<clinical_study>
  <!-- This xml conforms to an XML Schema at:
    https://clinicaltrials.gov/ct2/html/images/info/public.xsd -->
  <required_header>
    <download_date>ClinicalTrials.gov processed this data on September 20, 2023</download_date>
    <link_text>Link to the current ClinicalTrials.gov record.</link_text>
    <url>https://clinicaltrials.gov/ct2/show/NCT03021694</url>
  </required_header>
  <id_info>
    <org_study_id>Aminoacidemia_Whey/Casein</org_study_id>
    <nct_id>NCT03021694</nct_id>
  </id_info>
  <brief_title>Testing of Micellar Casein, Blended Micellar Casein and Native Whey</brief_title>
  <official_title>Testing of Micellar Casein, Blended Micellar Casein and Native Whey, Versus Native Whey to Determine Post-ingestion Aminoacidemia, Glycemia, and Insulinemia in Young Adult Men</official_title>
  <sponsors>
    <lead_sponsor>
      <agency>McMaster University</agency>
      <agency_class>Other</agency_class>
    </lead_sponsor>
  </sponsors>
  <source>McMaster University</source>
  <oversight_info>
    <has_dmc>No</has_dmc>
  </oversight_info>
  <brief_summary>
    <textblock>
      The importance of protein in nutrition is momentous to ones health. Dietary proteins are&#xD;
      essentially nutritional because they contain amino acids, which the body uses to build its&#xD;
      own proteins, as well as other molecules that are essential for life. Protein when consumed,&#xD;
      travels through your digestive system and is absorbed. They then enter the blood for&#xD;
      transport to bodily tissues, and therefore, can be detected by blood sampling. There are&#xD;
      differing amounts of each amino acid found in different types of protein supplements. Certain&#xD;
      amino acids (the essential amino acids) are helping in stimulating muscle growth and helping&#xD;
      to maintain muscle mass and function. It is important to understand how quickly these amino&#xD;
      acids can be detected in your blood as well as how they affect blood glucose (blood sugar)&#xD;
      and insulin activity. Understanding the effects of protein type on changes in levels of blood&#xD;
      amino acids, glucose and insulin will provide helpful insight for the suggestion of&#xD;
      supplement use.&#xD;
    </textblock>
  </brief_summary>
  <detailed_description>
    <textblock>
      The importance of protein in nutrition is momentous to ones health. Dietary proteins are&#xD;
      essentially nutritional because of their constituent amino acids, which the body uses to&#xD;
      synthesize its own proteins, as well as nitrogen-containing molecules that are essential for&#xD;
      life. The Recommended Dietary Allowance (RDA) for daily protein intake in healthy adults is&#xD;
      0.8 g/kgBW/day. Younger individuals who participate in recreational or competitive&#xD;
      activities, however, often attempt to go beyond the RDA by using protein supplements to help&#xD;
      increase performance. For example, it was demonstrated that protein supplementation in&#xD;
      conjunction with an eight-week resistance-training program elicited greater improvements in&#xD;
      muscle hypertrophy and strength when compared to carbohydrate supplementation in untrained&#xD;
      men. There were 3.2 to 17.5% increases in muscle cross-sectional area of the quadriceps&#xD;
      femoris musculature and 14.5 to 30.3% strength gains in the leg extensors. Furthermore,&#xD;
      several expert groups have recently advocated that certain individuals, such as older&#xD;
      persons, should increase their daily intake to 1.0 to 1.5 g/kgBW/day to support the&#xD;
      preservation of muscle and function. Other conditions also place greater than normal demands&#xD;
      on amino acids, such as hypercatabolic stressed states, like that experienced by burn&#xD;
      patients who's muscle protein breakdown rate increases by impairment to inward transmembrane&#xD;
      transport of circulating blood amino acids. It was also found that an experimental enriched&#xD;
      protein &quot;medical food&quot; comprised of 27% of calories as total protein resulted in postprandial&#xD;
      increases in MPS rates for 5 hours by ∼33% (0.073 ± 0.023%∙h-1 to 0.097 ± 0.033%∙h-1) in&#xD;
