Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis
The effects of essential amino acid (EAA) supplementation during moderate steady state (ie, endurance) exercise on postexercise skeletal muscle metabolism are not well described, and the potential role of supplemental leucine on muscle protein synthesis (MPS) and associated molecular responses remai...
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| Veröffentlicht in: | The American journal of clinical nutrition 2011-09, Vol.94 (3), p.809-818 |
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| creator | PASIAKOS, Stefan M MCCLUNG, Holly L MCCLUNG, James P MARGOLIS, Lee M ANDERSEN, Nancy E CLOUTIER, Gregory J PIKOSKY, Matthew A ROOD, Jennifer C FIELDING, Roger A YOUNG, Andrew J |
| description | The effects of essential amino acid (EAA) supplementation during moderate steady state (ie, endurance) exercise on postexercise skeletal muscle metabolism are not well described, and the potential role of supplemental leucine on muscle protein synthesis (MPS) and associated molecular responses remains to be elucidated.
This randomized crossover study examined whether EAA supplementation with 2 different concentrations of leucine affected post-steady state exercise MPS, whole-body protein turnover, and mammalian target of rapamycin 1 (mTORC1) intracellular signaling.
Eight adults completed 2 separate bouts of cycle ergometry [60 min, 60% VO(2)peak (peak oxygen uptake)]. Isonitrogenous (10 g EAA) drinks with different leucine contents [leucine-enriched (l)-EAA, 3.5 g leucine; EAA, 1.87 g leucine] were consumed during exercise. MPS and whole-body protein turnover were determined by using primed continuous infusions of [(2)H(5)]phenylalanine and [1-(13)C]leucine. Multiplex and immunoblot analyses were used to quantify mTORC1 signaling.
MPS was 33% greater (P < 0.05) after consumption of L-EAA (0.08 ± 0.01%/h) than after consumption of EAA (0.06 ± 0.01%/h). Whole-body protein breakdown and synthesis were lower (P < 0.05) and oxidation was greater (P < 0.05) after consumption of L-EAA than after consumption of EAA. Regardless of dietary treatment, multiplex analysis indicated that Akt and mammalian target of rapamycin phosphorylation were increased (P < 0.05) 30 min after exercise. Immunoblot analysis indicated that phosphorylation of ribosomal protein S6 and extracellular-signal regulated protein kinase increased (P < 0.05) and phosphorylation of eukaryotic elongation factor 2 decreased (P < 0.05) after exercise but was not affected by dietary treatment.
These findings suggest that increasing the concentration of leucine in an EAA supplement consumed during steady state exercise elicits a greater MPS response during recovery. This trial is registered at clinicaltrials.gov as NCT01366924. |
| doi_str_mv | 10.3945/ajcn.111.017061 |
| format | Article |
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This randomized crossover study examined whether EAA supplementation with 2 different concentrations of leucine affected post-steady state exercise MPS, whole-body protein turnover, and mammalian target of rapamycin 1 (mTORC1) intracellular signaling.
Eight adults completed 2 separate bouts of cycle ergometry [60 min, 60% VO(2)peak (peak oxygen uptake)]. Isonitrogenous (10 g EAA) drinks with different leucine contents [leucine-enriched (l)-EAA, 3.5 g leucine; EAA, 1.87 g leucine] were consumed during exercise. MPS and whole-body protein turnover were determined by using primed continuous infusions of [(2)H(5)]phenylalanine and [1-(13)C]leucine. Multiplex and immunoblot analyses were used to quantify mTORC1 signaling.
MPS was 33% greater (P < 0.05) after consumption of L-EAA (0.08 ± 0.01%/h) than after consumption of EAA (0.06 ± 0.01%/h). Whole-body protein breakdown and synthesis were lower (P < 0.05) and oxidation was greater (P < 0.05) after consumption of L-EAA than after consumption of EAA. Regardless of dietary treatment, multiplex analysis indicated that Akt and mammalian target of rapamycin phosphorylation were increased (P < 0.05) 30 min after exercise. Immunoblot analysis indicated that phosphorylation of ribosomal protein S6 and extracellular-signal regulated protein kinase increased (P < 0.05) and phosphorylation of eukaryotic elongation factor 2 decreased (P < 0.05) after exercise but was not affected by dietary treatment.
