Greater stimulation of myofibrillar protein synthesis with ingestion of whey protein isolate v. micellar casein at rest and after resistance exercise in elderly men.

We aimed to determine the effect of consuming pure isolated micellar casein or pure whey protein isolate on rates of myofibrillar protein synthesis (MPS) at rest and after resistance exercise in elderly men. Healthy elderly men (72 (sem 1) years; BMI 26·4 (sem 0·7) kg/m²) were divided into two groups (n 7 each) who received a primed, constant infusion of l-[ring-¹³C6]phenylalanine to measure MPS at rest and during 4 h of exercise recovery. Participants performed unilateral leg resistance exercise followed by the consumption of isonitrogenous quantities (20 g) of casein or whey. Blood essential amino acids and leucine concentration peaked 60 min post-drink and were greater in amplitude after whey protein ingestion (both, P < 0·05). MPS in the rested leg was 65 % higher (P = 0·002) after ingestion of whey (0·040 (sem 0·003) %/h) when compared with micellar casein (0·024 (sem 0·002) %/h). Similarly, resistance exercise-stimulated rates of MPS were greater (P < 0·001) after whey ingestion (0·059 (sem 0·005) %/h) v. micellar casein (0·035 (sem 0·002) %/h). We conclude that ingestion of isolated whey protein supports greater rates of MPS than micellar casein both at rest and after resistance exercise in healthy elderly men. This result is probably related to a greater hyperaminoacidaemia or leucinaemia with whey ingestion.

Bolus arginine supplementation affects neither muscle blood flow nor muscle protein synthesis in young men at rest or after resistance exercise.

The aim of this study was to investigate the ergogenic potential of arginine on NO synthesis, muscle blood flow, and skeletal muscle protein synthesis (MPS). Eight healthy young men (22.1 ± 2.6 y, 1.79 ± 0.06 m, 76.6 ± 6.2 kg; mean ± SD) participated in 2 trials where they performed a bout of unilateral leg resistance exercise and ingested a drink containing either 10 g essential amino acids with 10 g l-arginine (ARG) or an isonitrogenous control (CON). Femoral artery blood flow of both the nonexercised and exercised leg was measured continuously using pulsed-wave Doppler ultrasound, while rates of mixed and myofibrillar MPS were determined using a primed continuous infusion of L-[ring-(13)C(6)] or L-[ring-(2)H(5)]phenylalanine. The plasma arginine concentration increased 300% during the ARG trial but not during the CON trial (P < 0.001). Plasma nitrate, nitrite, and endothelin-1, all markers of NO synthesis, did not change during either the ARG or CON trial. Plasma growth hormone increased to a greater degree after exercise in the ARG trial than CON trial (P < 0.05). Femoral artery blood flow increased 270% above basal in the exercised leg (P < 0.001) but not in the nonexercised leg, with no differences between the ARG and CON trials. Mixed and myofibrillar MPS were both greater in the exercised leg compared with the nonexercised leg (P < 0.001), but did not differ between the ARG and CON treatments. We conclude that an oral bolus (10 g) of arginine does not increase NO synthesis or muscle blood flow. Furthermore, arginine does not enhance mixed or myofibrillar MPS either at rest or after resistance exercise beyond that achieved by feeding alone.

Body composition and strength changes in women with milk and resistance exercise.

PURPOSE: We aimed to determine whether women consuming fat-free milk versus isoenergetic carbohydrate after resistance exercise would see augmented gains in lean mass and reductions in fat mass similar to what we observed in young men. METHODS: Young women were randomized to drink either fat-free milk (MILK: n = 10; age (mean +/- SD) = 23.2 +/- 2.8 yr; BMI = 26.2 +/- 4.2 kg x m(-2)) or isoenergetic carbohydrate (CON: n = 10; age = 22.4 +/- 2.4 yr; BMI = 25.2 +/- 3.8 kg x m(-2)) immediately after and 1 h after exercise (2 x 500 mL). Subjects exercised 5 d x wk(-1) for 12 wk. Body composition changes were measured by dual-energy x-ray absorptiometry, and subjects' strength and fasting blood were measured before and after training. RESULTS: CON gained weight after training (CON: +0.86 +/- 0.4 kg, P < 0.05; MILK: +0.50 +/- 0.4 kg, P = 0.29). Lean mass increased with training in both groups (P < 0.01), with a greater net gain in MILK versus CON (1.9 +/- 0.2 vs 1.1 +/- 0.2 kg, respectively, P < 0.01). Fat mass decreased with training in MILK only (-1.6 +/- 0.4 kg, P < 0.01; CON: -0.3 +/- 0.3 kg, P = 0.41). Isotonic strength increased more in MILK than CON (P < 0.05) for some exercises. Serum 25-hydroxyvitamin D increased in both groups but to a greater extent in MILK than CON (+6.5 +/- 1.1 vs +2.8 +/- 1.3 nM, respectively, P < 0.05), and parathyroid hormone decreased only in MILK (-1.2 +/- 0.2 pM, P < 0.01). CONCLUSIONS: Heavy, whole-body resistance exercise with the consumption of milk versus carbohydrate in the early postexercise period resulted in greater muscle mass accretion, strength gains, fat mass loss, and a possible reduction in bone turnover in women after 12 wk. Our results, similar to those in men, highlight that milk is an effective drink to support favorable body composition changes in women with resistance training.