      advanced cancer patients. Thus, continually reassessing new and innovative nutrient therapies&#xD;
      is necessary for extending the findings of existing studies after technological advances, and&#xD;
      for providing nutritional support-to-support health.&#xD;
&#xD;
      It is well known that dietary protein is a powerful transient stimulator of the muscle&#xD;
      protein synthetic rate (MPS) whereby changes in MPS in response to feeding may be regulated&#xD;
      by specific downstream target proteins of mammalian target of rapamycin signaling, such as&#xD;
      S6K1, rpS6, and eIF2B. A meal deficient in protein, however, does not increase the rate of&#xD;
      MPS because a rise in the bioavailability of amino acids does not occur. In addition, the&#xD;
      source of dietary proteins has been shown to impact postprandial blood levels of amino acids.&#xD;
      The concept that certain types of proteins are &quot;fast acting&quot; or &quot;slow acting&quot; has been shown&#xD;
      to affect the postprandial profile of amino acids appearing in the systemic circulation.&#xD;
      Native whey and micellar casein are both dairy proteins that contain a similar amount of&#xD;
      essential (EAA), but blood EAA levels increase faster and to a higher level after the&#xD;
      consumption of whey protein. Differences in gastric emptying, digestion and absorption&#xD;
      kinetics between micellar casein and native whey are suggested to be the underlying factors.&#xD;
      Nonetheless, micellar casein protein has been shown to protract MPS in humans. Despite the&#xD;
      significant amount of information gained with respect to both of these protein sources, the&#xD;
      effects of combinatorial formulations on the postprandial profile of amino acids appearing in&#xD;
      the blood is less well known. The purpose of the present study is to test a novel blend of&#xD;
      micellar casein combined with native whey to determine post-ingestion aminoacidemia,&#xD;
      glycemia, and insulinemia in young adult men.&#xD;
    </textblock>
  </detailed_description>
  <overall_status>Completed</overall_status>
  <start_date type="Actual">January 13, 2017</start_date>
  <completion_date type="Actual">January 15, 2018</completion_date>
  <primary_completion_date type="Actual">September 10, 2017</primary_completion_date>
  <phase>N/A</phase>
  <study_type>Interventional</study_type>
  <has_expanded_access>No</has_expanded_access>
  <study_design_info>
    <allocation>Randomized</allocation>
    <intervention_model>Crossover Assignment</intervention_model>
    <primary_purpose>Treatment</primary_purpose>
    <masking>Triple (Participant, Investigator, Outcomes Assessor)</masking>
  </study_design_info>
  <primary_outcome>
    <measure>Postprandial blood amino acid concentrations</measure>
    <time_frame>360 minutes</time_frame>
    <description>repeated blood draws</description>
  </primary_outcome>
  <primary_outcome>
    <measure>Postprandial blood insulin concentrations</measure>
    <time_frame>360 minutes</time_frame>
    <description>repeated blood draws</description>
  </primary_outcome>
  <primary_outcome>
    <measure>Postprandial blood glucose concentrations</measure>
    <time_frame>360 minutes</time_frame>
    <description>repeated blood draws</description>
  </primary_outcome>
  <number_of_arms>3</number_of_arms>
  <enrollment type="Actual">10</enrollment>
  <condition>Dietary Modification</condition>
  <arm_group>
    <arm_group_label>Young Males Week 1</arm_group_label>
    <arm_group_type>Experimental</arm_group_type>
    <description>Six separate 3 x 14 [condition (micellar casein, micellar casein and native whey blend, and native whey) x time (-15min, 0 min, 15min, 30min, 45min, 60min, 90min, 150min, 180min, 210min, 240min, 270min, 300min, and 360min)] repeated measures ANOVAs will be used to analyze blood concentrations of leucine, ∑branched chain amino acids, ∑essential amino acids, ∑amino acids, glucose, and insulin.</description>
  </arm_group>
  <arm_group>
    <arm_group_label>Young Males Week 3</arm_group_label>
    <arm_group_type>Experimental</arm_group_type>