These findings suggest that increasing the concentration of leucine in an EAA supplement consumed during steady state exercise elicits a greater MPS response during recovery. This trial is registered at clinicaltrials.gov as NCT01366924.]]></description><identifier>ISSN: 0002-9165</identifier><identifier>EISSN: 1938-3207</identifier><identifier>DOI: 10.3945/ajcn.111.017061</identifier><identifier>PMID: 21775557</identifier><identifier>CODEN: AJCNAC</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Nutrition</publisher><subject>Adult ; Amino acids ; Bicycling - physiology ; Biological and medical sciences ; Cross-Over Studies ; Dietary Supplements ; Exercise ; Exercise - physiology ; Exercise Test ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Feeding. Feeding behavior ; Female ; Fundamental and applied biological sciences. Psychology ; Humans ; Isotopes ; Leucine - pharmacology ; Male ; Muscle Proteins - biosynthesis ; Musculoskeletal system ; Oxidation-Reduction ; Phosphorylation ; Protein Biosynthesis - drug effects ; Protein synthesis ; Proto-Oncogene Proteins c-akt - metabolism ; Ribosomal Protein S6 - metabolism ; Signal Transduction - drug effects ; Staining and Labeling ; TOR Serine-Threonine Kinases - metabolism ; Vertebrates: anatomy and physiology, studies on body, several organs or systems ; Young Adult</subject><ispartof>The American journal of clinical nutrition, 2011-09, Vol.94 (3), p.809-818</ispartof><rights>2015 INIST-CNRS</rights><rights>Copyright American Society for Clinical Nutrition, Inc. Sep 1, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a417t-9cd97cd505e2395760106524c4518ca39e602c83cda2494da4e19f2fdf63e2913</citedby><cites>FETCH-LOGICAL-a417t-9cd97cd505e2395760106524c4518ca39e602c83cda2494da4e19f2fdf63e2913</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24443498$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21775557$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>PASIAKOS, Stefan M</creatorcontrib><creatorcontrib>MCCLUNG, Holly L</creatorcontrib><creatorcontrib>MCCLUNG, James P</creatorcontrib><creatorcontrib>MARGOLIS, Lee M</creatorcontrib><creatorcontrib>ANDERSEN, Nancy E</creatorcontrib><creatorcontrib>CLOUTIER, Gregory J</creatorcontrib><creatorcontrib>PIKOSKY, Matthew A</creatorcontrib><creatorcontrib>ROOD, Jennifer C</creatorcontrib><creatorcontrib>FIELDING, Roger A</creatorcontrib><creatorcontrib>YOUNG, Andrew J</creatorcontrib><title>Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis</title><title>The American journal of clinical nutrition</title><addtitle>Am J Clin Nutr</addtitle><description><![CDATA[The effects of essential amino acid (EAA) supplementation during moderate steady state (ie, endurance) exercise on postexercise skeletal muscle metabolism are not well described, and the potential role of supplemental leucine on muscle protein synthesis (MPS) and associated molecular responses remains to be elucidated.
This randomized crossover study examined whether EAA supplementation with 2 different concentrations of leucine affected post-steady state exercise MPS, whole-body protein turnover, and mammalian target of rapamycin 1 (mTORC1) intracellular signaling.
Eight adults completed 2 separate bouts of cycle ergometry [60 min, 60% VO(2)peak (peak oxygen uptake)]. Isonitrogenous (10 g EAA) drinks with different leucine contents [leucine-enriched (l)-EAA, 3.5 g leucine; EAA, 1.87 g leucine] were consumed during exercise. MPS and whole-body protein turnover were determined by using primed continuous infusions of [(2)H(5)]phenylalanine and [1-(13)C]leucine. Multiplex and immunoblot analyses were used to quantify mTORC1 signaling.
MPS was 33% greater (P < 0.05) after consumption of L-EAA (0.08 ± 0.01%/h) than after consumption of EAA (0.06 ± 0.01%/h). Whole-body protein breakdown and synthesis were lower (P < 0.05) and oxidation was greater (P < 0.05) after consumption of L-EAA than after consumption of EAA. Regardless of dietary treatment, multiplex analysis indicated that Akt and mammalian target of rapamycin phosphorylation were increased (P < 0.05) 30 min after exercise. Immunoblot analysis indicated that phosphorylation of ribosomal protein S6 and extracellular-signal regulated protein kinase increased (P < 0.05) and phosphorylation of eukaryotic elongation factor 2 decreased (P < 0.05) after exercise but was not affected by dietary treatment.
