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Anabolic Effects of Whey and Casein After Strength Training in Young and Elderly

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ClinicalTrials.gov Identifier: NCT02968888
Recruitment Status : Completed
First Posted : November 21, 2016
Last Update Posted : April 10, 2018
Sponsor:
Collaborators:
Tine
The Research Council of Norway
Arkansas Children's Hospital Research Institute
Information provided by (Responsible Party):
Havard Hamarsland, Norwegian School of Sport Sciences

Brief 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. 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.

Condition or disease Intervention/treatment Phase
Healthy Young Elderly Other: Strength training Dietary Supplement: Milk 1% Dietary Supplement: Whey protein concentrate 80 Dietary Supplement: Native whey Not Applicable

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.


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Study Type : Interventional  (Clinical Trial)
Actual Enrollment : 43 participants
Allocation: Randomized
Intervention Model: Crossover Assignment
Masking: Triple (Participant, Care Provider, Outcomes Assessor)
Primary Purpose: Basic Science
Official Title: Effects of Whey and Casein Supplementation on Acute Anabolic Responses in Muscle After Strength Training in Young and Elderly
Study Start Date : August 2014
Actual Primary Completion Date : April 2015
Actual Study Completion Date : May 2017

Resource links provided by the National Library of Medicine

Drug Information available for: Casein

Arm Intervention/treatment
Placebo Comparator: Milk
Participants performed a bout of strength training and consumed 20g of milk protein
Other: Strength training
Dietary Supplement: Milk 1%
Experimental: Whey protein concentrate 80
Participants performed a bout of strength training and consumed 20g of whey protein concentrate 80
Other: Strength training
Dietary Supplement: Whey protein concentrate 80
Experimental: Native whey
Participants performed a bout of strength training and consumed 20g of native whey
Other: Strength training
Dietary Supplement: Native whey



Primary Outcome Measures :
  1. 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)

  2. 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)

  3. 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)

  4. 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)


Secondary Outcome Measures :
  1. 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 ]
    Biopsies from m. Vastus Lateralis was analyzed by western blot

  2. 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 ]
    Biopsies from m. Vastus Lateralis was analyzed by western blot

  3. 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 ]
    Biopsies from m. Vastus Lateralis was analyzed by western blot

  4. 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 ]
    Biopsies from m. Vastus Lateralis was analyzed by western blot

  5. 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 ]
    Biopsies from m. Vastus Lateralis was analyzed by western blot

  6. Intracellular translocation of Atrogin1 change from baseline [ Time Frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake ]
    Biopsies from m. Vastus Lateralis was analyzed by western blot

  7. Ubiquitin [ Time Frame: 30 min before, 1, 2.5 and 5 hours after training and protein intake ]
    Biopsies from m. Vastus Lateralis was analyzed by western blot

  8. 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 ]
  9. 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 ]
    Measured as unilateral isometric knee extension force (Nm) with 90° in the hip and knee joints.

