HealthyNCT02968888
Anabolic Effects of Whey and Casein After Strength Training in Young and Elderly
A study testing Strength training, Milk 1% and Whey protein concentrate 80 in people with Healthy and Young, run by Norwegian School of Sport Sciences at 1 site in Norway.
Trial summary
The aim of this study is to investigate the acute anabolic effects of native whey, whey protein concentrate 80 (WPC-80) and milk after a bout of strength training in young and elderly. Read more about this study
- Who is it for?
- Ages 18 years and olderHealthy volunteers can take part
- What is being tested?
- Strength training, Milk 1% and Whey protein concentrate 80
- Could I receive a placebo?
- Yes, some participants may receive a placebo
- How many people
- 43 participants
- Where
- 1 siteNorway
- Study dates
- Aug 2014to May 2017
- 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 years and older
- All sexes
- Healthy volunteers accepted
- Adult, Older adult
Who may be able to join
- Healthy in the sense that they can conduct training and testing
- Able to understand Norwegian language written and oral
- Between 18 and 45, or above 70 years of age
Who cannot join
- Diseases or injuries contraindicating participation
- Use of dietary supplements (e.g. proteins, vitamins and creatine)
- Lactose intolerance
- Allergy to milk
- Allergy towards local anesthetics (xylocain)
Trial locations and contacts
1 site in 1 country.
About this study
Official title: Effects of Whey and Casein Supplementation on Acute Anabolic Responses in Muscle After Strength Training in Young and Elderly
The aim of this study is to investigate the acute anabolic effects of native whey, whey protein concentrate 80 (WPC-80) and milk after a bout of strength training in young and elderly. The investigators hypothesize that native whey will give a greater stimulation of muscle protein synthesis and intracellular anabolic signaling than WPC-80, and that WPC-80 will give a stronger stimulus than milk.
Read the detailed description
Increasing or maintaining muscle mass is of great importance for populations ranging from athletes to patients and elderly. Resistance exercise and protein ingestion are two of the most potent stimulators of muscle protein synthesis. Both the physical characteristic of proteins (e.g. different digestion rates of whey and casein) and the amino acid composition, affects the potential of a certain protein to stimulate muscle protein synthesis. Given its superior ability to rapidly increase blood leucine concentrations to high levels, whey is often considered the most potent protein source to stimulate muscle protein synthesis. Native whey protein is produced by filtration of unprocessed milk. Consequently, native whey has different characteristics than WPC-80, which is exposed to heating and acidification. Because of the direct filtration of unprocessed milk, native whey is a more intact protein compared with WPC-80. Of special interest is the higher amounts of the highly anabolic amino acid leucine in native whey.
The higher levels of leucine can be of great interest for elderly individuals as some studies in elderly has shown an anabolic resistance to the effects of protein feeding and strength training. By increasing levels of leucine one might overcome this anabolic resistance in the elderly.
The aim of this double-blinded, randomized, partial cross-over study is to compare the acute fractional protein synthesis and intracellular signaling response to a bout of strength training and intake of 20 grams of protein from either native whey, whey protein concentrate 80 or milk, in young and old individuals. Furthermore, the investigators wil investigate fractional protein breakdown, markers of protein breakdown, amino acid concentrations in blood.
The investigators hypothesize that native whey will induce a greater anabolic response than whey protein concentrate 80, and that whey protein concentrate 80 will give a stronger anabolic response than milk.
- Being tested
- Strength training, Milk 1%, Whey protein concentrate 80, Native whey
What participants receive
What participants receive. In a randomised study each person is assigned to one group by chance.
