Meteorin-like is a hormone that regulates immune-adipose interactions to increase beige fat thermogenesis.

Exercise training benefits many organ systems and offers protection against metabolic disorders such as obesity and diabetes. Using the recently identified isoform of PGC1-α (PGC1-α4) as a discovery tool, we report the identification of meteorin-like (Metrnl), a circulating factor that is induced in muscle after exercise and in adipose tissue upon cold exposure. Increasing circulating levels of Metrnl stimulates energy expenditure and improves glucose tolerance and the expression of genes associated with beige fat thermogenesis and anti-inflammatory cytokines. Metrnl stimulates an eosinophil-dependent increase in IL-4 expression and promotes alternative activation of adipose tissue macrophages, which are required for the increased expression of the thermogenic and anti-inflammatory gene programs in fat. Importantly, blocking Metrnl actions in vivo significantly attenuates chronic cold-exposure-induced alternative macrophage activation and thermogenic gene responses. Thus, Metrnl links host-adaptive responses to the regulation of energy homeostasis and tissue inflammation and has therapeutic potential for metabolic and inflammatory diseases.

The Acute and Chronic influence of Exercise on Mitochondrial Dynamics in Skeletal Muscle.

Exercise and nutritional modulation are potent stimuli for eliciting increases in mitochondrial mass and function. Collectively, these beneficial adaptations are increasingly recognized to coincide with improvements to skeletal muscle health. Mitochondrial dynamics of fission and fusion are increasingly implicated as having a central role in mediating aspects of key organelle adaptions that are seen with exercise. Exercise-induced mitochondrial adaptations that dynamics have been implicated in are: 1) Increases to mitochondrial turnover, resulting from elevated rates of mitochondrial synthesis (biogenesis) and degradative (mitophagy) processes. 2) Morphological changes to the 3D tubular network, known as the mitochondrial reticulum, that mitochondria form in skeletal muscle. Notably, mitochondrial fission has also been implicated in coordinating increases in mitophagy, following acute exercise. Further, increased fusion following exercise training promotes increased connectivity of the mitochondrial reticulum and is associated with improved metabolism and mitochondrial function. However, the molecular basis and fashion in which exercise infers beneficial mitochondrial adaptations through mitochondrial dynamics remains poorly understood. This review attempts to highlight recent developments investigating the effects of exercise on mitochondrial dynamics, while attempting to offer a perspective of the methodological refinements and potential variables, such as substrate/glycogen availability, which should be considered going forward.

A single bout of strenuous exercise overcomes lipid-induced anabolic resistance to protein ingestion in overweight, middle-aged men.

High-circulating lipid availability attenuates protein feeding-induced muscle protein synthesis (MPS). Whether the combined effects of exercise and protein ingestion can rescue this inhibition is unknown. In a parallel-groups design, middle-aged sedentary males (n = 28) matched for fat-free mass and body mass index received a 5-h intravenous infusion of either saline/control (n = 9), 20% intralipid infusion (n = 9), or intralipid with concomitant exercise (n = 10). Two hours into each of these infusions, participants received a primed constant infusion of L-(ring-[13C]6)-phenylalanine. Muscle biopsies were taken immediately after control and lipid infusions, at which time, a 30-g protein beverage was ingested. Further biopsies were taken 2 and 4 h after protein ingestion. Intralipid increased plasma free fatty acid concentrations from ∼0.4-2 mM, resulting in an attenuated MPS response to protein ingestion, which was prevented by exercise. Intralipid resulted in a lower peak aminoacidemia following protein ingestion that was exacerbated by prior exercise, suggesting efficiency of the working skeletal muscle to utilize amino acid substrate to drive the postprandial anabolic response. We conclude that in the face of high-fat availability, exercise preserves the sensitivity of skeletal muscle to the anabolic properties of amino acids.-Smiles, W. J., Churchward-Venne, T. A., van Loon, L. J. C., Hawley, J. A., Camera, D. M. A single bout of strenuous exercise overcomes lipid-induced anabolic resistance to protein ingestion in overweight, middle-aged men.

