Muscle Protein SynthesisNCT01885429
Effect of Supplementing a Mixed Macronutrient Beverage With Graded Doses of Leucine on Myofibrillar Protein Synthesis
A study testing Low Protein Low Leucine Spike, Low Protein High Leucine Spike and Low Protein + High Leucine + BCAA Spike in people with Muscle Protein Synthesis, run by McMaster University at 1 site in Canada.
Trial 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. Read more about this study
- Who is it for?
- Ages 18 to 35 years, men onlyHealthy volunteers can take part
- Conditions the study is for
- Muscle Protein Synthesis
- What is being tested?
- Low Protein Low Leucine Spike, Low Protein High Leucine Spike and Low Protein + High Leucine + BCAA Spike
- Could I receive a placebo?
- No, everyone receives an active treatment
- How many people
- 40 participants
- Where
- 1 siteCanada
- Study dates
- Jan 2011to May 2011
- Phase
- Interventional
- Are there results?
- None posted in the registry
Key requirements
Who can take part, as listed by the sponsor. Only the study team can confirm whether you are eligible, so take this list to your doctor.
- Ages 18 to 35 years
- Men only
- Healthy volunteers accepted
- Adult
Who may be able to join
- Male
- Healthy and physically active (as determined by medical and activity questionnaire)
- 18-35 years of age
- 70-90 kg body mass
- Having given informed consent
Who cannot join
- Exhibiting health risk factors as identified on the health screening questionnaire
- Having any identified metabolic or intestinal disorders
- Tobacco use
- Aspirin use in the 4 days prior to the experimental trial
- Consumption of prescription medications or any performance enhancing agent
- Inability to endure the strenuous exercise bouts e.g. injuries
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- Alcohol intake during the 48 hours prior to each of the testing days
- Currently participating or having participated in another clinical trial during the last 4 weeks prior to the beginning of this study
- Have given blood in the last three weeks
- Verbal confirmation that they have used a substance on the WADA banned list within the last year
Trial locations and contacts
1 site in 1 country.
About this study
Official title: The Effect of a Leucine 'Spike' of a Sub-optimal Protein Dose on Acute Muscle Protein Synthesis
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.
Read the detailed description
The processes of muscle protein synthesis (MPS) and muscle protein breakdown (MPB) occur concurrently. This constant protein turnover allows the muscle fiber to change its protein structure if loading demands or diet changes. The plasticity of skeletal muscle to respond to altered loading and contractile patterns is evidence of the capacity for remodeling that a fiber can undergo. It is quite well documented for example that mitochondrial content increases with endurance-type work. In contrast, heavier loading leads to less change in mitochondrial content but increases in myofibrillar proteins. All of the aforementioned phenotypic adaptations represent a re-patterning of the muscle's genetic expression patterns, protein translation, and processes for breakdown of existing protein structures to 'insert' the new proteins. A persistent muscle protein turnover also provides for a constant mechanism of protein 'maintenance' by removing damaged proteins and replacing them with new proteins. Damage to proteins can come about through oxidation or simply mechanical damage due to high forces during lengthening contractions. Regardless of the mechanism the balance between the processes of muscle protein synthesis (MPS) and muscle protein breakdown (MPB) will determine the net gain, loss, or no change of proteins in the myofiber.
- Conditions
- Muscle Protein Synthesis
- Being tested
- Positive Control, Negative Control, Low Protein Low Leucine Spike, Low Protein High Leucine Spike, Low Protein + High Leucine + BCAA Spike
- Keywords
- Protein Turnover, Resistance Exercise, Whey Protein, Leucine
What participants receive
What participants receive. In a randomised study each person is assigned to one group by chance.
Positive ControlDietary supplement
Subject consumes 25g of whey protein following unilateral exercise
Negative ControlDietary supplement
Subject consumes 6.25g of whey protein following unilateral exercise
Low Protein Low Leucine SpikeDietary supplement
Subject consumes 6.25g of whey protein plus 3g of leucine following unilateral exercise
Low Protein High Leucine SpikeDietary supplement
Subject consumes 6.25g of whey protein plus 5g of leucine following unilateral exercise
Low Protein + High Leucine + BCAA SpikeDietary supplement
Subject consumes 6.25g of whey protein plus 5g of leucine plus valine and isoleucine (BCAA) following unilateral exercise
| Study group | Role | What they receive |
|---|---|---|
| Positive Control | Experimental | Group 1 (Positive(+) Control) will receive: 25g of whey protein. Positive Control Receives: Dietary Supplement: Positive Control |
| Negative Control | Experimental | Group 2 (Negative(-) Control) will receive: 6.25g whey. Negative Control Receives: Dietary Supplement: Negative Control |
| Low Protein + Low Leucine Spike | Experimental | Group 3 (Low Protein + Low Leucine Spike) will receive: 6.25g whey + low added leucine. Low Protein Low Leucine Spike Receives: Dietary Supplement: Low Protein Low Leucine Spike |
| Low Protein + High Leucine Spike | Experimental | Group 4 (Low Protein + High Leucine Spike) will receive: 6.25g whey + high added leucine. Low Protein High Leucine Spike Receives: Dietary Supplement: Low Protein High Leucine Spike |
| Low Protein + High Leucine + BCAA Spike | Experimental | Group 5 (Low Protein + High Leucine + BCAA Spike) will receive: 6.25g whey + added branched-chain amino acids. Low Protein + High Leucine + BCAA Spike Receives: Dietary Supplement: Low Protein + High Leucine + BCAA Spike |
What is being measured
The primary outcome is the main question the study is designed to answer.