    <description>Six separate 3 x 14 [condition (micellar casein, micellar casein and native whey blend, and native whey) x time (-15min, 0 min, 15min, 30min, 45min, 60min, 90min, 150min, 180min, 210min, 240min, 270min, 300min, and 360min)] repeated measures ANOVAs will be used to analyze blood concentrations of leucine, ∑branched chain amino acids, ∑essential amino acids, ∑amino acids, glucose, and insulin.</description>
  </arm_group>
  <arm_group>
    <arm_group_label>Young Males Week 5</arm_group_label>
    <arm_group_type>Experimental</arm_group_type>
    <description>Six separate 3 x 14 [condition (micellar casein, micellar casein and native whey blend, and native whey) x time (-15min, 0 min, 15min, 30min, 45min, 60min, 90min, 150min, 180min, 210min, 240min, 270min, 300min, and 360min)] repeated measures ANOVAs will be used to analyze blood concentrations of leucine, ∑branched chain amino acids, ∑essential amino acids, ∑amino acids, glucose, and insulin.</description>
  </arm_group>
  <intervention>
    <intervention_type>Dietary Supplement</intervention_type>
    <intervention_name>Testing of micellar casein, blended micellar casein and native whey, versus native whey to determine post-ingestion aminoacidemia, glycemia, and insulinemia in young adult men</intervention_name>
    <arm_group_label>Young Males Week 1</arm_group_label>
    <arm_group_label>Young Males Week 3</arm_group_label>
    <arm_group_label>Young Males Week 5</arm_group_label>
  </intervention>
  <eligibility>
    <criteria>
      <textblock>
        Inclusion Criteria:&#xD;
&#xD;
          -  10 participants will be included in this study.&#xD;
&#xD;
          -  Each participant will consume only one of the supplements in a double-blinded fashion&#xD;
             during three separate visits and there will be approximately 1 week between each&#xD;
             visit.&#xD;
&#xD;
          -  In order to participate in this study, each participant must be male, between the ages&#xD;
             of 18 and 30 years (inclusive) and cannot be a smoker or user of tobacco products.&#xD;
&#xD;
        Exclusion Criteria:&#xD;
&#xD;
          -  The exclusion requirements for this study include the following conditions:&#xD;
&#xD;
               -  Take any analgesic or anti-inflammatory drugs(s), prescription or&#xD;
                  non-prescription, chronically will be excluded. However, a washout period of 4&#xD;
                  weeks will be suitable for participation.&#xD;
&#xD;
               -  A history of neuromuscular problems or muscle and/or bone wasting diseases&#xD;
&#xD;
               -  Any acute or chronic illness, cardiac, pulmonary, liver, or kidney abnormalities,&#xD;
                  uncontrolled hypertension, insulin- or non-insulin dependent diabetes or other&#xD;
                  metabolic disorders-all ascertained through medical history screening&#xD;
                  questionnaires&#xD;
&#xD;
               -  Use medications known to affect protein metabolism (i.e. corticosteroids,&#xD;
                  non-steroidal anti-inflammatories, or prescription strength acne medications)&#xD;
      </textblock>
    </criteria>
    <gender>Male</gender>
    <minimum_age>18 Years</minimum_age>
    <maximum_age>30 Years</maximum_age>
    <healthy_volunteers>Accepts Healthy Volunteers</healthy_volunteers>
  </eligibility>
  <location>
    <facility>
      <name>Exercise Metabolism Research Laboratory, McMaster Univeristy</name>
      <address>
        <city>Hamilton</city>
        <state>Ontario</state>
        <zip>L8S 4K1</zip>
        <country>Canada</country>
      </address>
    </facility>
  </location>
  <location_countries>
    <country>Canada</country>
  </location_countries>
  <reference>
    <citation>Rand WM, Pellett PL, Young VR. Meta-analysis of nitrogen balance studies for estimating protein requirements in healthy adults. Am J Clin Nutr. 2003 Jan;77(1):109-27. doi: 10.1093/ajcn/77.1.109.</citation>
    <PMID>12499330</PMID>
  </reference>
  <reference>
    <citation>Coburn JW, Housh DJ, Housh TJ, Malek MH, Beck TW, Cramer JT, Johnson GO, Donlin PE. Effects of leucine and whey protein supplementation during eight weeks of unilateral resistance training. J Strength Cond Res. 2006 May;20(2):284-91. doi: 10.1519/R-17925.1.</citation>
