Hot-water immersion does not increase postprandial muscle protein synthesis rates during recovery from resistance-type exercise in healthy, young males

The purpose of this study was to assess the impact of postexercise hot-water immersion on postprandial myofibrillar protein synthesis rates during recovery from a single bout of resistance-type exercise in healthy, young men. Twelve healthy, adult men (age: 23 ± 1 y) performed a single bout of resistance-type exercise followed by 20 min of water immersion of both legs. One leg was immersed in hot water [46°C: hot-water immersion (HWI)], while the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine labeled milk protein with 45 g of carbohydrates. In addition, primed continuous L-[ring-2H5]-phenylalanine and L-[1-13C]-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. Muscle temperature immediately after water immersion was higher in the HWI compared with the CON leg (37.5 ± 0.1 vs. 35.2 ± 0.2°C; P < 0.001). Incorporation of dietary protein-derived L-[1-13C]-phenylalanine into myofibrillar protein did not differ between the HWI and CON leg during the 5-h recovery period (0.025 ± 0.003 vs. 0.024 ± 0.002 MPE; P = 0.953). Postexercise myofibrillar protein synthesis rates did not differ between the HWI and CON leg based upon L-[1-13C]-leucine (0.050 ± 0.005 vs. 0.049 ± 0.002%/h; P = 0.815) and L-[ring-2H5]-phenylalanine (0.048 ± 0.002 vs. 0.047 ± 0.003%/h; P = 0.877), respectively. Hot-water immersion during recovery from resistance-type exercise does not increase the postprandial rise in myofibrillar protein synthesis rates. In addition, postexercise hot-water immersion does not increase the capacity of the muscle to incorporate dietary protein-derived amino acids in muscle tissue protein during subsequent recovery

Ingestion of an ample amount of meat substitute based on a lysine-enriched,plant-based protein blend stimulates postprandial muscle proteinsynthesis to a similar extent as an isonitrogenous amount of chickenin healthy, young men

Plant-based proteins are considered to be less effective in their capacity to stimulate muscle protein synthesis when compared with animal-based protein sources, likely due to differences in amino acid contents. We compared the postprandial muscle protein synthetic response following the ingestion of a lysine-enriched plant-based protein product with an isonitrogenous amount of chicken. Twenty-four men (age 24 ± 5 years; BMI 22·9 ± 2·6 kg·m−2) participated in this parallel, double-blind, randomised controlled trial and consumed 40 g of protein as a lysine-enriched wheat and chickpea protein product (Plant, n 12) or chicken breast fillet (Chicken, n 12). Primed, continuous intravenous L-(ring-13C6)-phenylalanine infusions were applied while repeated blood and muscle samples were collected over a 5-h postprandial period to assess plasma amino acid responses, muscle protein synthesis rates and muscle anabolic signalling responses. Postprandial plasma leucine and essential amino acid concentrations were higher following Chicken (P < 0·001), while plasma lysine concentrations were higher throughout in Plant (P < 0·001). Total plasma amino acid concentrations did not differ between interventions (P = 0·181). Ingestion of both Plant and Chicken increased muscle protein synthesis rates from post-absorptive: 0·031 ± 0·011 and 0·031 ± 0·013 to postprandial: 0·046 ± 0·010 and 0·055 ± 0·015 % h−1, respectively (P-time < 0·001), with no differences between Plant and Chicken (time x treatment P = 0·068). Ingestion of 40 g of protein in the form of a lysine-enriched plant-based protein product increases muscle protein synthesis rates to a similar extent as an isonitrogenous amount of chicken in healthy, young men. Plant-based protein products sold as meat replacers may be as effective as animal-based protein sources to stimulate postprandial muscle protein synthesis rates in healthy, young individuals

Impact of protein coingestion on muscle protein synthesis during continuous endurance type exercise

This study investigates the impact of protein coingestion with carbohydrate on muscle protein synthesis during endurance type exercise. Twelve healthy male cyclists were studied during 2 h of fasted rest followed by 2 h of continuous cycling at 55% Wmax. During exercise, subjects received either 1.0 g·kg−1·h−1 carbohydrate ( CHO ) or 0.8 g·kg−1·h−1 carbohydrate with 0.2 g·kg−1·h−1 protein hydrolysate ( CHO+PRO ). Continuous intravenous infusions with l-[ring-13C6]phenylalanine and l-[ring-2H2]tyrosine were applied, and blood and muscle biopsies were collected to assess whole body protein turnover and muscle protein synthesis rates at rest and during exercise conditions. Protein coingestion stimulated whole body protein synthesis and oxidation rates during exercise by 22 ± 3 and 70 ± 17%, respectively ( P < 0.01 ). Whole body protein breakdown rates did not differ between experiments. As a consequence, whole body net protein balance was slightly negative in CHO and positive in the CHO+PRO treatment ( −4.9 ± 0.3 vs. 8.0 ± 0.3 μmol Phe·kg−1·h−1, respectively, P < 0.01 ). Mixed muscle protein fractional synthetic rates ( FSR ) were higher during exercise compared with resting conditions ( 0.058 ± 0.006 vs. 0.035 ± 0.006%/h in CHO and 0.070 ± 0.011 vs. 0.038 ± 0.005%/h in the CHO+PRO treatment, respectively, P < 0.05 ). FSR during exercise did not differ between experiments ( P = 0.46 ). We conclude that muscle protein synthesis is stimulated during continuous endurance type exercise activities when carbohydrate with or without protein is ingested. Protein coingestion does not further increase muscle protein synthesis rates during continuous endurance type exercise

