Nutrient Administration and Resistance Training

Skeletal muscle tissue is tightly regulated throughout our bodies by balancing its synthesis and breakdown. Many factors are known to exist that cause profound changes on the overall status of skeletal muscle, some of which include exercise, nutrition, hormonal influences and disease. Muscle hypertrophy results when protein synthesis is greater than protein breakdown. Resistance training is a popular form of exercise that has been shown to increase muscular strength and muscular hypertrophy. In general, resistance training causes a stimulation of protein synthesis as well as an increase in protein breakdown, resulting in a negative balance of protein. Providing nutrients, specifically amino acids, helps to stimulate protein synthesis and improve the overall net balance of protein. Strategies to increase the concentration and availability of amino acids after resistance exercise are of great interest and have been shown to effectively increase overall protein synthesis. [1-3] After exercise, providing carbohydrate has been shown to mildly stimulate protein synthesis while addition of free amino acids prior to and after exercise, specifically essential amino acids, causes a rapid pronounced increase in protein synthesis as well as protein balance.[1,3] Evidence exists for a dose-response relationship of infused amino acids while no specific regimen exists for optimal dosing upon ingestion. Ingestion of whole or intact protein sources (e.g., protein powders, meal-replacements) has been shown to cause similar improvements in protein balance after resistance exercise when compared to free amino acid supplements. Future research should seek to determine optimal dosing of ingested intact amino acids in addition to identifying the cellular mechanistic machinery (e.g. transcriptional and translational mechanisms) for causing the increase in protein synthesis

Comparative effects of whey and casein proteins on satiety in overweight and obese individuals: A randomized controlled trial

Background/Objective: Dairy protein seems to reduce appetite by increasing satiety and delaying the return of hunger and subsequently lowering energy intake compared with fat or carbohydrate. The aim of this study was to compare the effect of whey with that of casein proteins on satiety in overweight/obese individuals. Methods/Subjects: This was a randomized, parallel-design 12-week-long study. Seventy subjects with a body mass index between 25 and 40 kg/m2 and aged 18–65 years were randomized into one of three supplement groups: glucose control (n=25), casein (n=20) or whey (n=25) protein. Before commencing the study, at weeks 6 and 12 of the treatment, a Visual Analogue Scale (VAS) was used to measure subjective sensations of appetite before lunch and before dinner. Results: Rating for VAS (mm) at 6 and 12 weeks showed significantly higher satiety in the whey group compared with the casein (P=0.017 and P=0.025, respectively) or control (P=0.024 and P=0.032, respectively) groups when measured before lunch. Similarly, at 6 and 12 weeks, the score for fullness was also significantly higher in the whey group compared with both casein (P=0.038 and P=0.022, respectively) and control (P=0.020 and P=0.030, respectively) groups. However, these short-term effects on satiety from dairy whey proteins did not have any long-term effects on energy intake or body weight over 12 weeks compared with casein. Conclusions: Collectively, whey protein supplementation appears to have a positive and acute postprandial effect on satiety and fullness compared with casein and carbohydrate supplementation in overweight and obese individuals

Protein and Overtraining: Potential Applications for Free-Living Athletes

Despite a more than adequate protein intake in the general population, athletes have special needs and situations that bring it to the forefront. Overtraining is one example. Hard-training athletes are different from sedentary persons from the sub-cellular to whole-organism level. Moreover, competitive, "free-living" (less-monitored) athletes often encounter negative energy balance, sub-optimal dietary variety, injuries, endocrine exacerbations and immune depression. These factors, coupled with "two-a-day" practices and in-season demands require that protein not be dismissed as automatically adequate or worse, deleterious to health. When applying research to practice settings, one should consider methodological aspects such as population specificity and control variables such as energy balance. This review will address data pertinent to the topic of athletic protein needs, particularly from a standpoint of overtraining and soft tissue recovery. Research-driven strategies for adjusting nutrition and exercise assessments will be offered for consideration. Potentially helpful nutrition interventions for preventing and treating training complications will also be presented

Protein type, protein dose, and age modulate dietary protein digestion and phenylalanine absorption kinetics and plasma phenylalanine availability in humans