    <PMID>16686554</PMID>
  </reference>
  <reference>
    <citation>Bauer JM, Verlaan S, Bautmans I, Brandt K, Donini LM, Maggio M, McMurdo ME, Mets T, Seal C, Wijers SL, Ceda GP, De Vito G, Donders G, Drey M, Greig C, Holmback U, Narici M, McPhee J, Poggiogalle E, Power D, Scafoglieri A, Schultz R, Sieber CC, Cederholm T. Effects of a vitamin D and leucine-enriched whey protein nutritional supplement on measures of sarcopenia in older adults, the PROVIDE study: a randomized, double-blind, placebo-controlled trial. J Am Med Dir Assoc. 2015 Sep 1;16(9):740-7. doi: 10.1016/j.jamda.2015.05.021. Epub 2015 Jul 10.</citation>
    <PMID>26170041</PMID>
  </reference>
  <reference>
    <citation>Deutz NE, Bauer JM, Barazzoni R, Biolo G, Boirie Y, Bosy-Westphal A, Cederholm T, Cruz-Jentoft A, Krznaric Z, Nair KS, Singer P, Teta D, Tipton K, Calder PC. Protein intake and exercise for optimal muscle function with aging: recommendations from the ESPEN Expert Group. Clin Nutr. 2014 Dec;33(6):929-36. doi: 10.1016/j.clnu.2014.04.007. Epub 2014 Apr 24.</citation>
    <PMID>24814383</PMID>
  </reference>
  <reference>
    <citation>Murphy CH, Oikawa SY, Phillips SM. Dietary Protein to Maintain Muscle Mass in Aging: A Case for Per-meal Protein Recommendations. J Frailty Aging. 2016;5(1):49-58. doi: 10.14283/jfa.2016.80.</citation>
    <PMID>26980369</PMID>
  </reference>
  <reference>
    <citation>Biolo G, Fleming RY, Maggi SP, Nguyen TT, Herndon DN, Wolfe RR. Inverse regulation of protein turnover and amino acid transport in skeletal muscle of hypercatabolic patients. J Clin Endocrinol Metab. 2002 Jul;87(7):3378-84. doi: 10.1210/jcem.87.7.8699.</citation>
    <PMID>12107253</PMID>
  </reference>
  <reference>
    <citation>Tisdale MJ. Mechanisms of cancer cachexia. Physiol Rev. 2009 Apr;89(2):381-410. doi: 10.1152/physrev.00016.2008.</citation>
    <PMID>19342610</PMID>
  </reference>
  <reference>
    <citation>Koopman R, Crombach N, Gijsen AP, Walrand S, Fauquant J, Kies AK, Lemosquet S, Saris WH, Boirie Y, van Loon LJ. Ingestion of a protein hydrolysate is accompanied by an accelerated in vivo digestion and absorption rate when compared with its intact protein. Am J Clin Nutr. 2009 Jul;90(1):106-15. doi: 10.3945/ajcn.2009.27474. Epub 2009 May 27.</citation>
    <PMID>19474134</PMID>
  </reference>
  <reference>
    <citation>Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, Prior T, Tarnopolsky MA, Phillips SM. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr. 2009 Jan;89(1):161-8. doi: 10.3945/ajcn.2008.26401. Epub 2008 Dec 3.</citation>
    <PMID>19056590</PMID>
  </reference>
  <reference>
    <citation>Katsanos CS, Kobayashi H, Sheffield-Moore M, Aarsland A, Wolfe RR. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. Am J Physiol Endocrinol Metab. 2006 Aug;291(2):E381-7. doi: 10.1152/ajpendo.00488.2005. Epub 2006 Feb 28.</citation>
    <PMID>16507602</PMID>
  </reference>
  <reference>
    <citation>Luiking YC, Abrahamse E, Ludwig T, Boirie Y, Verlaan S. Protein type and caloric density of protein supplements modulate postprandial amino acid profile through changes in gastrointestinal behaviour: A randomized trial. Clin Nutr. 2016 Feb;35(1):48-58. doi: 10.1016/j.clnu.2015.02.013. Epub 2015 Mar 5.</citation>
    <PMID>25790724</PMID>
  </reference>
  <reference>
    <citation>Tipton KD, Elliott TA, Cree MG, Wolf SE, Sanford AP, Wolfe RR. Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise. Med Sci Sports Exerc. 2004 Dec;36(12):2073-81. doi: 10.1249/01.mss.0000147582.99810.c5.</citation>
    <PMID>15570142</PMID>
  </reference>
  <reference>
    <citation>Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrere B. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14930-5. doi: 10.1073/pnas.94.26.14930.</citation>
    <PMID>9405716</PMID>
  </reference>
  <verification_date>February 2018</verification_date>
  <study_first_submitted>January 11, 2017</study_first_submitted>
  <study_first_submitted_qc>January 12, 2017</study_first_submitted_qc>
  <study_first_posted type="Estimate">January 16, 2017</study_first_posted>
  <last_update_submitted>February 13, 2018</last_update_submitted>
