Naomi M. Cermak

Protein supplementation augments the adaptive response of skeletal muscle to resistance-type exercise training: a meta-analysis

BACKGROUND Protein ingestion after a single bout of resistance-type exercise stimulates net muscle protein accretion during acute postexercise recovery. Consequently, it is generally accepted that protein supplementation is required to maximize the adaptive response of the skeletal muscle to prolonged resistance-type exercise training. However, there is much discrepancy in the literature regarding the proposed benefits of protein supplementation during prolonged resistance-type exercise training in younger and older populations. OBJECTIVE The objective of the study was to define the efficacy of protein supplementation to augment the adaptive response of the skeletal muscle to prolonged resistance-type exercise training in younger and older populations. DESIGN A systematic review of interventional evidence was performed through the use of a random-effects meta-analysis model. Data from the outcome variables fat-free mass (FFM), fat mass, type I and II muscle fiber cross-sectional area, and 1 repetition maximum (1-RM) leg press strength were collected from randomized controlled trials (RCTs) investigating the effect of dietary protein supplementation during prolonged (>6 wk) resistance-type exercise training. RESULTS Data were included from 22 RCTs that included 680 subjects. Protein supplementation showed a positive effect for FFM (weighted mean difference: 0.69 kg; 95% CI: 0.47, 0.91 kg; P < 0.00001) and 1-RM leg press strength (weighted mean difference: 13.5 kg; 95% CI: 6.4, 20.7 kg; P < 0.005) compared with a placebo after prolonged resistance-type exercise training in younger and older subjects. CONCLUSION Protein supplementation increases muscle mass and strength gains during prolonged resistance-type exercise training in both younger and older subjects.

Acute endurance exercise increases the nuclear abundance of PGC-1α in trained human skeletal muscle

Peroxisome proliferator-activated receptor gamma coactivator (PGC-1alpha) is a transcriptional coactivator that plays a key role in coordinating mitochondrial biogenesis. Recent evidence has linked p38 MAPK and AMPK with activation of PGC-1alpha. It was recently shown in rodent skeletal muscle that acute endurance exercise causes a shift in the subcellular localization of PGC-1alpha from the cytosol to the nucleus, allowing PGC-1alpha to coactivate transcription factors and increase mitochondrial gene expression, but human data are limited and equivocal in this regard. Our purpose was to examine p38 MAPK and AMPK activation, and PGC-1alpha protein content in whole muscle, cytosolic, and nuclear fractions of human skeletal muscle following an acute bout of endurance exercise. Eight trained men (29 +/- 3 yr; Vo(2peak) = 55 +/- 2 ml.kg(-1).min(-1)) cycled for 90 min at approximately 65% of Vo(2peak) and needle biopsy samples (vastus lateralis) were obtained before and immediately after exercise. At rest, the majority of PGC-1alpha was detected in cytosolic compared with the nuclear fractions. In response to exercise, nuclear PGC-1alpha protein increased by 54% (P < 0.05), yet whole muscle PGC-1alpha protein was unchanged compared with rest. Whole muscle and cytosolic p38 MAPK phosphorylation increased several-fold immediately after exercise compared with rest (P < 0.05). Acetyl CoA carboxylase (ACC) phosphorylation, a marker of AMPK activation, was increased by approximately 5-fold in cytosolic fractions following exercise (P < 0.05). These data provide evidence that, in human skeletal muscle, activation of cytosolic p38 MAPK and AMPK may be potential signals that lead to increased nuclear abundance and activation of PGC-1alpha in response to an acute bout of endurance exercise.

Eccentric exercise increases satellite cell content in type II muscle fibers.