Divergent Regulation of Myotube Formation and Gene Expression by E2 and EPA during In-Vitro Differentiation of C2C12 Myoblasts.

Estrogen (E2) and polyunsaturated fatty acids (n-3PUFA) supplements independently support general wellbeing and enhance muscle regeneration in-vivo and myotube formation in-vitro. However, the combined effect of E2 and n-3PUFA on myoblast differentiation is not known. The purpose of the study was to identify whether E2 and n-3PUFA possess a synergistic effect on in-vitro myogenesis. Mouse C2C12 myoblasts, a reliable model to reiterate myogenic events in-vitro, were treated with 10nM E2 and 50µM eicosapentaenoic acid (EPA) independently or combined, for 0-24 h or 0-120 h during differentiation. Immunofluorescence, targeted qPCR and next generation sequencing (NGS) were used to characterize morphological changes and differential expression of key genes involved in the regulation of myogenesis and muscle function pathways. E2 increased estrogen receptor α (Erα) and the expression of the mitogen-activated protein kinase 11 (Mapk11) within 1 h of treatment and improved myoblast differentiation and myotube formation. A significant reduction (p < 0.001) in myotube formation and in the expression of myogenic regulatory factors Mrfs (MyoD, Myog and Myh1) and the myoblast fusion related gene, Tmem8c, was observed in the presence of EPA and the combined E2/EPA treatment. Additionally, EPA treatment at 48 h of differentiation inhibited the majority of genes associated with the myogenic and striated muscle contraction pathways. In conclusion, EPA and E2 had no synergistic effect on myotube formation in-vitro. Independently, EPA inhibited myoblast differentiation and overrides the stimulatory effect of E2 when used in combination with E2.

Dynamic proteome profiling of individual proteins in human skeletal muscle after a high-fat diet and resistance exercise.

It is generally accepted that muscle adaptation to resistance exercise (REX) training is underpinned by contraction-induced, increased rates of protein synthesis and dietary protein availability. By using dynamic proteome profiling (DPP), we investigated the contribution of both synthesis and breakdown to changes in abundance on a protein-by-protein basis in human skeletal muscle. Age-matched, overweight males consumed 9 d of a high-fat, low-carbohydrate diet during which time they either undertook 3 sessions of REX or performed no exercise. Precursor enrichment and the rate of incorporation of deuterium oxide into newly synthesized muscle proteins were determined by mass spectrometry. Ninety proteins were included in the DPP, with 28 proteins exhibiting significant responses to REX. The most common pattern of response was an increase in turnover, followed by an increase in abundance with no detectable increase in protein synthesis. Here, we provide novel evidence that demonstrates that the contribution of synthesis and breakdown to changes in protein abundance induced by REX differ on a protein-by-protein basis. We also highlight the importance of the degradation of individual muscle proteins after exercise in human skeletal muscle.-Camera, D. M., Burniston, J. G., Pogson, M. A., Smiles, W. J., Hawley, J. A. Dynamic proteome profiling of individual proteins in human skeletal muscle after a high-fat diet and resistance exercise.

Expression of microRNAs and target proteins in skeletal muscle of rats selectively bred for high and low running capacity.

