Early and long-term changes of equine skeletal muscle in response to endurance training and detraining
Twenty-four 4-year-old Andalusian (Spanish breed) stallions were used to examine the plasticity of myosin heavy chain (MHC) phenotype and the metabolic profile in horse skeletal muscle with long-term endurance-exercise training and detraining. Sixteen horses underwent a training programme based on a...
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description | Twenty-four 4-year-old Andalusian (Spanish breed) stallions were used to examine the plasticity of myosin heavy chain (MHC) phenotype and the metabolic profile in horse skeletal muscle with long-term endurance-exercise training and detraining. Sixteen horses underwent a training programme based on aerobic exercises for 8 months. Afterwards, they were kept in paddocks for 3 months. The remaining eight horses were used as controls. Three gluteus medius muscle biopsy samples were removed at depths of 20, 40 and 60 mm from each horse before (month 0), during (month 3) and after (month 8) training, and again after 3 months of detraining (month 11). MHC composition was analysed by electrophoresis and immunohistochemistry with anti-MHC monoclonal antibodies. Fibre areas, oxidative capacity and capillaries were studied histochemically. The activities of key muscle enzymes of aerobic (citrate synthase and 3-hydroxy-acyl-CoA-dehydrogenase) and anaerobic (phosphofructokinase and lactic dehydrogenase) metabolism and the intramuscular glycogen and triglyceride contents were also biochemically analysed. Early changes with training (3 months) included hypertrophy of type IIA fibres, a reduction of MHC-IIX with a concomitant increase of MHC-IIA, a rise in the number of high-oxidative fibres and in the activities of aerobic muscle enzymes and glycogen content. Long-term changes with training (8 months) were a further decline in the expression of MHC-IIX, an increase of slow MHC-I, additional increases of high-oxidative fibres, capillary density, activities of aerobic enzymes and endogenous glycogen; intramuscular lipid deposits also increased after 8 months of training whereas the activities of anaerobic enzymes declined. Most of exercise-induced alterations reverted after 3 months of detraining. These results indicate that endurance-exercise training induces a reversible transition of MHC composition in equine muscle in the order IIX-->IIA-->I, which is coordinated with changes in the metabolic properties of the muscle. Furthermore, a dose-response relationship was evident between the duration (in total) of training and the magnitude of muscle adaptations. |
doi_str_mv | 10.1007/s004240000408 |
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Sixteen horses underwent a training programme based on aerobic exercises for 8 months. Afterwards, they were kept in paddocks for 3 months. The remaining eight horses were used as controls. Three gluteus medius muscle biopsy samples were removed at depths of 20, 40 and 60 mm from each horse before (month 0), during (month 3) and after (month 8) training, and again after 3 months of detraining (month 11). MHC composition was analysed by electrophoresis and immunohistochemistry with anti-MHC monoclonal antibodies. Fibre areas, oxidative capacity and capillaries were studied histochemically. The activities of key muscle enzymes of aerobic (citrate synthase and 3-hydroxy-acyl-CoA-dehydrogenase) and anaerobic (phosphofructokinase and lactic dehydrogenase) metabolism and the intramuscular glycogen and triglyceride contents were also biochemically analysed. Early changes with training (3 months) included hypertrophy of type IIA fibres, a reduction of MHC-IIX with a concomitant increase of MHC-IIA, a rise in the number of high-oxidative fibres and in the activities of aerobic muscle enzymes and glycogen content. Long-term changes with training (8 months) were a further decline in the expression of MHC-IIX, an increase of slow MHC-I, additional increases of high-oxidative fibres, capillary density, activities of aerobic enzymes and endogenous glycogen; intramuscular lipid deposits also increased after 8 months of training whereas the activities of anaerobic enzymes declined. Most of exercise-induced alterations reverted after 3 months of detraining. These results indicate that endurance-exercise training induces a reversible transition of MHC composition in equine muscle in the order IIX-->IIA-->I, which is coordinated with changes in the metabolic properties of the muscle. Furthermore, a dose-response relationship was evident between the duration (in total) of training and the magnitude of muscle adaptations.