Contractile properties of muscle fibers from the deep and superficial digital flexors of horses
Equine digital flexor muscles have independent tendons but a nearly identical mechanical relationship to the main joint they act upon. Yet these muscles have remarkable diversity in architecture, ranging from long, unipennate fibers ("short" compartment of DDF) to very short, multipennate...
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creator | Butcher, M T Chase, P B Hermanson, J W Clark, A N Brunet, N M Bertram, J E A |
description | Equine digital flexor muscles have independent tendons but a nearly identical mechanical relationship to the main joint they act upon. Yet these muscles have remarkable diversity in architecture, ranging from long, unipennate fibers ("short" compartment of DDF) to very short, multipennate fibers (SDF). To investigate the functional relevance of the form of the digital flexor muscles, fiber contractile properties were analyzed in the context of architecture differences and in vivo function during locomotion. Myosin heavy chain (MHC) isoform fiber type was studied, and in vitro motility assays were used to measure actin filament sliding velocity (V(f)). Skinned fiber contractile properties [isometric tension (P(0)/CSA), velocity of unloaded shortening (V(US)), and force-Ca(2+) relationships] at both 10 and 30°C were characterized. Contractile properties were correlated with MHC isoform and their respective V(f). The DDF contained a higher percentage of MHC-2A fibers with myosin (heavy meromyosin) and V(f) that was twofold faster than SDF. At 30°C, P(0)/CSA was higher for DDF (103.5 ± 8.75 mN/mm(2)) than SDF fibers (81.8 ± 7.71 mN/mm(2)). Similarly, V(US) (pCa 5, 30°C) was faster for DDF (2.43 ± 0.53 FL/s) than SDF fibers (1.20 ± 0.22 FL/s). Active isometric tension increased with increasing Ca(2+) concentration, with maximal Ca(2+) activation at pCa 5 at each temperature in fibers from each muscle. In general, the collective properties of DDF and SDF were consistent with fiber MHC isoform composition, muscle architecture, and the respective functional roles of the two muscles in locomotion. |
doi_str_mv | 10.1152/ajpregu.00510.2009 |
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Yet these muscles have remarkable diversity in architecture, ranging from long, unipennate fibers ("short" compartment of DDF) to very short, multipennate fibers (SDF). To investigate the functional relevance of the form of the digital flexor muscles, fiber contractile properties were analyzed in the context of architecture differences and in vivo function during locomotion. Myosin heavy chain (MHC) isoform fiber type was studied, and in vitro motility assays were used to measure actin filament sliding velocity (V(f)). Skinned fiber contractile properties [isometric tension (P(0)/CSA), velocity of unloaded shortening (V(US)), and force-Ca(2+) relationships] at both 10 and 30°C were characterized. Contractile properties were correlated with MHC isoform and their respective V(f). The DDF contained a higher percentage of MHC-2A fibers with myosin (heavy meromyosin) and V(f) that was twofold faster than SDF. At 30°C, P(0)/CSA was higher for DDF (103.5 ± 8.75 mN/mm(2)) than SDF fibers (81.8 ± 7.71 mN/mm(2)). Similarly, V(US) (pCa 5, 30°C) was faster for DDF (2.43 ± 0.53 FL/s) than SDF fibers (1.20 ± 0.22 FL/s). Active isometric tension increased with increasing Ca(2+) concentration, with maximal Ca(2+) activation at pCa 5 at each temperature in fibers from each muscle. In general, the collective properties of DDF and SDF were consistent with fiber MHC isoform composition, muscle architecture, and the respective functional roles of the two muscles in locomotion.</description><identifier>ISSN: 0363-6119</identifier><identifier>EISSN: 1522-1490</identifier><identifier>DOI: 10.1152/ajpregu.00510.2009</identifier><identifier>PMID: 20702801</identifier><identifier>CODEN: AJPRDO</identifier><language>eng</language><publisher>United States: American Physiological Society</publisher><subject>Animals ; Biomechanical Phenomena ; Body Temperature - physiology ; Calcium ; Calcium - physiology ; Cell Movement ; Electrophoresis, Polyacrylamide Gel ; Female ; Horses ; Horses - physiology ; Immunohistochemistry ; Isometric Contraction ; Joints - physiology ; Locomotion - physiology ; Male ; Muscle Contraction - physiology ; Muscle Fibers, Skeletal - chemistry ; Muscle Fibers, Skeletal - classification ; Muscle Fibers, Skeletal - physiology ; Muscle, Skeletal - physiology ; Muscular system ; Myosin Heavy Chains - metabolism ; Myosins - chemistry ; Myosins - metabolism ; Physiology ; Tendons ; Tendons - physiology</subject><ispartof>American journal of physiology. Regulatory, integrative and comparative physiology, 2010-10, Vol.299 (4), p.R996-R1005</ispartof><rights>Copyright American Physiological