  10. 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 ]
  11. 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 ]
  12. Serum urea [ Time Frame: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake ]
  13. Serum ureic acid [ Time Frame: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake ]
  14. Serum creatine kinase [ Time Frame: 180 and 60 min before, and 60, 10, 180 and 300 min after training and protein intake ]
  15. Change in ATP-binding cassette transporter (ABCA1) messenger ribonucleic acid (mRNA) [ Time Frame: 1 hour after training and protein intake ]
  16. Change in ABCA1 mRNA [ Time Frame: 5 hous after training and protein intake ]
  17. Change in BRCA1-A complex subunit Abraxas (ABRA1) mRNA [ Time Frame: 1 hour after training and protein intake ]
  18. Change in ABRA1 mRNA [ Time Frame: 5 hours after training and protein intake ]
  19. Change in alfa-actin (ACTA1) mRNA [ Time Frame: 1 hour after training and protein intake ]
  20. Change in ACTA1 mRNA [ Time Frame: 5 hours after training and protein intake ]
  21. Change in C-C motif chemokine 2 (CCL2) mRNA [ Time Frame: 1 hour after training and protein intake ]
  22. Change in CCL2 mRNA [ Time Frame: 5 hours after training and protein intake ]
  23. Change in C-C motif chemokine 3 (CCL3) mRNA [ Time Frame: 1 hour after training and protein intake ]
  24. Change in CCL3 mRNA [ Time Frame: 5 hours after training and protein intake ]
  25. Change in C-C motif chemokine 5 (CCL5) mRNA [ Time Frame: 1 hour after training and protein intake ]
  26. Change in CCL5 mRNA [ Time Frame: 5 hours after training and protein intake ]
  27. Change in C-C motif chemokine 8 (CCL8) mRNA [ Time Frame: 1 hour after training and protein intake ]
  28. Change in CCL8 mRNA [ Time Frame: 5 hours after training and protein intake ]
  29. Change in platelet glycoprotein 4 (CD36) mRNA [ Time Frame: 1 hour after training and protein intake ]
  30. Change in CD36 mRNA [ Time Frame: 5 hours after training and protein intake ]
  31. Change in cholesterol 25-hydroxylase (CH25H) mRNA [ Time Frame: 1 hour after training and protein intake ]
  32. Change in CH25H mRNA [ Time Frame: 5 hours after training and protein intake ]
  33. Change in granulocyte colony-stimulating factor (CSF3) mRNA [ Time Frame: 1 hour after training and protein intake ]
  34. Change in CSF3 mRNA [ Time Frame: 5 hours after training and protein intake ]
  35. Change in C-X-C motif chemokine 16 (CXCL16) mRNA [ Time Frame: 1 hour after training and protein intake ]
  36. Change in CXCL16 mRNA [ Time Frame: 5 hours after training and protein intake ]
  37. Change in F-box only protein 32 (FBXO32) mRNA [ Time Frame: 1 hour after training and protein intake ]
  38. Change in FBXO32 mRNA [ Time Frame: 5 hours after training and protein intake ]
  39. Change in growth-regulated alpha protein (CXCL1) mRNA [ Time Frame: 1 hour after training and protein intake ]
  40. Change in CXCL1 mRNA [ Time Frame: 5 hours after training and protein intake ]
  41. Change in matrix metalloproteinase-9 (MMP9) mRNA [ Time Frame: 1 hour after training and protein intake ]
  42. Change in MMP9 mRNA [ Time Frame: 5 hours after training and protein intake ]
  43. Change in forkhead box protein O1 (FOXO1) mRNA [ Time Frame: 1 hour after training and protein intake ]
  44. Change in FOXO1 mRNA [ Time Frame: 5 hours after training and protein intake ]
  45. Change in forkhead box protein O3 (FOXO3A) mRNA [ Time Frame: 1 hour after training and protein intake ]
  46. Change in FOXO3A mRNA [ Time Frame: 5 hours after training and protein intake ]
  47. Change in hepatocyte growth factor (HGF) mRNA [ Time Frame: 1 hour after training and protein intake ]
  48. Change in HGF mRNA [ Time Frame: 5 hours after training and protein intake ]
  49. Change in insulin-like growth factor I (IGF1) mRNA [ Time Frame: 1 hour after training and protein intake ]
  50. Change in IGF1 mRNA [ Time Frame: 5 hours after training and protein intake ]
  51. Change in interleukin-10 (IL10) mRNA [ Time Frame: 1 hour after training and protein intake ]
  52. Change in IL10 mRNA [ Time Frame: 5 hours after training and protein intake ]
  53. Change in interleukin-17D (IL17D) mRNA [ Time Frame: 1 hour after training and protein intake ]
  54. Change in IL17D mRNA [ Time Frame: 5 hours after training and protein intake ]
  55. Change in interleukin-1B (IL1B) mRNA [ Time Frame: 1 hour after training and protein intake ]
  56. Change in IL1B mRNA [ Time Frame: 5 hours after training and protein intake ]
  57. Change in interleukin-1 receptor antagonist protein (IL1RN) mRNA [ Time Frame: 1 hour after training and protein intake ]
  58. Change in IL1RN mRNA [ Time Frame: 5 hours after training and protein intake ]
  59. Change in interleukin-6 (IL6) mRNA [ Time Frame: 1 hour after training and protein intake ]
  60. Change in IL6 mRNA [ Time Frame: 5 hours after training and protein intake ]
  61. Change in interleukin-8 (IL8) mRNA [ Time Frame: 1 hour after training and protein intake ]
  62. Change in IL8 mRNA [ Time Frame: 5 hours after training and protein intake ]
  63. Change in transcription factor jun-B (JUNB) mRNA [ Time Frame: 1 hour after training and protein intake ]
  64. Change in JUNB mRNA [ Time Frame: 5 hours after training and protein intake ]
  65. Change in kit ligand (KITLG) mRNA [ Time Frame: 1 hour after training and protein intake ]
  66. Change in KITLG mRNA [ Time Frame: 5 hours after training and protein intake ]
  67. Change in myostatin (MSTN) mRNA [ Time Frame: 1 hour after training and protein intake ]
  68. Change in MSTN mRNA [ Time Frame: 5 hours after training and protein intake ]
  69. Change in myosin-1 (MYH1) mRNA [ Time Frame: 1 hour after training and protein intake ]
  70. Change in MYH1 mRNA [ Time Frame: 5 hours after training and protein intake ]
  71. Change in myosin-2 (MYH2) mRNA [ Time Frame: 1 hour after training and protein intake ]
  72. Change in MYH2 mRNA [ Time Frame: 5 hours after training and protein intake ]
  73. Change in myosin-7 (MYH7) mRNA [ Time Frame: 1 hour after training and protein intake ]
  74. Change in MYH7 mRNA [ Time Frame: 5 hours after training and protein intake ]
  75. Change in oxysterols receptor LXR-alpha (NR1H3) mRNA [ Time Frame: 1 hour after training and protein intake ]
  76. Change in NR1H3 mRNA [ Time Frame: 5 hours after training and protein intake ]
  77. Change in nuclear receptor subfamily 4 group A member 3 (NR4A3) mRNA [ Time Frame: 1 hour after training and protein intake ]
  78. Change in NR4A3 mRNA [ Time Frame: 5 hours after training and protein intake ]
  79. Change in peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PPARGC1A) mRNA [ Time Frame: 1 hour after training and protein intake ]
  80. Change in PPARGC1A mRNA [ Time Frame: 5 hours after training and protein intake ]
  81. Change in prostaglandin G/H synthase 2 (PTGS2) mRNA [ Time Frame: 1 hour after training and protein intake ]
  82. Change in PTGS2 mRNA [ Time Frame: 5 hours after training and protein intake ]
  83. Change in proton-coupled amino acid transporter 1 (SLC36A1) mRNA [ Time Frame: 1 hour after training and protein intake ]
  84. Change in SLC36A1 mRNA [ Time Frame: 5 hours after training and protein intake ]
  85. Change in sodium-coupled neutral amino acid transporter 2 (SLC38A2) mRNA [ Time Frame: 1 hour after training and protein intake ]
  86. Change in SLC38A2 mRNA [ Time Frame: 5 hours after training and protein intake ]
  87. Change in 4F2 cell-surface antigen heavy chain (SLC3A2) mRNA [ Time Frame: 1 hour after training and protein intake ]
  88. Change in SLC3A2 mRNA [ Time Frame: 5 hours after training and protein intake ]
  89. Change in large neutral amino acids transporter small subunit 1 (SLC7A5) mRNA [ Time Frame: 1 hour after training and protein intake ]
  90. Change in SLC7A5 mRNA [ Time Frame: 5 hours after training and protein intake ]
  91. Change in toll-like receptor 2 (TLR2) mRNA [ Time Frame: 1 hour after training and protein intake ]
  92. Change in TLR2 mRNA [ Time Frame: 5 hours after training and protein intake ]
  93. Change in tumor necrosis factor (TNF) mRNA [ Time Frame: 1 hour after training and protein intake ]
  94. Change in TNF mRNA [ Time Frame: 5 hours after training and protein intake ]
  95. Change in E3 ubiquitin-protein ligase TRIM63 (TRIM63) mRNA [ Time Frame: 1 hour after training and protein intake ]
  96. Change in E3 ubiquitin-protein ligase TRIM63 (TRIM63) mRNA [ Time Frame: 5 hours after training and protein intake ]


