scholarly journals No independent or combined effects of vitamin D and conjugated linoleic acids on muscle protein synthesis in older adults: a randomized, double-blind, placebo-controlled clinical trial

2020 ◽  
Vol 112 (5) ◽  
pp. 1382-1389
Author(s):  
Stephan van Vliet ◽  
Alan Fappi ◽  
Dominic N Reeds ◽  
Bettina Mittendorfer
Keyword(s):  
Older Adults ◽  
Vitamin D ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Controlled Clinical Trial ◽  
Double Blind ◽  
Before And After ◽  
Myofibrillar Protein Synthesis

ABSTRACT Background Aging is associated with skeletal muscle anabolic resistance (i.e., reduced muscle protein synthesis during anabolic conditions such as hyperaminoacidemia). The results from studies conducted in cell culture systems and animals suggest that both vitamin D and conjugated linoleic acids (CLAs) stimulate muscle protein synthesis. Objectives To conduct a randomized, double-blind, placebo-controlled clinical trial to determine the independent and combined effects of dietary vitamin D and CLA supplementation on myofibrillar protein synthesis rates in sedentary older adults. Methods Thirty-two sedentary, older adults were randomized to receive either: 1) 2000 IU vitamin D-3 (Vit D) per day; 2) 4000 mg CLA per day; 3) both Vit D (2000 IU/d) and CLA (4000 mg/d); or 4) placebo for 8 wk. Myofibrillar protein synthesis rates were evaluated by using intravenous [ring-2H5]phenylalanine infusion in conjunction with muscle biopsies during basal, postabsorptive conditions and during combined amino acid and insulin infusion before and after the supplementation period. Results Before the intervention, basal myofibrillar protein synthesis rates were not different among groups (Placebo: 0.033 ± 0.003; Vit D: 0.034 ± 0.002; CLA: 0.029 ± 0.005; Vit D + CLA: 0.038 ± 0.005 %·h-1), and hyperinsulinemia–hyperaminoacidemia increased myofibrillar protein synthesis rates by ∼35%. Compared with placebo, neither Vit D nor CLA nor combined Vit D + CLA supplementation affected the basal myofibrillar protein synthesis rates (placebo: 0.040 ± 0.004%/h; Vit D: 0.044 ± 0.006%/h; CLA: 0.039 ± 0.006%/h; Vit D + CLA: 0.040 ± 0.007%/h) or the hyperinsulinemia–hyperaminoacidemia–induced increase in myofibrillar protein synthesis (percentage increase from basal before and after the interventions: placebo, 30 ± 11 and 36 ± 11; Vit D, 38 ± 8 and 34 ± 10; CLA, 50 ± 14 and 51 ± 16; Vit D + CLA, 29 ± 15 and 35 ± 8). Conclusions Vitamin D and/or CLA supplementation, at the doses provided in our study, does not have muscle anabolic effects in sedentary older adults. The study was registered at clinicaltrials.gov (NCT03115775).

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 No differences in muscle protein synthesis rates following ingestion of wheat protein, milk protein, and their protein blend in healthy, young males

2021 ◽  
pp. 1-38
Author(s):  
Philippe J.M. Pinckaers ◽  
Imre W.K. Kouw ◽  
Floris K. Hendriks ◽  
Janneau M.X. van Kranenburg ◽  
Lisette C.P.G.M. de Groot ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Milk Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Wheat Protein ◽  
Double Blind ◽  
Young Males ◽  
Protein Milk ◽  
Myofibrillar Protein Synthesis

ABSTRACT Plant-derived proteins have been suggested to have less anabolic properties when compared with animal-derived proteins. Whether blends of plant- and animal-derived proteins can compensate for their lesser anabolic potential has not been assessed. This study compares post-prandial muscle protein synthesis rates following the ingestion of milk protein with wheat protein or a blend of wheat plus milk protein in healthy, young males. In a randomized, double blind, parallel-group design, 36 males (23±3 y) received a primed continuous L-[ring-13C6]-phenylalanine infusion after which they ingested 30 g milk protein (MILK), 30 g wheat protein (WHEAT), or a 30 g blend combining 15 g wheat plus 15 g milk protein (WHEAT+MILK). Blood and muscle biopsies were collected frequently for 5 hours to assess post-prandial plasma amino acid profiles and subsequent myofibrillar protein synthesis rates. Ingestion of protein increased myofibrillar protein synthesis rates in all treatments (P<0.001). Post-prandial myofibrillar protein synthesis rates did not differ between MILK vs WHEAT (0.053±0.013 vs 0.056±0.012 %∙h-1, respectively; t-test P=0.56) or between MILK vs WHEAT+MILK (0.053±0.013 vs 0.059±0.025 %∙h-1, respectively; t-test P=0.46). In conclusion, ingestion of 30 g milk protein, 30 g wheat protein, or a blend of 15 g wheat plus 15 g milk protein increases muscle protein synthesis rates in young males. Furthermore, muscle protein synthesis rates following the ingestion of 30 g milk protein do not differ from rates observed after ingesting 30 g wheat protein or a blend with 15 g milk plus 15 g wheat protein in healthy, young males.

scholarly journals Effect of Aerobic Exercise Training and Essential Amino Acid Supplementation for 24 Weeks on Physical Function, Body Composition, and Muscle Metabolism in Healthy, Independent Older Adults: A Randomized Clinical Trial

2018 ◽  
Vol 74 (10) ◽  
pp. 1598-1604 ◽  
Author(s):  
Melissa M Markofski ◽  
Kristofer Jennings ◽  
Kyle L Timmerman ◽  
Jared M Dickinson ◽  
Christopher S Fry ◽  
...  
Keyword(s):  
Older Adults ◽  
Clinical Trial ◽  
Body Composition ◽  
Protein Synthesis ◽  
Muscle Strength ◽  
Randomized Clinical Trial ◽  
Walking Speed ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Before And After

Abstract Background Essential amino acids (EAA) and aerobic exercise (AE) acutely and independently stimulate skeletal muscle protein anabolism in older adults. Objective In this Phase 1, double-blind, placebo-controlled, randomized clinical trial, we determined if chronic EAA supplementation, AE training, or a combination of the two interventions could improve muscle mass and function by stimulating muscle protein synthesis. Methods We phone-screened 971, enrolled 109, and randomized 50 independent, low-active, nonfrail, and nondiabetic older adults (age 72 ± 1 years). We used a 2 × 2 factorial design. The interventions were: daily nutritional supplementation (15 g EAA or placebo) and physical activity (supervised AE training 3 days/week or monitored habitual activity) for 24 weeks. Muscle strength, physical function, body composition, and muscle protein synthesis were measured before and after the 24-week intervention. Results Forty-five subjects completed the 24-week intervention. VO2peak and walking speed increased (p < .05) in both AE groups, irrespective of supplementation type, but muscle strength increased only in the EAA + AE group (p < .05). EAA supplementation acutely increased (p < .05) muscle protein synthesis from basal both before and after the intervention, with a larger increase in the EAA + AE group after the intervention. Total and regional lean body mass did not change significantly with any intervention. Conclusions In nonfrail, independent, healthy older adults AE training increased walking speed and aerobic fitness, and, when combined with EAA supplementation, it also increased muscle strength and EAA-stimulated muscle protein synthesis. These increases occurred without improvements in muscle mass.

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 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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