Rehabilitation Nutrition for Injury Recovery of Athletes: The Role of Macronutrient Intake

Josse et al., 2011 [29] Protein 90 healthy, premenopausal, overweight, and obese women were randomized to 3 groups (n = 30/group): high protein, high dairy, adequate protein, medium dairy, and adequate protein, low dairy hypocaloric diets. Diet- and exercise-induced weight loss with higher protein and increased dairy product intakes promotes more favorable body composition changes in women characterized by greater total and visceral fat loss and lean mass gain. Hartman et al., 2007 [30] Protein 56 healthy young men who trained 5 days/week for 12 weeks randomly assigned to consume drinks immediately and again 1 h after exercise: fat-free milk. (Milk; n = 18); fat-free soy protein (Soy; n = 19) that was isoenergetic, isonitrogenous, and macronutrient ratio matched to Milk; or maltodextrin that was isoenergetic with Milk and Soy (control group; n = 19). Post-exercise consumption of milk promotes greater hypertrophy during the early stages of resistance training in novice weightlifters when compared with isoenergetic soy or carbohydrate consumption. Areta et al., 2013 [37] Protein 24 healthy trained males were assigned to three groups of 8 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, 4 × 20 g every 3 h; or 2 × 40 g every 6 h. 20 g of whey protein consumed every 3 h was superior to either more frequent (every 1.5 h) or less frequent (every 6 h) feeding patterns for stimulating MPS (muscle protein synthesis) throughout the day. Moore et al., 2008 [34] Protein 6 healthy young men undertook 5 intense leg-based resistance exercise programs. After exercise, participants consumed, in a randomized order, drinks containing 0, 5, 10, 20, or 40 g, whole egg protein. Ingestion of 20 g intact protein is sufficient to maximally stimulate muscle and albumin protein synthesis after resistance exercise, which corresponds to ~8–9 g essential amino acids (EAAs) and ~1.8 g leucine. 4 to 6 meals high in protein for athletes during resistant training to maximize muscle strength and muscle mass. BCAA (Branched-chain amino acid) and mainly leucine play a prominent role in stimulating MPS during resistant training to maximize muscle strength and muscle mass. Mamerow et al., 2014 [35] Protein 7-day crossover feeding design study with a 30-day washout period, to examine changes in muscle protein synthesis in response to isoenergetic and isonitrogenous diets with protein at breakfast, lunch, and dinner distributed evenly or skewed on 8 participants. 24 h muscle synthesis rate was 25% more effective in healthy women and men when fed with protein evenly distributed across breakfast, lunch and dinner compared to isoenergetic and isonitrogenous diets with uneven protein distribution across meals. Tang et al., 2009 [39] Protein 3 groups of 6 healthy young men performed a bout of unilateral leg resistance exercise followed by the consumption of a drink containing an equivalent content of essential amino acids (10 g) as either whey hydrolysate, micellar casein, or soy protein isolate. All protein sources significantly increased muscle protein synthesis rates both at rest and in response to resistance exercise. Burd et al., 2012 [40] Protein Healthy elderly men were divided into two groups of 7 & performed unilateral leg resistance exercise followed by the consumption of isonitrogenous quantities (20 g) of casein or whey. Ingestion of isolated whey protein supports greater rates of MPS than micellar casein both at rest and after resistance exercise in healthy elderly men. Pennings et al., 2011 [42] Protein 48 older men were randomly assigned to ingest a meal-like amount (20 g) of intrinsically l-[1-(13)C]phenylalanine-labeled whey, casein, or casein hydrolysate. Protein ingestion was combined with continuous intravenous l-[ring-(2)H(5)]phenylalanine infusion to assess in vivo digestion and absorption kinetics of dietary protein. Whey protein is more effective on postprandial muscle protein accretion than casein and casein hydrolysate in older mend to whey’s faster digestion and absorption kinetics and higher leucine content. Rittig et al., 2017 [43] Protein Randomized crossover trial to compare a specific leucine-rich whey protein beverage (LWH) with isocaloric CHO (carbohydrates), soy protein (SOY), and soy protein +3 