  <last_update_submitted_qc>February 13, 2018</last_update_submitted_qc>
  <last_update_posted type="Actual">February 15, 2018</last_update_posted>
  <responsible_party>
    <responsible_party_type>Principal Investigator</responsible_party_type>
    <investigator_affiliation>McMaster University</investigator_affiliation>
    <investigator_full_name>Stuart Phillips</investigator_full_name>
    <investigator_title>Professor</investigator_title>
  </responsible_party>
  <intervention_browse>
    <!-- CAUTION:  The following MeSH terms are assigned with an imperfect algorithm            -->
    <mesh_term>Caseins</mesh_term>
  </intervention_browse>
  <patient_data>
    <sharing_ipd>No</sharing_ipd>
  </patient_data>
  <!-- Results have not yet been posted for this study                                          -->
</clinical_study>


download date: ClinicalTrials.gov processed this data on September 20, 2023
link text: Link to the current ClinicalTrials.gov record.
url: https://clinicaltrials.gov/ct2/show/NCT03021694
org study id: Aminoacidemia_Whey/Casein
nct id: NCT03021694
lead sponsor: 
has dmc: No
The importance of protein in nutrition is momentous to ones health. Dietary proteins are
      essentially nutritional because they contain amino acids, which the body uses to build its
      own proteins, as well as other molecules that are essential for life. Protein when consumed,
      travels through your digestive system and is absorbed. They then enter the blood for
      transport to bodily tissues, and therefore, can be detected by blood sampling. There are
      differing amounts of each amino acid found in different types of protein supplements. Certain
      amino acids (the essential amino acids) are helping in stimulating muscle growth and helping
      to maintain muscle mass and function. It is important to understand how quickly these amino
      acids can be detected in your blood as well as how they affect blood glucose (blood sugar)
      and insulin activity. Understanding the effects of protein type on changes in levels of blood
      amino acids, glucose and insulin will provide helpful insight for the suggestion of
      supplement use.
The importance of protein in nutrition is momentous to ones health. Dietary proteins are
      essentially nutritional because of their constituent amino acids, which the body uses to
      synthesize its own proteins, as well as nitrogen-containing molecules that are essential for
      life. The Recommended Dietary Allowance (RDA) for daily protein intake in healthy adults is
      0.8 g/kgBW/day. Younger individuals who participate in recreational or competitive
      activities, however, often attempt to go beyond the RDA by using protein supplements to help
      increase performance. For example, it was demonstrated that protein supplementation in
      conjunction with an eight-week resistance-training program elicited greater improvements in
      muscle hypertrophy and strength when compared to carbohydrate supplementation in untrained
      men. There were 3.2 to 17.5% increases in muscle cross-sectional area of the quadriceps
      femoris musculature and 14.5 to 30.3% strength gains in the leg extensors. Furthermore,
      several expert groups have recently advocated that certain individuals, such as older
      persons, should increase their daily intake to 1.0 to 1.5 g/kgBW/day to support the
      preservation of muscle and function. Other conditions also place greater than normal demands
      on amino acids, such as hypercatabolic stressed states, like that experienced by burn
      patients who's muscle protein breakdown rate increases by impairment to inward transmembrane
      transport of circulating blood amino acids. It was also found that an experimental enriched
      protein "medical food" comprised of 27% of calories as total protein resulted in postprandial
      increases in MPS rates for 5 hours by ∼33% (0.073 ± 0.023%∙h-1 to 0.097 ± 0.033%∙h-1) in
      advanced cancer patients. Thus, continually reassessing new and innovative nutrient therapies
      is necessary for extending the findings of existing studies after technological advances, and
      for providing nutritional support-to-support health.

