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Gain or loss of skeletal muscle mass is due largely to the establishment of an imbalance between rates of protein synthesis and degradation. A key determinant of the rate of protein synthesis is translation initiation, a process regulated in part through binding of initiator methionyl-tRNA (met-tRNA_i) and messenger RNA (mRNA) to a 40S ribosomal subunit. Either the met-tRNA_i or mRNA binding step can become limiting for protein synthesis. Furthermore, the mRNA binding step can modulate translation of specific mRNAs with or without changes in the overall rate of protein synthesis. This report highlights molecular mechanisms involved in mediating control of the mRNA binding step in translation initiation. Particular attention is given to the effect of exercise on this step and to how the branched-chain amino acid leucine stimulates muscle protein synthesis after exercise. Potential mechanisms for exercise induced increase in muscle mass are discussed.

Protein, protein hydrolysates, and amino acids have become popular ingredients in sports nutrition. The use of protein, protein hydrolysates, and amino acid mixtures has multiple applications when aiming to improve post exercise recovery. After exhaustive endurance-type exercise, muscle glycogen repletion is the most important factor determining the time needed to recover. Coingestion of relatively small amounts of protein and/or amino acids with carbohydrate can be used to augment postprandial insulin secretion and accelerate muscle glycogen synthesis rates. Furthermore, it has been well established that ingesting protein, protein hydrolysates, and amino acid can stimulate protein synthesis and inhibit protein breakdown and, as such, improve net muscle protein balance after resistance- or endurance-type exercise. The latter has been suggested to lead to a more effective adaptive response to each successive exercise bout. To augment net muscle protein accretion, athletes involved in resistance-type exercise generally ingest both protein and carbohydrate during post exercise recovery. However, carbohydrate ingestion after resistance-type exercise does not seem to be warranted to further stimulate muscle protein synthesis or improve whole-body protein balance when ample protein has already been ingested. Because resistance-type exercise is also associated with a substantial reduction in muscle glycogen content, it would be preferred to coingest some carbohydrate when aiming to accelerate glycogen repletion. More research is warranted to assess the impact of ingesting different proteins, protein hydrolysates, and/or amino acids on muscle protein accretion after exercise.

Resistance exercise can effectively result in an increase in muscle mass, or hypertrophy, which generally becomes apparent after several weeks of training. Muscle hypertrophy requires muscle protein synthesis to exceed protein breakdown during an extended time period. It has been firmly established that the interaction between exercise and nutrition (i.e., protein intake) is necessary to attain net protein accretion in skeletal muscle. The stimulation of protein synthesis is caused in part by stimulation of mRNA translation initiation. There is relatively little information on the response of intracellular signaling controlling mRNA translation to exercise and nutrition, especially in humans, but the available data in humans seem to suggest that a single bout of resistance exercise does not substantially enhance PI-3 kinase/mTOR signaling during the first 2 h after exercise. Moreover, it is demonstrated that the ingestion of protein or amino acids after exercise is crucial to further stimulate molecular signaling that controls translation initiation. The aim of this review is to provide an overview of the intracellular signaling related to translational control and to provide a summary of the current knowledge about the response of the signaling pathways controlling the anabolic response to exercise and nutrient intake in vivo in humans.

Water polo is an aquatic team sport that requires endurance, strength, power, swimming speed, agility, tactical awareness, and specific technical skills, including ball control. Unlike other team sports, few researchers have examined the nutritional habits of water polo athletes or potential dietary strategies that improve performance in water polo match play. Water polo players are typically well muscled, taller athletes; female players display higher levels of adiposity compared with their male counterparts. Positional differences exist: Center players are heavier and have higher body fat levels compared with perimeter players. Knowledge of the physical differences that exist among water polo players offers the advantage of player identification as well as individualizing nutrition strategies to optimize desired physique goals. Individual dietary counseling is warranted to ensure dietary adequacy, and in cases of physique manipulation. Performance in games and during quality workouts is likely to improve by adopting strategies that promote high carbohydrate availability, although research specific to water polo is lacking. A planned approach incorporating strategies to facilitate muscle glycogen refueling and muscle protein synthesis should be implemented following intensified training sessions and matches, particularly when short recovery times are scheduled. Although sweat losses of water polo players are less than what is reported for land-based athletes, specific knowledge allows for appropriate planning of carbohydrate intake strategies for match play and training. Postgame strategies to manage alcohol intake should be developed with input from the senior player group to minimize the negative consequences on recovery and player welfare.

