scholarly journals A single session of neuromuscular electrical stimulation does not augment postprandial muscle protein accretion

2016 ◽  
Vol 311 (1) ◽  
pp. E278-E285 ◽  
Author(s):  
Marlou L. Dirks ◽  
Benjamin T. Wall ◽  
Irene Fleur Kramer ◽  
Antoine H. Zorenc ◽  
Joy P. B. Goessens ◽  
...  
Keyword(s):  
Electrical Stimulation ◽  
Food Intake ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Neuromuscular Electrical Stimulation ◽  
Myofibrillar Protein ◽  
Single Session ◽  
Postprandial Period ◽  
Healthy Elderly ◽  
Protein Ingestion

The loss of muscle mass and strength that occurs with aging, termed sarcopenia, has been (at least partly) attributed to an impaired muscle protein synthetic response to food intake. Previously, we showed that neuromuscular electrical stimulation (NMES) can stimulate fasting muscle protein synthesis rates and prevent muscle atrophy during disuse. We hypothesized that NMES prior to protein ingestion would increase postprandial muscle protein accretion. Eighteen healthy elderly (69 ± 1 yr) males participated in this study. After a 70-min unilateral NMES protocol was performed, subjects ingested 20 g of intrinsically l-[1-13C]phenylalanine-labeled casein. Plasma samples and muscle biopsies were collected to assess postprandial mixed muscle and myofibrillar protein accretion as well as associated myocellular signaling during a 4-h postprandial period in both the control (CON) and stimulated (NMES) leg. Protein ingestion resulted in rapid increases in both plasma phenylalanine concentrations and l-[1-13C]phenylalanine enrichments, which remained elevated during the entire 4-h postprandial period ( P < 0.05). Mixed-muscle protein-bound l-[1-13C]phenylalanine enrichments increased significantly over time following protein ingestion, with no differences between the CON (0.0164 ± 0.0019 MPE) and NMES (0.0164 ± 0.0019 MPE) leg ( P > 0.05). In agreement, no differences were observed in the postprandial rise in myofibrillar protein bound l-[1-13C]phenylalanine enrichments between the CON and NMES legs (0.0115 ± 0.0014 vs. 0.0133 ± 0.0013 MPE, respectively, P > 0.05). Significant increases in mTOR and P70S6K phosphorylation status were observed in the NMES-stimulated leg only ( P < 0.05). We conclude that a single session of NMES prior to food intake does not augment postprandial muscle protein accretion in healthy 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 Neuromuscular electrical stimulation prior to presleep protein feeding stimulates the use of protein-derived amino acids for overnight muscle protein synthesis

2017 ◽  
Vol 122 (1) ◽  
pp. 20-27 ◽  
Author(s):  
Marlou L. Dirks ◽  
Bart B. L. Groen ◽  
Rinske Franssen ◽  
Janneau van Kranenburg ◽  
Luc J. C. van Loon
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Electrical Stimulation ◽  
Dietary Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Neuromuscular Electrical Stimulation ◽  
Older Men ◽  
Protein Ingestion ◽  
Protein Feeding

Short periods of muscle disuse result in substantial skeletal muscle atrophy. Recently, we showed that both neuromuscular electrical stimulation (NMES) as well as presleep dietary protein ingestion represent effective strategies to stimulate muscle protein synthesis rates. In this study, we test our hypothesis that NMES can augment the use of presleep protein-derived amino acids for overnight muscle protein synthesis in older men. Twenty healthy, older [69 ± 1 (SE) yr] men were subjected to 24 h of bed rest, starting at 8:00 AM. In the evening, volunteers were subjected to 70-min 1-legged NMES, while the other leg served as nonstimulated control (CON). Immediately following NMES, 40 g of intrinsically l-[1-13C]-phenylalanine labeled protein was ingested prior to sleep. Blood samples were taken throughout the night, and muscle biopsies were obtained from both legs in the evening and the following morning (8 h after protein ingestion) to assess dietary protein-derived l-[1-13C]-phenylalanine enrichments in myofibrillar protein. Plasma phenylalanine concentrations and plasma l-[1-13C]-phenylalanine enrichments increased significantly following protein ingestion and remained elevated for up to 6 h after protein ingestion ( P < 0.05). During overnight sleep, myofibrillar protein-bound l-[1-13C]-phenylalanine enrichments (MPE) increased to a greater extent in the stimulated compared with the control leg (0.0344 ± 0.0019 vs. 0.0297 ± 0.0016 MPE, respectively; P < 0.01), representing 18 ± 6% greater incorporation of presleep protein-derived amino acids in the NMES compared with CON leg. In conclusion, application of NMES prior to presleep protein feeding stimulates the use of dietary protein-derived amino acids for overnight muscle protein synthesis in older men. NEW & NOTEWORTHY Neuromuscular electrical stimulation (NMES) as well as presleep dietary protein ingestion represent effective strategies to stimulate muscle protein synthesis rates. Here we demonstrate that in older men after a day of bed rest, the application of NMES prior to presleep protein feeding stimulates the use of dietary protein-derived amino acids for overnight muscle protein synthesis by 18% compared with presleep protein feeding only.

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 Neuromuscular electrical stimulation increases muscle protein synthesis rates in type 2 diabetic men

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Nicholas A. Burd ◽  
Benjamin T. Wall ◽  
Marlou L. Dirks ◽  
Lex B. Verdijk ◽  
Tim Snijders ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Electrical Stimulation ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Neuromuscular Electrical Stimulation ◽  
Type 2 Diabetic

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 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.

Protein ingestion increases muscle protein synthesis after, but not during, endurance exercise

2010 ◽  
Vol 44 (14) ◽  
pp. i6-i7 ◽  
Author(s):  
C. Hulston ◽  
E. Wolsk ◽  
T. Grondahl ◽  
C. Yfanti ◽  
G. van Hall
Keyword(s):  
Protein Synthesis ◽  
Endurance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Protein Ingestion
Sign in / Sign up

Export Citation Format

Share Document