Signaling Pathways Involved in Translational Control of Protein Synthesis in Skeletal Muscle by Leucine
Numerous reports established that in skeletal muscle the indispensable branched-chain amino acid leucine is unique in its ability to initiate signal transduction pathways that modulate translation initiation. Oral administration of leucine stimulates protein synthesis in association with hyperphosph...
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| Veröffentlicht in: | The Journal of nutrition 2001-03, Vol.131 (3), p.856S-860S |
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| creator | Anthony, Joshua C. Anthony, Tracy G. Kimball, Scot R. Jefferson, Leonard S. |
| description | Numerous reports established that in skeletal muscle the indispensable branched-chain amino acid leucine is unique in its ability to initiate signal transduction pathways that modulate translation initiation. Oral administration of leucine stimulates protein synthesis in association with hyperphosphorylation of the translational repressor, eukaryotic initiation factor (eIF) 4E binding protein 1 (4E-BP1), resulting in enhanced availability of the mRNA cap-binding protein eIF4E, for binding eIF4G and forming the active eIF4F complex. In addition, leucine enhances phosphorylation of the 70-kDa ribosomal protein S6 kinase (S6K1). These results suggest that leucine upregulates protein synthesis in skeletal muscle by enhancing both the activity and synthesis of proteins involved in mRNA translation. The stimulatory effects of leucine on translation initiation are mediated in part through the protein kinase mammalian target of rapamycin (mTOR), where both insulin signaling and leucine signaling converge to promote a maximal response. |
| doi_str_mv | 10.1093/jn/131.3.856S |
| format | Article |
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Oral administration of leucine stimulates protein synthesis in association with hyperphosphorylation of the translational repressor, eukaryotic initiation factor (eIF) 4E binding protein 1 (4E-BP1), resulting in enhanced availability of the mRNA cap-binding protein eIF4E, for binding eIF4G and forming the active eIF4F complex. In addition, leucine enhances phosphorylation of the 70-kDa ribosomal protein S6 kinase (S6K1). These results suggest that leucine upregulates protein synthesis in skeletal muscle by enhancing both the activity and synthesis of proteins involved in mRNA translation. The stimulatory effects of leucine on translation initiation are mediated in part through the protein kinase mammalian target of rapamycin (mTOR), where both insulin signaling and leucine signaling converge to promote a maximal response.</description><identifier>ISSN: 0022-3166</identifier><identifier>EISSN: 1541-6100</identifier><identifier>DOI: 10.1093/jn/131.3.856S</identifier><identifier>PMID: 11238774</identifier><identifier>CODEN: JONUAI</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Immunosuppressive Agents - pharmacology ; insulin ; Insulin - physiology ; leucine ; Leucine - physiology ; Muscle Proteins - biosynthesis ; Muscle Proteins - genetics ; Muscle, Skeletal - drug effects ; Muscle, Skeletal - metabolism ; Phosphorylation ; Protein Biosynthesis - physiology ; protein synthesis ; Rats ; RNA, Messenger ; Signal Transduction - physiology ; Sirolimus - pharmacology ; skeletal muscle ; Striated muscle. Tendons ; translation initiation ; Vertebrates: osteoarticular system, musculoskeletal system</subject><ispartof>The Journal of nutrition, 2001-03, Vol.131 (3), p.856S-860S</ispartof><rights>2001 American Society for Nutrition.</rights><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-add70239a3d805f31c38980fd86dd19421ab7fa73083910fa40196dc79b3db513</citedby><cites>FETCH-LOGICAL-c471t-add70239a3d805f31c38980fd86dd19421ab7fa73083910fa40196dc79b3db513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1054998$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11238774$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Anthony, Joshua C.</creatorcontrib><creatorcontrib>Anthony, Tracy G.</creatorcontrib><creatorcontrib>Kimball, Scot R.</creatorcontrib><creatorcontrib>Jefferson, Leonard S.</creatorcontrib><title>Signaling Pathways Involved in Translational Control of Protein Synthesis in Skeletal Muscle by Leucine</title><title>The Journal of nutrition</title><addtitle>J Nutr</addtitle><description>Numerous reports established that in skeletal muscle the indispensable branched-chain amino acid leucine is unique in its ability to initiate signal transduction pathways that modulate translation initiation. Oral administration of leucine stimulates protein synthesis in association with hyperphosphorylation of the translational repressor, eukaryotic initiation factor (eIF) 4E binding protein 1 (4E-BP1), resulting in enhanced availability of the mRNA cap-binding protein eIF4E, for binding eIF4G and forming the active eIF4F complex. In addition, leucine enhances phosphorylation of the 70-kDa ribosomal protein S6 kinase (S6K1). These results suggest that leucine upregulates protein synthesis in skeletal muscle by enhancing both the activity and synthesis of proteins involved in mRNA translation. The stimulatory effects of leucine on translation initiation are mediated in part through the protein kinase mammalian target of rapamycin (mTOR), where both insulin signaling and leucine signaling converge to promote a maximal response.