scholarly journals The Combination of Fasting, Acute Resistance Exercise, and Protein Ingestion Led to Different Responses of Autophagy Markers in Gastrocnemius and Liver Samples

Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 641 ◽  
Author(s):  
Ana P. Pinto ◽  
Tales S. Vieira ◽  
Bruno B. Marafon ◽  
Gabriela Batitucci ◽  
Elisa M. B. Cabrera ◽  
...  

The present study verified the responses of proteins related to the autophagy pathway after 10 h of fast with resistance exercise and protein ingestion in skeletal muscle and liver samples. The rats were distributed into five experimental groups: control (CT; sedentary and without gavage after fast), exercise immediately (EXE-imm; after fast, rats were submitted to the resistance protocol and received water by gavage immediately after exercise), exercise after 1 h (EXE-1h; after fast, rats were submitted to the resistance protocol and received water by gavage 1 h after exercise), exercise and supplementation immediately after exercise (EXE/Suppl-imm; after fast, rats were submitted to the resistance protocol and received a mix of casein: whey protein 1:1 (w/w) by gavage immediately after exercise), exercise and supplementation 1 h after exercise (EXE/Suppl-1h; after fast, rats were submitted to the resistance protocol and received a mix of casein: whey protein 1:1 (w/w) by gavage 1 h after exercise). In summary, the current findings show that the combination of fasting, acute resistance exercise, and protein blend ingestion (immediately or 1 h after the exercise stimulus) increased the serum levels of leucine, insulin, and glucose, as well as the autophagy protein contents in skeletal muscle, but decreased other proteins related to the autophagic pathway in the liver. These results deserve further mechanistic investigations since athletes are combining fasting with physical exercise to enhance health and performance outcomes.

2012 ◽  
Vol 37 (1) ◽  
pp. 21-30 ◽  
Author(s):  
Michelle M. Farnfield ◽  
Leigh Breen ◽  
Kate A. Carey ◽  
Andrew Garnham ◽  
David Cameron-Smith

Purpose: To investigate the impact of whey protein ingestion and resistance exercise training on the phosphorylation of mRNA translational signalling proteins in the skeletal muscle of young and old men. Methods: Sixteen healthy young (aged 18–25 years) and 15 healthy older men (aged 60–75 years) completed 12 weeks of resistance exercise and were randomly assigned to consume a whey protein (WPI) or placebo drink after each session. Muscle biopsies were collected before and 2 h after an acute exercise bout at the beginning and the end of training. Results: All subjects significantly increased strength after following strength training. Phosphorylation of mTOR was significantly greater in the WPI groups compared with placebo for both younger and older subjects. Phosphorylation of p70S6K, eIF4G, and 4EBP1 was greater for older subjects consuming WPI. Phosphorylation of rpS6, eIF4G, and 4EBP1 tended to increase in the younger subjects that had consumed WPI. Post-training, younger subjects demonstrated a similar pattern of mTOR phosphorylation as seen pre-training. In contrast, the initial heightened phosphorylation of mTOR, p70S6K, rpS6, and eIF4G in older muscle to combined resistance exercise and WPI ingestion became less pronounced after repeated training sessions. Conclusions: In the untrained state, resistance exercise coupled with WPI increases the phosphorylation of proteins involved in mRNA translation compared with exercise alone. Post-training, WPI- and exercise-induced protein phosphorylation was reduced in older men, but not in younger men. Thus, strategies to induce hypertrophy should utilize protein and resistance training concurrently. Further investigations should delineate interventions that will maintain sensitivity to anabolic stimuli in older populations.


Author(s):  
Jessica M. Moon ◽  
Kayla M. Ratliff ◽  
Julia C. Blumkaitis ◽  
Patrick S. Harty ◽  
Hannah A. Zabriskie ◽  
...  