These findings suggest that increasing the concentration of leucine in an EAA supplement consumed during steady state exercise elicits a greater MPS response during recovery. This trial is registered at clinicaltrials.gov as NCT01366924.]]></description><subject>Adult</subject><subject>Amino acids</subject><subject>Bicycling - physiology</subject><subject>Biological and medical sciences</subject><subject>Cross-Over Studies</subject><subject>Dietary Supplements</subject><subject>Exercise</subject><subject>Exercise - physiology</subject><subject>Exercise Test</subject><subject>Extracellular Signal-Regulated MAP Kinases - metabolism</subject><subject>Feeding. Feeding behavior</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Isotopes</subject><subject>Leucine - pharmacology</subject><subject>Male</subject><subject>Muscle Proteins - biosynthesis</subject><subject>Musculoskeletal system</subject><subject>Oxidation-Reduction</subject><subject>Phosphorylation</subject><subject>Protein Biosynthesis - drug effects</subject><subject>Protein synthesis</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>Ribosomal Protein S6 - metabolism</subject><subject>Signal Transduction - drug effects</subject><subject>Staining and Labeling</subject><subject>TOR Serine-Threonine Kinases - metabolism</subject><subject>Vertebrates: anatomy and physiology, studies on body, several organs or systems</subject><subject>Young Adult</subject><issn>0002-9165</issn><issn>1938-3207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1v1DAQhi0EotvCmRuykHrM1p-xfUQVFKSVuJRzZOwJ61XiBE8isX-hvxqvdktPM_Y8fsd6CPnA2VY6pe_8IeQt53zLuGEtf0U23EnbSMHMa7JhjInG8VZfkWvEA2NcKNu-JVeCG6O1NhvytIM1pAwN5JLCHiIFRMhL8gP1Y8oT9SFFius8DzDWgV_SlGlcS8q_6ThFKH4Bigv4eKzldIC_UELC2uS9zwGQzlMFnm_HFcMAdC7TAilTPOZlD5jwHXnT-wHh_aXekJ9fvzzef2t2Px6-33_eNV5xszQuRGdC1EyDkE6blnHWaqGC0twGLx20TAQrQ_RCORW9Au560ce-lSAclzfk0zm3_uDPCrh0h2ktua7srFXWGuZMhe7OUCgTYoG-m0safTl2nHUn9d1JfVfVd2f19cXHS-z6a4T4n392XYHbC-Ax-KEv1U3CF04pJZWz8h_ZMpAl</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>PASIAKOS, Stefan M</creator><creator>MCCLUNG, Holly L</creator><creator>MCCLUNG, James P</creator><creator>MARGOLIS, Lee M</creator><creator>ANDERSEN, Nancy E</creator><creator>CLOUTIER, Gregory J</creator><creator>PIKOSKY, Matthew A</creator><creator>ROOD, Jennifer C</creator><creator>FIELDING, Roger A</creator><creator>YOUNG, Andrew J</creator><general>American Society for Nutrition</general><general>American Society for Clinical Nutrition, Inc</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7T7</scope><scope>7TS</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>NAPCQ</scope><scope>P64</scope></search><sort><creationdate>20110901</creationdate><title>Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis</title><author>PASIAKOS, Stefan M ; MCCLUNG, Holly L ; MCCLUNG, James P ; MARGOLIS, Lee M ; ANDERSEN, Nancy E ; CLOUTIER, Gregory J ; PIKOSKY, Matthew A ; ROOD, Jennifer C ; FIELDING, Roger A ; YOUNG, Andrew J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a417t-9cd97cd505e2395760106524c4518ca39e602c83cda2494da4e19f2fdf63e2913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adult</topic><topic>Amino acids</topic><topic>Bicycling - physiology</topic><topic>Biological and medical sciences</topic><topic>Cross-Over Studies</topic><topic>Dietary Supplements</topic><topic>Exercise</topic><topic>Exercise - physiology</topic><topic>Exercise Test</topic><topic>Extracellular Signal-Regulated MAP Kinases - metabolism</topic><topic>Feeding. Feeding behavior</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Isotopes</topic><topic>Leucine - pharmacology</topic><topic>Male</topic><topic>Muscle Proteins - biosynthesis</topic><topic>Musculoskeletal system</topic><topic>Oxidation-Reduction</topic><topic>Phosphorylation</topic><topic>Protein Biosynthesis - drug effects</topic><topic>Protein synthesis</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>Ribosomal Protein S6 - metabolism</topic><topic>Signal Transduction - drug effects</topic><topic>Staining and Labeling</topic><topic>TOR Serine-Threonine Kinases - metabolism</topic><topic>Vertebrates: anatomy and physiology, studies on body, several organs or systems</topic><topic>Young Adult</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>PASIAKOS, Stefan M</creatorcontrib><creatorcontrib>MCCLUNG, Holly