Quantitative analysis of muscle fibre type and myosin heavy chain distribution in the frog hindlimb: implications for locomotory design
To investigate the design of the frog muscular system for jumping, fibre type distribution and myosin heavy chain (MHC) isoform composition were quantified in the hindlimb muscles of Rana pipiens. Muscles were divided into two groups: five large extensor muscles which were predicted to shorten and p...
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Veröffentlicht in: | Journal of muscle research and cell motility 1998-10, Vol.19 (7), p.717-731 |
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description | To investigate the design of the frog muscular system for jumping, fibre type distribution and myosin heavy chain (MHC) isoform composition were quantified in the hindlimb muscles of Rana pipiens. Muscles were divided into two groups: five large extensor muscles which were predicted to shorten and produce mechanical power during jumping (JP), and four much smaller muscles commonly used in muscle physiology studies, but that do not shorten or produce power during jumping (NJP). fibres were classified as one of four different types (type 1, 2, 3 or tonic) or an intermediate type (type 1-2) based on their relative myosin-ATPase reactivity and MHC immunoreactivity in muscle cross-sections according to previous nomenclature established for amphibian skeletal muscle. Type 1 fibres correspond to the fastest and most powerful of the twitch fibres, and type 3 fibres are the slowest and least powerful. Myosin-ATPase histochemistry revealed that the JP muscles were composed primarily of type 1 fibres (89%) with a small percentage of type 2 (7%) and intermediate type 1-2 fibres (4%). The fibre type composition of NJP muscles was more evenly distributed between type 1 (29%), type 2 (46%) and type 1-2 (24%) fibres. Tonic fibres comprised less than 2% of the muscle cross-section in both JP and NJP groups. Similarly, MHC composition determined by quantitative SDS-PAGE revealed that JP muscles were composed predominantly of type 1 MHC (86%), with a balance of type 2 MHC (14%). The opposite pattern was found for MHC composition in the NJP muscles: type 1 (28%), type 2 (66%) and type 3 (6%). These results demonstrate that the large extensor muscles that produce the power required for jumping have a fibre type distribution that enables them to generate high levels of mechanical power, with the type 1 isoform accounting for 85-90% of the total MHC content. |
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Muscles were divided into two groups: five large extensor muscles which were predicted to shorten and produce mechanical power during jumping (JP), and four much smaller muscles commonly used in muscle physiology studies, but that do not shorten or produce power during jumping (NJP). fibres were classified as one of four different types (type 1, 2, 3 or tonic) or an intermediate type (type 1-2) based on their relative myosin-ATPase reactivity and MHC immunoreactivity in muscle cross-sections according to previous nomenclature established for amphibian skeletal muscle. Type 1 fibres correspond to the fastest and most powerful of the twitch fibres, and type 3 fibres are the slowest and least powerful. Myosin-ATPase histochemistry revealed that the JP muscles were composed primarily of type 1 fibres (89%) with a small percentage of type 2 (7%) and intermediate type 1-2 fibres (4%). The fibre type composition of NJP muscles was more evenly distributed between type 1 (29%), type 2 (46%) and type 1-2 (24%) fibres. Tonic fibres comprised less than 2% of the muscle cross-section in both JP and NJP groups. Similarly, MHC composition determined by quantitative SDS-PAGE revealed that JP muscles were composed predominantly of type 1 MHC (86%), with a balance of type 2 MHC (14%). The opposite pattern was found for MHC composition in the NJP muscles: type 1 (28%), type 2 (66%) and type 3 (6%). These results demonstrate that the large extensor muscles that produce the power required for jumping have a fibre type distribution that enables them to generate high levels of mechanical power, with the type 1 isoform accounting for 85-90% of the total MHC content.</description><identifier>ISSN: 0142-4319</identifier><identifier>EISSN: 1573-2657</identifier><identifier>DOI: 10.1023/A:1005466432372</identifier><identifier>PMID: 9836143</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Animals ; Biomechanical Phenomena ; Electrophoresis, Polyacrylamide Gel ; Freshwater ; Hindlimb - anatomy & histology ; Hindlimb - metabolism ; Locomotion - physiology ; Male ; Muscle Fibers, Fast-Twitch - chemistry ; Muscle Fibers, Skeletal - chemistry ; Muscle Fibers, Skeletal - classification ; Muscle Fibers, Skeletal - physiology ; Muscle Fibers, Skeletal - ultrastructure ; Muscle Fibers, Slow-Twitch - chemistry ; Muscle, Skeletal - chemistry ; Muscle, Skeletal - physiology ; Muscle, Skeletal - ultrastructure ; Muscular system ; Myosin Heavy Chains - analysis ; Myosin Heavy Chains - classification ; Myosins - analysis ; Protein Isoforms - analysis ; Proteins ; Rana pipiens ; Rana pipiens - anatomy & histology ; Rana pipiens - physiology ; Space life sciences</subject><ispartof>Journal of muscle research and cell motility, 1998-10, Vol.19 (7), p.717-731</ispartof><rights>Kluwer Academic Publishers 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c310t-f2f4951cabfa880eb4ba568a12cac554aa7a982008b6c3140acb8229d66d19273</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9836143$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lutz, G J</creatorcontrib><creatorcontrib>Bremner, S</creatorcontrib><creatorcontrib>Lajevardi, N</creatorcontrib><creatorcontrib>Lieber, R L</creatorcontrib><creatorcontrib>Rome, L C</creatorcontrib><title>Quantitative analysis of muscle fibre type and myosin heavy chain distribution in the frog hindlimb: implications for locomotory design</title><title>Journal of muscle research and cell motility</title><addtitle>J Muscle Res Cell Motil</addtitle><description>To investigate the design of the frog muscular system for jumping, fibre type distribution and myosin heavy chain (MHC) isoform composition were quantified in the hindlimb muscles of Rana pipiens. Muscles were divided into two groups: five large extensor muscles which were predicted to shorten and produce mechanical power during jumping (JP), and four much smaller muscles commonly used in muscle physiology studies, but that do not shorten or produce power during jumping (NJP). fibres were classified as one of four different types (type 1, 2, 3 or tonic) or an intermediate type (type 1-2) based on their relative myosin-ATPase reactivity and MHC immunoreactivity in muscle cross-sections according to previous nomenclature established for amphibian skeletal muscle. Type 1 fibres correspond to the fastest and most powerful of the twitch fibres, and type 3 fibres are the slowest and least powerful. Myosin-ATPase histochemistry revealed that the JP muscles were composed primarily of type 1 fibres (89%) with a small percentage of type 2 (7%) and intermediate type 1-2 fibres (4%). The fibre type composition of NJP muscles was more evenly distributed between type 1 (29%), type 2 (46%) and type 1-2 (24%) fibres. Tonic fibres comprised less than 2% of the muscle cross-section in both JP and NJP groups. Similarly, MHC composition determined by quantitative SDS-PAGE revealed that JP muscles were composed predominantly of type 1 MHC (86%), with a balance of type 2 MHC (14%). The opposite pattern was found for MHC composition in the NJP muscles: type 1 (28%), type 2 (66%) and type 3 (6%). These results demonstrate that the large extensor muscles that produce the power required for jumping have a fibre type distribution that enables them to generate high levels of mechanical power, with the type 1 isoform accounting for 85-90% of the total MHC content.</description><subject>Animals</subject><subject>Biomechanical Phenomena</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Freshwater</subject><subject>Hindlimb - anatomy & histology</subject><subject>Hindlimb - metabolism</subject><subject>Locomotion - physiology</subject><subject>Male</subject><subject>Muscle Fibers, Fast-Twitch - chemistry</subject><subject>Muscle Fibers, Skeletal - chemistry</subject><subject>Muscle Fibers, Skeletal - classification</subject><subject>Muscle Fibers, Skeletal - physiology</subject><subject>Muscle Fibers, Skeletal - ultrastructure</subject><subject>Muscle Fibers, Slow-Twitch - chemistry</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Muscle, Skeletal - physiology</subject><subject>Muscle, Skeletal - ultrastructure</subject><subject>Muscular system</subject><subject>Myosin Heavy Chains - analysis</subject><subject>Myosin Heavy Chains - classification</subject><subject>Myosins - analysis</subject><subject>Protein Isoforms - analysis</subject><subject>Proteins</subject><subject>Rana pipiens</subject><subject>Rana pipiens - anatomy & histology</subject><subject>Rana pipiens - physiology</subject><subject>Space life sciences</subject><issn>0142-4319</issn><issn>1573-2657</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkU1LxDAQhoMo6_px9iQED96q-W7rTRa_QBBBz8skTd1I26xJutBf4N82i3vy4mlmmOd9DjMInVFyRQnj17c3lBAplBKc8ZLtoTmVJS-YkuU-mhMqWCE4rQ_RUYyfJKM1YzM0qyuuqOBz9P06wpBcguQ2FsMA3RRdxL7F_RhNZ3HrdLA4TevttsH95KMb8MrCZsJmBblvXEzB6TE5P-A8p1VOBf-BV25oOtfrG-z6decMbImIWx9w543vffJhwo2N7mM4QQctdNGe7uoxer-_e1s8Fs8vD0-L2-fCcEpS0bJW1JIa0C1UFbFaaJCqAsoMGCkFQAl1xQiptMoJQcDoirG6UaqhNSv5Mbr89a6D_xptTMveRWO7Dgbrx7gsc7QWkv0L0pIrQYnK4MUf8NOPIR8yyxSXFZPl1na-g0bd22a5Dq6HMC13f-A_LBuMBg</recordid><startdate>19981001</startdate><enddate>19981001</enddate><creator>Lutz, G J</creator><creator>Bremner, S</creator><creator>Lajevardi, N</creator><creator>Lieber, R L</creator><creator>Rome, L C</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QP</scope><scope>7RV</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19981001</creationdate><title>Quantitative analysis of muscle fibre type and myosin heavy chain distribution in the frog hindlimb: implications for locomotory design</title><author>Lutz, G J ; Bremner, S ; Lajevardi, N ; Lieber, R L ; Rome, L