Change from baseline in myofibrillar protein synthesis
Myofibrillar protein synthesis will be determined by the standard precursor-product method as described previously and routinely measured and published.
Measured: In the first 1.5h after exercise/feeding and from 1.5-4.5h after exercise/feeding
Timeline
From the start of the study to its completion; the mark is today. Estimated dates are the sponsor’s plan.
- First posted25 Jun 2013 (estimated)
- Study startJan 2011
- Primary completionMay 2011
- Study completionMay 2011
Resources
- Official record on ClinicalTrials.govThe registry entry this page is built from, with its full change history.
- Other trials for Muscle Protein SynthesisStudies of the same condition, open and under way.
- More trials run by McMaster UniversityThe sponsor's other registered studies.
- What the trial phases meanHow a treatment moves from first tests in people to approval.
More details
For doctors and researchers: how the study is designed, who runs it, and its registry IDs.
Study design
- Study type
- Interventional
- Phase
- Phase N/A
- Primary purpose
- Basic science
- Allocation
- Randomised
- Intervention model
- Parallel groups
- Masking
- Double blind
- Who is masked
- Participant, Investigator
- Enrolment
- 40 participants (actual)
Sponsor and investigators
- Lead sponsor
- McMaster University
- Sponsor type
- University, hospital or other
- Responsible party
- Sponsor
- Investigators
- Stuart M Phillips, PhD, Principal investigator, McMaster University
IDs, dates and publications
- ClinicalTrials.gov ID
- NCT01885429
- Sponsor's protocol ID
- 10.32.NRC
- Status last verified
- Jul 2013
- First submitted
- 23 Apr 2013
- Last updated
- 30 Jul 2013
- Results posted
- No
- Data monitoring committee
- No
Study at a glance
From the registry record, last updated by the sponsor on 30 Jul 2013. Recruitment status is as the sponsor reported it: confirm with the study team.
- Official title
- The Effect of a Leucine 'Spike' of a Sub-optimal Protein Dose on Acute Muscle Protein Synthesis
- ClinicalTrials.gov ID
- NCT01885429
- Acronym / sponsor ID
- 10.32.NRC
- Conditions
- Muscle Protein Synthesis
- Keywords
- Protein Turnover, Resistance Exercise, Whey Protein, Leucine
- Study type
- Interventional
- Recruitment status
- Completed
- Enrolment
- 40 participants (actual)
- Lead sponsor
- McMaster UniversityUniversity, hospital or other
- Study start
- Jan 2011
- Primary completion
- May 2011 (actual)
- Study completion
- May 2011 (actual)
- First posted
- 25 Jun 2013 (estimated)
- Results
- Not posted in the source record
Clinical summary
The research question as the sponsor registered it. This describes what the study plans to test, not what it found.
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.
Detailed description
The processes of muscle protein synthesis (MPS) and muscle protein breakdown (MPB) occur concurrently. This constant protein turnover allows the muscle fiber to change its protein structure if loading demands or diet changes. The plasticity of skeletal muscle to respond to altered loading and contractile patterns is evidence of the capacity for remodeling that a fiber can undergo. It is quite well documented for example that mitochondrial content increases with endurance-type work. In contrast, heavier loading leads to less change in mitochondrial content but increases in myofibrillar proteins. All of the aforementioned phenotypic adaptations represent a re-patterning of the muscle's genetic expression patterns, protein translation, and processes for breakdown of existing protein structures to 'insert' the new proteins. A persistent muscle protein turnover also provides for a constant mechanism of protein 'maintenance' by removing damaged proteins and replacing them with new proteins. Damage to proteins can come about through oxidation or simply mechanical damage due to high forces during lengthening contractions. Regardless of the mechanism the balance between the processes of muscle protein synthesis (MPS) and muscle protein breakdown (MPB) will determine the net gain, loss, or no change of proteins in the myofiber.