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunosuppressive Agents - pharmacology</subject><subject>insulin</subject><subject>Insulin - physiology</subject><subject>leucine</subject><subject>Leucine - physiology</subject><subject>Muscle Proteins - biosynthesis</subject><subject>Muscle Proteins - genetics</subject><subject>Muscle, Skeletal - drug effects</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Biosynthesis - physiology</subject><subject>protein synthesis</subject><subject>Rats</subject><subject>RNA, Messenger</subject><subject>Signal Transduction - physiology</subject><subject>Sirolimus - pharmacology</subject><subject>skeletal muscle</subject><subject>Striated muscle. Tendons</subject><subject>translation initiation</subject><subject>Vertebrates: osteoarticular system, musculoskeletal system</subject><issn>0022-3166</issn><issn>1541-6100</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10EtvEzEUhmELgWgoLNkiLxC7SX3Gc_MSRVwqBVEpZW157DOpg2MX25Mq_x5HiVQ2rM7m0aejl5D3wJbABL_Z-RvgsOTLoe02L8gC2gaqDhh7SRaM1XXFoeuuyJuUdowxaMTwmlwB1Hzo-2ZBthu79cpZv6V3Kj88qWOit_4Q3AENtZ7eR-WTU9mGougq-ByDo2GidzFkLGBz9PkBk00nvfmNDnOBP-akHdLxSNc4a-vxLXk1KZfw3eVek19fv9yvvlfrn99uV5_XlW56yJUypmc1F4qbgbUTB80HMbDJDJ0xIJoa1NhPquds4ALYpBoGojO6FyM3Ywv8mnw67z7G8GfGlOXeJo3OKY9hTrLvRMuF4AVWZ6hjSCniJB-j3at4lMDkqazceVnKSi5PZYv_cBmexz2aZ31JWcDHC1BJKzeVcNqmf1bbRoihsP7MsFQ4WIwyaYteo7ERdZYm2P988BcVJ5RL</recordid><startdate>20010301</startdate><enddate>20010301</enddate><creator>Anthony, Joshua C.</creator><creator>Anthony, Tracy G.</creator><creator>Kimball, Scot R.</creator><creator>Jefferson, Leonard S.</creator><general>Elsevier Inc</general><general>American Society for Nutritional Sciences</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>20010301</creationdate><title>Signaling Pathways Involved in Translational Control of Protein Synthesis in Skeletal Muscle by Leucine</title><author>Anthony, Joshua C. ; Anthony, Tracy G. ; Kimball, Scot R. ; Jefferson, Leonard S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-add70239a3d805f31c38980fd86dd19421ab7fa73083910fa40196dc79b3db513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunosuppressive Agents - pharmacology</topic><topic>insulin</topic><topic>Insulin - physiology</topic><topic>leucine</topic><topic>Leucine - physiology</topic><topic>Muscle Proteins - biosynthesis</topic><topic>Muscle Proteins - genetics</topic><topic>Muscle, Skeletal - drug effects</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Biosynthesis - physiology</topic><topic>protein synthesis</topic><topic>Rats</topic><topic>RNA, Messenger</topic><topic>Signal Transduction - physiology</topic><topic>Sirolimus - pharmacology</topic><topic>skeletal muscle</topic><topic>Striated muscle. Tendons</topic><topic>translation initiation</topic><topic>Vertebrates: osteoarticular system, musculoskeletal system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anthony, Joshua C.</creatorcontrib><creatorcontrib>Anthony, Tracy G.</creatorcontrib><creatorcontrib>Kimball, Scot R.</creatorcontrib><creatorcontrib>Jefferson, Leonard S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>MEDLINE - Academic</collection><jtitle>The Journal of nutrition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Anthony, Joshua C.</au><au>Anthony, Tracy G.</au><au>Kimball, Scot R.</au><au>Jefferson, Leonard S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Signaling Pathways Involved in Translational Control of Protein Synthesis in Skeletal Muscle by Leucine</atitle><jtitle>The Journal of nutrition</jtitle><addtitle>J Nutr</addtitle><date>2001-03-01</date><risdate>2001</risdate><volume>131</volume><issue>3</issue><spage>856S</spage><epage>860S</epage><pages>856S-860S</pages><issn>0022-3166</issn><eissn>1541-6100</eissn><coden>JONUAI</coden><abstract>Numerous reports established that in skeletal muscle the indispensable branched-chain amino acid leucine is unique in its ability to initiate signal transduction pathways that modulate translation initiation. Oral administration of leucine stimulates protein synthesis in association with hyperphosphorylation of the translational repressor, eukaryotic initiation factor (eIF) 4E binding protein 1 (4E-BP1), resulting in enhanced availability of the mRNA cap-binding protein eIF4E, for binding eIF4G and forming the active eIF4F complex. In addition, leucine enhances phosphorylation of the 70-kDa ribosomal protein S6 kinase (S6K1). These results suggest that leucine upregulates protein synthesis in skeletal muscle by enhancing both the activity and synthesis of proteins involved in mRNA translation. The stimulatory effects of leucine on translation initiation are mediated in part through the protein kinase mammalian target of rapamycin (mTOR), where both insulin signaling and leucine signaling converge to promote a maximal response.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>11238774</pmid><doi>10.1093/jn/131.3.856S</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Biological and medical sciences Fundamental and applied biological sciences. Psychology Immunosuppressive Agents - pharmacology insulin Insulin - physiology leucine Leucine - physiology Muscle Proteins - biosynthesis Muscle Proteins - genetics Muscle, Skeletal - drug effects Muscle, Skeletal - metabolism Phosphorylation Protein Biosynthesis - physiology protein synthesis Rats RNA, Messenger Signal Transduction - physiology Sirolimus - pharmacology skeletal muscle Striated muscle. Tendons translation initiation Vertebrates: osteoarticular system, musculoskeletal system |
| title | Signaling Pathways Involved in Translational Control of Protein Synthesis in Skeletal Muscle by Leucine |
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