C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c310t-f2f4951cabfa880eb4ba568a12cac554aa7a982008b6c3140acb8229d66d19273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Biomechanical Phenomena</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Freshwater</topic><topic>Hindlimb - anatomy & histology</topic><topic>Hindlimb - metabolism</topic><topic>Locomotion - physiology</topic><topic>Male</topic><topic>Muscle Fibers, Fast-Twitch - chemistry</topic><topic>Muscle Fibers, Skeletal - chemistry</topic><topic>Muscle Fibers, Skeletal - classification</topic><topic>Muscle Fibers, Skeletal - physiology</topic><topic>Muscle Fibers, Skeletal - ultrastructure</topic><topic>Muscle Fibers, Slow-Twitch - chemistry</topic><topic>Muscle, Skeletal - chemistry</topic><topic>Muscle, Skeletal - physiology</topic><topic>Muscle, Skeletal - ultrastructure</topic><topic>Muscular system</topic><topic>Myosin Heavy Chains - analysis</topic><topic>Myosin Heavy Chains - classification</topic><topic>Myosins - analysis</topic><topic>Protein Isoforms - analysis</topic><topic>Proteins</topic><topic>Rana pipiens</topic><topic>Rana pipiens - anatomy & histology</topic><topic>Rana pipiens - physiology</topic><topic>Space life sciences</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lutz, G J</creatorcontrib><creatorcontrib>Bremner, S</creatorcontrib><creatorcontrib>Lajevardi, N</creatorcontrib><creatorcontrib>Lieber, R L</creatorcontrib><creatorcontrib>Rome, L C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of muscle research and cell motility</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lutz, G J</au><au>Bremner, S</au><au>Lajevardi, N</au><au>Lieber, R L</au><au>Rome, L C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative analysis of muscle fibre type and myosin heavy chain distribution in the frog hindlimb: implications for locomotory design</atitle><jtitle>Journal of muscle research and cell motility</jtitle><addtitle>J Muscle Res Cell Motil</addtitle><date>1998-10-01</date><risdate>1998</risdate><volume>19</volume><issue>7</issue><spage>717</spage><epage>731</epage><pages>717-731</pages><issn>0142-4319</issn><eissn>1573-2657</eissn><abstract>To investigate the design of the frog muscular system for jumping, fibre type distribution and myosin heavy chain (MHC) isoform composition were quantified in the hindlimb muscles of Rana pipiens. Muscles were divided into two groups: five large extensor muscles which were predicted to shorten and produce mechanical power during jumping (JP), and four much smaller muscles commonly used in muscle physiology studies, but that do not shorten or produce power during jumping (NJP). fibres were classified as one of four different types (type 1, 2, 3 or tonic) or an intermediate type (type 1-2) based on their relative myosin-ATPase reactivity and MHC immunoreactivity in muscle cross-sections according to previous nomenclature established for amphibian skeletal muscle. Type 1 fibres correspond to the fastest and most powerful of the twitch fibres, and type 3 fibres are the slowest and least powerful. Myosin-ATPase histochemistry revealed that the JP muscles were composed primarily of type 1 fibres (89%) with a small percentage of type 2 (7%) and intermediate type 1-2 fibres (4%). The fibre type composition of NJP muscles was more evenly distributed between type 1 (29%), type 2 (46%) and type 1-2 (24%) fibres. Tonic fibres comprised less than 2% of the muscle cross-section in both JP and NJP groups. Similarly, MHC composition determined by quantitative SDS-PAGE revealed that JP muscles were composed predominantly of type 1 MHC (86%), with a balance of type 2 MHC (14%). The opposite pattern was found for MHC composition in the NJP muscles: type 1 (28%), type 2 (66%) and type 3 (6%). These results demonstrate that the large extensor muscles that produce the power required for jumping have a fibre type distribution that enables them to generate high levels of mechanical power, with the type 1 isoform accounting for 85-90% of the total MHC content.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>9836143</pmid><doi>10.1023/A:1005466432372</doi><tpages>15</tpages></addata></record> |
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subjects | Animals Biomechanical Phenomena Electrophoresis, Polyacrylamide Gel Freshwater Hindlimb - anatomy & histology Hindlimb - metabolism Locomotion - physiology Male Muscle Fibers, Fast-Twitch - chemistry Muscle Fibers, Skeletal - chemistry Muscle Fibers, Skeletal - classification Muscle Fibers, Skeletal - physiology Muscle Fibers, Skeletal - ultrastructure Muscle Fibers, Slow-Twitch - chemistry Muscle, Skeletal - chemistry Muscle, Skeletal - physiology Muscle, Skeletal - ultrastructure Muscular system Myosin Heavy Chains - analysis Myosin Heavy Chains - classification Myosins - analysis Protein Isoforms - analysis Proteins Rana pipiens Rana pipiens - anatomy & histology Rana pipiens - physiology Space life sciences |
title | Quantitative analysis of muscle fibre type and myosin heavy chain distribution in the frog hindlimb: implications for locomotory design |
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