g HMB (hydroxymethylbutyrate) during fasting-induced catabolic conditions LWH and HMB have superior anabolic effects on muscle protein kinetics after 36 h of fasting, and LWH distinctly activates the mTOR pathway. These novel findings suggest that leucine-rich whey protein and/or HMB are specifically beneficial during fasting-induced catabolic conditions. Res et al., 2012 [45] Protein 16 healthy young males performed a single bout of resistance-type exercise in the evening after a full day of dietary standardization followed by recovery nutrition (20 g of protein, 60 g of CHO) immediately after exercise. Thereafter, 30 min before sleep (2330 h), subjects ingested a beverage with protein or placebo. Protein ingested immediately before sleep is effectively digested and absorbed, thereby stimulating muscle protein synthesis and improving whole-body protein balance during post exercise overnight recovery. Witard et al., 2013 [46] Protein 48 volunteers consumed a standardized, high-protein (0.54 g/kg body mass) breakfast. 3 h later, they underwent a bout of unilateral exercise and ingested 0, 10, 20, or 40 g whey protein isolate immediately (∼10 min) after exercise. A 20-g dose of whey protein is sufficient for the maximal stimulation of post-absorptive rates of myofibrillar MPS in rested and exercised muscle of ~80-kg resistance-trained, young men. A dose of whey protein >20 g stimulates amino acid oxidation and ureagenesis. Yang et al., 2012 [47] Protein 37 elderly men completed a bout of unilateral leg-based resistance exercise before ingesting 0, 10, 20 or 40 g of whey protein isolate. Resistance exercise increases MPS in the elderly at all protein doses, but to a greater extent with 40 g of whey ingestion, in contrast to younger adults, in whom post-exercise rates of MPS are saturated with 20 g of protein, exercised muscles of older adults respond to higher protein doses. Katsanos et al., 2005 [58] Leucine 2 elderly (n = 10 & 10) and 2 young (n = 8 & 8) groups were studied before and after ingestion of 6.7 g of EAAs with different %leucine. increasing the proportion of leucine in a mixture of EAA can reverse an attenuated response of muscle protein synthesis in elderly but does not result in further stimulation of muscle protein synthesis in young subjects. Dijk et al., 2018 [59] Leucine Overnight fasted C57/BL6RJ mice at 25-mo of age received an oral gavage with leucine or whey-protein enriched with leucine (0.75 g/kg bodyweight total leucine in both) or 0.5 mL water (fasted control). MPS is stimulated in aged mice by leucine-enriched whey protein but not by leucine administration only. Wall et al., 2013 [60] Leucine 24 elderly men randomly assigned to ingest 20 g intrinsically L-[1-(13)C]phenylalanine-labeled casein protein with (PRO+LEU) or without (PRO) 2.5 g crystalline leucine. Leucine co-ingestion with a bolus of pure dietary protein further stimulates post-prandial muscle protein synthesis rates in elderly men. Wilkinson et al., 2013 [63] Leucine and HMB 15 young healthy men, who were recreationally active but not involved in a formal training program, were randomized to receive 3.42 g HMB or 3.42 g Leucine. HMB and Leucine ↑ anabolic signaling but it was more pronounced with Leucine. HMB consumption also attenuated muscle protein breakdown in an insulin-independent manner. Deutz et al., 2013 [64] HMB Randomized, controlled, double-blinded, parallel-group design study was carried out in 24 healthy (SPPB ≥ 9) older adult subjects (20 women, 4 men), confined to complete bed rest for ten days, followed by resistance training rehabilitation for eight weeks. The experimental group received HMB (calcium salt, 1.5 g twice daily—total 3 g/day) and the control group an inactive placebo powder. HMB supplementation preserves muscle mass during 10 days of bed rest. Zhao et al., 2018 [66] pipecolic acid Analysis of metabolomic profiles of 136 Caucasian women who exercised 3 times per week. Pipecolic acid was positively associated with muscle mass and muscle strength, but negatively associated with age. Sato et al., 2013 [67] Lysine Fasted rats were administered 22.8–570 mg Lys/100 g body weight and the rates of myofibrillar protein degradation were assessed for 0–6 h after Lys administration. Lys is able to suppress myofibrillar protein degradation at least partially through the