This is the final version. Available from the publisher via the DOI in this record.BACKGROUND: Dietary protein ingestion stimulates muscle protein synthesis by providing amino acids to the muscle. The magnitude and duration of the postprandial increase in muscle protein synthesis rates are largely determined by dietary protein digestion and amino acid absorption kinetics. OBJECTIVE: We assessed the impact of protein type, protein dose, and age on dietary protein digestion and amino acid absorption kinetics in vivo in humans. METHODS: We included data from 18 randomized controlled trials with a total of 602 participants [age: 53 ± 23 y; BMI (kg/m2): 24.8 ± 3.3] who consumed various quantities of intrinsically l-[1-13C]-phenylalanine-labeled whey (n = 137), casein (n = 393), or milk (n = 72) protein and received intravenous infusions of l-[ring-2H5]-phenylalanine, which allowed us to assess protein digestion and phenylalanine absorption kinetics and the postprandial release of dietary protein-derived phenylalanine into the circulation. The effect of aging on these processes was assessed in a subset of 82 young (aged 22 ± 3 y) and 83 older (aged 71 ± 5 y) individuals. RESULTS: A total of 50% ± 14% of dietary protein-derived phenylalanine appeared in the circulation over a 5-h postprandial period. Casein ingestion resulted in a smaller (45% ± 11%), whey protein ingestion in an intermediate (57% ± 10%), and milk protein ingestion in a greater (65% ± 13%) fraction of dietary protein-derived phenylalanine appearing in the circulation (P < 0.001). The postprandial availability of dietary protein-derived phenylalanine in the circulation increased with the ingestion of greater protein doses (P < 0.05). Protein digestion and phenylalanine absorption kinetics were attenuated in older when compared with young individuals, with 45% ± 10% vs. 51% ± 14% of dietary protein-derived phenylalanine appearing in the circulation, respectively (P = 0.001). CONCLUSIONS: Protein type, protein dose, and age modulate dietary protein digestion and amino acid absorption kinetics and subsequent postprandial plasma amino acid availability in vivo in humans. These trials were registered at clinicaltrials.gov as NCT00557388, NCT00936039, NCT00991523, NCT01317511, NCT01473576, NCT01576848, NCT01578590, NCT01615276, NCT01680146, NCT01820975, NCT01986842, and NCT02596542, and at http://www.trialregister.nl as NTR3638, NTR3885, NTR4060, NTR4429, and NTR4492

Mathematical Computations in the Management of Public Construction Work in Mesopotamia (End of the Third and Beginning of the Second Millennium BCE)

The aim of this chapter is to examine what types of computations Mesopotamian scribes were trained when dealing with building activities. Its aim is also to try to determine how far these calculation methods were actually used in practice. In order to do this we examine mathematical and administrative texts dealing with construction activities as well as archaeological and ethnographical data. Two types of texts provide the information on mathematical calculations for construction on which we draw: mathematical texts and practical administrative texts. We distinguish between three different steps in these computations. The first is the use of labor norms. In this category we find the daily tasks (called iškarum) expected from unskilled workers. The second step is the use of coefficients to calculate a magnitude on the basis of other magnitudes (determining a volume from a given weight, for instance). The last step consists of exercises dealing with several types of tasks, using combined coefficients. Finally, by drawing on some administrative construction texts, we try to check whether or not these computations were actually used in practice

Ingestion of Casein in a Milk Matrix Modulates Dietary Protein Digestion and Absorption Kinetics but Does Not Modulate Postprandial Muscle Protein Synthesis in Older Men

BACKGROUND: The slow digestion and amino acid absorption kinetics of isolated micellar casein have been held responsible for its relatively lower postprandial muscle protein synthetic response compared with rapidly digested proteins such as isolated whey. However, casein is normally consumed within a milk matrix. We hypothesized that protein digestion and absorption kinetics and the subsequent muscle protein synthetic response after micellar casein ingestion are modulated by the milk matrix. OBJECTIVE: The aim of this study was to determine the impact of the milk matrix on casein protein digestion and absorption kinetics and postprandial muscle protein synthesis in older men. METHODS: In a parallel-group design, 32 healthy older men (aged 71 +/- 1 y) received a primed continuous infusion of L-[ring-2H5]-phenylalanine, L-[ring-3,5-2H2]-tyrosine, and L-[1-13C]-leucine, and ingested 25 g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine labeled casein dissolved in bovine milk serum (Cas+Serum) or water (Cas). Plasma samples and muscle biopsies were collected in the postabsorptive state and for 300 min in the postprandial period to examine whole-body and skeletal muscle protein metabolism. RESULTS: Casein ingestion increased plasma leucine and phenylalanine concentrations and L-[1-13C]-phenylalanine enrichments, with a more rapid rise after Cas vs. Cas+Serum. Nonetheless, dietary protein-derived phenylalanine availability did not differ between Cas+Serum (47 +/- 2% mean +/- SEM) and Cas (46 +/- 3%) when assessed over the 300-min postprandial period (P = 0.80). The milk matrix did not modulate postprandial myofibrillar protein synthesis rates from 0 to 120 min (0.038 +/- 0.005 vs. 0.031 +/- 0.007%/h) or from 120 to 300 min (0.052 +/- 0.004 vs. 0.067 +/- 0.005%/h) after Cas+Serum vs. Cas. Similarly, no treatment differences in muscle protein-bound L-[1-13C]-phenylalanine enrichments were observed at 120 min (0.003 +/- 0.001 vs. 0.002 +/- 0.001) or 300 min (0.015 +/- 0.002 vs. 0.016 +/- 0.002 mole percent excess) after Cas+Serum vs. Cas. CONCLUSIONS: Casein ingestion in a milk matrix delays protein digestion and absorption but does not modulate postprandial muscle protein synthesis when compared to the ingestion of micellar casein only in healthy older men. This trial was registered at Nederlands Trial Register as NTR4429