Dataset Information

Postexercise muscle glycogen synthesis with glucose, galactose, and combined galactose-glucose ingestion.

ABSTRACT: Ingested galactose can enhance postexercise liver glycogen repletion when combined with glucose but effects on muscle glycogen synthesis are unknown. In this double-blind randomized study participants [7 men and 2 women; V̇o_2max: 51.1 (8.7) mL·kg^-1·min^-1] completed three trials of exhaustive cycling exercise followed by a 4-h recovery period, during which carbohydrates were ingested at the rate of 1.2 g·kg^-1·h^-1 comprising glucose (GLU), galactose (GAL) or galactose + glucose (GAL + GLU; 1:2 ratio). The increase in vastus lateralis skeletal-muscle glycogen concentration during recovery was higher with GLU relative to GAL + GLU [contrast: +50 mmol·(kg DM)^-1; 95%CL 10, 89; P = 0.021] and GAL [+46 mmol·(kg DM)^-1; 95%CL 8, 84; P = 0.024] with no difference between GAL + GLU and GAL [-3 mmol·(kg DM)^-1; 95%CL -44, 37; P = 0.843]. Plasma glucose concentration in GLU was not significantly different vs. GAL + GLU (+ 0.41 mmol·L^-1; 95%CL 0.13, 0.94) but was significantly lower than GAL (-0.75 mmol·L^-1; 95%CL -1.34, -0.17) and also lower in GAL vs. GAL + GLU (-1.16 mmol·^-1; 95%CL -1.80, -0.53). Plasma insulin was higher in GLU + GAL and GLU compared with GAL but not different between GLU + GAL and GLU. Plasma galactose concentration was higher in GAL compared with GLU (3.35 mmol·L^-1; 95%CL 3.07, 3.63) and GAL + GLU (3.22 mmol·L^-1; 95%CL 3.54, 2.90) with no difference between GLU + GAL (0.13 mmol·L^-1; 95%CL -0.11, 0.37) and GLU. Compared with galactose or a galactose + glucose blend, glucose feeding was more effective in postexercise muscle glycogen synthesis. Comparable muscle glycogen synthesis was observed with galactose-glucose coingestion and exclusive galactose-only ingestion.NEW & NOTEWORTHY Postexercise galactose-glucose coingestion or exclusive galactose-only ingestion resulted in a lower rate of skeletal-muscle glycogen replenishment compared with exclusive glucose-only ingestion. Comparable muscle glycogen synthesis was observed with galactose-glucose coingestion and exclusive galactose-only ingestion.

SUBMITTER: Podlogar T

PROVIDER: S-EPMC10864004 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature

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Postexercise muscle glycogen synthesis with glucose, galactose, and combined galactose-glucose ingestion.

Podlogar Tim T Shad Brandon J BJ Seabright Alex P AP Odell Oliver J OJ Lord Samuel O SO Civil Rita R Salgueiro Rafael B RB Shepherd Emma L EL Lalor Patricia F PF Elhassan Yasir S YS Lai Yu-Chiang YC Rowlands David S DS Wallis Gareth A GA

American journal of physiology. Endocrinology and metabolism 20231018 6

Ingested galactose can enhance postexercise liver glycogen repletion when combined with glucose but effects on muscle glycogen synthesis are unknown. In this double-blind randomized study participants [7 men and 2 women; V̇o2max: 51.1 (8.7) mL·kg-1·min-1] completed three trials of exhaustive cycling exercise followed by a 4-h recovery period, during which carbohydrates were ingested at the rate of 1.2 g·kg-1·h-1 comprising glucose (GLU), gal ...[more]