INTRODUCTION Satellite cells (SCs) are of key importance in skeletal muscle tissue growth, repair, and regeneration. A single bout of high-force eccentric exercise has been demonstrated to increase mixed muscle SC content after 1-7 d of postexercise recovery. However, little is known about fiber type-specific changes in SC content and their activation status within 24 h of postexercise recovery. METHODS Nine recreationally active young men (23 ± 1 yr) performed 300 eccentric actions of the knee extensors on an isokinetic dynamometer. Skeletal muscle biopsies from the vastus lateralis were collected preexercise and 24 h postexercise. Muscle fiber type-specific SC content and the number of activated SCs were determined by immunohistochemical analyses. RESULTS There was no difference between Type I and Type II muscle fiber SC content before exercise. SC content significantly increased 24 h postexercise in Type II muscle fibers (from 0.085 ± 0.012 to 0.133 ± 0.016 SCs per fiber, respectively; P < 0.05), whereas there was no change in Type I fibers. In accordance, activation status increased from preexercise to 24 h postexercise as demonstrated by the increase in the number of DLK1+ SCs in Type II muscle fibers (from 0.027 ± 0.008 to 0.070 ± 0.017 SCs per muscle fiber P < 0.05). Although no significant changes were observed in the number of Ki-67+ SCs, we did observe an increase in the number of proliferating cell nuclear antigen-positive SCs after 24 h of postexercise recovery. CONCLUSION A single bout of high-force eccentric exercise increases muscle fiber SC content and activation status in Type II but not Type I muscle fibers.

Intermittent and continuous high‐intensity exercise training induce similar acute but different chronic muscle adaptations

What is the central question of this study? How important is the interval in high‐intensity interval training (HIIT)? What is the main finding and its importance? The intermittent nature of HIIT is important for maximizing skeletal muscle adaptations to this type of exercise, at least when a relatively small total volume of work is performed in an ‘all‐out’ manner. The protein signalling responses to an acute bout of HIIT were generally not predictive of training‐induced outcomes. Nonetheless, a single session of exercise lasting <10 min including warm‐up, performed three times per week for 6 weeks, was sufficient to improve maximal aerobic capacity.

Diffusion tensor MRI to assess skeletal muscle disruption following eccentric exercise

Introduction: Structural evidence of exercise‐induced muscle disruption has traditionally involved histological analysis of muscle tissue obtained by needle biopsy, however, there are multiple limitations with this technique. Recently, diffusion tensor magnetic resonance imaging (DT‐MRI) has been successfully demonstrated to noninvasively assess skeletal muscle abnormalities induced by traumatic injury. Methods: To determine the potential for DT‐MRI to detect musculoskeletal changes after a bout of eccentric exercise, 10 healthy men performed 300 eccentric actions on an isokinetic dynamometer. DT‐MRI measurements and muscle biopsies from the vastus lateralis were obtained before and 24 h post‐exercise. Results: Z‐band streaming was higher 24 h post‐exercise compared with baseline (P < 0.05). The histological indices of damage coincided with changes in DT‐MRI parameters of fractional anisotropy (FA) and apparent diffusion coefficient; reflecting altered skeletal muscle geometry (P < 0.05). Z‐band streaming quantified per fiber correlated with FA (r = −0.512; P < 0.05). Conclusions: DT‐MRI can detect changes in human skeletal muscle structure following eccentric exercise. Muscle Nerve 46: 42–50, 2012

Muscle metabolism during exercise with carbohydrate or protein-carbohydrate ingestion.