Abstract Background Large (48-g), isonitrogenous doses of rice and whey protein have previously been shown to stimulate similar adaptations to resistance training, but the impact of consuming smaller doses has yet to be compared. We evaluated the ability of 24-g doses of rice or whey protein concentrate to augment adaptations following 8 weeks of resistance training. Methods Healthy resistance-trained males (n = 24, 32.8 ± 6.7 years, 179.3 ± 8.5 cm, 87.4 ± 8.5 kg, 27.2 ± 1.9 kg/m2, 27.8 ± 6.0% fat) were randomly assigned and matched according to fat-free mass to consume 24-g doses of rice (n = 12, Growing Naturals, LLC) or whey (n = 12, NutraBio Labs, Inc.) protein concentrate for 8 weeks while completing a standardized resistance training program. Body composition (DXA), muscular strength (one-repetition maximum [1RM]) and endurance (repetitions to fatigue [RTF] at 80% 1RM) using bench press (BP) and leg press (LP) exercises along with anaerobic capacity (Wingate) were assessed before and after the intervention. Subjects were asked to maintain regular dietary habits and record dietary intake every 2 weeks. Outcomes were assessed using 2 × 2 mixed (group x time) factorial ANOVA with repeated measures on time and independent samples t-tests using the change scores from baseline. A p-value of 0.05 and 95% confidence intervals on the changes between groups were used to determine outcomes. Results No baseline differences (p > 0.05) were found for key body composition and performance outcomes. No changes (p > 0.05) in dietary status occurred within or between groups (34 ± 4 kcal/kg/day, 3.7 ± 0.77 g/kg/day, 1.31 ± 0.28 g/kg/day, 1.87 ± 0.23 g/kg/day) throughout the study for daily relative energy (34 ± 4 kcals/kg/day), carbohydrate (3.7 ± 0.77 g/kg/day), fat (1.31 ± 0.28 g/kg/day), and protein (1.87 ± 0.23 g/kg/day) intake. Significant main effects for time were revealed for body mass (p = 0.02), total body water (p = 0.01), lean mass (p = 0.008), fat-free mass (p = 0.007), BP 1RM (p = 0.02), BP volume (p = 0.04), and LP 1RM (p = 0.01). Changes between groups were similar for body mass (− 0.88, 2.03 kg, p = 0.42), fat-free mass (− 0.68, 1.99 kg, p = 0.32), lean mass (− 0.73, 1.91 kg, p = 0.37), fat mass (− 0.48, 1.02 kg, p = 0.46), and % fat (− 0.63, 0.71%, p = 0.90). No significant between group differences were seen for BP 1RM (− 13.8, 7.1 kg, p = 0.51), LP 1RM (− 38.8, 49.6 kg, p = 0.80), BP RTF (− 2.02, 0.35 reps, p = 0.16), LP RTF (− 1.7, 3.3 reps, p = 0.50), and Wingate peak power (− 72.5, 53.4 watts, p = 0.76) following the eight-week supplementation period. Conclusions Eight weeks of daily isonitrogenous 24-g doses of rice or whey protein in combination with an eight-week resistance training program led to similar changes in body composition and performance outcomes. Retroactively registered on as NCT04411173.


2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 656-656
Author(s):  
Amadeo Salvador ◽  
Colleen McKenna ◽  
Andrew Askow ◽  
Hsin-Yu Fang ◽  
Sarah Burke ◽  
...  

Abstract Objectives Yes-Associated Protein (YAP) is implicated as a regulator of the post-exercise skeletal muscle response through mechanical transduction. We recently observed that resistance exercise (RE) increased both total (t) and phosphorylated (p) muscle YAP content, which correlated with extracellular signal-regulated kinase 1/2 (Erk1/2). Other anabolic signaling pathways (i.e., mTORC1) are known to be potentiated by the combined stimuli of RE and protein ingestion during post-exercise recovery. However, the impact of protein ingestion on t- and p-muscle YAP content during recovery from RE is unknown. Therefore, we aimed to determine the nutrient sensitivity of YAP in both an acute and chronic exercise setting in aging skeletal muscle. Methods Acute study: 13 untrained older women (59.8 ± 0.5 y) were randomized to perform an acute bout of unilateral RE (3 sets × 12 repetitions at 65% of one repetition maximum) followed by the ingestion of whey protein (0.3 g/kg lean body mass) or water. Muscle biopsies of both the rested and exercised legs were collected before and during the postprandial period. Chronic study: 20 untrained middle-aged men and women (47.5 ± 0.3 y) performed 3 weeks of whole body RE (3 d/wk) with moderate or high protein intake set at 1.2 g/kg/d or 1.6 g/kg/d, respectively. Muscle biopsies were taken weekly in the rested state. Total and phosphorylated YAPSer127 and Erk1/2Thr202/Tyr204 were examined by western blotting. Results Acute study: Protein ingestion decreased t- and p-YAP compared to the water condition in the non-exercised leg (main effect: P < 0.04). There was no change in t- or p-YAP, regardless of condition, in the exercised-leg throughout recovery (P = 0.88). There was no change in p/t ratio of Erk1/2 in the exercised or non-exercised leg.  Chronic study: There was no change in either p- or t-YAP in moderate and high protein conditions throughout training (both, P > 0.05). There was a decrease in t-Erk1/2 irrespective of condition (P = 0.04). There was no change in p/t ratio of Erk1/2 throughout training. There was a significant correlation between t-Erk1/2 and t-YAP (r = 0.741 and P < 0.001). Conclusions Protein ingestion mediated an acute down-regulation of YAP in the postprandial-state. However, resistance training did not modulate YAP content in aged skeletal muscle tissue. Funding Sources Funded by Beef Checkoff. AFS is supported by CAPES-Brazil.


2015 ◽  
Vol 40 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Nicholas A. Burd ◽  
Nicolas Tardif ◽  
Olav Rooyackers ◽  
Luc J.C. van Loon

The measurement of mitochondrial protein synthesis after food ingestion, contractile activity, and/or disease is often used to provide insight into skeletal muscle adaptations that occur in the longer term. Studies have shown that protein ingestion stimulates mitochondrial protein synthesis in human skeletal muscle. Minor differences in the stimulation of mitochondrial protein synthesis occur after a single bout of resistance or endurance exercise. There appear to be no measurable differences in mitochondrial protein synthesis between critically ill patients and aged-matched controls. However, the mitochondrial protein synthetic response is reduced at a more advanced age. In this paper, we discuss the challenges involved in the measurement of human skeletal muscle mitochondrial protein synthesis rates based on stable isotope amino acid tracer methods. Practical guidelines are discussed to improve the reliability of the measurement of mitochondrial protein synthesis rates. The value of the measurement of mitochondrial protein synthesis after a single meal or exercise bout on the prediction of the longer term skeletal muscle mass and performance outcomes in both the healthy and disease populations requires more work, but we emphasize that the measurements need to be reliable to be of any value to the field.


