scholarly journals Whey Protein Supplementation Preserves Postprandial Myofibrillar Protein Synthesis during Short-Term Energy Restriction in Overweight and Obese Adults

2014 ◽  
Vol 145 (2) ◽  
pp. 246-252 ◽  
Author(s):  
Amy J Hector ◽  
George R Marcotte ◽  
Tyler A Churchward-Venne ◽  
Caoileann H Murphy ◽  
Leigh Breen ◽  
...  
Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 845
Author(s):  
Robert W. Davies ◽  
Joseph J. Bass ◽  
Brian P. Carson ◽  
Catherine Norton ◽  
Marta Kozior ◽  
...  

Background: The aim of this study was to investigate the effect of whey protein supplementation on myofibrillar protein synthesis (myoPS) and muscle recovery over a 7-d period of intensified resistance training (RT). Methods: In a double-blind randomised parallel group design, 16 resistance-trained men aged 18 to 35 years completed a 7-d RT protocol, consisting of three lower-body RT sessions on non-consecutive days. Participants consumed a controlled diet (146 kJ·kg−1·d−1, 1.7 g·kg−1·d−1 protein) with either a whey protein supplement or an isonitrogenous control (0.33 g·kg−1·d−1 protein). To measure myoPS, 400 ml of deuterium oxide (D2O) (70 atom %) was ingested the day prior to starting the study and m. vastus lateralis biopsies were taken before and after RT-intervention. Myofibrillar fractional synthetic rate (myoFSR) was calculated via deuterium labelling of myofibrillar-bound alanine, measured by gas chromatography-pyrolysis-isotope ratio mass spectrometry (GC-Pyr-IRMS). Muscle recovery parameters (i.e., countermovement jump height, isometric-squat force, muscle soreness and serum creatine kinase) were assessed daily. Results: MyoFSR PRE was 1.6 (0.2) %∙d−1 (mean (SD)). Whey protein supplementation had no effect on myoFSR (p = 0.771) or any recovery parameter (p = 0.390–0.989). Conclusions: Over an intense 7-d RT protocol, 0.33 g·kg−1·d−1 of supplemental whey protein does not enhance day-to-day measures of myoPS or postexercise recovery in resistance-trained men.


2015 ◽  
Vol 308 (9) ◽  
pp. E734-E743 ◽  
Author(s):  
Caoileann H. Murphy ◽  
Tyler A. Churchward-Venne ◽  
Cameron J. Mitchell ◽  
Nathan M. Kolar ◽  
Amira Kassis ◽  
...  

Strategies to enhance weight loss with a high fat-to-lean ratio in overweight/obese older adults are important since lean loss could exacerbate sarcopenia. We examined how dietary protein distribution affected muscle protein synthesis during energy balance (EB), energy restriction (ER), and energy restriction plus resistance training (ER + RT). A 4-wk ER diet was provided to overweight/obese older men (66 ± 4 yr, 31 ± 5 kg/m2) who were randomized to either a balanced (BAL: 25% daily protein/meal × 4) or skewed (SKEW: 7:17:72:4% daily protein/meal; n = 10/group) pattern. Myofibrillar and sarcoplasmic protein fractional synthetic rates (FSR) were measured during a 13-h primed continuous infusion of l-[ ring-13C6]phenylalanine with BAL and SKEW pattern of protein intake in EB, after 2 wk ER, and after 2 wk ER + RT. Fed-state myofibrillar FSR was lower in ER than EB in both groups ( P < 0.001), but was greater in BAL than SKEW ( P = 0.014). In ER + RT, fed-state myofibrillar FSR increased above ER in both groups and in BAL was not different from EB ( P = 0.903). In SKEW myofibrillar FSR remained lower than EB ( P = 0.002) and lower than BAL ( P = 0.006). Fed-state sarcoplasmic protein FSR was reduced similarly in ER and ER + RT compared with EB ( P < 0.01) in both groups. During ER in overweight/obese older men a BAL consumption of protein stimulated the synthesis of muscle contractile proteins more effectively than traditional, SKEW distribution. Combining RT with a BAL protein distribution “rescued” the lower rates of myofibrillar protein synthesis during moderate ER.