INTRODUCTION Ingesting protein (PRO) with CHO during prolonged exercise is purported to improve performance compared with CHO alone by altering the regulation of skeletal muscle energy provision. However, no study has directly investigated this issue. We tested the hypothesis that compared with CHO alone, coingestion of PRO would alter markers of metabolic control, including the magnitude of glycogen use and the net expansion of the tricarboxylic acid cycle intermediate pool, which has been linked to the capacity for oxidative energy delivery. METHODS Eight trained men (mean +/- SE: age = 29 +/- 2 yr; VO2peak = 55 +/- 2 mL x kg(-1) x min(-1)) cycled at 69% +/- 1% VO2peak for 90 min on two occasions, and biopsy samples (vastus lateralis) were obtained before and after exercise. In a randomized, double-blind manner, subjects ingested one of two drinks during exercise that contained either 6% CHO or 6% CHO + 2% PRO (CHO + PRO) at a rate of 1 L x h(-1) to deliver 60 g x h(-1) CHO +/- 20 g x h(-1) PRO. RESULTS CHO + PRO ingestion increased the plasma concentration of branched chain (561 +/- 46 vs 301 +/- 32 micromol x L(-1)) and essential amino acids (1071 +/- 98 vs 670 +/- 71 micromol x L(-1)) after exercise versus CHO (both P values <or=0.05). However, net muscle glycogen use (CHO + PRO = 223 +/- 31 vs CHO = 185 +/- 38 mmol x kg(-1) dry weight) and tricarboxylic acid cycle intermediate expansion (CHO + PRO = 2.3 +/- 0.7 vs CHO = 2.1 +/- 0.2 mmol x kg(-1) dry weight) were similar between trials. Blood creatine kinase activity and 20-km time trial performance measured approximately 24 h after the first exercise bout were not different between treatments. CONCLUSION When trained men ingest CHO at a rate on the upper end of the range generally recommended to improve endurance performance, coingestion of PRO does not alter specific markers proposed to reflect an enhanced capacity for skeletal muscle energy delivery.

Dietary Protein Considerations to Support Active Aging

Given our rapidly aging world-wide population, the loss of skeletal muscle mass with healthy aging (sarcopenia) represents an important societal and public health concern. Maintaining or adopting an active lifestyle alleviates age-related muscle loss to a certain extent. Over time, even small losses of muscle tissue can hinder the ability to maintain an active lifestyle and, as such, contribute to the development of frailty and metabolic disease. Considerable research focus has addressed the application of dietary protein supplementation to support exercise-induced gains in muscle mass in younger individuals. In contrast, the role of dietary protein in supporting the maintenance (or gain) of skeletal muscle mass in active older persons has received less attention. Older individuals display a blunted muscle protein synthetic response to dietary protein ingestion. However, this reduced anabolic response can largely be overcome when physical activity is performed in close temporal proximity to protein consumption. Moreover, recent evidence has helped elucidate the optimal type and amount of dietary protein that should be ingested by the older adult throughout the day in order to maximize the skeletal muscle adaptive response to physical activity. Evidence demonstrates that when these principles are adhered to, muscle maintenance or hypertrophy over prolonged periods can be further augmented in active older persons. The present review outlines the current understanding of the role that dietary protein occupies in the lifestyle of active older adults as a means to increase skeletal muscle mass, strength and function, and thus support healthier aging.

Ingestion of glucose or sucrose prevents liver but not muscle glycogen depletion during prolonged endurance-type exercise in trained cyclists

The purpose of this study was to define the effect of glucose ingestion compared with sucrose ingestion on liver and muscle glycogen depletion during prolonged endurance-type exercise. Fourteen cyclists completed two 3-h bouts of cycling at 50% of peak power output while ingesting either glucose or sucrose at a rate of 1.7 g/min (102 g/h). Four cyclists performed an additional third test for reference in which only water was consumed. We employed (13)C magnetic resonance spectroscopy to determine liver and muscle glycogen concentrations before and after exercise. Expired breath was sampled during exercise to estimate whole body substrate use. After glucose and sucrose ingestion, liver glycogen levels did not show a significant decline after exercise (from 325 ± 168 to 345 ± 205 and 321 ± 177 to 348 ± 170 mmol/l, respectively; P > 0.05), with no differences between treatments. Muscle glycogen concentrations declined (from 101 ± 49 to 60 ± 34 and 114 ± 48 to 67 ± 34 mmol/l, respectively; P < 0.05), with no differences between treatments. Whole body carbohydrate utilization was greater with sucrose (2.03 ± 0.43 g/min) vs. glucose (1.66 ± 0.36 g/min; P < 0.05) ingestion. Both liver (from 454 ± 33 to 283 ± 82 mmol/l; P < 0.05) and muscle (from 111 ± 46 to 67 ± 31 mmol/l; P < 0.01) glycogen concentrations declined during exercise when only water was ingested. Both glucose and sucrose ingestion prevent liver glycogen depletion during prolonged endurance-type exercise. Sucrose ingestion does not preserve liver glycogen concentrations more than glucose ingestion. However, sucrose ingestion does increase whole body carbohydrate utilization compared with glucose ingestion. This trial was registered at https://www.clinicaltrials.gov as NCT02110836.