2010 ◽  
Vol 42 ◽  
pp. 776
Author(s):  
Matthew Cooke ◽  
Paul LaBounty ◽  
Thomas Buford ◽  
Liz Redd ◽  
Geoffrey Hudson ◽  
...  

2020 ◽  
Vol 111 (3) ◽  
pp. 708-718 ◽  
Author(s):  
Sara Y Oikawa ◽  
Michael J Kamal ◽  
Erin K Webb ◽  
Chris McGlory ◽  
Steven K Baker ◽  
...  

ABSTRACT Background Aging appears to attenuate the response of skeletal muscle protein synthesis (MPS) to anabolic stimuli such as protein ingestion (and the ensuing hyperaminoacidemia) and resistance exercise (RE). Objectives The purpose of this study was to determine the effects of protein quality on feeding- and feeding plus RE–induced increases of acute and longer-term MPS after ingestion of whey protein (WP) and collagen protein (CP). Methods In a double-blind parallel-group design, 22 healthy older women (mean ± SD age: 69 ± 3 y, n = 11/group) were randomly assigned to consume a 30-g supplement of either WP or CP twice daily for 6 d. Participants performed unilateral RE twice during the 6-d period to determine the acute (via [13C6]-phenylalanine infusion) and longer-term (ingestion of deuterated water) MPS responses, the primary outcome measures. Results Acutely, WP increased MPS by a mean ± SD 0.017 ± 0.008%/h in the feeding-only leg (Rest) and 0.032 ± 0.012%/h in the feeding plus exercise leg (Exercise) (both P < 0.01), whereas CP increased MPS only in Exercise (0.012 ± 0.013%/h) (P < 0.01) and MPS was greater in WP than CP in both the Rest and Exercise legs (P = 0.02). Longer-term MPS increased by 0.063 ± 0.059%/d in Rest and 0.173 ± 0.104%/d in Exercise (P < 0.0001) with WP; however, MPS was not significantly elevated above baseline in Rest (0.011 ± 0.042%/d) or Exercise (0.020 ± 0.034%/d) with CP. Longer-term MPS was greater in WP than in CP in both Rest and Exercise (P < 0.001). Conclusions Supplementation with WP elicited greater increases in both acute and longer-term MPS than CP supplementation, which is suggestive that WP is a more effective supplement to support skeletal muscle retention in older women than CP. This trial was registered at clinicaltrials.gov as NCT03281434.


2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Paul Reidy ◽  
Dillon K Walker ◽  
Jared M Dickinson ◽  
David M Gundermann ◽  
Micah J Drummond ◽  
...  

Author(s):  
Tom P Aird ◽  
Andrew J Farquharson ◽  
Kate M Bermingham ◽  
Aifric O'Sullivan ◽  
Janice E Drew ◽  
...  

Sprint interval training (SIT) is a time efficient alternative to endurance exercise, conferring beneficial skeletal muscle metabolic adaptations. Current literature has investigated the nutritional regulation of acute and chronic exercise-induced metabolic adaptations in muscle following endurance exercise, principally comparing the impact of training in fasted and carbohydrate-fed (CHO) conditions. Alternative strategies such as exercising in low CHO, protein-fed conditions remain poorly characterised, specifically pertaining to adaptations associated with SIT. Thus, this study aimed to compare the metabolic and performance adaptations to acute and short term SIT in the fasted state with pre-exercise hydrolysed (WPH) or concentrate (WPC) whey protein supplementation. In healthy males, pre-exercise protein ingestion did not alter exercise-induced increases in PGC-1α, PDK4, SIRT1, and PPAR-δ mRNA expression following acute SIT. However, supplementation of WPC and WPH beneficially altered acute exercise-induced SIRT4 and CD36 mRNA expression, respectively. Pre-exercise protein ingestion attenuated acute exercise-induced increases in muscle pan-acetylation, and PARP1 protein content compared with fasted SIT. Acute serum metabolomic differences confirmed greater pre-exercise amino acid delivery in protein-fed compared with fasted conditions. Following 3 weeks of SIT, training-induced increases in mitochondrial enzymatic activity and exercise performance were similar across nutritional groups. Interestingly, resting muscle acetylation status was favourably regulated in WPH conditions following training. Such findings suggest pre-exercise WPC and WPH ingestion positively influences metabolic adaptations to SIT compared to fasted training, resulting in either similar or enhanced performance adaptations. Future studies investigating nutritional modulation of metabolic adaptations to exercise are warranted to build upon these novel findings.


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