Impairments in mitochondrial function and substrate metabolism are implicated in the etiology of obesity and Type 2 diabetes. MicroRNAs (miRNAs) can degrade mRNA or repress protein translation and have been implicated in the development of such disorders. We used a contrasting rat model system of selectively bred high- (HCR) or low- (LCR) intrinsic running capacity with established differences in metabolic health to investigate the molecular mechanisms through which miRNAs regulate target proteins mediating mitochondrial function and substrate oxidation processes. Quantification of select miRNAs using the rat miFinder miRNA PCR array revealed differential expression of 15 skeletal muscles (musculus tibialis anterior) miRNAs between HCR and LCR rats (14 with higher expression in LCR; P < 0.05). Ingenuity Pathway Analysis predicted these altered miRNAs to collectively target multiple proteins implicated in mitochondrial dysfunction and energy substrate metabolism. Total protein abundance of citrate synthase (CS; miR-19 target) and voltage-dependent anion channel 1 (miR-7a target) were higher in HCR compared with LCR cohorts (~57 and ~26%, respectively; P < 0.05). A negative correlation was observed for miR-19a-3p and CS (r = 0.32, P = 0.015) protein expression. To determine whether miR-19a-3p can regulate CS in vitro, we performed luciferase reporter and transfection assays in C2C12 myotubes. MiR-19a-3p binding to the CS untranslated region did not change luciferase reporter activity; however, miR-19a-3p transfection decreased CS protein expression (∼70%; P < 0.05). The differential miRNA expression targeting proteins implicated in mitochondrial dysfunction and energy substrate metabolism may contribute to the molecular basis, mediating the divergent metabolic health profiles of LCR and HCR rats.

Fenugreek increases insulin-stimulated creatine content in L6C11 muscle myotubes.

PURPOSE: Creatine uptake by muscle cells is increased in the presence of insulin. Accordingly, compounds with insulin-like actions may also augment creatine uptake. The aim of this study was to investigate whether Trigonella foenum-graecum (fenugreek), an insulin mimetic, increases total intracellular creatine levels in vitro. METHODS: Total cellular creatine content was measured fluorometrically in L6C11 muscle myotubes treated for 1, 4, and 24 h with 0.5 mM creatine (CR), CR and 20 µg/mL fenugreek seed extract (CR + FEN), CR and 100 nM insulin (CR + INS), and CR + INS + FEN (n = 6 per treatment group). Alterations in the expression of the sodium- and chloride-dependent creatine transporter, SLC6A8, and key signaling proteins in the PI3-K/Akt pathway were determined. RESULTS: Compared to control (CON), CR + INS + FEN increased total creatine content after 4 h (P < 0.05), whereas all conditions increased SLC6A8 protein expression above CON at this time (P < 0.05). Changes in insulin signaling were demonstrated via increases in AktThr308 phosphorylation, with CR + INS > CON and CR at 1 h (P < 0.05) and with CR + INS + FEN > CON, CR, and CR + INS at 4 h (P < 0.05). In contrast, no changes in PKCζ/λ or GLUT4 phosphorylation were detected. CONCLUSION: Fenugreek, when combined with insulin, modulates creatine content via a mechanism which is independent of the activity of SLC6A8, suggesting that an alternative mechanism is responsible for the regulation and facilitation of insulin-mediated creatine uptake in skeletal muscle cells.

Acute low-intensity cycling with blood-flow restriction has no effect on metabolic signaling in human skeletal muscle compared to traditional exercise.

PURPOSE: Autophagy is an intracellular degradative system sensitive to hypoxia and exercise-induced perturbations to cellular bioenergetics. We determined the effects of low-intensity endurance-based exercise performed with blood-flow restriction (BFR) on cell signaling adaptive responses regulating autophagy and substrate metabolism in human skeletal muscle. METHODS: In a randomized cross-over design, nine young, healthy but physically inactive males completed three experimental trials separated by 1 week of recovery consisting of either a resistance exercise bout (REX: 4 × 10 leg press repetitions, 70% 1-RM), endurance exercise (END: 30 min cycling, 70% VO2peak), or low-intensity cycling with BFR (15 min, 40% VO2peak). A resting muscle biopsy was obtained from the vastus lateralis 2 weeks prior to the first exercise trial and 3 h after each exercise bout. RESULTS: END increased ULK1Ser757 phosphorylation above rest and BFR (~37 to 51%, P < 0.05). Following REX, there were significant elevations compared to rest (~348%) and BFR (~973%) for p38γ MAPKThr180/Tyr182 phosphorylation (P < 0.05). Parkin content was lower following BFR cycling compared to REX (~20%, P < 0.05). There were no exercise-induced changes in select markers of autophagy following BFR. Genes implicated in substrate metabolism (HK2 and PDK4) were increased above rest (~143 to 338%) and BFR cycling (~212 to 517%) with END (P < 0.001). CONCLUSION: A single bout of low-intensity cycling with BFR is insufficient to induce intracellular "stress" responses (e.g., high rates of substrate turnover and local hypoxia) necessary to activate skeletal muscle autophagy signaling.