PMID: 37850935

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Project description:Key pointsProtein ingestion and cooling are strategies employed by athletes to improve postexercise recovery and, as such, to facilitate muscle conditioning. However, whether cooling affects postprandial protein handling and subsequent muscle protein synthesis rates during recovery from exercise has not been assessed. We investigated the effect of postexercise cooling on the incorporation of dietary protein-derived amino acids into muscle protein and acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during recovery from resistance-type exercise over 2 weeks. Cold-water immersion during recovery from resistance-type exercise lowers the capacity of the muscle to take up and/or direct dietary protein-derived amino acids towards de novo myofibrillar protein accretion. In addition, cold-water immersion during recovery from resistance-type exercise lowers myofibrillar protein synthesis rates during prolonged resistance-type exercise training. Individuals aiming to improve skeletal muscle conditioning should reconsider applying cooling as a part of their postexercise recovery strategy.AbstractWe measured the impact of postexercise cooling on acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during adaptation to resistance-type exercise over 2 weeks. Twelve healthy males (aged 21 ± 2 years) performed a single resistance-type exercise session followed by water immersion of both legs for 20 min. One leg was immersed in cold water (8°C: CWI), whereas the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g of intrinsically (l-[1-13 C]-phenylalanine and l-[1-13 C]-leucine) labelled milk protein with 45 g of carbohydrates. In addition, primed continuous l-[ring-2 H5 ]-phenylalanine and l-[1-13 C]-leucine infusions were applied, with frequent collection of blood and muscle samples to assess myofibrillar protein synthesis rates in vivo over a 5 h recovery period. In addition, deuterated water (2 H2 O) was applied with the collection of saliva, blood and muscle biopsies over 2 weeks to assess the effects of postexercise cooling with protein intake on myofibrillar protein synthesis rates during more prolonged resistance-type exercise training (thereby reflecting short-term training adaptation). Incorporation of dietary protein-derived l-[1-13 C]-phenylalanine into myofibrillar protein was significantly lower in CWI compared to CON (0.016 ± 0.006 vs. 0.021 ± 0.007 MPE; P = 0.016). Postexercise myofibrillar protein synthesis rates were lower in CWI compared to CON based upon l-[1-13 C]-leucine (0.058 ± 0.011 vs. 0.072 ± 0.017% h-1 , respectively; P = 0.024) and l-[ring-2 H5 ]-phenylalanine (0.042 ± 0.009 vs. 0.053 ± 0.013% h-1 , respectively; P = 0.025). Daily myofibrillar protein synthesis rates assessed over 2 weeks were significantly lower in CWI compared to CON (1.48 ± 0.17 vs. 1.67 ± 0.36% day-1 , respectively; P = 0.042). Cold-water immersion during recovery from resistance-type exercise reduces myofibrillar protein synthesis rates and, as such, probably impairs muscle conditioning.

Project description:BACKGROUNDInsulin resistance results from impaired skeletal muscle glucose transport/phosphorylation, linked to augmented lipid availability. Despite greater intramuscular lipids, athletes are highly insulin sensitive, which could result from higher rates of insulin-stimulated glycogen synthesis or glucose transport/phosphorylation and oxidation. Thus, we examined the time course of muscle glycogen and glucose-6-phosphate concentrations during low and high systemic lipid availability.METHODSEight endurance-trained and 9 sedentary humans (VO2 peak: 56 ± 2 vs. 33 ± 2 mL/kg/min, P < 0.05) underwent 6-hour hyperinsulinemic-isoglycemic clamp tests with infusions of triglycerides or saline in a randomized crossover design. Glycogen and glucose-6-phosphate concentrations were monitored in vastus lateralis muscles using 13C/31P magnetic resonance spectroscopy.RESULTSAthletes displayed a 25% greater (P < 0.05) insulin-stimulated glucose disposal rate (Rd) than sedentary participants. During Intralipid infusion, insulin sensitivity remained higher in the athletes (ΔRd: 25 ± 3 vs. 17 ± 3 μmol/kg/min, P < 0.05), supported by higher glucose transporter type 4 protein expression than in sedentary humans. Compared to saline infusion, AUC of glucose-6-phosphate remained unchanged during Intralipid infusion in athletes (1.6 ± 0.2 mmol/L vs. 1.4 ± 0.2 [mmol/L] × h, P = n.s.) but tended to decrease by 36% in sedentary humans (1.7 ± 0.4 vs. 1.1 ± 0.1 [mmol/L] × h, P < 0.059). This drop was accompanied by a 72% higher rate of net glycogen synthesis in the athletes upon Intralipid infusion (47 ± 9 vs. 13 ± 3 μmol/kg/min, P < 0.05).CONCLUSIONAthletes feature higher skeletal muscle glucose disposal and glycogen synthesis during increased lipid availability, which primarily results from maintained insulin-stimulated glucose transport with increased myocellular glucose-6-phosphate levels for subsequent glycogen synthesis.TRIAL REGISTRATIONClinicalTrials.gov NCT01229059.FUNDINGGerman Federal Ministry of Health (BMG).