2018 ◽  
Vol 50 (5S) ◽  
pp. 370
Author(s):  
Brandon J. Shad ◽  
Andrew M. Holwerda ◽  
Yasir S. Elhassan ◽  
Luc J.C. van Loon ◽  
Janice L. Thompson ◽  
...  

2020 ◽  
Vol 318 (2) ◽  
pp. E117-E130 ◽  
Author(s):  
Sean P. Kilroe ◽  
Jonathan Fulford ◽  
Andrew M. Holwerda ◽  
Sarah R. Jackman ◽  
Benjamin P. Lee ◽  
...  

Short-term muscle disuse has been reported to lower both postabsorptive and postprandial myofibrillar protein synthesis rates. This study assessed the impact of disuse on daily myofibrillar protein synthesis rates following short-term (2 and 7 days) muscle disuse under free living conditions. Thirteen healthy young men (age: 20 ± 1 yr; BMI: 23 ± 1 kg/m−2) underwent 7 days of unilateral leg immobilization via a knee brace, with the nonimmobilized leg acting as a control. Four days before immobilization participants ingested 400 mL of 70% deuterated water, with 50-mL doses consumed daily thereafter. Upper leg bilateral MRI scans and muscle biopsies were collected before and after 2 and 7 days of immobilization to determine quadriceps volume and daily myofibrillar protein synthesis rates. Immobilization reduced quadriceps volume in the immobilized leg by 1.7 ± 0.3 and 6.7 ± 0.6% after 2 and 7 days, respectively, with no changes in the control leg. Over the 1-wk immobilization period, myofibrillar protein synthesis rates were 36 ± 4% lower in the immobilized (0.81 ± 0.04%/day) compared with the control (1.26 ± 0.04%/day) leg ( P < 0.001). Myofibrillar protein synthesis rates in the control leg did not change over time ( P = 0.775), but in the immobilized leg they were numerically lower during the 0- to 2-day period (16 ± 6%, 1.11 ± 0.09%/day, P = 0.153) and were significantly lower during the 2- to 7-day period (44 ± 5%, 0.70 ± 0.06%/day, P < 0.001) when compared with the control leg. We conclude that 1 wk of muscle disuse induces a rapid and sustained decline in daily myofibrillar protein synthesis rates in healthy young men.


2012 ◽  
Vol 108 (6) ◽  
pp. 958-962 ◽  
Author(s):  
Nicholas A. Burd ◽  
Yifan Yang ◽  
Daniel R. Moore ◽  
Jason E. Tang ◽  
Mark A. Tarnopolsky ◽  
...  

We aimed to determine the effect of consuming pure isolated micellar casein or pure whey protein isolate on rates of myofibrillar protein synthesis (MPS) at rest and after resistance exercise in elderly men. Healthy elderly men (72 (sem 1) years; BMI 26·4 (sem 0·7) kg/m2) were divided into two groups (n 7 each) who received a primed, constant infusion of l-[ring-13C6]phenylalanine to measure MPS at rest and during 4 h of exercise recovery. Participants performed unilateral leg resistance exercise followed by the consumption of isonitrogenous quantities (20 g) of casein or whey. Blood essential amino acids and leucine concentration peaked 60 min post-drink and were greater in amplitude after whey protein ingestion (both, P < 0·05). MPS in the rested leg was 65 % higher (P = 0·002) after ingestion of whey (0·040 (sem 0·003) %/h) when compared with micellar casein (0·024 (sem 0·002) %/h). Similarly, resistance exercise-stimulated rates of MPS were greater (P < 0·001) after whey ingestion (0·059 (sem 0·005) %/h) v. micellar casein (0·035 (sem 0·002) %/h). We conclude that ingestion of isolated whey protein supports greater rates of MPS than micellar casein both at rest and after resistance exercise in healthy elderly men. This result is probably related to a greater hyperaminoacidaemia or leucinaemia with whey ingestion.


2014 ◽  
Vol 307 (1) ◽  
pp. E71-E83 ◽  
Author(s):  
Tyler A. Churchward-Venne ◽  
Lisa M. Cotie ◽  
Maureen J. MacDonald ◽  
Cameron J. Mitchell ◽  
Todd Prior ◽  
...  

