Effect of Supplementing a Mixed Macronutrient Beverage With Graded Doses of Leucine on Myofibrillar Protein Synthesis

NCT01885429 · Status: COMPLETED · Phase: NA · Type: INTERVENTIONAL · Enrollment: 40

Last updated 2013-07-30

No results posted yet for this study

Summary

Muscle mass is normally maintained through the regulated balance between the processes of protein synthesis (i.e. making new muscle proteins) and protein breakdown (breaking down old muscle proteins). Proteins are composed of amino acids and we know that amino acids increase muscle protein synthesis. However, not all amino acids are the same. Essential amino acids are ones that must be consumed through food, while non-essential amino acids can be made by our body. Interestingly, the essential amino acids are all that are required to increase the rate of muscle protein synthesis. In addition, the essential amino acid leucine appears to be particularly important in regulating protein synthesis. However, how leucine is able to increase protein synthesis is not entirely understood. Previously, it has been shown that 20-25 g of high-quality protein, such as that found in milk (whey), appears to be the amount of protein that maximizes the rate of muscle protein synthesis after performing a bout of resistance exercise. Thus, we aim to measure the synthesis of new muscle proteins after ingesting different amounts of protein and amino acids. We will measure muscle protein synthesis after consumption of the beverage a participant is randomized to in a leg that has done no exercise ( ie. a rested leg) and in the other leg that has done resistance exercise. Amino acids are 'strung-together' to make protein. The 'essential' amino acids must be consumed through food because our body cannot make them, thus they are consumed when you eat protein rich foods like milk or chicken. Leucine, isoleucine, and valine are simply 3 of the 8 essential amino acids that make up dietary protein. Unlike essential amino acids, 'non-essential' amino acids may be synthesized by the body, however they are also present in protein rich foods like chicken or milk. We aim to determine if it is the leucine content found in 25 g of whey protein that is primarily responsible for maximizing muscle protein synthesis at rest and following resistance exercise. We also wish to determine how muscle genes and metabolism respond to this protocol.

Conditions

  • Muscle Protein Synthesis

Interventions

DIETARY_SUPPLEMENT

Positive Control

Subject consumes 25g of whey protein following unilateral exercise

DIETARY_SUPPLEMENT

Negative Control

Subject consumes 6.25g of whey protein following unilateral exercise

DIETARY_SUPPLEMENT

Low Protein Low Leucine Spike

Subject consumes 6.25g of whey protein plus 3g of leucine following unilateral exercise

DIETARY_SUPPLEMENT

Low Protein High Leucine Spike

Subject consumes 6.25g of whey protein plus 5g of leucine following unilateral exercise

DIETARY_SUPPLEMENT

Low Protein + High Leucine + BCAA Spike

Subject consumes 6.25g of whey protein plus 5g of leucine plus valine and isoleucine (BCAA) following unilateral exercise

Sponsors & Collaborators

Principal Investigators

  • Stuart M Phillips, PhD · McMaster University

Study Design

Allocation
RANDOMIZED
Purpose
BASIC_SCIENCE
Masking
DOUBLE
Model
PARALLEL

Eligibility

Min Age
18 Years
Max Age
35 Years
Sex
MALE
Healthy Volunteers
Yes

Timeline & Regulatory

Start
2011-01-31
Primary Completion
2011-05-31
Completion
2011-05-31

Countries

  • Canada

Study Locations

More Related Trials

Entities

Read the full study record

This page highlights key information. For complete eligibility criteria, study locations, investigator contacts, and the full protocol, visit the original record on ClinicalTrials.gov.

View NCT01885429 on ClinicalTrials.gov