Project description:BackgroundPrevious work demonstrated that a soy-dairy protein blend (PB) prolongs hyperaminoacidemia and muscle protein synthesis in young adults after resistance exercise.ObjectiveWe investigated the effect of PB in older adults. We hypothesized that PB would prolong hyperaminoacidemia, enhancing mechanistic target of rapamycin complex 1 (mTORC1) signaling and muscle protein anabolism compared with a whey protein isolate (WPI).MethodsThis double-blind, randomized controlled trial studied men 55-75 y of age. Subjects consumed 30 g protein from WPI or PB (25% soy, 25% whey, and 50% casein) 1 h after leg extension exercise (8 sets of 10 repetitions at 70% one-repetition maximum). Blood and muscle amino acid concentrations and basal and postexercise muscle protein turnover were measured by using stable isotopic methods. Muscle mTORC1 signaling was assessed by immunoblotting.ResultsBoth groups increased amino acid concentrations (P < 0.05) and mTORC1 signaling after protein ingestion (P < 0.05). Postexercise fractional synthesis rate (FSR; P ≥ 0.05), fractional breakdown rate (FBR; P ≥ 0.05), and net balance (P = 0.08) did not differ between groups. WPI increased FSR by 67% (mean ± SEM: rest: 0.05% ± 0.01%; postexercise: 0.09% ± 0.01%; P < 0.05), decreased FBR by 46% (rest: 0.17% ± 0.01%; postexercise: 0.09% ± 0.03%; P < 0.05), and made net balance less negative (P < 0.05). PB ingestion did not increase FSR (rest: 0.07% ± 0.03%; postexercise: 0.09% ± 0.01%; P ≥ 0.05), tended to decrease FBR by 42% (rest: 0.25% ± 0.08%; postexercise: 0.15% ± 0.08%; P = 0.08), and made net balance less negative (P < 0.05). Within-group percentage of change differences were not different between groups for FSR, FBR, or net balance (P ≥ 0.05).ConclusionsWPI and PB ingestion after exercise in older men induced similar responses in hyperaminoacidemia, mTORC1 signaling, muscle protein synthesis, and breakdown. These data add new evidence for the use of whey or soy-dairy PBs as targeted nutritional interventions to counteract sarcopenia. This trial was registered at clinicaltrials.gov as NCT01847261.