</description><identifier>ISSN: 0031-6768</identifier><identifier>EISSN: 1432-2013</identifier><identifier>DOI: 10.1007/s004240000408</identifier><identifier>PMID: 11211112</identifier><language>eng</language><publisher>Germany: Springer Nature B.V</publisher><subject>3-Hydroxyacyl CoA Dehydrogenases - analysis ; Activities ; Animals ; Biopsy ; Capillaries - anatomy & histology ; Citrate (si)-Synthase - analysis ; Electrophoresis, Polyacrylamide Gel ; Glycogen - analysis ; Horses - physiology ; Immunohistochemistry ; L-Lactate Dehydrogenase - analysis ; Lactic Acid - blood ; Male ; Muscle Fibers, Skeletal - chemistry ; Muscle Fibers, Skeletal - metabolism ; Muscle Fibers, Skeletal - ultrastructure ; Muscle, Skeletal - anatomy & histology ; Muscle, Skeletal - chemistry ; Muscle, Skeletal - physiology ; Myosin Heavy Chains - analysis ; Oxidation-Reduction ; Phosphofructokinase-1 - analysis ; Physical Conditioning, Animal ; Physical Endurance ; Physical Exertion ; Physical fitness ; Proteins ; Triglycerides - analysis</subject><ispartof>Pflügers Archiv, 2000-12, Vol.441 (2-3), p.263-274</ispartof><rights>Springer-Verlag 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-b876a562f666f66af874a977b646d40c414f95bec0c1e290abaafa4107373d963</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/11211112$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Serrano, A L</creatorcontrib><creatorcontrib>Quiroz-Rothe, E</creatorcontrib><creatorcontrib>Rivero, J L</creatorcontrib><title>Early and long-term changes of equine skeletal muscle in response to endurance training and detraining</title><title>Pflügers Archiv</title><addtitle>Pflugers Arch</addtitle><description>Twenty-four 4-year-old Andalusian (Spanish breed) stallions were used to examine the plasticity of myosin heavy chain (MHC) phenotype and the metabolic profile in horse skeletal muscle with long-term endurance-exercise training and detraining. Sixteen horses underwent a training programme based on aerobic exercises for 8 months. Afterwards, they were kept in paddocks for 3 months. The remaining eight horses were used as controls. Three gluteus medius muscle biopsy samples were removed at depths of 20, 40 and 60 mm from each horse before (month 0), during (month 3) and after (month 8) training, and again after 3 months of detraining (month 11). MHC composition was analysed by electrophoresis and immunohistochemistry with anti-MHC monoclonal antibodies. Fibre areas, oxidative capacity and capillaries were studied histochemically. The activities of key muscle enzymes of aerobic (citrate synthase and 3-hydroxy-acyl-CoA-dehydrogenase) and anaerobic (phosphofructokinase and lactic dehydrogenase) metabolism and the intramuscular glycogen and triglyceride contents were also biochemically analysed. Early changes with training (3 months) included hypertrophy of type IIA fibres, a reduction of MHC-IIX with a concomitant increase of MHC-IIA, a rise in the number of high-oxidative fibres and in the activities of aerobic muscle enzymes and glycogen content. Long-term changes with training (8 months) were a further decline in the expression of MHC-IIX, an increase of slow MHC-I, additional increases of high-oxidative fibres, capillary density, activities of aerobic enzymes and endogenous glycogen; intramuscular lipid deposits also increased after 8 months of training whereas the activities of anaerobic enzymes declined. Most of exercise-induced alterations reverted after 3 months of detraining. These results indicate that endurance-exercise training induces a reversible transition of MHC composition in equine muscle in the order IIX-->IIA-->I, which is coordinated with changes in the metabolic properties of the muscle. Furthermore, a dose-response relationship was evident between the duration (in total) of training and the magnitude of muscle adaptations.