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 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 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.

Effects Of Whey, Casein, Or Milk Protein Ingestion On Muscle Protein Synthesis After Endurance Exercise

2014 ◽  
Vol 46 ◽  
pp. 99
Author(s):  
Atsushi Kanda ◽  
Kyosuke Nakayama ◽  
Chiaki Sanbongi ◽  
Masashi Nagata ◽  
Shuji Ikegami ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Endurance Exercise ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Protein Ingestion

scholarly journals Effects of Whey, Caseinate, or Milk Protein Ingestion on Muscle Protein Synthesis after Exercise

Nutrients ◽  
2016 ◽  
Vol 8 (6) ◽  
pp. 339 ◽  
Author(s):  
Atsushi Kanda ◽  
Kyosuke Nakayama ◽  
Chiaki Sanbongi ◽  
Masashi Nagata ◽  
Shuji Ikegami ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Protein Ingestion

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 Mycoprotein ingestion stimulates protein synthesis rates to a greater extent than milk protein in rested and exercised skeletal muscle of healthy young men: a randomized controlled trial

2020 ◽  
Vol 112 (2) ◽  
pp. 318-333 ◽  
Author(s):  
Alistair J Monteyne ◽  
Mariana O C Coelho ◽  
Craig Porter ◽  
Doaa R Abdelrahman ◽  
Thomas S O Jameson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
G Protein ◽  
Milk Protein ◽  
Treatment Time ◽  
Muscle Protein ◽  
Young Men ◽  
Vastus Lateralis Muscle ◽  
Single Bolus ◽  
Protein Ingestion

ABSTRACT Background Mycoprotein is a fungal-derived sustainable protein-rich food source, and its ingestion results in systemic amino acid and leucine concentrations similar to that following milk protein ingestion. Objective We assessed the mixed skeletal muscle protein synthetic response to the ingestion of a single bolus of mycoprotein compared with a leucine-matched bolus of milk protein, in rested and exercised muscle of resistance-trained young men. Methods Twenty resistance-trained healthy young males (age: 22 ± 1 y, body mass: 82 ± 2 kg, BMI: 25 ± 1 kg·m−2) took part in a randomized, double-blind, parallel-group study. Participants received primed, continuous infusions of L-[ring-2H5]phenylalanine and ingested either 31 g (26.2 g protein: 2.5 g leucine) milk protein (MILK) or 70 g (31.5 g protein: 2.5 g leucine) mycoprotein (MYCO) following a bout of unilateral resistance-type exercise (contralateral leg acting as resting control). Blood and m. vastus lateralis muscle samples were collected before exercise and protein ingestion, and following a 4-h postprandial period to assess mixed muscle fractional protein synthetic rates (FSRs) and myocellular signaling in response to the protein beverages in resting and exercised muscle. Results Mixed muscle FSRs increased following MILK ingestion (from 0.036 ± 0.008 to 0.052 ± 0.006%·h−1 in rested, and 0.035 ± 0.008 to 0.056 ± 0.005%·h−1 in exercised muscle; P &lt;0.01) but to a greater extent following MYCO ingestion (from 0.025 ± 0.006 to 0.057 ± 0.004%·h−1 in rested, and 0.024 ± 0.007 to 0.072 ± 0.005%·h−1 in exercised muscle; P &lt;0.0001) (treatment × time interaction effect; P &lt;0.05). Postprandial FSRs trended to be greater in MYCO compared with MILK (0.065 ± 0.004 compared with 0.054 ± 0.004%·h−1, respectively; P = 0.093) and the postprandial rise in FSRs was greater in MYCO compared with MILK (Delta 0.040 ± 0.006 compared with Delta 0.018 ± 0.005%·h−1, respectively; P &lt;0.01). Conclusions The ingestion of a single bolus of mycoprotein stimulates resting and postexercise muscle protein synthesis rates, and to a greater extent than a leucine-matched bolus of milk protein, in resistance-trained young men. This trial was registered at clinicaltrials.gov as 660065600.

scholarly journals Branched-Chain Amino Acid Fortification Does Not Restore Muscle Protein Synthesis Rates following Ingestion of Lower- Compared with Higher-Dose Mycoprotein

2020 ◽  
Vol 150 (11) ◽  
pp. 2931-2941 ◽  
Author(s):  
Alistair J Monteyne ◽  
Mariana O C Coelho ◽  
Craig Porter ◽  
Doaa R Abdelrahman ◽  
Thomas S O Jameson ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
G Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Young Men ◽  
Quadriceps Muscle ◽  
Double Blind ◽  
Protein Ingestion ◽  
Branched Chain

ABSTRACT Background We have shown that ingesting a large bolus (70 g) of the fungal-derived, whole food mycoprotein robustly stimulates muscle protein synthesis (MPS) rates. Objective The aim of this study was to determine if a lower dose (35 g) of mycoprotein enriched with branched-chain amino acids (BCAAs) stimulates MPS to the same extent as 70 g of mycoprotein in resistance-trained young men. Methods Nineteen men [aged 22 ± 1 y, BMI (kg/m2): 25 ± 1] took part in a randomized, double-blind, parallel-group study. Participants received primed, continuous infusions of l-[ring-2H5]phenylalanine and ingested either 70 g mycoprotein (31.5 g protein; MYCO; n = 10) or 35 g BCAA-enriched mycoprotein (18.7 g protein: matched on BCAA content; ENR; n = 9) following a bout of unilateral resistance exercise. Blood and bilateral quadriceps muscle samples were obtained before exercise and protein ingestion and during a 4-h postprandial period to assess MPS in rested and exercised muscle. Two- and 3-factor ANOVAs were used to detect differences in plasma amino acid kinetics and mixed muscle fractional synthetic rates, respectively. Results Postprandial plasma BCAA concentrations increased more rapidly and to a larger degree in ENR compared with MYCO. MPS increased with protein ingestion (P ≤ 0.05) but to a greater extent following MYCO (from 0.025% ± 0.006% to 0.057% ± 0.004% · h−1 in rested muscle, and from 0.024% ± 0.007% to 0.072% ± 0.005% · h−1 in exercised muscle; P &lt; 0.0001) compared with ENR (from 0.031% ± 0.003% to 0.043% ± 0.005% · h−1 in rested muscle, and 0.027% ± 0.005% to 0.052% ± 0.005% · h−1 in exercised muscle; P &lt; 0.01) ingestion. Postprandial MPS rates were greater in MYCO compared with ENR (P &lt; 0.01). Conclusions The ingestion of lower-dose BCAA-enriched mycoprotein stimulates resting and postexercise MPS rates, but to a lesser extent compared with the ingestion of a BCAA-matched 70-g mycoprotein bolus in healthy young men. This trial was registered at clinicaltrials.gov as 660065600.

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