      It is well known that dietary protein is a powerful transient stimulator of the muscle
      protein synthetic rate (MPS) whereby changes in MPS in response to feeding may be regulated
      by specific downstream target proteins of mammalian target of rapamycin signaling, such as
      S6K1, rpS6, and eIF2B. A meal deficient in protein, however, does not increase the rate of
      MPS because a rise in the bioavailability of amino acids does not occur. In addition, the
      source of dietary proteins has been shown to impact postprandial blood levels of amino acids.
      The concept that certain types of proteins are "fast acting" or "slow acting" has been shown
      to affect the postprandial profile of amino acids appearing in the systemic circulation.
      Native whey and micellar casein are both dairy proteins that contain a similar amount of
      essential (EAA), but blood EAA levels increase faster and to a higher level after the
      consumption of whey protein. Differences in gastric emptying, digestion and absorption
      kinetics between micellar casein and native whey are suggested to be the underlying factors.
      Nonetheless, micellar casein protein has been shown to protract MPS in humans. Despite the
      significant amount of information gained with respect to both of these protein sources, the
      effects of combinatorial formulations on the postprandial profile of amino acids appearing in
      the blood is less well known. The purpose of the present study is to test a novel blend of
      micellar casein combined with native whey to determine post-ingestion aminoacidemia,
      glycemia, and insulinemia in young adult men.
allocation: Randomized
intervention model: Crossover Assignment
primary purpose: Treatment
masking: Triple (Participant, Investigator, Outcomes Assessor)
measure: Postprandial blood amino acid concentrations
time frame: 360 minutes
description: repeated blood draws
measure: Postprandial blood insulin concentrations
time frame: 360 minutes
description: repeated blood draws
measure: Postprandial blood glucose concentrations
time frame: 360 minutes
description: repeated blood draws
arm group label: Young Males Week 1
arm group type: Experimental
description: Six separate 3 x 14 [condition (micellar casein, micellar casein and native whey blend, and native whey) x time (-15min, 0 min, 15min, 30min, 45min, 60min, 90min, 150min, 180min, 210min, 240min, 270min, 300min, and 360min)] repeated measures ANOVAs will be used to analyze blood concentrations of leucine, ∑branched chain amino acids, ∑essential amino acids, ∑amino acids, glucose, and insulin.
arm group label: Young Males Week 3
arm group type: Experimental
description: Six separate 3 x 14 [condition (micellar casein, micellar casein and native whey blend, and native whey) x time (-15min, 0 min, 15min, 30min, 45min, 60min, 90min, 150min, 180min, 210min, 240min, 270min, 300min, and 360min)] repeated measures ANOVAs will be used to analyze blood concentrations of leucine, ∑branched chain amino acids, ∑essential amino acids, ∑amino acids, glucose, and insulin.
arm group label: Young Males Week 5
arm group type: Experimental
description: Six separate 3 x 14 [condition (micellar casein, micellar casein and native whey blend, and native whey) x time (-15min, 0 min, 15min, 30min, 45min, 60min, 90min, 150min, 180min, 210min, 240min, 270min, 300min, and 360min)] repeated measures ANOVAs will be used to analyze blood concentrations of leucine, ∑branched chain amino acids, ∑essential amino acids, ∑amino acids, glucose, and insulin.
intervention type: Dietary Supplement
intervention name: Testing of micellar casein, blended micellar casein and native whey, versus native whey to determine post-ingestion aminoacidemia, glycemia, and insulinemia in young adult men
arm group label: Young Males Week 1
arm group label: Young Males Week 3
arm group label: Young Males Week 5
criteria: 
gender: Male
minimum age: 18 Years
maximum age: 30 Years
healthy volunteers: Accepts Healthy Volunteers
facility: 
country: Canada
citation: Rand WM, Pellett PL, Young VR. Meta-analysis of nitrogen balance studies for estimating protein requirements in healthy adults. Am J Clin Nutr. 2003 Jan;77(1):109-27. doi: 10.1093/ajcn/77.1.109.
PMID: 12499330
citation: Coburn JW, Housh DJ, Housh TJ, Malek MH, Beck TW, Cramer JT, Johnson GO, Donlin PE. Effects of leucine and whey protein supplementation during eight weeks of unilateral resistance training. J Strength Cond Res. 2006 May;20(2):284-91. doi: 10.1519/R-17925.1.