Protein coingestion with alcohol following strenuous exercise attenuates alcohol-induced intramyocellular apoptosis and inhibition of autophagy.

Alcohol ingestion decreases postexercise rates of muscle protein synthesis, but the mechanism(s) (e.g., increased protein breakdown) underlying this observation is unknown. Autophagy is an intracellular "recycling" system required for homeostatic substrate and organelle turnover; its dysregulation may provoke apoptosis and lead to muscle atrophy. We investigated the acute effects of alcohol ingestion on autophagic cell signaling responses to a bout of concurrent (combined resistance- and endurance-based) exercise. In a randomized crossover design, eight physically active males completed three experimental trials of concurrent exercise with either postexercise ingestion of alcohol and carbohydrate (12 ± 2 standard drinks; ALC-CHO), energy-matched alcohol and protein (ALC-PRO), or protein (PRO) only. Muscle biopsies were taken at rest and 2 and 8 h postexercise. Select autophagy-related gene (Atg) proteins decreased compared with rest with ALC-CHO (P < 0.05) but not ALC-PRO. There were parallel increases (P < 0.05) in p62 and PINK1 commensurate with a reduction in BNIP3 content, indicating a diminished capacity for mitochondria-specific autophagy (mitophagy) when alcohol and carbohydrate were coingested. DNA fragmentation increased in both alcohol conditions (P < 0.05); however, nuclear AIF accumulation preceded this apoptotic response with ALC-CHO only (P < 0.05). In contrast, increases in the nuclear content of p53, TFEB, and PGC-1α in ALC-PRO were accompanied by markers of mitochondrial biogenesis at the transcriptional (Tfam, SCO2, and NRF-1) and translational (COX-IV, ATPAF1, and VDAC1) level (P < 0.05). We conclude that alcohol ingestion following exercise triggers apoptosis, whereas the anabolic properties of protein coingestion may stimulate mitochondrial biogenesis to protect cellular homeostasis.

Effects of skeletal muscle energy availability on protein turnover responses to exercise.

Skeletal muscle adaptation to exercise training is a consequence of repeated contraction-induced increases in gene expression that lead to the accumulation of functional proteins whose role is to blunt the homeostatic perturbations generated by escalations in energetic demand and substrate turnover. The development of a specific 'exercise phenotype' is the result of new, augmented steady-state mRNA and protein levels that stem from the training stimulus (i.e. endurance or resistance based). Maintaining appropriate skeletal muscle integrity to meet the demands of training (i.e. increases in myofibrillar and/or mitochondrial protein) is regulated by cyclic phases of synthesis and breakdown, the rate and turnover largely determined by the protein's half-life. Cross-talk among several intracellular systems regulating protein synthesis, breakdown and folding is required to ensure protein equilibrium is maintained. These pathways include both proteasomal and lysosomal degradation systems (ubiquitin-mediated and autophagy, respectively) and the protein translational and folding machinery. The activities of these cellular pathways are bioenergetically expensive and are modified by intracellular energy availability (i.e. macronutrient intake) and the 'training impulse' (i.e. summation of the volume, intensity and frequency). As such, exercise-nutrient interactions can modulate signal transduction cascades that converge on these protein regulatory systems, especially in the early post-exercise recovery period. This review focuses on the regulation of muscle protein synthetic response-adaptation processes to divergent exercise stimuli and how intracellular energy availability interacts with contractile activity to impact on muscle remodelling.

Modulation of autophagy signaling with resistance exercise and protein ingestion following short-term energy deficit.