Strength trainingOther
Milk 1%Dietary supplement
Whey protein concentrate 80Dietary supplement
Native wheyDietary supplement
| Study group | Role | What they receive |
|---|---|---|
| Milk | Placebo comparator | Participants performed a bout of strength training and consumed 20g of milk protein Receives: Other: Strength training; Dietary Supplement: Milk 1% |
| Whey protein concentrate 80 | Experimental | Participants performed a bout of strength training and consumed 20g of whey protein concentrate 80 Receives: Other: Strength training; Dietary Supplement: Whey protein concentrate 80 |
| Native whey | Experimental | Participants performed a bout of strength training and consumed 20g of native whey Receives: Other: Strength training; Dietary Supplement: Native whey |
What is being measured
The primary outcome is the main question the study is designed to answer.
Mixed muscle fractional synthetic rate
A continous infusion of a stable isotope (phe D5) is used to measure incorporation of tracer into muscle (biopsies from m. vastus lateralis)
Measured: Three to one hours prior to a bout of strength training and protein consumption
Mixed muscle fractional synthetic rate
A continous infusion of a stable isotope (phe D5) is used to measure incorporation of tracer into muscle (biopsies from m. vastus lateralis)
Measured: One to five hours after a bout of strength training and protein consumption
Mixed muscle fractional synthetic rate
Two boluses of tracer (phe13C6 and phe15N) was used to measure incorporation of tracer into muscle (biopsies from m. vastus lateralis)
Measured: From three to five hours after a bout of strength training and protein consumption
Mixed muscle fractional breakdown rate
Two boluses of tracer (phe13C6 and phe15N) was used to measure the dilution of tracer in muscle (biopsies from m. vastus lateralis)
Measured: From three to five hours after a bout of strength training and protein consumption
Secondary outcomes (96)
Ratio of phosphorylated to total ribosomal protein S6 kinase beta-1(P70S6K) change from baseline
Biopsies from m. Vastus Lateralis was analyzed by western blot
Measured: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Phosphorylation of phosphorylated to total eukaryotic elongation factor 2 (eEF-2) change from baseline
Biopsies from m. Vastus Lateralis was analyzed by western blot
Measured: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Phosphorylation of phosphorylated to total eukaryotic translation initiation factor 4E-binding protein 1 (4EBP-1) change from baseline
Biopsies from m. Vastus Lateralis was analyzed by western blot
Measured: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Intracellular translocation of forkhead box O3 (FOXO3a) change from baseline
Biopsies from m. Vastus Lateralis was analyzed by western blot
Measured: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Intracellular translocation of muscle RING-finger protein-1 (Murf-1) change from baseline
Biopsies from m. Vastus Lateralis was analyzed by western blot
Measured: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Intracellular translocation of Atrogin1 change from baseline
Biopsies from m. Vastus Lateralis was analyzed by western blot
Measured: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Ubiquitin
Biopsies from m. Vastus Lateralis was analyzed by western blot
Measured: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Plasma amino acid concentration
Measured: 180 and 60 min before, and 45, 60, 75, 120, 160, 180, 200, 220 and 300 min after training and protein intake
Muscle force generating capacity change from baseline
Measured as unilateral isometric knee extension force (Nm) with 90° in the hip and knee joints.