Information from the National Library of Medicine

Choosing to participate in a study is an important personal decision. Talk with your doctor and family members or friends about deciding to join a study. To learn more about this study, you or your doctor may contact the study research staff using the contacts provided below. For general information, Learn About Clinical Studies.


Layout table for eligibility information
Ages Eligible for Study:   18 Years and older   (Adult, Older Adult)
Sexes Eligible for Study:   All
Accepts Healthy Volunteers:   Yes
Criteria

Inclusion Criteria:

  • 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

Exclusion Criteria:

  • 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)

Information from the National Library of Medicine

To learn more about this study, you or your doctor may contact the study research staff using the contact information provided by the sponsor.

Please refer to this study by its ClinicalTrials.gov identifier (NCT number): NCT02968888


Locations
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Norway
Norwegian School of Sport Sciences
Oslo, Norway, 0863
Sponsors and Collaborators
Norwegian School of Sport Sciences
Tine
The Research Council of Norway
Arkansas Children's Hospital Research Institute

Publications automatically indexed to this study by ClinicalTrials.gov Identifier (NCT Number):
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Responsible Party: Havard Hamarsland, PhD student, Norwegian School of Sport Sciences
ClinicalTrials.gov Identifier: NCT02968888     History of Changes
Other Study ID Numbers: Tine acute
First Posted: November 21, 2016    Key Record Dates
Last Update Posted: April 10, 2018
Last Verified: April 2018
Individual Participant Data (IPD) Sharing Statement:
Plan to Share IPD: Undecided

Additional relevant MeSH terms:
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Caseins
Chelating Agents
Sequestering Agents
Molecular Mechanisms of Pharmacological Action