Super-relaxed state of myosin in human skeletal muscle is fiber-type dependent
The myosin super-relaxed state (SRX) in skeletal muscle is hypothesized to play an important role in regulating muscle contractility and thermogenesis in humans but has only been examined in model organisms. Here we report the first human skeletal muscle SRX measurements, using quantitative epifluor...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 2020-12, Vol.319 (6), p.C1158-C1162 |
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| container_title | American Journal of Physiology: Cell Physiology |
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| creator | Phung, Lien A. Foster, Aurora D. Miller, Mark S. Lowe, Dawn A. Thomas, David D. |
| description | The myosin super-relaxed state (SRX) in skeletal muscle is hypothesized to play an important role in regulating muscle contractility and thermogenesis in humans but has only been examined in model organisms. Here we report the first human skeletal muscle SRX measurements, using quantitative epifluorescence microscopy of fluorescent 2'/3'-O-(N-meth-ylanthraniloyl) ATP (mant-ATP) single-nucleotide turnover. Myosin heavy chain (MHC) isoform expression was determined using gel electrophoresis for each permeabilized vastus lateralis fiber, to allow for novel comparisons of SRX between fiber types. We find that the fraction of myosin in SRX is less in MHC IIA fibers than in MHC I and IIAX fibers (P = 0.008). ATP turnover of SRX is faster in MHC IIAX fibers compared with MHC I and IIA fibers (P = 0.001). We conclude that SRX biochemistry is measurable in human skeletal muscle, and our data indicate that SRX depends on fiber type as classified by MHC isoform. Extension from this preliminary work would provide further understanding regarding the role of SRX in human muscle physiology. |
| doi_str_mv | 10.1152/ajpcell.00396.2020 |
| format | Article |
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Here we report the first human skeletal muscle SRX measurements, using quantitative epifluorescence microscopy of fluorescent 2'/3'-O-(N-meth-ylanthraniloyl) ATP (mant-ATP) single-nucleotide turnover. Myosin heavy chain (MHC) isoform expression was determined using gel electrophoresis for each permeabilized vastus lateralis fiber, to allow for novel comparisons of SRX between fiber types. We find that the fraction of myosin in SRX is less in MHC IIA fibers than in MHC I and IIAX fibers (P = 0.008). ATP turnover of SRX is faster in MHC IIAX fibers compared with MHC I and IIA fibers (P = 0.001). We conclude that SRX biochemistry is measurable in human skeletal muscle, and our data indicate that SRX depends on fiber type as classified by MHC isoform. Extension from this preliminary work would provide further understanding regarding the role of SRX in human muscle physiology.</description><identifier>ISSN: 0363-6143</identifier><identifier>EISSN: 1522-1563</identifier><identifier>DOI: 10.1152/ajpcell.00396.2020</identifier><identifier>PMID: 32997515</identifier><language>eng</language><publisher>BETHESDA: Amer Physiological Soc</publisher><subject>Adult ; Cell Biology ; Humans ; Life Sciences & Biomedicine ; Muscle Contraction - physiology ; Muscle Fibers, Skeletal - metabolism ; Myosin Heavy Chains - metabolism ; Physiology ; Protein Isoforms - metabolism ; Quadriceps Muscle - cytology ; Quadriceps Muscle - metabolism ; Rapid Report ; Science & Technology ; Thermogenesis - physiology ; Young Adult</subject><ispartof>American Journal of Physiology: Cell Physiology, 2020-12, Vol.319 (6), p.C1158-C1162</ispartof><rights>Copyright © 2020 the American Physiological Society 2020 American Physiological Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>13</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000632705500006</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c402t-ac980124406c1b380f8ec4eb938024538085ff31113bb2d0b838681b6dc4eedc3</citedby><cites>FETCH-LOGICAL-c402t-ac980124406c1b380f8ec4eb938024538085ff31113bb2d0b838681b6dc4eedc3</cites><orcidid>0000-0002-5784-9289 ; 0000-0002-8822-2040</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,782,786,887,3043,27933,27934,28257</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32997515$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Phung, Lien A.</creatorcontrib><creatorcontrib>Foster, Aurora D.</creatorcontrib><creatorcontrib>Miller, Mark S.</creatorcontrib><creatorcontrib>Lowe, Dawn A.</creatorcontrib><creatorcontrib>Thomas, David D.</creatorcontrib><title>Super-relaxed state of myosin in human skeletal muscle is fiber-type dependent</title><title>American Journal of Physiology: Cell Physiology</title><addtitle>AM J PHYSIOL-CELL PH</addtitle><addtitle>Am J Physiol Cell Physiol</addtitle><description>The myosin super-relaxed state (SRX) in skeletal muscle is hypothesized to play an important role in regulating muscle contractility and thermogenesis in humans but has only been examined in model organisms. 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Extension from this preliminary work would provide further understanding regarding the role of SRX in human muscle physiology.