Measured: 15 min before, 15 and 300 min after, and 24 hours after training and protein intake
Plasma glucose
Measured: 180 and 60 min before, and 45, 60, 75, 120, 160, 180, 200, 220 and 300 min after training and protein intake
Plasma insulin
Measured: 180 and 60 min before, and 45, 60, 75, 120, 160, 180, 200, 220 and 300 min after training and protein intake
Serum urea
Measured: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake
Serum ureic acid
Measured: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake
Serum creatine kinase
Measured: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake
Change in ATP-binding cassette transporter (ABCA1) messenger ribonucleic acid (mRNA)
Measured: 1 hour after training and protein intake
Change in ABCA1 mRNA
Measured: 5 hous after training and protein intake
Change in BRCA1-A complex subunit Abraxas (ABRA1) mRNA
Measured: 1 hour after training and protein intake
Change in ABRA1 mRNA
Measured: 5 hours after training and protein intake
Change in alfa-actin (ACTA1) mRNA
Measured: 1 hour after training and protein intake
Change in ACTA1 mRNA
Measured: 5 hours after training and protein intake
Change in C-C motif chemokine 2 (CCL2) mRNA
Measured: 1 hour after training and protein intake
Change in CCL2 mRNA
Measured: 5 hours after training and protein intake
Change in C-C motif chemokine 3 (CCL3) mRNA
Measured: 1 hour after training and protein intake
Change in CCL3 mRNA
Measured: 5 hours after training and protein intake
Change in C-C motif chemokine 5 (CCL5) mRNA
Measured: 1 hour after training and protein intake
Change in CCL5 mRNA
Measured: 5 hours after training and protein intake
Change in C-C motif chemokine 8 (CCL8) mRNA
Measured: 1 hour after training and protein intake
Change in CCL8 mRNA
Measured: 5 hours after training and protein intake
Change in platelet glycoprotein 4 (CD36) mRNA
Measured: 1 hour after training and protein intake
Change in CD36 mRNA
Measured: 5 hours after training and protein intake
Change in cholesterol 25-hydroxylase (CH25H) mRNA
Measured: 1 hour after training and protein intake
Change in CH25H mRNA
Measured: 5 hours after training and protein intake
Change in granulocyte colony-stimulating factor (CSF3) mRNA
Measured: 1 hour after training and protein intake
Change in CSF3 mRNA
Measured: 5 hours after training and protein intake
Change in C-X-C motif chemokine 16 (CXCL16) mRNA
Measured: 1 hour after training and protein intake
Change in CXCL16 mRNA
Measured: 5 hours after training and protein intake
Change in F-box only protein 32 (FBXO32) mRNA
Measured: 1 hour after training and protein intake
Change in FBXO32 mRNA
Measured: 5 hours after training and protein intake
Change in growth-regulated alpha protein (CXCL1) mRNA
Measured: 1 hour after training and protein intake
Change in CXCL1 mRNA
Measured: 5 hours after training and protein intake
Change in matrix metalloproteinase-9 (MMP9) mRNA
Measured: 1 hour after training and protein intake
Change in MMP9 mRNA
Measured: 5 hours after training and protein intake
Change in forkhead box protein O1 (FOXO1) mRNA
Measured: 1 hour after training and protein intake
Change in FOXO1 mRNA
Measured: 5 hours after training and protein intake
Change in forkhead box protein O3 (FOXO3A) mRNA
Measured: 1 hour after training and protein intake
Change in FOXO3A mRNA
Measured: 5 hours after training and protein intake
Change in hepatocyte growth factor (HGF) mRNA
Measured: 1 hour after training and protein intake
Change in HGF mRNA
Measured: 5 hours after training and protein intake
Change in insulin-like growth factor I (IGF1) mRNA
Measured: 1 hour after training and protein intake
Change in IGF1 mRNA
Measured: 5 hours after training and protein intake
Change in interleukin-10 (IL10) mRNA
Measured: 1 hour after training and protein intake
Change in IL10 mRNA
Measured: 5 hours after training and protein intake
Change in interleukin-17D (IL17D) mRNA
Measured: 1 hour after training and protein intake
Change in IL17D mRNA
Measured: 5 hours after training and protein intake
Change in interleukin-1B (IL1B) mRNA
Measured: 1 hour after training and protein intake