autophagic-lysosomal pathway, not the ubiquitin-proteasomal pathway, whereas Lys might be unable to stimulate protein synthesis within this time frame. Sato et al., 2016 [69] Lysine & metabolites Exploration of the effect of Lys metabolites, L-2-aminoadipic acid (2-AA) and L-pipecolic acid (Pip), on protein turnover in C2C12 myotubes. In C2C12 myotubes, L-2-aminoadipic acid could suppress autophagy and pipecolic acid could stimulate the rates of protein synthesis, and these metabolites may contribute to exert effect of Lysine on protein turnover. Howarth et al., 2010 [48] Carbohydrates 6 men cycled at approximately 75% peak O2 uptake (Vo(2peak)) to exhaustion to reduce body CHO stores and then consumed either a high-CHO or low-CHO diet for 2 days before the trial in random order. The whole-body net protein balance was reduced in the L-CHO group, largely due to a decrease in whole body protein synthesis. Smith et al., 2011 [51] Fat 9 25–45-year-old healthy subjects supplemented for 8 weeks with 4 g of Lovaza®/day. Basal muscle protein fractional synthesis rate and basal signaling element phosphorylation remained unchanged after LCn-3PUFA supplementation, but the anabolic response to insulin and amino acid infusion was greater. Muscle protein concentration and the protein/DNA ratio were both greater after supplementation. Smith et al., 2010 [52] Fat 16 healthy, older adults were randomized to receive either omega-3 fatty acids or corn oil for 8 weeks. Omega-3 fatty acid supplementation had no effect on the basal rate of muscle protein synthesis, but augmented the hyperaminoacidemia-hyperinsulinemia-induced increase in the rate of muscle protein synthesis, accompanied by greater increases in p70s6k(Thr389) phosphorylation. Musumeci et al., 2013 [55] Fat Morphological Study on experimental bones. Inflammation process causes stress to chondrocytes that will die as a biological defense mechanism, and will also increase the survival of new chondrocytes for maintaining cell homeostasis.
Healthy diet plays important anti-inflammatory role. Fito et al., 2007 [71] Fat Randomized Controlled Trial with 372 subjects at high cardiovascular risk who were recruited into PREDIMED trial. Individuals at high cardiovascular risk who improved their diet toward a TMD pattern showed significant reductions in cellular lipid levels and LDL oxidation. Otranto et al., 2010 [74] Omega-3 fatty acids 30 days before wounding, rats were started on daily supplements of sunflower oil, linseed oil, fish oil, or water. On day 0, an excisional wound was made on the back of each animal and euthanasia was undertaken on day 14. Different types of edible oils delayed cutaneous wound healing, negatively affecting collagen regeneration. You et al., 2010 [76] Omega-3 fatty acids Rats were fed a corn-oil- (control) or fish-oil-based diet for 2 weeks, and then subjected to 10 days hindlimb immobilization while still receiving the same diets. Rats with high fish oil diets experienced less muscle loss during hind limb immobilization. Vidmar et al., 2016 [77] Omega-3 fatty acids Prospective, randomized, controlled, and single blinded clinical trial, with 25 patients who underwent anterior cruciate ligament reconstruction, randomly assigned to 2 g of omega-3 for 15 days after surgery and control (no supplementation). Omega-3 supplementation benefited the modulation of oxidative biomarkers during rehabilitation of patients who had undergone knee surgery. Shaw et al., 2019 [75] Leucine, omega-3 fatty acids Comparison of rehabilitation program undertaken by two professional rugby athletes’ anterior cruciate ligament (ACL), with the addition of an evidence-based supplementation (gelatine and vitamin C) and exercise protocol focused on collagenous tissue. Players undertook a structured rehabilitation program for 34 weeks before being clinically assessed ready to play. Players saw minimal changes in body composition in the early rehabilitation period (P1—0.8 kg; P2—0.4 kg). Leg lean mass reduced in both legs of Player 1 (Injured—0.8 kg, Non-injured—0.6 kg) at 17 weeks, with Player 2 only experiencing a loss of 0.3 kg of lean tissue in the injured leg. Both players returned to baseline body compositions after 24 weeks. Leg strength returned to a maximum at 24 and 15 weeks, respectively, with knee function returning to baseline by 30 weeks.