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 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 Sodium nitrate co-ingestion with protein does not augment postprandial muscle protein synthesis rates in older, type 2 diabetes patients

2016 ◽  
Vol 311 (2) ◽  
pp. E325-E334 ◽  
Author(s):  
Imre W. K. Kouw ◽  
Naomi M. Cermak ◽  
Nicholas A. Burd ◽  
Tyler A. Churchward-Venne ◽  
Joan M. Senden ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Protein Synthesis ◽  
Dietary Protein ◽  
De Novo ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Protein Ingestion ◽  
Diabetes Patients

The age-related anabolic resistance to protein ingestion is suggested to be associated with impairments in insulin-mediated capillary recruitment and postprandial muscle tissue perfusion. The present study investigated whether dietary nitrate co-ingestion with protein improves muscle protein synthesis in older, type 2 diabetes patients. Twenty-four men with type 2 diabetes (72 ± 1 yr, 26.7 ± 1.4 m/kg2 body mass index, 7.3 ± 0.4% HbA1C) received a primed continuous infusion of l-[ring-2H5]phenylalanine and l-[1-13C]leucine and ingested 20 g of intrinsically l-[1-13C]phenylalanine- and l-[1-13C]leucine-labeled protein with (PRONO3) or without (PRO) sodium nitrate (0.15 mmol/kg). Blood and muscle samples were collected to assess protein digestion and absorption kinetics and postprandial muscle protein synthesis rates. Upon protein ingestion, exogenous phenylalanine appearance rates increased in both groups ( P < 0.001), resulting in 55 ± 2% and 53 ± 2% of dietary protein-derived amino acids becoming available in the circulation over the 5h postprandial period in the PRO and PRONO3 groups, respectively. Postprandial myofibrillar protein synthesis rates based on l-[ring-2H5]phenylalanine did not differ between groups (0.025 ± 0.004 and 0.021 ± 0.007%/h over 0–2 h and 0.032 ± 0.004 and 0.030 ± 0.003%/h over 2–5 h in PRO and PRONO3, respectively, P = 0.7). No differences in incorporation of dietary protein-derived l-[1-13C]phenylalanine into de novo myofibrillar protein were observed at 5 h (0.016 ± 0.002 and 0.014 ± 0.002 mole percent excess in PRO and PRONO3, respectively, P = 0.8). Dietary nitrate co-ingestion with protein does not modulate protein digestion and absorption kinetics, nor does it further increase postprandial muscle protein synthesis rates or the incorporation of dietary protein-derived amino acids into de novo myofibrillar protein in older, type 2 diabetes patients.

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

2019 ◽  
Vol 149 (9) ◽  
pp. 1533-1542 ◽  
Author(s):  
Imre W K Kouw ◽  
Jan Willem van Dijk ◽  
Astrid M H Horstman ◽  
Irene Fleur Kramer ◽  
Joy P B Goessens ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Myofibrillar Protein ◽  
Whole Body ◽  
Protein Digestion ◽  
Body Protein ◽  
Postprandial Period ◽  
Protein Ingestion ◽  
Myofibrillar Protein Synthesis

ABSTRACT Background Excess lipid availability has been associated with the development of anabolic resistance. As such, obesity may be accompanied by impairments in muscle protein metabolism. Objective We hypothesized that basal and postprandial muscle protein synthesis rates are lower in obese than in lean men. Methods Twelve 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. Results Exogenous 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). Conclusions Basal, 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.

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 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 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.

scholarly journals Endocrine Responses During Overnight Recovery From Exercise: Impact of Nutrition and Relationships With Muscle Protein Synthesis

2011 ◽  
Vol 21 (5) ◽  
pp. 398-409 ◽  
Author(s):  
James A. Betts ◽  
Milou Beelen ◽  
Keith A. Stokes ◽  
Wim H.M. Saris ◽  
Luc J.C. van Loon
Keyword(s):  
Growth Hormone ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Vastus Lateralis ◽  
Total Testosterone ◽  
Double Blind ◽  
Before And After ◽  
Protein Ingestion ◽  
Postexercise Recovery

Nocturnal endocrine responses to exercise performed in the evening and the potential role of nutrition are poorly understood. To gain novel insight, 10 healthy men ingested carbohydrate with (C+P) and without (C) protein in a randomized order and double-blind manner during 2 hr of interval cycling followed by resistancetype exercise and into early postexercise recovery. Blood samples were obtained hourly throughout 9 hr of postexercise overnight recovery for analysis of key hormones. Muscle samples were taken from the vastus lateralis before and after exercise and then again the next morning (7 a.m.) to calculate mixed-muscle protein fractional synthetic rate (FSR). Overnight plasma hormone concentrations were converted into overall responses (expressed as area under the concentration curve) and did not differ between treatments for either growth hormone (1,464 ± 257 vs. 1,432 ± 164 pg/ml · 540 min) or total testosterone (18.3 ± 1.2 vs. 17.9 ± 1.2 nmol/L · 540 min, C and C+P, respectively). In contrast, the overnight cortisol response was higher with C+P (102 ± 11 nmol/L · 540 min) than with C (81 ± 8 nmol/L · 540 min; p = .02). Mixed-muscle FSR did not differ between C and C+P during overnight recovery (0.062% ± 0.006% and 0.062% ± 0.009%/hr, respectively) and correlated significantly with the plasma total testosterone response (r = .7, p < .01). No correlations with FSR were apparent for the response of growth hormone (r = –.2, p = .4), cortisol (r = .1, p = .6), or the ratio of testosterone to cortisol (r = .2, p = .5). In conclusion, protein ingestion during and shortly after exercise does not modulate the endocrine response or muscle protein synthesis during overnight recovery.

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

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.

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