Change in IL1B mRNA
Measured: 5 hours after training and protein intake
Change in interleukin-1 receptor antagonist protein (IL1RN) mRNA
Measured: 1 hour after training and protein intake
Change in IL1RN mRNA
Measured: 5 hours after training and protein intake
Change in interleukin-6 (IL6) mRNA
Measured: 1 hour after training and protein intake
Change in IL6 mRNA
Measured: 5 hours after training and protein intake
Change in interleukin-8 (IL8) mRNA
Measured: 1 hour after training and protein intake
Change in IL8 mRNA
Measured: 5 hours after training and protein intake
Change in transcription factor jun-B (JUNB) mRNA
Measured: 1 hour after training and protein intake
Change in JUNB mRNA
Measured: 5 hours after training and protein intake
Change in kit ligand (KITLG) mRNA
Measured: 1 hour after training and protein intake
Change in KITLG mRNA
Measured: 5 hours after training and protein intake
Change in myostatin (MSTN) mRNA
Measured: 1 hour after training and protein intake
Change in MSTN mRNA
Measured: 5 hours after training and protein intake
Change in myosin-1 (MYH1) mRNA
Measured: 1 hour after training and protein intake
Change in MYH1 mRNA
Measured: 5 hours after training and protein intake
Change in myosin-2 (MYH2) mRNA
Measured: 1 hour after training and protein intake
Change in MYH2 mRNA
Measured: 5 hours after training and protein intake
Change in myosin-7 (MYH7) mRNA
Measured: 1 hour after training and protein intake
Change in MYH7 mRNA
Measured: 5 hours after training and protein intake
Change in oxysterols receptor LXR-alpha (NR1H3) mRNA
Measured: 1 hour after training and protein intake
Change in NR1H3 mRNA
Measured: 5 hours after training and protein intake
Change in nuclear receptor subfamily 4 group A member 3 (NR4A3) mRNA
Measured: 1 hour after training and protein intake
Change in NR4A3 mRNA
Measured: 5 hours after training and protein intake
Change in peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PPARGC1A) mRNA
Measured: 1 hour after training and protein intake
Change in PPARGC1A mRNA
Measured: 5 hours after training and protein intake
Change in prostaglandin G/H synthase 2 (PTGS2) mRNA
Measured: 1 hour after training and protein intake
Change in PTGS2 mRNA
Measured: 5 hours after training and protein intake
Change in proton-coupled amino acid transporter 1 (SLC36A1) mRNA
Measured: 1 hour after training and protein intake
Change in SLC36A1 mRNA
Measured: 5 hours after training and protein intake
Change in sodium-coupled neutral amino acid transporter 2 (SLC38A2) mRNA
Measured: 1 hour after training and protein intake
Change in SLC38A2 mRNA
Measured: 5 hours after training and protein intake
Change in 4F2 cell-surface antigen heavy chain (SLC3A2) mRNA
Measured: 1 hour after training and protein intake
Change in SLC3A2 mRNA
Measured: 5 hours after training and protein intake
Change in large neutral amino acids transporter small subunit 1 (SLC7A5) mRNA
Measured: 1 hour after training and protein intake
Change in SLC7A5 mRNA
Measured: 5 hours after training and protein intake
Change in toll-like receptor 2 (TLR2) mRNA
Measured: 1 hour after training and protein intake
Change in TLR2 mRNA
Measured: 5 hours after training and protein intake
Change in tumor necrosis factor (TNF) mRNA
Measured: 1 hour after training and protein intake
Change in TNF mRNA
Measured: 5 hours after training and protein intake
Change in E3 ubiquitin-protein ligase TRIM63 (TRIM63) mRNA
Measured: 1 hour after training and protein intake
Change in E3 ubiquitin-protein ligase TRIM63 (TRIM63) mRNA
Measured: 5 hours after training and protein intake
Timeline
From the start of the study to its completion; the mark is today. Estimated dates are the sponsor’s plan.
- First posted21 Nov 2016 (estimated)
- Study startAug 2014
- Primary completionApr 2015
- Study completionMay 2017
Resources
- Official record on ClinicalTrials.govThe registry entry this page is built from, with its full change history.
- Publications (1)Papers the sponsor has linked to this study.
- Other trials for HealthyStudies of the same condition, open and under way.