Study design
- Primary purpose
- Basic science
- Allocation
- Randomised
- Intervention model
- Parallel groups
- Masking
- Double blind (participant, investigator)
- Number of arms
- 5
| Arm | Type | Receives |
|---|---|---|
| Positive Control | Experimental | Dietary Supplement: Positive ControlGroup 1 (Positive(+) Control) will receive: 25g of whey protein. Positive Control |
| Negative Control | Experimental | Dietary Supplement: Negative ControlGroup 2 (Negative(-) Control) will receive: 6.25g whey. Negative Control |
| Low Protein + Low Leucine Spike | Experimental | Dietary Supplement: Low Protein Low Leucine SpikeGroup 3 (Low Protein + Low Leucine Spike) will receive: 6.25g whey + low added leucine. Low Protein Low Leucine Spike |
| Low Protein + High Leucine Spike | Experimental | Dietary Supplement: Low Protein High Leucine SpikeGroup 4 (Low Protein + High Leucine Spike) will receive: 6.25g whey + high added leucine. Low Protein High Leucine Spike |
| Low Protein + High Leucine + BCAA Spike | Experimental | Dietary Supplement: Low Protein + High Leucine + BCAA SpikeGroup 5 (Low Protein + High Leucine + BCAA Spike) will receive: 6.25g whey + added branched-chain amino acids. Low Protein + High Leucine + BCAA Spike |
Who may qualify
- Ages
- 18 to 35 years
- Sex
- Male only
- Healthy volunteers
- Accepted
- Age groups
- Adult
Key inclusion criteria (5 listed)
- Male
- Healthy and physically active (as determined by medical and activity questionnaire)
- 18-35 years of age
- 70-90 kg body mass
- Having given informed consent
Key exclusion criteria (10 listed)
- Exhibiting health risk factors as identified on the health screening questionnaire
- Having any identified metabolic or intestinal disorders
- Tobacco use
- Aspirin use in the 4 days prior to the experimental trial
- Consumption of prescription medications or any performance enhancing agent
Eligibility is decided by the study team after screening; this overview does not establish that a patient qualifies. Full inclusion and exclusion criteria.
Interventions
| Intervention | Type | Arms |
|---|---|---|
| Positive ControlSubject consumes 25g of whey protein following unilateral exercise | Dietary supplement | Positive Control |
| Negative ControlSubject consumes 6.25g of whey protein following unilateral exercise | Dietary supplement | Negative Control |
| Low Protein Low Leucine SpikeSubject consumes 6.25g of whey protein plus 3g of leucine following unilateral exercise | Dietary supplement | Low Protein + Low Leucine Spike |
| Low Protein High Leucine SpikeSubject consumes 6.25g of whey protein plus 5g of leucine following unilateral exercise | Dietary supplement | Low Protein + High Leucine Spike |
| Low Protein + High Leucine + BCAA SpikeSubject consumes 6.25g of whey protein plus 5g of leucine plus valine and isoleucine (BCAA) following unilateral exercise | Dietary supplement | Low Protein + High Leucine + BCAA Spike |
Primary outcome
Change from baseline in myofibrillar protein synthesis
Time frame: In the first 1.5h after exercise/feeding and from 1.5-4.5h after exercise/feeding
Myofibrillar protein synthesis will be determined by the standard precursor-product method as described previously and routinely measured and published.
Results and safety
The study is completed, but results are not available in the source record. That does not mean the treatment did or did not work.
Research links
- Official record on ClinicalTrials.govLast updated by the sponsor 30 Jul 2013.
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Referral and contact
AzTrials does not enrol participants or take referrals. Contact the study team or a site listed below; they decide who can take part. This study is not recruiting at the moment.
Stuart M Phillips, PhD principal investigator
McMaster University
1 site in 1 country: see every site and its status.
Questions about this trial
What is this clinical trial studying?
A study testing Low Protein Low Leucine Spike, Low Protein High Leucine Spike and Low Protein + High Leucine + BCAA Spike in people with Muscle Protein Synthesis, run by McMaster University at 1 site in Canada.
The full registered description is in the About this study section and the official record.
Who may be eligible to take part?
The sponsor lists 5 inclusion and 10 exclusion criteria. Eligibility is decided by the study team after screening, so read the full criteria and contact a listed site.
Is this clinical trial currently recruiting?
The record says: finished, as of the sponsor's last update on 30 Jul 2013. Status can change between updates, so confirm with the study contact before making plans.
Where is the study taking place?
The record lists 1 site in Canada. Whether a site is taking part right now should be confirmed with that site. See every site.
What are the possible benefits and risks?
They depend on the study and the treatment, and no study can promise a benefit. The study team explains the known risks during informed consent, before anyone joins; the record itself does not list them.
Are results available for this study?
The study is completed, but results are not available in the source record. That does not mean the treatment did or did not work.
How can a doctor refer a patient or contact the research team?
The record lists no contact. The official record names the sponsor, who can be asked directly. AzTrials does not enrol participants or take referrals.
What does the primary outcome measure?
Change from baseline in myofibrillar protein synthesis (time frame: In the first 1.5h after exercise/feeding and from 1.5-4.5h after exercise/feeding). It is what the study was designed to measure, not a finding.
Where can I read the original study information?
Does a listing mean the treatment is approved or proven to work?
No. A listing means the study is registered. It does not show that the treatment is safe, works, or is approved by a regulator.
How often is this information updated?
AzTrials copies changed records from ClinicalTrials.gov every night and reloads the whole registry every week. The sponsor last updated this record on 30 Jul 2013.