Aging is associated with anabolic resistance, a reduced sensitivity of myofibrillar protein synthesis (MPS) to postprandial hyperaminoacidemia, particularly with low protein doses. Impairments in postprandial skeletal muscle blood flow and/or microvascular perfusion with hyperaminoacidemia and hyperinsulinemia may contribute to anabolic resistance. We examined whether providing citrulline, a precursor for arginine and nitric oxide synthesis, would increase arterial blood flow, skeletal muscle microvascular perfusion, MPS, and signaling through mTORC1. Twenty-one elderly males (65–80 yr) completed acute unilateral resistance exercise prior to being assigned to ingest a high dose (45 g) of whey protein (WHEY) or a low dose (15 g) of whey protein with 10 g of citrulline (WHEY + CIT) or with 10 g of nonessential amino acids (WHEY + NEAA). A primed, continuous infusion of l-[ ring-13C6] phenylalanine with serial muscle biopsies was used to measure MPS and protein phosphorylation, whereas ultrasound was used to measure microvascular circulation under basal and postprandial conditions in both a rested (FED) and exercised (EX-FED) leg. Argininemia was greater in WHEY + CIT vs. WHEY and WHEY + NEAA from 30 to 300 min postexercise ( P < 0.001), but there were no treatment differences in blood flow or microvascular perfusion (all P > 0.05). Phosphorylation of p70S6K-Thr389was greater in WHEY vs. WHEY + NEAA ( P = 0.02). Postprandial MPS was greater in WHEY vs. WHEY + CIT and WHEY + NEAA under both FED (WHEY: ∼128%; WHEY + CIT: ∼56%; WHEY + NEAA: ∼38%) and EX-FED (WHEY: ∼251%; WHEY + CIT: ∼124%; WHEY + NEAA: ∼108%) conditions ( P = 0.003). Citrulline coingestion with a low quantity of protein was ineffective in augmenting the anabolic properties of protein compared with nonessential amino acids.


2016 ◽  
Vol 311 (6) ◽  
pp. E964-E973 ◽  
Author(s):  
Benjamin T. Wall ◽  
Nicholas A. Burd ◽  
Rinske Franssen ◽  
Stefan H. M. Gorissen ◽  
Tim Snijders ◽  
...  

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.


Nutrients ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 1657 ◽  
Author(s):  
Robert W. Davies ◽  
Joseph J. Bass ◽  
Brian P. Carson ◽  
Catherine Norton ◽  
Marta Kozior ◽  
...  

The aim of this study was to test the effects of two disparate isonitrogenous, isocaloric pre-exercise feeds on deuterium-oxide (D2O) derived measures of myofibrillar protein synthesis (myoPS) in humans. Methods: In a double-blind parallel group design, 22 resistance-trained men aged 18 to 35 years ingested a meal (6 kcal·kg−1, 0.8 g·kg−1 carbohydrate, 0.2 g·kg−1 fat) with 0.33 g·kg−1 nonessential amino acids blend (NEAA) or whey protein (WHEY), prior to resistance exercise (70% 1RM back-squats, 10 reps per set to failure, 25% duty cycle). Biopsies of M. vastus lateralis were obtained pre-ingestion (PRE) and +3 h post-exercise (POST). The myofibrillar fractional synthetic rate (myoFSR) was calculated via deuterium labelling of myofibrillar-bound alanine, measured by gas chromatography–pyrolysis–isotope ratio mass spectrometry (GC-Pyr-IRMS). Data are a mean percentage change (95% CI). Results: There was no discernable change in myoFSR following NEAA (10(−5, 25) %, p = 0.235), whereas an increase in myoFSR was observed after WHEY (28 (13, 43) %, p = 0.003). Conclusions: Measured by a D2O tracer technique, a disparate myoPS response was observed between NEAA and WHEY. Pre-exercise ingestion of whey protein increased post-exercise myoPS, whereas a NEAA blend did not, supporting the use of NEAA as a viable isonitrogenous negative control.


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