- 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
- Crossover
- Masking
- Triple blind
- Who is masked
- Participant, Care provider, Outcomes assessor
- Enrolment
- 43 participants (actual)
Sponsor and investigators
- Lead sponsor
- Norwegian School of Sport Sciences
- Sponsor type
- University, hospital or other
- Collaborators
- Tine, The Research Council of Norway, Arkansas Children's Hospital Research Institute
- Responsible party
- Principal investigator, Havard Hamarsland, Norwegian School of Sport Sciences
IDs, dates and publications
- ClinicalTrials.gov ID
- NCT02968888
- Sponsor's protocol ID
- Tine acute
- Status last verified
- Apr 2018
- First submitted
- 10 Nov 2016
- Last updated
- 10 Apr 2018
- Results posted
- No
- Data monitoring committee
- No
- Individual data sharing
- Undecided
Publications
Hamarsland H, Nordengen AL, Nyvik Aas S, Holte K, Garthe I, Paulsen G, Cotter M, Borsheim E, Benestad HB, Raastad T. Native whey protein with high levels of leucine results in similar post-exercise muscular anabolic responses as regular whey protein: a randomized controlled trial. J Int Soc Sports Nutr. 2017 Nov 21;14:43. doi: 10.1186/s12970-017-0202-y. eCollection 2017.
PubMed 29200982
Study at a glance
From the registry record, last updated by the sponsor on 10 Apr 2018. Recruitment status is as the sponsor reported it: confirm with the study team.
- Official title
- Effects of Whey and Casein Supplementation on Acute Anabolic Responses in Muscle After Strength Training in Young and Elderly
- ClinicalTrials.gov ID
- NCT02968888
- Acronym / sponsor ID
- Tine acute
- Study type
- Interventional
- Recruitment status
- Completed
- Enrolment
- 43 participants (actual)
- Lead sponsor
- Norwegian School of Sport SciencesUniversity, hospital or other
- Collaborators
- Tine, The Research Council of Norway, Arkansas Children's Hospital Research Institute
- Study start
- Aug 2014
- Primary completion
- Apr 2015 (actual)
- Study completion
- May 2017 (actual)
- First posted
- 21 Nov 2016 (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.
The aim of this study is to investigate the acute anabolic effects of native whey, whey protein concentrate 80 (WPC-80) and milk after a bout of strength training in young and elderly. The investigators hypothesize that native whey will give a greater stimulation of muscle protein synthesis and intracellular anabolic signaling than WPC-80, and that WPC-80 will give a stronger stimulus than milk.
Detailed description
Increasing or maintaining muscle mass is of great importance for populations ranging from athletes to patients and elderly. Resistance exercise and protein ingestion are two of the most potent stimulators of muscle protein synthesis. Both the physical characteristic of proteins (e.g. different digestion rates of whey and casein) and the amino acid composition, affects the potential of a certain protein to stimulate muscle protein synthesis. Given its superior ability to rapidly increase blood leucine concentrations to high levels, whey is often considered the most potent protein source to stimulate muscle protein synthesis. Native whey protein is produced by filtration of unprocessed milk. Consequently, native whey has different characteristics than WPC-80, which is exposed to heating and acidification. Because of the direct filtration of unprocessed milk, native whey is a more intact protein compared with WPC-80. Of special interest is the higher amounts of the highly anabolic amino acid leucine in native whey.
The higher levels of leucine can be of great interest for elderly individuals as some studies in elderly has shown an anabolic resistance to the effects of protein feeding and strength training. By increasing levels of leucine one might overcome this anabolic resistance in the elderly.
The aim of this double-blinded, randomized, partial cross-over study is to compare the acute fractional protein synthesis and intracellular signaling response to a bout of strength training and intake of 20 grams of protein from either native whey, whey protein concentrate 80 or milk, in young and old individuals. Furthermore, the investigators wil investigate fractional protein breakdown, markers of protein breakdown, amino acid concentrations in blood.
The investigators hypothesize that native whey will induce a greater anabolic response than whey protein concentrate 80, and that whey protein concentrate 80 will give a stronger anabolic response than milk.