Autophagy contributes to remodeling of skeletal muscle and is sensitive to contractile activity and prevailing energy availability. We investigated changes in targeted genes and proteins with roles in autophagy following 5 days of energy balance (EB), energy deficit (ED), and resistance exercise (REX) after ED. Muscle biopsies from 15 subjects (8 males, 7 females) were taken at rest following 5 days of EB [45 kcal·kg fat free mass (FFM)(-1)·day(-1)] and 5 days of ED (30 kcal·kg FFM(-1)·day(-1)). After ED, subjects completed a bout of REX and consumed either placebo (PLA) or 30 g whey protein (PRO) immediately postexercise. Muscle biopsies were obtained at 1 and 4 h into recovery in each trial. Resting protein levels of autophagy-related gene protein 5 (Atg5) decreased after ED compared with EB (∼23%, P < 0.001) and remained below EB from 1 to 4 h postexercise in PLA (∼17%) and at 1 h in PRO (∼18%, P < 0.05). In addition, conjugated Atg5 (cAtg12) decreased below EB in PLA at 4 h (∼20, P < 0.05); however, its values were increased above this time point in PRO at 4 h alongside increases in FOXO1 above EB (∼22-26%, P < 0.05). Notably, these changes were subsequent to increases in unc-51-like kinase 1(Ser757) phosphorylation (∼60%) 1 h postexercise in PRO. No significant changes in gene expression of selected autophagy markers were found, but EGR-1 increased above ED and EB in PLA (∼417-864%) and PRO (∼1,417-2,731%) trials 1 h postexercise (P < 0.001). Postexercise protein availability, compared with placebo, can selectively promote autophagic responses to REX in ED.

Resistance exercise with low glycogen increases p53 phosphorylation and PGC-1α mRNA in skeletal muscle.

PURPOSE: We determined the effect of reduced muscle glycogen availability on cellular pathways regulating mitochondrial biogenesis and substrate utilization after a bout of resistance exercise. METHODS: Eight young, recreationally trained men undertook a glycogen depletion protocol of one-leg cycling to fatigue (LOW), while the contralateral (control) leg rested (CONT). Following an overnight fast, subjects completed 8 sets of 5 unilateral leg press repetitions (REX) at 80 % 1 Repetition Maximum (1RM) on each leg. Subjects consumed 500 mL protein/CHO beverage (20 g whey + 40 g maltodextrin) upon completion of REX and 2 h later. Muscle biopsies were obtained at rest and 1 and 4 h after REX in both legs. RESULTS: Resting muscle glycogen was higher in the CONT than LOW leg (~384 ± 114 vs 184 ± 36 mmol kg(-1) dry wt; P < 0.05), and 1 h and 4 h post-exercise (P < 0.05). Phosphorylation of p53(Ser15) increased 1 h post-exercise in LOW (~115 %, P < 0.05) and was higher than CONT at this time point (~87 %, P < 0.05). p38MAPK(Thr180/Tyr182) phosphorylation increased 1 h post-exercise in both CONT and LOW (~800-900 %; P < 0.05) but remained above rest at 4 h only in CONT (~585 %, P < 0.05; different between legs P < 0.05). Peroxisome proliferator-activated receptor gamma coactivator-1α (PGC-1α) mRNA was elevated 4 h post-exercise in LOW (~200 %, P < 0.05; different between legs P < 0.05). There were no changes in Fibronectin type III domain-containing protein 5 (FNDC5) mRNA for CONT or LOW legs post-exercise. CONCLUSION: Undertaking resistance exercise with low glycogen availability may enhance mitochondrial-related adaptations through p53 and PGC-1α-mediated signalling.

Reduced resting skeletal muscle protein synthesis is rescued by resistance exercise and protein ingestion following short-term energy deficit.

