants ingested 20 g of protein immediately after exercise plus 60 g of protein presleep (PRO group; n = 8) or equivalent boluses of carbohydrate (CON; n = 8). The subsequent morning participants received primed, continuous infusions of l-[ ring-2H5]phenylalanine and l-[1-13C]leucine combined with ingestion of 20 g intrinsically l-[1-13C]phenylalanine- and l-[1-13C]leucine-labeled protein to assess postprandial protein handling and myofibrillar protein synthesis in the rested and exercised leg in CON and PRO. Exercise increased postabsorptive myofibrillar protein synthesis rates the subsequent day ( P < 0.001), with no differences between CON and PRO. Protein ingested in the morning increased myofibrillar protein synthesis in both the exercised and rested leg ( P < 0.01), with no differences between treatments. Myofibrillar protein bound l-[1-13C]phenylalanine enrichments were greater in the exercised (0.016 ± 0.002 and 0.015 ± 0.002 MPE in CON and PRO, respectively) vs. rested (0.010 ± 0.002 and 0.009 ± 0.002 MPE in CON and PRO, respectively) leg ( P < 0.05), with no differences between treatments ( P > 0.05). The additive effects of resistance-type exercise and protein ingestion on myofibrillar protein synthesis persist for more than 12 h after exercise and are not modulated by protein consumption during acute postexercise recovery. This work provides evidence of an extended window of opportunity where presleep protein supplementation can be an effective nutrient timing strategy to optimize skeletal muscle reconditioning.

scholarly journals Dose-response effects of dietary protein on muscle protein synthesis during recovery from endurance exercise in young men: a double-blind randomized trial

2020 ◽  
Vol 112 (2) ◽  
pp. 303-317 ◽  
Author(s):  
Tyler A Churchward-Venne ◽  
Philippe J M Pinckaers ◽  
Joey S J Smeets ◽  
Milan W Betz ◽  
Joan M Senden ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
G Protein ◽  
Endurance Exercise ◽  
Dietary Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Mitochondrial Protein ◽  
Whole Body ◽  
Double Blind ◽  
Body Protein

ABSTRACT Background Protein ingestion increases skeletal muscle protein synthesis rates during recovery from endurance exercise. Objectives We aimed to determine the effect of graded doses of dietary protein co-ingested with carbohydrate on whole-body protein metabolism, and skeletal muscle myofibrillar (MyoPS) and mitochondrial (MitoPS) protein synthesis rates during recovery from endurance exercise. Methods In a randomized, double-blind, parallel-group design, 48 healthy, young, endurance-trained men (mean ± SEM age: 27 ± 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 45 g carbohydrate with either 0 (0 g PRO), 15 (15 g PRO), 30 (30 g PRO), or 45 (45 g PRO) g intrinsically l-[1-13C]-phenylalanine and l-[1-13C]-leucine labeled milk protein after endurance exercise. Blood and muscle biopsy samples were collected over 360 min of postexercise recovery to assess whole-body protein metabolism and both MyoPS and MitoPS rates. Results Protein intake resulted in ∼70%–74% of the ingested protein-derived phenylalanine appearing in the circulation. Whole-body net protein balance increased dose-dependently after ingestion of 0, 15, 30, or 45 g protein (mean ± SEM: −0.31± 0.16, 5.08 ± 0.21, 10.04 ± 0.30, and 13.49 ± 0.55 μmol phenylalanine · kg−1 · h−1, respectively; P &lt; 0.001). 30 g PRO stimulated a ∼46% increase in MyoPS rates (%/h) compared with 0 g PRO and was sufficient to maximize MyoPS rates after endurance exercise. MitoPS rates were not increased after protein ingestion; however, incorporation of dietary protein–derived l-[1-13C]-phenylalanine into de novo mitochondrial protein increased dose-dependently after ingestion of 15, 30, and 45 g protein at 360 min postexercise (0.018 ± 0.002, 0.034 ± 0.002, and 0.046 ± 0.003 mole percentage excess, respectively; P &lt; 0.001). Conclusions Protein ingested after endurance exercise is efficiently digested and absorbed into the circulation. Whole-body net protein balance and dietary protein–derived amino acid incorporation into mitochondrial protein respond to increasing protein intake in a dose-dependent manner. Ingestion of 30 g protein is sufficient to maximize MyoPS rates during recovery from a single bout of endurance exercise. This trial was registered at trialregister.nl as NTR5111.

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