Considerations for a protein-focused screening instrument in clinical nutrition assessment.

Physiological stress during injury and surgery negatively impacts protein balance and muscle mass maintenance. Adequate perioperative protein intake may attenuate muscle atrophy to maintain and facilitate functional recovery, particularly in older adults; yet, screening tools routinely used in clinical settings do not specifically assess protein intake when assessing nutrition risk. Although assessing malnutrition is a priority, suboptimal protein intake in non-malnourished patients should also be identified given protein's critical role in muscle health. This opinion paper highlights the potential for using a clinically appropriate protein-focused screener for rapid and efficient characterization of protein intake.

Effect of High-Protein Diets on Integrated Myofibrillar Protein Synthesis before Anterior Cruciate Ligament Reconstruction: A Randomized Controlled Pilot Study.

Increasing dietary protein intake during periods of muscle disuse may mitigate the resulting decline in muscle protein synthesis (MPS). The purpose of this randomized pilot study was to determine the effect of increased protein intake during periods of disuse before anterior cruciate ligament (ACL) reconstruction on myofibrillar protein synthesis (MyoPS), and proteolytic and myogenic gene expression. Six healthy, young males (30 ± 9 y) were randomized to consume a high-quality, optimal protein diet (OP; 1.9 g·kg−1·d−1) or adequate protein diet (AP; 1.2 g·kg−1·d−1) for two weeks before ACL reconstruction. Muscle biopsies collected during surgery were used to measure integrated MyoPS during the intervention (via daily deuterium oxide ingestion) and gene expression at the time of surgery. MyoPS tended to be higher, with a large effect size in OP compared to AP (0.71 ± 0.1 and 0.54 ± 0.1%·d−1; p = 0.076; g = 1.56). Markers of proteolysis and myogenesis were not different between groups (p > 0.05); however, participants with greater MyoPS exhibited lower levels of MuRF1 gene expression compared to those with lower MyoPS (r = −0.82, p = 0.047). The data from this pilot study reveal a potential stimulatory effect of increased daily protein intake on MyoPS during injury-mediated disuse conditions that warrants further investigation.

Testosterone supplementation upregulates androgen receptor expression and translational capacity during severe energy deficit.

Testosterone supplementation during energy deficit promotes whole body lean mass accretion, but the mechanisms underlying that effect remain unclear. To elucidate those mechanisms, skeletal muscle molecular adaptations were assessed from muscle biopsies collected before, 1 h, and 6 h after exercise and a mixed meal (40 g protein, 1 h postexercise) following 14 days of weight maintenance (WM) and 28 days of an exercise- and diet-induced 55% energy deficit (ED) in 50 physically active nonobese men treated with 200 mg testosterone enanthate/wk (TEST) or placebo (PLA) during the ED. Participants (n = 10/group) exhibiting substantial increases in leg lean mass and total testosterone (TEST) were compared with those exhibiting decreases in both of these measures (PLA). Resting androgen receptor (AR) protein content was higher and fibroblast growth factor-inducible 14 (Fn14), IL-6 receptor (IL-6R), and muscle ring-finger protein-1 gene expression was lower in TEST vs. PLA during ED relative to WM (P < 0.05). Changes in inflammatory, myogenic, and proteolytic gene expression did not differ between groups after exercise and recovery feeding. Mechanistic target of rapamycin signaling (i.e., translational efficiency) was also similar between groups at rest and after exercise and the mixed meal. Muscle total RNA content (i.e., translational capacity) increased more during ED in TEST than PLA (P < 0.05). These findings indicate that attenuated proteolysis at rest, possibly downstream of AR, Fn14, and IL-6R signaling, and increased translational capacity, not efficiency, may drive lean mass accretion with testosterone administration during energy deficit.

Chocolate milk and endurance exercise recovery: protein balance, glycogen, and performance.