Bouldering competitions are held up to International level and governed by the International Federation of Sport Climbing. Bouldering has been selected to feature at the 2020 Olympic Games in Tokyo, however, physiological qualities and nutritional requirements to optimize performance remain inadequately defined due to large gaps in the literature. The primary goals of training include optimizing the capacity of the anaerobic energy systems and developing sport-specific strength, with emphasis on the isometric function of the forearm flexors responsible for grip. Bouldering athletes typically possess a lean physique, similar to the characteristics of sport climbers with reported body fat values of 6–12%. Athletes strive for a low body weight to improve power to weight ratio and limit the load on the extremities. Specialized nutritional support is uncommon and poor nutritional practices such as chronic carbohydrate restriction are prevalent, compromising the health of the athletes. The high intensity nature of bouldering demands a focus on adequate carbohydrate availability. Protein intake and timing should be structured to maximize muscle protein synthesis and recovery, with the literature suggesting 0.25–0.3 g/kg in 3–4 hr intervals. Supplementing with creatine and b-alanine may provide some benefit by augmenting the capacity of the anaerobic systems. Boulderers are encouraged to seek advice from nutrition experts to enhance performance, particularly important when weight loss is the desired outcome. Further research is warranted across all nutritional aspects of bouldering which is summarized in this review.

Evidence suggests that increasing protein distribution may be desirable to promote muscle protein synthesis (MPS) in combination with resistance exercise. However, there is a threshold above which additional protein consumption has limited benefit for MPS and may promote protein loss due to increased oxidation. This study aimed to measure daily protein intake and protein distribution in a cohort of rugby players. Twenty-five developing elite rugby union athletes (20.5 ± 2.3 years, 100.2 ± 13.3 kg, 184.4 ± 7.4 cm) were assessed at the start and end of a rugby preseason. Using a 7-day food diary the reported daily protein intake was 2.2 ± 0.7 g·kg·day^-1 which exceeds daily recommendations. The reported carbohydrate intake was 3.6 ± 1.3 g·kg·day^-1 which may reflect a suboptimal intake or dietary underreporting. In general, the rugby athletes were regularly consuming more than 20 g of protein; 3.8 ± 0.9 times per day (68 ± 18% of eating occasions). In addition to documenting current dietary intakes, an excess protein estimation score was calculated to determine how frequently the rugby athletes consumed protein above a known effective dose with a margin of error. 2.0 ± 0.9 eating occasions contained protein in excess of doses (20 g) known to promote MPS. Therefore, it is currently unclear whether the consumption of regular large doses of protein will benefit rugby athletes via increasing protein distribution, or whether high protein intakes may have unintended effects including a reduction in carbohydrate and/or energy intake.

We previously reported an increase in skeletal muscle protein synthesis during fasted and fed recovery from nonexhaustive aerobic exercise (Harber et al., 2010). The current study examined skeletal muscle intracellular signaling in the same subjects to further investigate mechanisms of skeletal muscle protein metabolism with and without feeding following aerobic exercise. Eight males (VO_2peak: 52 ± 2 ml⁻¹.kg⁻¹.min⁻¹) performed 60-min of cycle ergometry at 72 ± 1% VO_2peak on two occasions in a counter-balanced design. Exercise trials differed only in the postexercise nutritional intervention: EX-FED (5kcal, 0.83g carbohydrate, 0.37g protein, 0.03g fat per kg body weight) and EX-FAST (noncaloric, isovolumic placebo) ingested immediately and one hour after exercise. Muscle biopsies were obtained from the vastus lateralis at rest (on a separate day) and two hours postexercise to assess intracellular signaling via western blotting of p70S6K1, eEF2, 4EBP1, AMPKα and p38 MAPK. p70S6K1 phosphorylation was elevated (p < .05) in EX-FED relative to REST and EX-FAST. eEF2, 4EBP1, AMPKα and p38 MAPK signaling were unaltered at 2h after exercise independent of feeding status when expressed as the ratio of phosphorylated to total protein normalized to actin. These data demonstrate that feeding after a nonexhaustive bout of aerobic exercise stimulates skeletal muscle p70S6K1 intracellular signaling favorable for promoting protein synthesis which may, as recent literature has suggested, better prepare the muscle for subsequent exercise bouts. These data provide further support into the role of feeding on mechanisms regulating muscle protein metabolism during recovery from aerobic exercise.

While effects of the two classes of proteins found in milk (i.e., soluble proteins, including whey, and casein) on muscle protein synthesis have been well investigated after a single bout of resistance exercise (RE), the combined effects of these two proteins on the muscle responses to resistance training (RT) have not yet been investigated. Therefore, the aim of this study was to examine the effects of protein supplementation varying by the ratio between milk soluble proteins (fast-digested protein) and casein (slow-digested protein) on the muscle to a 9-week RT program. In a double-blind protocol, 31 resistance-trained men, were assigned to 3 groups receiving a drink containing 20g of protein comprising either 100% of fast protein (FP(100), n = 10), 50% of fast and 50% of slow proteins (FP(50), n = 11) or 20% of fast protein and 80% of casein (FP(20), n = 10) at the end of training bouts. Body composition (DXA), and maximal strength in dynamic and isometric were analyzed before and after RT. Moreover, blood plasma aminoacidemia kinetic after RE was measured. The results showed a higher leucine bioavailability after ingestion of FP(100) and FP(50) drinks, when compared with FP(20) (p< .05). However, the RT-induced changes in lean body mass (p < .01), dynamic (p < .01), and isometric muscle strength (p < .05) increased similarly in all experimental groups. To conclude, compared with the FP(20) group, the higher rise in plasma amino acids following the ingestion of FP(100) and FP(50) did not lead to higher muscle long-term adaptations.