Society Oct 2010</rights><rights>Copyright © 2010 the American Physiological Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c428t-ffdc390f648e0e45849b7e9dbb714f5c4c935fc78d7793e0609e952150ea294a3</citedby><cites>FETCH-LOGICAL-c428t-ffdc390f648e0e45849b7e9dbb714f5c4c935fc78d7793e0609e952150ea294a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,3025,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20702801$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Butcher, M T</creatorcontrib><creatorcontrib>Chase, P B</creatorcontrib><creatorcontrib>Hermanson, J W</creatorcontrib><creatorcontrib>Clark, A N</creatorcontrib><creatorcontrib>Brunet, N M</creatorcontrib><creatorcontrib>Bertram, J E A</creatorcontrib><title>Contractile properties of muscle fibers from the deep and superficial digital flexors of horses</title><title>American journal of physiology. Regulatory, integrative and comparative physiology</title><addtitle>Am J Physiol Regul Integr Comp Physiol</addtitle><description>Equine digital flexor muscles have independent tendons but a nearly identical mechanical relationship to the main joint they act upon. Yet these muscles have remarkable diversity in architecture, ranging from long, unipennate fibers ("short" compartment of DDF) to very short, multipennate fibers (SDF). To investigate the functional relevance of the form of the digital flexor muscles, fiber contractile properties were analyzed in the context of architecture differences and in vivo function during locomotion. Myosin heavy chain (MHC) isoform fiber type was studied, and in vitro motility assays were used to measure actin filament sliding velocity (V(f)). Skinned fiber contractile properties [isometric tension (P(0)/CSA), velocity of unloaded shortening (V(US)), and force-Ca(2+) relationships] at both 10 and 30°C were characterized. Contractile properties were correlated with MHC isoform and their respective V(f). The DDF contained a higher percentage of MHC-2A fibers with myosin (heavy meromyosin) and V(f) that was twofold faster than SDF. At 30°C, P(0)/CSA was higher for DDF (103.5 ± 8.75 mN/mm(2)) than SDF fibers (81.8 ± 7.71 mN/mm(2)). Similarly, V(US) (pCa 5, 30°C) was faster for DDF (2.43 ± 0.53 FL/s) than SDF fibers (1.20 ± 0.22 FL/s). Active isometric tension increased with increasing Ca(2+) concentration, with maximal Ca(2+) activation at pCa 5 at each temperature in fibers from each muscle. In general, the collective properties of DDF and SDF were consistent with fiber MHC isoform composition, muscle architecture, and the respective functional roles of the two muscles in locomotion.</description><subject>Animals</subject><subject>Biomechanical Phenomena</subject><subject>Body Temperature - physiology</subject><subject>Calcium</subject><subject>Calcium - physiology</subject><subject>Cell Movement</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Horses</subject><subject>Horses - physiology</subject><subject>Immunohistochemistry</subject><subject>Isometric Contraction</subject><subject>Joints - physiology</subject><subject>Locomotion - physiology</subject><subject>Male</subject><subject>Muscle Contraction - physiology</subject><subject>Muscle Fibers, Skeletal - chemistry</subject><subject>Muscle Fibers, Skeletal - classification</subject><subject>Muscle Fibers, Skeletal - physiology</subject><subject>Muscle, Skeletal - physiology</subject><subject>Muscular system</subject><subject>Myosin Heavy Chains - metabolism</subject><subject>Myosins - chemistry</subject><subject>Myosins - metabolism</subject><subject>Physiology</subject><subject>Tendons</subject><subject>Tendons - physiology</subject><issn>0363-6119</issn><issn>1522-1490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdUcuO1DAQtBCInR34AQ4o4sIpS_sVxxckNOIlrcQFzpbjtGc8SuJgJ2j37_HMDivgVFJ3Vamri5BXFG4oleydPc4J9-sNgCwjBqCfkE1ZsJoKDU_JBnjD64ZSfUWucz4CgOCCPydXDBSwFuiGmF2clmTdEgas5hRnTEvAXEVfjWt2ZehDhylXPsWxWg5Y9YhzZae-ymsh--CCHao-7MNS0A94F9NZfiiI-QV55u2Q8eUFt-THp4_fd1_q22-fv-4-3NZOsHapve8d1-Ab0SKgkK3QnULdd52iwksnnObSO9X2SmmO0IBGLRmVgJZpYfmWvH_wndduxN7hKdVg5hRGm-5NtMH8u5nCwezjL8O0VLx4bsnbi0GKP1fMixlDdjgMdsK4ZqNkw6GlZ-ab_5jHuKappCsk1TIJ5clbwh5ILsWcE_rHUyiYU3vm0p45t2dO7RXR679DPEr-1MV_A-0LmWA</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>Butcher, M T</creator><creator>Chase, P B</creator><creator>Hermanson, J W</creator><creator>Clark, A N</creator><creator>Brunet, N M</creator><creator>Bertram, J E A</creator><general>American Physiological Society</general><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>7QR</scope><scope>7TS</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20101001</creationdate><title>Contractile properties of muscle fibers from the deep and superficial digital flexors of horses</title><author>Butcher, M T ; Chase, P B ; Hermanson, J W ; Clark, A N ; Brunet, N M ; Bertram, J E