Study design
- Primary purpose
- Basic science
- Allocation
- Randomised
- Intervention model
- Crossover
- Masking
- Triple blind (participant, care provider, outcomes assessor)
- Number of arms
- 3
| Arm | Type | Receives |
|---|---|---|
| Milk | Placebo comparator | Other: Strength training, Dietary Supplement: Milk 1%Participants performed a bout of strength training and consumed 20g of milk protein |
| Whey protein concentrate 80 | Experimental | Other: Strength training, Dietary Supplement: Whey protein concentrate 80Participants performed a bout of strength training and consumed 20g of whey protein concentrate 80 |
| Native whey | Experimental | Other: Strength training, Dietary Supplement: Native wheyParticipants performed a bout of strength training and consumed 20g of native whey |
Who may qualify
- Ages
- 18 years and older
- Sex
- All
- Healthy volunteers
- Accepted
- Age groups
- Adult, Older adult
Key inclusion criteria (3 listed)
- Healthy in the sense that they can conduct training and testing
- Able to understand Norwegian language written and oral
- Between 18 and 45, or above 70 years of age
Key exclusion criteria (5 listed)
- Diseases or injuries contraindicating participation
- Use of dietary supplements (e.g. proteins, vitamins and creatine)
- Lactose intolerance
- Allergy to milk
- Allergy towards local anesthetics (xylocain)
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 |
|---|---|---|
| Strength training | Other | Milk, Native whey, Whey protein concentrate 80 |
| Milk 1% | Dietary supplement | Milk |
| Whey protein concentrate 80 | Dietary supplement | Whey protein concentrate 80 |
| Native whey | Dietary supplement | Native whey |
Primary outcome
Mixed muscle fractional synthetic rate
Time frame: Three to one hours prior to a bout of strength training and protein consumption
A continous infusion of a stable isotope (phe D5) is used to measure incorporation of tracer into muscle (biopsies from m. vastus lateralis)
Mixed muscle fractional synthetic rate
Time frame: One to five hours after a bout of strength training and protein consumption
A continous infusion of a stable isotope (phe D5) is used to measure incorporation of tracer into muscle (biopsies from m. vastus lateralis)
Mixed muscle fractional synthetic rate
Time frame: From three to five hours after a bout of strength training and protein consumption
Two boluses of tracer (phe13C6 and phe15N) was used to measure incorporation of tracer into muscle (biopsies from m. vastus lateralis)
Mixed muscle fractional breakdown rate
Time frame: From three to five hours after a bout of strength training and protein consumption
Two boluses of tracer (phe13C6 and phe15N) was used to measure the dilution of tracer in muscle (biopsies from m. vastus lateralis)
96 secondary outcomes
Ratio of phosphorylated to total ribosomal protein S6 kinase beta-1(P70S6K) change from baseline
Time frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Phosphorylation of phosphorylated to total eukaryotic elongation factor 2 (eEF-2) change from baseline
Time frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Phosphorylation of phosphorylated to total eukaryotic translation initiation factor 4E-binding protein 1 (4EBP-1) change from baseline
Time frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Intracellular translocation of forkhead box O3 (FOXO3a) change from baseline
Time frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Intracellular translocation of muscle RING-finger protein-1 (Murf-1) change from baseline
Time frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Intracellular translocation of Atrogin1 change from baseline
Time frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Ubiquitin
Time frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake
Plasma amino acid concentration
Time frame: 180 and 60 min before, and 45, 60, 75, 120, 160, 180, 200, 220 and 300 min after training and protein intake
Muscle force generating capacity change from baseline
Time frame: 15 min before, 15 and 300 min after, and 24 hours after training and protein intake
Plasma glucose
Time frame: 180 and 60 min before, and 45, 60, 75, 120, 160, 180, 200, 220 and 300 min after training and protein intake
Plasma insulin
Time frame: 180 and 60 min before, and 45, 60, 75, 120, 160, 180, 200, 220 and 300 min after training and protein intake