The myofibrillar protein synthesis (MPS) response to resistance exercise (REX) and protein ingestion during energy deficit (ED) is unknown. In young men (n = 8) and women (n = 7), we determined protein signaling and resting postabsorptive MPS during energy balance [EB; 45 kcal·kg fat-free mass (FFM)(-1)·day(-1)] and after 5 days of ED (30 kcal·kg FFM(-1)·day(-1)) as well as MPS while in ED after acute REX in the fasted state and with the ingestion of whey protein (15 and 30 g). Postabsorptive rates of MPS were 27% lower in ED than EB (P < 0.001), but REX stimulated MPS to rates equal to EB. Ingestion of 15 and 30 g of protein after REX in ED increased MPS ~16 and ~34% above resting EB (P < 0.02). p70 S6K Thr(389) phosphorylation increased above EB only with combined exercise and protein intake (~2-7 fold, P < 0.05). In conclusion, short-term ED reduces postabsorptive MPS; however, a bout of REX in ED restores MPS to values observed at rest in EB. The ingestion of protein after REX further increases MPS above resting EB in a dose-dependent manner. We conclude that combining REX with increased protein availability after exercise enhances rates of skeletal muscle protein synthesis during short-term ED and could in the long term preserve muscle mass.

High-Protein Diets during either Resistance or Concurrent Training Have No Detrimental Effect on Bone Parameters in Resistance-Trained Males.

BACKGROUND: The effects of combining resistance training (RT) and concurrent training (CT; resistance + endurance training) with varied protein doses on bone measures remain poorly understood. Hence, we conducted a comparison of the impacts of two high-protein diets (1.6 or 3.2 g kg-1 d-1) over 16 weeks in resistance-trained males, either with CT or RT alone. METHODS: A total of forty-eight males, all of whom were resistance-trained, had the following demographics: 26.6 ± 6 years, body mass index: 25.6 ± 2.9 kg m-2 administered either 3.2 g kg-1 d-1 protein (CT2; n = 12; RT2; n = 12) or 1.6 g kg-1 d-1 protein (CT1; n = 12; RT1; n = 12) during 16 weeks (four sessions·w-1). Bone parameters were assessed pre- and post-intervention. RESULTS: There was no significant interaction between the intervention group and time for the legs, arms, ribs, or pelvis area BMC and BMD (p > 0.05). For the BMD of the pelvis and the BMC of the right ribs, however, there were significant time effects noted (p < 0.05). Furthermore, there was a significant interaction between the intervention group and time in the lumbar and thoracic spines, with a particular time effect noted for the thoracic spine region (p < 0.05). The regional differences in skeletal responses to the intervention are highlighted by these data. CONCLUSION: Our findings show that the intake of two high-protein diets combined with RT and CT during 16 weeks had no adverse effects on bone tissue parameters. While these findings indicate that protein intake between 2 and 3 times the current RDI does not promote bone demineralization when consumed in conjunction with exercise, future studies investigating the long-term effects of chronic high protein intake on bone tissue health are warranted.

Effects of exercise modality combined with moderate hypoxia on blood glucose regulation in adults with overweight.

Purpose: This study aimed to investigate the combined effects of moderate hypoxia with three different exercise modes on glucose regulation in healthy overweight adults. Methods: Thirteen overweight males (age: 31 ± 4 years; body fat 26.3 ± 3.2%) completed three exercise trials in a randomized crossover design involving 60 min cycling exercise at 90% lactate threshold (LOW), sprint interval training (20 × 4 s all-out; SIT) and lower limb functional bodyweight exercises (8 sets of 4 × 20 s; FEX) under moderate hypoxia (FiO2 = 16.5%). Post-exercise oral glucose tolerance test (OGTT) was performed following each trial. Heart rate, oxygen saturation (SpO2), physical activity enjoyment scale (PACES), and perceptual measures were recorded during each exercise session. Venous blood was collected pre-, immediately post-, and 24 h post-exercise and analysed for plasma glucose and insulin, incremental area under curve (iAUC), and circulating microRNA expression (c-miRs-486-5p, -126-5p, and -21-5p). Interstitial glucose concentrations were measured using continuous glucose monitoring (CGM). Results: Post-exercise OGTT iAUC for plasma glucose and insulin concentration were lower in SIT and LOW vs. control (p < 0.05) while post-exercise interstitial glucose iAUC and c-miRs were not different between exercise modes. Heart rate was greater in SIT vs. LOW and FEX, and FEX vs. LOW (p < 0.05), SpO2 was lower in SIT, while PACES was not different between exercise modes. Perceptual measures were greater in SIT vs. LOW and FEX. Conclusion: Acute SIT and LOW under moderate hypoxia improved post-exercise plasma insulin compared to FEX exercises. Considering SIT was also time-efficient, well tolerated, and enjoyable for participants, this may be the preferred exercise modality for improving glucose regulation in adult males with overweight when combined with moderate hypoxia.