A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c428t-ffdc390f648e0e45849b7e9dbb714f5c4c935fc78d7793e0609e952150ea294a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Biomechanical Phenomena</topic><topic>Body Temperature - physiology</topic><topic>Calcium</topic><topic>Calcium - physiology</topic><topic>Cell Movement</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Horses</topic><topic>Horses - physiology</topic><topic>Immunohistochemistry</topic><topic>Isometric Contraction</topic><topic>Joints - physiology</topic><topic>Locomotion - physiology</topic><topic>Male</topic><topic>Muscle Contraction - physiology</topic><topic>Muscle Fibers, Skeletal - chemistry</topic><topic>Muscle Fibers, Skeletal - classification</topic><topic>Muscle Fibers, Skeletal - physiology</topic><topic>Muscle, Skeletal - physiology</topic><topic>Muscular system</topic><topic>Myosin Heavy Chains - metabolism</topic><topic>Myosins - chemistry</topic><topic>Myosins - metabolism</topic><topic>Physiology</topic><topic>Tendons</topic><topic>Tendons - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Butcher, M T</creatorcontrib><creatorcontrib>Chase, P B</creatorcontrib><creatorcontrib>Hermanson, J W</creatorcontrib><creatorcontrib>Clark, A N</creatorcontrib><creatorcontrib>Brunet, N M</creatorcontrib><creatorcontrib>Bertram, J E A</creatorcontrib><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>Chemoreception Abstracts</collection><collection>Physical Education Index</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>American journal of physiology. Regulatory, integrative and comparative physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Butcher, M T</au><au>Chase, P B</au><au>Hermanson, J W</au><au>Clark, A N</au><au>Brunet, N M</au><au>Bertram, J E A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Contractile properties of muscle fibers from the deep and superficial digital flexors of horses</atitle><jtitle>American journal of physiology. Regulatory, integrative and comparative physiology</jtitle><addtitle>Am J Physiol Regul Integr Comp Physiol</addtitle><date>2010-10-01</date><risdate>2010</risdate><volume>299</volume><issue>4</issue><spage>R996</spage><epage>R1005</epage><pages>R996-R1005</pages><issn>0363-6119</issn><eissn>1522-1490</eissn><coden>AJPRDO</coden><abstract>Equine digital flexor muscles have independent tendons but a nearly identical mechanical relationship to the main joint they act upon. Yet these muscles have remarkable diversity in architecture, ranging from long, unipennate fibers ("short" compartment of DDF) to very short, multipennate fibers (SDF). To investigate the functional relevance of the form of the digital flexor muscles, fiber contractile properties were analyzed in the context of architecture differences and in vivo function during locomotion. Myosin heavy chain (MHC) isoform fiber type was studied, and in vitro motility assays were used to measure actin filament sliding velocity (V(f)). Skinned fiber contractile properties [isometric tension (P(0)/CSA), velocity of unloaded shortening (V(US)), and force-Ca(2+) relationships] at both 10 and 30°C were characterized. Contractile properties were correlated with MHC isoform and their respective V(f). The DDF contained a higher percentage of MHC-2A fibers with myosin (heavy meromyosin) and V(f) that was twofold faster than SDF. At 30°C, P(0)/CSA was higher for DDF (103.5 ± 8.75 mN/mm(2)) than SDF fibers (81.8 ± 7.71 mN/mm(2)). Similarly, V(US) (pCa 5, 30°C) was faster for DDF (2.43 ± 0.53 FL/s) than SDF fibers (1.20 ± 0.22 FL/s). Active isometric tension increased with increasing Ca(2+) concentration, with maximal Ca(2+) activation at pCa 5 at each temperature in fibers from each muscle. In general, the collective properties of DDF and SDF were consistent with fiber MHC isoform composition, muscle architecture, and the respective functional roles of the two muscles in locomotion.</abstract><cop>United States</cop><pub>American Physiological Society</pub><pmid>20702801</pmid><doi>10.1152/ajpregu.00510.2009</doi><oa>free_for_read</oa></addata></record> |
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subjects | Animals Biomechanical Phenomena Body Temperature - physiology Calcium Calcium - physiology Cell Movement Electrophoresis, Polyacrylamide Gel Female Horses Horses - physiology Immunohistochemistry Isometric Contraction Joints - physiology Locomotion - physiology Male Muscle Contraction - physiology Muscle Fibers, Skeletal - chemistry Muscle Fibers, Skeletal - classification Muscle Fibers, Skeletal - physiology Muscle, Skeletal - physiology Muscular system Myosin Heavy Chains - metabolism Myosins - chemistry Myosins - metabolism Physiology Tendons Tendons - physiology |
title | Contractile properties of muscle fibers from the deep and superficial digital flexors of horses |
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