Increase in S6K1 phosphorylation in human skeletal muscle following resistance exercise occurs mainly in type II muscle fibres

To investigate the in vivo effects of resistance exercise on translational control in human skeletal muscle, we determined the phosphorylation of AMP-activated kinase (AMPK), eukaryotic initiation factor 4E-binding protein (4E-BP1), p70/p85-S6 protein kinase (S6K1), and ribosomal S6 protein (S6). Furthermore, we investigated whether changes in the phosphorylation of S6K1 are muscle fiber type specific. Eight male subjects performed a single high-intensity resistance exercise session. Muscle biopsies were collected before and immediately after exercise and after 30 and 120 min of postexercise recovery. The phosphorylation statuses of AMPK, 4E-BP1, S6K1, and S6 were determined by Western blotting with phospho-specific and pan antibodies. To determine fiber type-specific changes in the phosphorylation status of S6K1, immunofluorescence microscopy was applied. AMPK phosphorylation was increased approximately threefold immediately after resistance exercise, whereas 4E-BP1 phosphorylation was reduced to 27 &plusmn; 6% of preexercise values. Phosphorylation of S6K1 at Thr421/Ser424 was increased 2- to 2.5-fold during recovery but did not induce a significant change in S6 phosphorylation. Phosphorylation of S6K1 was more pronounced in the type II vs. type I muscle fibers. Before exercise, phosphorylated S6K1 was predominantly located in the nuclei. After 2 h of postexercise recovery, phospho-S6K1 was primarily located in the cytosol of type II muscle fibers. We conclude that resistance exercise effectively increases the phosphorylation of S6K1 on Thr421/Ser424, which is not associated with a substantial increase in S6 phosphorylation in a fasted state.<br /

Amino acid absorption and subsequent muscle protein accretion following graded intakes of whey protein in elderly men

Whey protein ingestion has been shown to effectively stimulate postprandial muscle protein accretion in older adults. However, the impact of the amount of whey protein ingested on protein digestion and absorption kinetics, whole body protein balance, and postprandial muscle protein accretion remains to be established. We aimed to fill this gap by including 33 healthy, older men ( 73 ± 2 yr ) who were randomly assigned to ingest 10, 20, or 35 g of intrinsically l-[1-13C]phenylalanine-labeled whey protein ( n = 11/treatment ). Ingestion of labeled whey protein was combined with continuous intravenous l-[ring-2H5]phenylalanine and l-[ring-2H2]tyrosine infusion to assess the metabolic fate of whey protein-derived amino acids. Dietary protein digestion and absorption rapidly increased following ingestion of 10, 20, and 35 g whey protein, with the lowest and highest ( peak ) values observed following 10 and 35 g, respectively ( P < 0.05 ). Whole body net protein balance was positive in all groups ( 19 ± 1, 37 ± 2, and 58 ± 2 μmol/kg ), with the lowest and highest values observed following ingestion of 10 and 35 g, respectively ( P < 0.05 ). Postprandial muscle protein accretion, assessed by l-[1-13C]phenylalanine incorporation in muscle protein, was higher following ingestion of 35 g when compared with 10 ( P < 0.01 ) or 20 ( P < 0.05 ) g. We conclude that ingestion of 35 g whey protein results in greater amino acid absorption and subsequent stimulation of de novo muscle protein synthesis compared with the ingestion of 10 or 20 g whey protein in healthy, older men

A single session of neuromuscular electrical stimulation does not augment postprandial muscle protein accretion

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 ). 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

臺灣北部沿海工業區環境影響評估

Aims: Exercise combined with adipose tissue lipolytic inhibition augments intramuscular lipid and glycogen use in type 2 diabetes patients. The present study investigates the impact of adipose tissue lipolytic inhibition during exercise on subsequent postprandial glycemic control in type 2 diabetes patients. Methods: Fourteen male type 2 diabetes patients (age 65 ± 2 years, HbA1c 6.7 ± 0.1% (50 ± 2 mmol/mol)) participated in a double-blind placebo-controlled randomized cross-over study in which subjects performed endurance-type exercise after being administered 250 mg of a nicotinic acid analogue (acipimox; ACP) or a placebo (PLA). A control experiment was included in which no exercise was performed (CON). Results: Sixty minutes of endurance-type exercise (at 45% Wpeak) did not significantly lower circulating plasma glucose and insulin excursions in PLA when compared with CON (P = .300). Acipimox administration strongly reduced circulating plasma FFA concentrations during exercise (P < .001). Circulating plasma glucose and insulin excursions were substantially lower during 7.5 h of recovery from exercise (i.e. postprandial) in ACP when compared with either CON (P = .041 and P = .002, respectively) or PLA (P = .009 and P = .001, respectively). Conclusions: Collectively, exercise with adipose tissue lipolytic inhibition reduces postprandial blood glucose and insulin excursions and, as such, further improves glycemic control in male type 2 diabetes patients