</description><subject>Adult</subject><subject>Cell Biology</subject><subject>Humans</subject><subject>Life Sciences & Biomedicine</subject><subject>Muscle Contraction - physiology</subject><subject>Muscle Fibers, Skeletal - metabolism</subject><subject>Myosin Heavy Chains - metabolism</subject><subject>Physiology</subject><subject>Protein Isoforms - metabolism</subject><subject>Quadriceps Muscle - cytology</subject><subject>Quadriceps Muscle - metabolism</subject><subject>Rapid Report</subject><subject>Science & Technology</subject><subject>Thermogenesis - physiology</subject><subject>Young Adult</subject><issn>0363-6143</issn><issn>1522-1563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>AOWDO</sourceid><sourceid>EIF</sourceid><recordid>eNqNkcFu1DAQhi0EotvCC3CofERCWcZ24jgXJLSCUqmCA-3Zsp0JdUnsNE5o9-3xstsV3JAse-T5_pnR_IS8YbBmrOLvzd3osO_XAKKRaw4cnpFVTvCCVVI8JysQUhSSleKEnKZ0BwAll81LciJ409QVq1bk6_dlxKmYsDeP2NI0mxlp7OiwjckHms_tMphA00_scTY9HZbkeqQ-0c7brJy3I9IWRwwthvkVedGZPuHrw3tGbj5_ut58Ka6-XVxuPl4VrgQ-F8Y1ChgvS5COWaGgU-hKtE0OeVnlW1VdJxhjwlreglVCScWsbDOFrRNn5MO-7rjYIX_k1pPp9Tj5wUxbHY3X_2aCv9U_4i9d1w2XtcgF3h4KTPF-wTTrwafdNk3AuCSdZ6uVqLlSGeV71E0xpQm7YxsGemeEPhih_xihd0Zk0fnfAx4lT5vPgNoDD2hjl5zH4PCIZauk4DVUFezCjc---Bg2cQlzlr77f6n4DdECp6k</recordid><startdate>20201201</startdate><enddate>20201201</enddate><creator>Phung, Lien A.</creator><creator>Foster, Aurora D.</creator><creator>Miller, Mark S.</creator><creator>Lowe, Dawn A.</creator><creator>Thomas, David D.</creator><general>Amer Physiological Soc</general><general>American Physiological Society</general><scope>AOWDO</scope><scope>BLEPL</scope><scope>DTL</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><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5784-9289</orcidid><orcidid>https://orcid.org/0000-0002-8822-2040</orcidid></search><sort><creationdate>20201201</creationdate><title>Super-relaxed state of myosin in human skeletal muscle is fiber-type dependent</title><author>Phung, Lien A. ; Foster, Aurora D. ; Miller, Mark S. ; Lowe, Dawn A. ; Thomas, David D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c402t-ac980124406c1b380f8ec4eb938024538085ff31113bb2d0b838681b6dc4eedc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Adult</topic><topic>Cell Biology</topic><topic>Humans</topic><topic>Life Sciences & Biomedicine</topic><topic>Muscle Contraction - physiology</topic><topic>Muscle Fibers, Skeletal - metabolism</topic><topic>Myosin Heavy Chains - metabolism</topic><topic>Physiology</topic><topic>Protein Isoforms - metabolism</topic><topic>Quadriceps Muscle - cytology</topic><topic>Quadriceps Muscle - metabolism</topic><topic>Rapid Report</topic><topic>Science & Technology</topic><topic>Thermogenesis - physiology</topic><topic>Young Adult</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Phung, Lien A.</creatorcontrib><creatorcontrib>Foster, Aurora D.</creatorcontrib><creatorcontrib>Miller, Mark S.</creatorcontrib><creatorcontrib>Lowe, Dawn A.</creatorcontrib><creatorcontrib>Thomas, David D.</creatorcontrib><collection>Web of Science - Science Citation Index Expanded - 2020</collection><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>American Journal of Physiology: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Phung, Lien A.</au><au>Foster, Aurora D.</au><au>Miller, Mark S.</au><au>Lowe, Dawn A.</au><au>Thomas, David D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Super-relaxed state of myosin in human skeletal muscle is fiber-type dependent</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><stitle>AM J PHYSIOL-CELL PH</stitle><addtitle>Am J Physiol Cell Physiol</addtitle><date>2020-12-01</date><risdate>2020</risdate><volume>319</volume><issue>6</issue><spage>C1158</spage><epage>C1162</epage><pages>C1158-C1162</pages><issn>0363-6143</issn><eissn>1522-1563</eissn><abstract>The myosin super-relaxed state (SRX) in skeletal muscle is hypothesized to play an important role in regulating muscle contractility and thermogenesis in humans but has only been examined in model organisms. Here we report the first human skeletal muscle SRX measurements, using quantitative epifluorescence microscopy of fluorescent 2'/3'-O-(N-meth-ylanthraniloyl) ATP (mant-ATP) single-nucleotide turnover. Myosin heavy chain (MHC) isoform expression was determined using gel electrophoresis for each permeabilized vastus lateralis fiber, to allow for novel comparisons of SRX between fiber types. We find that the fraction of myosin in SRX is less in MHC IIA fibers than in MHC I and IIAX fibers (P = 0.008). ATP turnover of SRX is faster in MHC IIAX fibers compared with MHC I and IIA fibers (P = 0.001). We conclude that SRX biochemistry is measurable in human skeletal muscle, and our data indicate that SRX depends on fiber type as classified by MHC isoform. 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| subjects | Adult Cell Biology Humans Life Sciences & Biomedicine Muscle Contraction - physiology Muscle Fibers, Skeletal - metabolism Myosin Heavy Chains - metabolism Physiology Protein Isoforms - metabolism Quadriceps Muscle - cytology Quadriceps Muscle - metabolism Rapid Report Science & Technology Thermogenesis - physiology Young Adult |
| title | Super-relaxed state of myosin in human skeletal muscle is fiber-type dependent |
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