Association between changes in lean mass, muscle strength, endurance, and power following resistance or concurrent training with differing high protein diets in resistance-trained young males.

Background: We assessed the relationship of changes in upper and lower body lean mass with muscle strength, endurance and power responses following two high protein diets (1.6 or 3.2 g.kg-1.d-1) during 16 weeks of either concurrent training (CT) or resistance training (RT) in resistance-trained young males. Methods: Forty-eight resistance-trained young males (age: 26 ± 6 yr., body mass index: 25.6 ± 2.9 kg.m-2) performed 16 weeks (four sessions·wk.-1) of CT or RT with either 1.6 g.kg-1.d-1 protein (CT + 1.6; n = 12; RT + 1.6; n = 12) or 3.2 g.kg-1.d-1 protein (CT + 3.2; n = 12; RT + 3.2; n = 12). Relationships between upper (left arm + right arm + trunk lean mass) and lower body (left leg + right leg lean mass) lean mass changes with changes in muscle performance were assessed using Pearson's correlation coefficients. Results: For upper body, non-significant weak positive relationships were observed between change in upper body lean mass and change in pull-up (r = 0.183, p = 0.234), absolute chest press strength (r = 0.159, p = 0.302), chest press endurance (r = 0.041, p = 0.792), and relative chest press strength (r = 0.097, p = 0.529) while non-significant weak negative relationships were observed for changes in absolute upper body power (r = -0.236, p = 0.123) and relative upper body power (r = -0.203, p = 0.185). For lower body, non-significant weak positive relationships were observed between the change in lower body lean mass with change in vertical jump (r = 0.145, p = 0.346), absolute lower body power (r = 0.109, p = 0.480), absolute leg press strength (r = 0.073, p = 0.638), leg press endurance (r < 0.001, p = 0.998), relative leg press strength (r = 0.089, p = 0.564), and relative lower body power (r = 0.150, p = 0.332). Conclusion: Changes in muscle strength, endurance and power adaptation responses following 16 weeks of either CT or RT with different high protein intakes were not associated with changes in lean mass in resistance-trained young males. These findings indicate that muscle hypertrophy has a small, or negligible, contributory role in promoting functional adaptations with RT or CT, at least over a 16-week period.

Timing and distribution of protein ingestion during prolonged recovery from resistance exercise alters myofibrillar protein synthesis.

Quantity and timing of protein ingestion are major factors regulating myofibrillar protein synthesis (MPS). However, the effect of specific ingestion patterns on MPS throughout a 12 h period is unknown. We determined how different distributions of protein feeding during 12 h recovery after resistance exercise affects anabolic responses in skeletal muscle. Twenty-four healthy trained males were assigned to three groups (n = 8/group) and undertook a bout of resistance exercise followed by ingestion of 80 g of whey protein throughout 12 h recovery in one of the following protocols: 8 × 10 g every 1.5 h (PULSE); 4 × 20 g every 3 h (intermediate: INT); or 2 × 40 g every 6 h (BOLUS). Muscle biopsies were obtained at rest and after 1, 4, 6, 7 and 12 h post exercise. Resting and post-exercise MPS (l-[ring-(13)C6] phenylalanine), and muscle mRNA abundance and cell signalling were assessed. All ingestion protocols increased MPS above rest throughout 1-12 h recovery (88-148%, P < 0.02), but INT elicited greater MPS than PULSE and BOLUS (31-48%, P < 0.02). In general signalling showed a BOLUS>INT>PULSE hierarchy in magnitude of phosphorylation. MuRF-1 and SLC38A2 mRNA were differentially expressed with BOLUS. In conclusion, 20 g of whey protein consumed every 3 h was superior to either PULSE or BOLUS feeding patterns for stimulating MPS throughout the day. This study provides novel information on the effect of modulating the distribution of protein intake on anabolic responses in skeletal muscle and has the potential to maximize outcomes of resistance training for attaining peak muscle mass.

