Leucine supplementation of a low-protein mixed macronutrient beverage enhances myofibrillar protein synthesis in young men: a double-blind, randomized trial123

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ABSTRACT

Background:

Leucine is a key amino acid involved in the regulation of skeletal muscle protein synthesis.

Objective:

We assessed the effect of the supplementation of a lower-protein mixed macronutrient beverage with varying doses of leucine or a mixture of branched chain amino acids (BCAAs) on myofibrillar protein synthesis (MPS) at rest and after exercise.

Design:

In a parallel group design, 40 men (21 ± 1 y) completed unilateral knee-extensor resistance exercise before the ingestion of 25 g whey protein (W25) (3.0 g leucine), 6.25 g whey protein (W6) (0.75g leucine), 6.25 g whey protein supplemented with leucine to 3.0 g total leucine (W6+Low-Leu), 6.25 g whey protein supplemented with leucine to 5.0 g total leucine (W6+High-Leu), or 6.25 g whey protein supplemented with leucine, isoleucine, and valine to 5.0 g total leucine. A primed continuous infusion of l-[ring-13C6] phenylalanine with serial muscle biopsies was used to measure MPS under baseline fasted and postprandial conditions in both a rested (response to feeding) and exercised (response to combined feeding and resistance exercise) leg.

Results:

The area under the blood leucine curve was greatest for the W6+High-Leu group compared with the W6 and W6+Low-Leu groups (P < 0.001). In the postprandial period, rates of MPS were increased above baseline over 0–1.5 h in all treatments. Over 1.5–4.5 h, MPS remained increased above baseline after all treatments but was greatest after W25 (∼267%) and W6+High-Leu (∼220%) treatments (P = 0.002).

Conclusions:

A low-protein (6.25 g) mixed macronutrient beverage can be as effective as a high-protein dose (25 g) at stimulating increased MPS rates when supplemented with a high (5.0 g total leucine) amount of leucine. These results have important implications for formulations of protein beverages designed to enhance muscle anabolism. This trial was registered at clinicaltrials.gov as NCT 1530646.

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1

From the Exercise Metabolism Research Group, Departments of Kinesiology (TAC-V, LB, DMDD, AJH, CJM, and SMP) and Neurology (SKB), McMaster University, Hamilton, Canada, and the Nestlé Research Centre, Nestec Ltd, Lausanne, Switzerland (DRM, TS, DB, and EAO).

2

Supported by Nestec Ltd and the Natural Sciences and Engineering Research Council of Canada (postgraduate scholarship to TAC-V).

3

Address correspondence to SM Phillips, McMaster University, 1280 Main Street West, Hamilton, Ontario L8S 4K1, Canada. E-mail: [email protected].

4

Abbreviations used: Akt, protein kinase B; AUCneg, AUC below baseline; AUCpos, AUC above baseline; BCAA, branched-chain amino acid; Cmax, maximum concentration; EAA, essential amino acid; eEF2, eukaryotic elongation factor 2; EX-FED, response to combined feeding and resistance exercise; FED, response to feeding; FSR, fractional synthetic rate; MPS, myofibrillar protein synthesis; mTOR, mechanistic target of rapamycin; Tmax, time of maximum concentration; W6, 6.25 g whey protein; W6+BCAAs, 6.25 g whey protein supplemented with leucine, isoleucine, and valine to 5.0 g total leucine; W6+High-Leu, 6.25 g whey protein supplemented with leucine to 5.0 g total leucine; W6+Low-Leu, 6.25 g whey protein supplemented with leucine to 3.0 g total leucine; W25, 25 g whey protein; 1-RM, single-repetition maximum strength; 4E-BP1, eukaryotic initiation factor 4E binding protein 1.