Serum urea
Time frame: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake
Serum ureic acid
Time frame: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake
Serum creatine kinase
Time frame: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake
Change in ATP-binding cassette transporter (ABCA1) messenger ribonucleic acid (mRNA)
Time frame: 1 hour after training and protein intake
Change in ABCA1 mRNA
Time frame: 5 hous after training and protein intake
Change in BRCA1-A complex subunit Abraxas (ABRA1) mRNA
Time frame: 1 hour after training and protein intake
Change in ABRA1 mRNA
Time frame: 5 hours after training and protein intake
Change in alfa-actin (ACTA1) mRNA
Time frame: 1 hour after training and protein intake
Change in ACTA1 mRNA
Time frame: 5 hours after training and protein intake
Change in C-C motif chemokine 2 (CCL2) mRNA
Time frame: 1 hour after training and protein intake
Change in CCL2 mRNA
Time frame: 5 hours after training and protein intake
Change in C-C motif chemokine 3 (CCL3) mRNA
Time frame: 1 hour after training and protein intake
Change in CCL3 mRNA
Time frame: 5 hours after training and protein intake
Change in C-C motif chemokine 5 (CCL5) mRNA
Time frame: 1 hour after training and protein intake
Change in CCL5 mRNA
Time frame: 5 hours after training and protein intake
Change in C-C motif chemokine 8 (CCL8) mRNA
Time frame: 1 hour after training and protein intake
Change in CCL8 mRNA
Time frame: 5 hours after training and protein intake
Change in platelet glycoprotein 4 (CD36) mRNA
Time frame: 1 hour after training and protein intake
Change in CD36 mRNA
Time frame: 5 hours after training and protein intake
Change in cholesterol 25-hydroxylase (CH25H) mRNA
Time frame: 1 hour after training and protein intake
Change in CH25H mRNA
Time frame: 5 hours after training and protein intake
Change in granulocyte colony-stimulating factor (CSF3) mRNA
Time frame: 1 hour after training and protein intake
Change in CSF3 mRNA
Time frame: 5 hours after training and protein intake
Change in C-X-C motif chemokine 16 (CXCL16) mRNA
Time frame: 1 hour after training and protein intake
Change in CXCL16 mRNA
Time frame: 5 hours after training and protein intake
Change in F-box only protein 32 (FBXO32) mRNA
Time frame: 1 hour after training and protein intake
Change in FBXO32 mRNA
Time frame: 5 hours after training and protein intake
Change in growth-regulated alpha protein (CXCL1) mRNA
Time frame: 1 hour after training and protein intake
Change in CXCL1 mRNA
Time frame: 5 hours after training and protein intake
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 10 Apr 2018.
- Derived from this study: PubMed 29200982Hamarsland H, Nordengen AL, Nyvik Aas S, Holte K, Garthe I, Paulsen G, Cotter M, Borsheim E, Benestad HB, Raastad T. Native whey protein with high levels of leucine results in similar post-exercise muscular anabolic responses as regular whey protein: a randomized controlled trial. J Int Soc Sports Nutr. 2017 Nov 21;14:43. doi: 10.1186/s12970-017-0202-y. eCollection 2017.
- Individual participant dataSharing planned: Undecided
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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.
The record lists no contact. Use the official record to reach the sponsor.
1 site in 1 country: see every site and its status.
Questions about this trial
What is this clinical trial studying?
A study testing Strength training, Milk 1% and Whey protein concentrate 80 in people with Healthy and Young, run by Norwegian School of Sport Sciences at 1 site in Norway.
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 3 inclusion and 5 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 10 Apr 2018. 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 Norway. 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. Some participants in this study may receive a placebo. 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?
Mixed muscle fractional synthetic rate (time frame: Three to one hours prior to a bout of strength training and protein consumption). The study lists 4 primary outcomes in all. It is what the study was designed to measure, not a finding.
Where can I read the original study information?
On the ClinicalTrials.gov record for NCT02968888, which also lists 1 linked publication.
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 10 Apr 2018.