PURPOSE: This study examined effects of fat-free chocolate milk (MILK) consumption on kinetic and cellular markers of protein turnover, muscle glycogen, and performance during recovery from endurance exercise. METHODS: Male runners participated in two trials separated by 1 wk and consumed either MILK or a nonnitrogenous isocaloric carbohydrate (CHO) control beverage (CON) after a 45-min run at 65% of V˙O(2peak). Postexercise muscle protein fractional synthetic rate (FSR) and whole-body protein turnover were determined during 3 h of recovery using muscle biopsies and primed constant infusions of L-[ring-²H5]phenylalanine and L-[1-¹³C]leucine, respectively. Phosphorylation of translational signaling proteins and activity of proteolytic molecules were determined using Western blotting and enzymatic activity assays. Muscle glycogen was quantified, and treadmill time to exhaustion was determined after the recovery period. RESULTS: Consuming MILK after exercise resulted in higher mixed muscle FSR with lower whole-body proteolysis and synthesis compared with CON (P ≤ 0.05). Phosphorylation of eIF4E-BP1 and FOXO3a was higher for MILK (P < 0.01), whereas Akt phosphorylation was lower during recovery regardless of dietary treatment (P < 0.05). Enzymatic activity assays indicated lower caspase-3 activity during recovery for MILK (P < 0.01) and higher 26S proteasome activity for CON (P < 0.01). Muscle glycogen was not affected by either dietary treatment; however, time to exhaustion was greater for MILK than for CON (P < 0.05). CONCLUSIONS: The effects of consumption of MILK after endurance exercise on FSR, signaling molecules of skeletal muscle protein turnover, leucine kinetics, and performance measures suggest unique benefits of milk compared with a CHO-only beverage.

Acute energy deprivation affects skeletal muscle protein synthesis and associated intracellular signaling proteins in physically active adults.

To date, few studies have characterized the influence of energy deprivation on direct measures of skeletal muscle protein turnover. In this investigation, we characterized the effect of an acute, moderate energy deficit (10 d) on mixed muscle fractional synthetic rate (FSR) and associated intracellular signaling proteins in physically active adults. Eight men and 4 women participated in a 20-d, 2-phase diet intervention study: weight maintenance (WM) and energy deficient (ED; approximately 80% of estimated energy requirements). Dietary protein (1.5 g x kg(-1) x d(-1)) and fat (approximately 30% of total energy) were constant for WM and ED. FSR and intracellular signaling proteins were measured on d 10 of both interventions using a primed, constant infusion of [(2)H(5)]-phenylalanine and Western blotting techniques, respectively. Participants lost approximately 1 kg body weight during ED (P < 0.0001). FSR was reduced approximately 19% (P < 0.05) for ED (0.06 +/- 0.01%/h) compared with WM (0.074 +/- 0.01%/h). Protein kinase B and eukaryotic initiation factor 4E binding protein 1 phosphorylation were lower (P < 0.05) during ED compared with WM. AMP activated protein kinase phosphorylation decreased (P < 0.05) over time regardless of energy status. These findings show that FSR and associated synthetic intracellular signaling proteins are downregulated in response to an acute, moderate energy deficit in physically active adults and provide a basis for future studies assessing the impact of prolonged, and perhaps more severe, energy restriction on skeletal muscle protein turnover.

Aerobic exercise training increases skeletal muscle protein turnover in healthy adults at rest.

The effect of a 4-wk aerobic exercise training program (30-45 min, 3-5 d/wk, >or=65% maximal heart rate) on mixed skeletal muscle protein fractional synthetic rate (FSR), fractional breakdown rate (FBR), and net protein balance (FSR - FBR) (NET) was examined in 8 healthy, previously unfit men and women [21.0+/- 0.4 y, 163.7+/- 4.4 cm, 75.6+/- 5.7 kg, 33.5+/- 4.1% body fat, VO(2 peak) 38.6+/- 2.3 mL/(kg.min)] fed eucaloric diets providing 0.85 g protein/(kg.d) for the 6-wk study. Measurements were made at baseline after 2 wk of diet intervention only, and after 4 wk of aerobic exercise training and diet intervention. Primed continuous infusions of ring-[(2)H(5)]-phenylalanine (2 micromol/kg; 0.05 micromol/(kg.min) and [(15)N]-phenylalanine (2 micromol/kg; 0.05 micromol/(kg.min) were used to assess skeletal muscle protein turnover at rest via the precursor-product method. Endurance training improved cardiovascular fitness, with a significant increase in VO(2 peak) (P<0.01) and a significant decrease in running time on a standard course (P<0.01). There were o significant changes in body mass or composition. There was a significant increase in FSR (0.077+/- 0.007 vs. 0.089+/- 0.006%/h, P<0.05) and decrease in NET (FSR - FBR) (-0.023 +/-0.004 vs. -0.072 +/- 0.012%/h, P < 0.05); FBR tended to increase (0.105+/- 0.014 vs. 0.143+/- 0.018%/h; P=0.06) after training. Findings show that aerobic training for 4 wk increases skeletal muscle protein turnover in previously unfit subjects.