Effects of 16 weeks of two different high-protein diets with either resistance or concurrent training on body composition, muscular strength and performance, and markers of liver and kidney function in resistance-trained males.

PURPOSE: It is unclear whether resistance (RT) and concurrent training (CT; resistance plus endurance training) combined with different protein intakes have differential effects on muscle hypertrophy, strength, and performance. Therefore, we compared the effects of two high-protein diets (1.6 or 3.2 g.kg-1.d-1) during 16 weeks of either CT or RT alone in resistance-trained males. METHODS: Forty-eight resistance-trained males (age: 26 ± 6 yr, body mass index: 25.6 ± 2.9 kg.m-2) performed 16 weeks (four sessions·w-1) of CT or RT with either 1.6 g.kg-1.d-1 protein (CT1; n = 12; RT1; n = 12) or 3.2 g.kg-1.d-1 protein (CT2; n = 12; RT2; n = 12). Training adaptations were assessed pre-, mid-, and post-intervention. RESULTS: All measures of performance (endurance, vertical jump, and pull-up), lean mass, muscle strength, and power significantly increased post-intervention in all groups, but peak power gains were greater in RT2 compared with RT1 and CT1 (p < .05). VO2max significantly increased in both CT groups (p < .001). Select biochemical markers of kidney and liver function significantly increased within the RT2 and CT2 groups (p < .05), however, no between-group differences were apparent (p > .05). CONCLUSIONS: With the exception of peak power, intake of 1.6 g.kg-1.d-1 of protein appears sufficient to maximize gains in lean mass, muscle strength, performance, and aerobic capacity during both RT and CT without influencing markers of kidney and liver function, indicating this daily protein amount is effective and safely tolerated in young, healthy adults.

Isolate Whey Protein Promotes Fluid Balance and Endurance Capacity Better Than Isolate Casein and Carbohydrate-Electrolyte Solution in a Warm, Humid Environment.

Protein ingestion is known to enhance post-exercise hydration. Whether the type of protein (i.e., whey, casein) can alter this response is unknown. Accordingly, this study aimed to compare the effects of the addition of milk-derived whey isolate or casein protein to carbohydrate-electrolyte (CE) drinks on post-exercise rehydration and endurance capacity. Thirty male soldiers (age: 24 ± 2.1 y; VO2max: 49.3 ± 4.7 mL/kg/min) were recruited. Upon losing ~2.2% of body mass by running in warm and humid conditions (32.3 °C, 76% relative humidity [RH]), participants ingested either a CE solution (66 g/L carbohydrate [CHO]), or CE plus isolate whey protein (CEW, 44 g/L CHO, 22 g/L isolate whey), or CE plus isolate casein protein (CEC, 44 g/L CHO, 22 g/L isolate casein) beverage in a volume equal to 150% of body mass loss. At the end of the 3 h rehydration period, a positive fluid balance was higher with CEW (0.22 L) compared to CEC (0.19 L) and CE (0.12 L). Overall mean fluid retention was higher in CEW (80.35%) compared with the CE (76.67%) and CEC trials (78.65%). The time of the endurance capacity test [Cooper 2.4 km (1.5 miles) run test] was significantly higher in CEC (14.25 ± 1.58 min) and CE [(12.90 ± 1.01 min; (p = 0.035)] than in CEW [(11.40 ± 1.41 min); (p = 0.001)]. The findings of this study indicate that the inclusion of isolate whey protein in a CE solution yields superior outcomes in terms of rehydration and enhanced endurance capacity, as compared to consuming the CE solution alone or in conjunction with isolate casein protein.