Project description:Pea protein is an attractive nonanimal-derived protein source to support dietary protein requirements. However, although high in leucine, a low methionine content has been suggested to limit its anabolic potential. Mycoprotein has a complete amino acid profile which, at least in part, may explain its ability to robustly stimulate myofibrillar protein synthesis (MyoPS) rates. We hypothesized that an inferior postexercise MyoPS response would be seen following ingestion of pea protein compared with mycoprotein, which would be (partially) rescued by blending the two sources. Thirty-three healthy, young [age: 21 ± 1 yr, body mass index (BMI): 24 ± 1 kg·m-2] and resistance-trained participants received primed, continuous infusions of l-[ring-2H5]phenylalanine and completed a bout of whole body resistance exercise before ingesting 25 g of protein from mycoprotein (MYC, n = 11), pea protein (PEA, n = 11), or a blend (39% MYC, 61% PEA) of the two (BLEND, n = 11). Blood and muscle samples were taken pre-, 2 h, and 4 h postexercise/protein ingestion to assess postabsorptive and postprandial postexercise myofibrillar protein fractional synthetic rates (FSRs). Protein ingestion increased plasma essential amino acid and leucine concentrations (time effect; P < 0.0001), but more rapidly in BLEND and PEA compared with MYC (time × condition interaction; P < 0.0001). From similar postabsorptive values (MYC, 0.026 ± 0.008%·h-1; PEA, 0.028 ± 0.007%·h-1; BLEND, 0.026 ± 0.006%·h-1), resistance exercise and protein ingestion increased myofibrillar FSRs (time effect; P < 0.0001) over a 4-h postprandial period (MYC, 0.076 ± 0.004%·h-1; PEA, 0.087 ± 0.01%·h-1; BLEND, 0.085 ± 0.01%·h-1), with no differences between groups (all; P > 0.05). These data show that all three nonanimal-derived protein sources have utility in supporting postexercise muscle reconditioning.NEW & NOTEWORTHY This study provides evidence that pea protein (PEA), mycoprotein (MYC), and their blend (BLEND) can support postexercise myofibrillar protein synthesis rates following a bout of whole body resistance exercise. Furthermore, these data suggest that a methionine deficiency in pea may not limit its capacity to stimulate an acute increase in muscle protein synthesis (MPS).

Project description:Essential amino acid (EAA) ingestion enhances postexercise muscle protein synthesis, and, in particular, the anabolic response of older adults appears sensitive to the quantity of ingested leucine. The effect of leucine ingestion on muscle breakdown following resistance exercise (RE) is less understood. The purpose of this study was to identify the impact of postexercise leucine ingestion on the ubiquitin proteasome and autophagosomal-lysosomal systems following acute RE in older men. Subjects (72 ± 2 yr) performed RE and 1 h postexercise ingested 10 g of EAA containing a leucine quantity similar to quality protein (control, 1.8 g leucine, n = 7) or enriched in leucine (leucine, 3.5 g leucine, n = 8). Stable isotope infusion and muscle biopsies (vastus lateralis) obtained at rest and 2, 5, and 24 h postexercise were used to examine protein content (Western blot), mRNA expression (RT-quantitative PCR), and muscle protein fractional breakdown rate (FBR). Muscle-specific RING finger 1 mRNA increased in both groups at 2 and 5 h (P < 0.05). LC3 mRNA increased, and the LC3BII-to-LC3BI ratio decreased at all postexercise time points in control (P < 0.05). Conversely, LC3 mRNA only increased at 2 h, and the LC3BII-to-LC3BI ratio only decreased at 2 and 5 h in leucine (P < 0.05). Tumor necrosis factor receptor-associated factor-6 mRNA increased (P < 0.05) in control at 5 h. FBR was not statistically different between groups or from basal 24 h postexercise (P > 0.05). These data indicate that ingesting a larger quantity of leucine following RE may further reduce postexercise skeletal muscle autophagy in older men; however, it does not appear to influence the acute postexercise elevation in markers of the ubiquitin proteasome system or the breakdown of intact proteins.NEW & NOTEWORTHY The impact of postexercise leucine ingestion on processes of skeletal muscle breakdown in older adults is not well understood. Additional postexercise leucine ingestion appears to further reduce autophagy, but it does not interfere with the increase in ubiquitin proteasome system markers or the breakdown of intact proteins in skeletal muscle of older men. Postexercise leucine ingestion may promote a healthier protein pool and favorable muscle adaptations in older adults through greater accretion of myofibrillar proteins.

Dataset Information

Postexercise muscle glycogen synthesis with glucose, galactose, and combined galactose-glucose ingestion.

Publications

Postexercise muscle glycogen synthesis with glucose, galactose, and combined galactose-glucose ingestion.

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