The role of milk- and soy-based protein in support of muscle protein synthesis and muscle protein accretion in young and elderly persons.

The balance between muscle protein synthesis (MPS) and muscle protein breakdown (MPB) is dependent on protein consumption and the accompanying hyperaminoacidemia, which stimulates a marked rise in MPS and mild suppression of MPB. In the fasting state, however, MPS declines sharply and MPB is increased slightly. Ultimately, the balance between MPS and MPB determines the net rate of muscle growth. Accretion of new muscle mass beyond that of normal growth can occur following periods of intense resistance exercise. Such muscle accretion is an often sought-after goal of athletes. There needs to be, however, an increased appreciation of the role that preservation of muscle can play in offsetting morbidities associated with the sarcopenia of aging, such as type 2 diabetes and declines in metabolic rate that can lead to fat mass accumulation followed by the onset or progression of obesity. Emerging evidence shows that consumption of different types of proteins can have different stimulatory effects on the amplitude and possibly duration that MPS is elevated after feeding; this may be particularly significant after resistance exercise. This effect may be due to differences in the fundamental amino acid composition of the protein (i.e., its amino acid score) and its rate of digestion. Milk proteins, specifically casein and whey, are the highest quality proteins and are quite different in terms of their rates of digestion and absorption. New data suggest that whey protein is better able to support MPS than is soy protein, a finding that may explain the greater ability of whey protein to support greater net muscle mass gains with resistance exercise. This review focuses on evidence showing the differences in responses of MPS, and ultimately muscle protein accretion, to consumption of milk- and soy-based supplemental protein sources in humans.

Immobilization induces anabolic resistance in human myofibrillar protein synthesis with low and high dose amino acid infusion.

We tested the hypothesis that increasing blood amino acid (AA) availability would counter the physical inactivity-induced reduction in muscle protein synthesis. We determined how 14 days of unilateral knee immobilization affected quadriceps myofibrillar protein synthesis (MPS) in young healthy subjects (10 men, 2 women, 21 +/- 1 years; 80.2 +/- 4.0 kg, mean +/- S.E.M.) in the post-absorptive state and after infusing AA (10% Primene) at low or high doses (43 and 261 mg kg(-1) h(-1)). Muscle cross-sectional area (MRI) and peak isometric torque declined in the immobilized leg (-5.0 +/- 1.2% and -25 +/- 3%, respectively, both P < 0.005), but were unchanged (all P > 0.6) in the non-immobilized leg. Immobilization induced a 27% decline in the rate of post-absorptive MPS (immobilized, 0.027 +/- 0.003: non-immobilized, 0.037 +/- 0.003% h(-1); P < 0.001). Regardless of dose, AA infusion stimulated a greater rise in MPS in the non-immobilized legs; at 4 h MPS was greater by +54 +/- 12% with low dose and +68 +/- 17% with high dose AA infusion (both P < 0.001). There was some evidence of delayed responsiveness of phosphorylation of Akt to high doses of AA and p70S6k at both doses but no marked differences in that of mTOR, GSK3beta or eEF2. Phosphorylation of focal adhesion kinase (Tyr(576/577)) was reduced (P < 0.05) with immobilization. We observed no change in polyubiquitinated protein content after immobilization. We confirm that 14 days of immobilization reduces MPS in the post-absorptive state and this diminution is reduced but not abolished by increased provision of AA, even at high rates. The immobilization-induced decline in post-absorptive MPS with the 'anabolic resistance' to amino acids can account for much of immobilization-induced muscle atrophy.

Minimal whey protein with carbohydrate stimulates muscle protein synthesis following resistance exercise in trained young men.

Whey protein is a supplemental protein source often used by athletes, particularly those aiming to gain muscle mass; however, direct evidence for its efficacy in stimulating muscle protein synthesis (MPS) is lacking. We aimed to determine the impact of consuming whey protein on skeletal muscle protein turnover in the post-exercise period. Eight healthy resistance-trained young men (age=21+/-1 .0 years; BMI=26.8+/-0.9 kg/m2 (means+/-SE)) participated in a double-blind randomized crossover trial in which they performed a unilateral leg resistance exercise workout (EX: 4 sets of knee extensions and 4 sets of leg press; 8-10 repetitions/set; 80% of maximal), such that one leg was not exercised and acted as a rested (RE) comparator. After exercise, subjects consumed either an isoenergetic whey protein plus carbohydrate beverage (WHEY: 10 g protein and 21 g fructose) or a carbohydrate-only beverage (CHO: 21 g fructose and 10 g maltodextran). Subjects received pulse-tracer injections of L-[ring-2H5]phenylalanine and L-[15N]phenylalanine to measure MPS. Exercise stimulated a rise in MPS in the WHEY-EX and CHO-EX legs, which were greater than MPS in the WHEY-RE leg and the CHO-RE leg (all p<0.05), respectively. The rate of MPS in the WHEY-EX leg was greater than in the CHO-EX leg (p<0.001). We conclude that a small dose (10 g) of whey protein with carbohydrate (21 g) can stimulate a rise in MPS after resistance exercise in trained young men that would be supportive of a positive net protein balance, which, over time, would lead to hypertrophy.