The use of doubly labeled milk protein to measure postprandial muscle protein synthesis rates in vivo in humans

We aimed to determine the impact of precursor pool dilution on the assessment of postprandial myofibrillar protein synthesis rates (MPS). A Holstein dairy cow was infused with large amounts of L-[1-(13)C]phenylalanine and L-[1-(13)C]leucine, and the milk was collected and fractionated. The enrichment levels in the casein were 38.7 and 9.3 mole percent excess, respectively. In a subsequent human experiment, 11 older men (age: 71 ± 1 y, body mass index: 26 ± 0.1 kg·m(-2)) received a primed constant infusion of L-[ring-(2)H5]phenylalanine and L-[1-(13)C]leucine. Blood and muscle samples were collected before and after the ingestion of 20-g doubly labeled casein to assess postprandial MPS based on the 1) constant tracer infusion of L-[ring-(2)H5]phenylalanine, 2) ingestion of intrinsically L-[1-(13)C]phenylalanine-labeled casein, and 3) constant infusion of L-[1-(13)C]leucine in combination with the ingestion of intrinsically L-[1-(13)C]leucine-labeled casein. Postprandial MPS was increased (P < 0.05) after protein ingestion (∼70% above postabsorptive values) based on the L-[1-(13)C]leucine tracer. There was no significant stimulation of postprandial MPS (∼27% above postabsorptive values) when the calculated fractional synthesis rate was based on the L-[ring-(2)H5]phenylalanine (P = 0.2). Comparisons of postprandial MPS based on the primed continuous infusion of L-[1-(13)C]leucine or the ingestion of intrinsically L-[1-(13)C]phenylalanine-labeled casein protein demonstrated differences compared with the primed continuous infusion of L-[ring-(2)H5]phenylalanine (P > 0.05). Our findings confirm that the postprandial MPS assessed using the primed continuous tracer infusion approach may differ if tracer steady-state conditions in the precursor pools are perturbed. The use of intrinsically doubly labeled protein provides a method to study the metabolic fate of the ingested protein and the subsequent postprandial MPS response.

A single dose of sodium nitrate does not improve oral glucose tolerance in patients with type 2 diabetes mellitus

Dietary nitrate (NO3(-)) supplementation has been proposed as an emerging treatment strategy for type 2 diabetes. We hypothesized that ingestion of a single bolus of dietary NO3(-) ingestion improves oral glucose tolerance in patients with type 2 diabetes. Seventeen men with type 2 diabetes (glycated hemoglobin, 7.3% ± 0.2%) participated in a randomized crossover experiment. The subjects ingested a glucose beverage 2.5 hours after consumption of either sodium NO3(-) (0.15 mmol NaNO3(-) · kg(-1)) or a placebo solution. Venous blood samples were collected before ingestion of the glucose beverage and every 30 minutes thereafter during a 2-hour period to assess postprandial plasma glucose and insulin concentrations. The results show that plasma NO3(-) and nitrite levels were increased after NaNO3(-) as opposed to placebo ingestion (treatment-effect, P = .001). Despite the elevated plasma NO3(-) and nitrite levels, ingestion of NaNO3(-) did not attenuate the postprandial rise in plasma glucose and insulin concentrations (time × treatment interaction, P = .41 for glucose, P = .93 for insulin). Despite the lack of effect on oral glucose tolerance, basal plasma glucose concentrations measured 2.5 hours after NaNO3(-) ingestion were lower when compared with the placebo treatment (7.5 ± 0.4 vs 8.3 ± 0.4 mmol/L, respectively; P = .04). We conclude that ingestion of a single dose of dietary NO3(-) does not improve subsequent oral glucose tolerance in patients with type 2 diabetes.