L</creatorcontrib><creatorcontrib>MCCLUNG, James P</creatorcontrib><creatorcontrib>MARGOLIS, Lee M</creatorcontrib><creatorcontrib>ANDERSEN, Nancy E</creatorcontrib><creatorcontrib>CLOUTIER, Gregory J</creatorcontrib><creatorcontrib>PIKOSKY, Matthew A</creatorcontrib><creatorcontrib>ROOD, Jennifer C</creatorcontrib><creatorcontrib>FIELDING, Roger A</creatorcontrib><creatorcontrib>YOUNG, Andrew J</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Physical Education Index</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The American journal of clinical nutrition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>PASIAKOS, Stefan M</au><au>MCCLUNG, Holly L</au><au>MCCLUNG, James P</au><au>MARGOLIS, Lee M</au><au>ANDERSEN, Nancy E</au><au>CLOUTIER, Gregory J</au><au>PIKOSKY, Matthew A</au><au>ROOD, Jennifer C</au><au>FIELDING, Roger A</au><au>YOUNG, Andrew J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis</atitle><jtitle>The American journal of clinical nutrition</jtitle><addtitle>Am J Clin Nutr</addtitle><date>2011-09-01</date><risdate>2011</risdate><volume>94</volume><issue>3</issue><spage>809</spage><epage>818</epage><pages>809-818</pages><issn>0002-9165</issn><eissn>1938-3207</eissn><coden>AJCNAC</coden><abstract><![CDATA[The effects of essential amino acid (EAA) supplementation during moderate steady state (ie, endurance) exercise on postexercise skeletal muscle metabolism are not well described, and the potential role of supplemental leucine on muscle protein synthesis (MPS) and associated molecular responses remains to be elucidated.
This randomized crossover study examined whether EAA supplementation with 2 different concentrations of leucine affected post-steady state exercise MPS, whole-body protein turnover, and mammalian target of rapamycin 1 (mTORC1) intracellular signaling.
Eight adults completed 2 separate bouts of cycle ergometry [60 min, 60% VO(2)peak (peak oxygen uptake)]. Isonitrogenous (10 g EAA) drinks with different leucine contents [leucine-enriched (l)-EAA, 3.5 g leucine; EAA, 1.87 g leucine] were consumed during exercise. MPS and whole-body protein turnover were determined by using primed continuous infusions of [(2)H(5)]phenylalanine and [1-(13)C]leucine. Multiplex and immunoblot analyses were used to quantify mTORC1 signaling.
MPS was 33% greater (P < 0.05) after consumption of L-EAA (0.08 ± 0.01%/h) than after consumption of EAA (0.06 ± 0.01%/h). Whole-body protein breakdown and synthesis were lower (P < 0.05) and oxidation was greater (P < 0.05) after consumption of L-EAA than after consumption of EAA. Regardless of dietary treatment, multiplex analysis indicated that Akt and mammalian target of rapamycin phosphorylation were increased (P < 0.05) 30 min after exercise. Immunoblot analysis indicated that phosphorylation of ribosomal protein S6 and extracellular-signal regulated protein kinase increased (P < 0.05) and phosphorylation of eukaryotic elongation factor 2 decreased (P < 0.05) after exercise but was not affected by dietary treatment.
These findings suggest that increasing the concentration of leucine in an EAA supplement consumed during steady state exercise elicits a greater MPS response during recovery. This trial is registered at clinicaltrials.gov as NCT01366924.]]></abstract><cop>Bethesda, MD</cop><pub>American Society for Nutrition</pub><pmid>21775557</pmid><doi>10.3945/ajcn.111.017061</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adult Amino acids Bicycling - physiology Biological and medical sciences Cross-Over Studies Dietary Supplements Exercise Exercise - physiology Exercise Test Extracellular Signal-Regulated MAP Kinases - metabolism Feeding. Feeding behavior Female Fundamental and applied biological sciences. Psychology Humans Isotopes Leucine - pharmacology Male Muscle Proteins - biosynthesis Musculoskeletal system Oxidation-Reduction Phosphorylation Protein Biosynthesis - drug effects Protein synthesis Proto-Oncogene Proteins c-akt - metabolism Ribosomal Protein S6 - metabolism Signal Transduction - drug effects Staining and Labeling TOR Serine-Threonine Kinases - metabolism Vertebrates: anatomy and physiology, studies on body, several organs or systems Young Adult |
| title | Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis |
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