PMID: 16686554
citation: Bauer JM, Verlaan S, Bautmans I, Brandt K, Donini LM, Maggio M, McMurdo ME, Mets T, Seal C, Wijers SL, Ceda GP, De Vito G, Donders G, Drey M, Greig C, Holmback U, Narici M, McPhee J, Poggiogalle E, Power D, Scafoglieri A, Schultz R, Sieber CC, Cederholm T. Effects of a vitamin D and leucine-enriched whey protein nutritional supplement on measures of sarcopenia in older adults, the PROVIDE study: a randomized, double-blind, placebo-controlled trial. J Am Med Dir Assoc. 2015 Sep 1;16(9):740-7. doi: 10.1016/j.jamda.2015.05.021. Epub 2015 Jul 10.
PMID: 26170041
citation: Deutz NE, Bauer JM, Barazzoni R, Biolo G, Boirie Y, Bosy-Westphal A, Cederholm T, Cruz-Jentoft A, Krznaric Z, Nair KS, Singer P, Teta D, Tipton K, Calder PC. Protein intake and exercise for optimal muscle function with aging: recommendations from the ESPEN Expert Group. Clin Nutr. 2014 Dec;33(6):929-36. doi: 10.1016/j.clnu.2014.04.007. Epub 2014 Apr 24.
PMID: 24814383
citation: Murphy CH, Oikawa SY, Phillips SM. Dietary Protein to Maintain Muscle Mass in Aging: A Case for Per-meal Protein Recommendations. J Frailty Aging. 2016;5(1):49-58. doi: 10.14283/jfa.2016.80.
PMID: 26980369
citation: Biolo G, Fleming RY, Maggi SP, Nguyen TT, Herndon DN, Wolfe RR. Inverse regulation of protein turnover and amino acid transport in skeletal muscle of hypercatabolic patients. J Clin Endocrinol Metab. 2002 Jul;87(7):3378-84. doi: 10.1210/jcem.87.7.8699.
PMID: 12107253
citation: Tisdale MJ. Mechanisms of cancer cachexia. Physiol Rev. 2009 Apr;89(2):381-410. doi: 10.1152/physrev.00016.2008.
PMID: 19342610
citation: Koopman R, Crombach N, Gijsen AP, Walrand S, Fauquant J, Kies AK, Lemosquet S, Saris WH, Boirie Y, van Loon LJ. Ingestion of a protein hydrolysate is accompanied by an accelerated in vivo digestion and absorption rate when compared with its intact protein. Am J Clin Nutr. 2009 Jul;90(1):106-15. doi: 10.3945/ajcn.2009.27474. Epub 2009 May 27.
PMID: 19474134
citation: Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, Prior T, Tarnopolsky MA, Phillips SM. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr. 2009 Jan;89(1):161-8. doi: 10.3945/ajcn.2008.26401. Epub 2008 Dec 3.
PMID: 19056590
citation: Katsanos CS, Kobayashi H, Sheffield-Moore M, Aarsland A, Wolfe RR. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. Am J Physiol Endocrinol Metab. 2006 Aug;291(2):E381-7. doi: 10.1152/ajpendo.00488.2005. Epub 2006 Feb 28.
PMID: 16507602
citation: Luiking YC, Abrahamse E, Ludwig T, Boirie Y, Verlaan S. Protein type and caloric density of protein supplements modulate postprandial amino acid profile through changes in gastrointestinal behaviour: A randomized trial. Clin Nutr. 2016 Feb;35(1):48-58. doi: 10.1016/j.clnu.2015.02.013. Epub 2015 Mar 5.
PMID: 25790724
citation: Tipton KD, Elliott TA, Cree MG, Wolf SE, Sanford AP, Wolfe RR. Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise. Med Sci Sports Exerc. 2004 Dec;36(12):2073-81. doi: 10.1249/01.mss.0000147582.99810.c5.
PMID: 15570142
citation: Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrere B. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14930-5. doi: 10.1073/pnas.94.26.14930.
PMID: 9405716
responsible party type: Principal Investigator
investigator affiliation: McMaster University
investigator full name: Stuart Phillips
investigator title: Professor
mesh term: Caseins
sharing ipd: No