</description><subject>3-Hydroxyacyl CoA Dehydrogenases - analysis</subject><subject>Activities</subject><subject>Animals</subject><subject>Biopsy</subject><subject>Capillaries - anatomy & histology</subject><subject>Citrate (si)-Synthase - analysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Glycogen - analysis</subject><subject>Horses - physiology</subject><subject>Immunohistochemistry</subject><subject>L-Lactate Dehydrogenase - analysis</subject><subject>Lactic Acid - blood</subject><subject>Male</subject><subject>Muscle Fibers, Skeletal - chemistry</subject><subject>Muscle Fibers, Skeletal - metabolism</subject><subject>Muscle Fibers, Skeletal - ultrastructure</subject><subject>Muscle, Skeletal - anatomy & histology</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Muscle, Skeletal - physiology</subject><subject>Myosin Heavy Chains - analysis</subject><subject>Oxidation-Reduction</subject><subject>Phosphofructokinase-1 - analysis</subject><subject>Physical Conditioning, Animal</subject><subject>Physical Endurance</subject><subject>Physical Exertion</subject><subject>Physical fitness</subject><subject>Proteins</subject><subject>Triglycerides - analysis</subject><issn>0031-6768</issn><issn>1432-2013</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</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>eNqFkc1L7TAQxYM80evVpVsJbyFuqpNkmvQuRfwCwY2uS5pOr_W16TVpF_e_N-oV8S10hmE48OPA4TB2KOBUAJizCIASIQ1CscVmApXMJAj1h80AlMi00cUu24vxOTESC7nDdoWQIo2csebShm7Nra95N_hlNlLouXuyfkmRDw2nl6n1xOM_6mi0He-n6DrireeB4mrwkfg4cPL1FKx3SQTb-tYv3x1r-pT7bLuxXaSDzZ-zx6vLh4ub7O7--vbi_C5ziHrMqsJom2vZaK3T2aYwaBfGVBp1jeBQYLPIK3LgBMkF2MraxqIAo4yqF1rN2fGH7yoMLxPFsezb6KjrrKdhiqWReQ5Sql9BUQg0GmUCT34GQWEhTC4xoX__Q5-HKfiUt0w5QCqRds6yD8iFIcZATbkKbW_DOjmVb42W3xpN_NHGdKp6qr_oTYXqFUBomeI</recordid><startdate>20001201</startdate><enddate>20001201</enddate><creator>Serrano, A L</creator><creator>Quiroz-Rothe, E</creator><creator>Rivero, J L</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>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QP</scope><scope>7TK</scope><scope>7TS</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</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>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>20001201</creationdate><title>Early and long-term changes of equine skeletal muscle in response to endurance training and detraining</title><author>Serrano, A L ; Quiroz-Rothe, E ; Rivero, J L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-b876a562f666f66af874a977b646d40c414f95bec0c1e290abaafa4107373d963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>3-Hydroxyacyl CoA Dehydrogenases - analysis</topic><topic>Activities</topic><topic>Animals</topic><topic>Biopsy</topic><topic>Capillaries - anatomy & histology</topic><topic>Citrate (si)-Synthase - analysis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Glycogen - analysis</topic><topic>Horses - physiology</topic><topic>Immunohistochemistry</topic><topic>L-Lactate Dehydrogenase - analysis</topic><topic>Lactic Acid - blood</topic><topic>Male</topic><topic>Muscle Fibers, Skeletal - chemistry</topic><topic>Muscle Fibers, Skeletal - metabolism</topic><topic>Muscle Fibers, Skeletal - ultrastructure</topic><topic>Muscle, Skeletal - anatomy & histology</topic><topic>Muscle, Skeletal - chemistry</topic><topic>Muscle, Skeletal - physiology</topic><topic>Myosin Heavy Chains - analysis</topic><topic>Oxidation-Reduction</topic><topic>Phosphofructokinase-1 - analysis</topic><topic>Physical Conditioning, Animal</topic><topic>Physical Endurance</topic><topic>Physical Exertion</topic><topic>Physical fitness</topic><topic>Proteins</topic><topic>Triglycerides - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Serrano, A L</creatorcontrib><creatorcontrib>Quiroz-Rothe, E</creatorcontrib><creatorcontrib>Rivero, J L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Physical Education Index</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Pflügers Archiv</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Serrano, A L</au><au>Quiroz-Rothe, E</au><au>Rivero, J L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Early and long-term changes of equine skeletal muscle in response to endurance training and detraining</atitle><jtitle>Pflügers Archiv</jtitle><addtitle>Pflugers Arch</addtitle><date>2000-12-01</date><risdate>2000</risdate><volume>441</volume><issue>2-3</issue><spage>263</spage><epage>274</epage><pages>263-274</pages><issn>0031-6768</issn><eissn>1432-2013</eissn><abstract>Twenty-four 4-year-old Andalusian (Spanish breed) stallions were used to examine the plasticity of myosin heavy chain (MHC) phenotype and the metabolic profile in horse skeletal muscle with long-term endurance-exercise training and detraining. Sixteen horses underwent a training programme based on aerobic exercises for 8 months. Afterwards, they were kept in paddocks for 3 months. The remaining eight horses were used as controls. Three gluteus medius muscle biopsy samples were removed at depths of 20, 40 and 60 mm from each horse before (month 0), during (month 3) and after (month 8) training, and again after 3 months of detraining (month 11). MHC composition was analysed by electrophoresis and immunohistochemistry with anti-MHC monoclonal antibodies. Fibre areas, oxidative capacity and capillaries were studied histochemically. The activities of key muscle enzymes of aerobic (citrate synthase and 3-hydroxy-acyl-CoA-dehydrogenase) and anaerobic (phosphofructokinase and lactic dehydrogenase) metabolism and the intramuscular glycogen and triglyceride contents were also biochemically analysed. Early changes with training (3 months) included hypertrophy of type IIA fibres, a reduction of MHC-IIX with a concomitant increase of MHC-IIA, a rise in the number of high-oxidative fibres and in the activities of aerobic muscle enzymes and glycogen content. Long-term changes with training (8 months) were a further decline in the expression of MHC-IIX, an increase of slow MHC-I, additional increases of high-oxidative fibres, capillary density, activities of aerobic enzymes and endogenous glycogen; intramuscular lipid deposits also increased after 8 months of training whereas the activities of anaerobic enzymes declined. Most of exercise-induced alterations reverted after 3 months of detraining. These results indicate that endurance-exercise training induces a reversible transition of MHC composition in equine muscle in the order IIX-->IIA-->I, which is coordinated with changes in the metabolic properties of the muscle. Furthermore, a dose-response relationship was evident between the duration (in total) of training and the magnitude of muscle adaptations.</abstract><cop>Germany</cop><pub>Springer Nature B.V</pub><pmid>11211112</pmid><doi>10.1007/s004240000408</doi><tpages>12</tpages></addata></record> |
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subjects | 3-Hydroxyacyl CoA Dehydrogenases - analysis Activities Animals Biopsy Capillaries - anatomy & histology Citrate (si)-Synthase - analysis Electrophoresis, Polyacrylamide Gel Glycogen - analysis Horses - physiology Immunohistochemistry L-Lactate Dehydrogenase - analysis Lactic Acid - blood Male Muscle Fibers, Skeletal - chemistry Muscle Fibers, Skeletal - metabolism Muscle Fibers, Skeletal - ultrastructure Muscle, Skeletal - anatomy & histology Muscle, Skeletal - chemistry Muscle, Skeletal - physiology Myosin Heavy Chains - analysis Oxidation-Reduction Phosphofructokinase-1 - analysis Physical Conditioning, Animal Physical Endurance Physical Exertion Physical fitness Proteins Triglycerides - analysis |
title | Early and long-term changes of equine skeletal muscle in response to endurance training and detraining |
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