Document Detail

New insights into skeletal muscle fibre types in the dog with particular focus towards hybrid myosin phenotypes.
MedLine Citation:
PMID:  16163488     Owner:  NLM     Status:  MEDLINE    
Electrophoresis, immunoblots, immunohistochemistry and image analysis methods were applied to characterise canine trunk and appendicular muscle fibres according to their myosin heavy chain (MyHC) composition and to determine, on a fibre-to-fibre basis, the correlation between contractile [MyHC (s), myofibrillar ATPase (mATPase) and sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) isoforms], metabolic [succinate dehydrogenase (SDH) and glycerol-3-phosphate dehydrogenase (GPDH) activities and glycogen and phospholamban (PLB) content] and morphological (cross-sectional area and capillary and nuclear densities) features of individual myofibres. An accurate delineation of MyHC-based fibre types was obtained with the developed immunohistochemical method, which showed high sensitivity and objectivity to delineate hybrid fibres with overwhelming dominance of one MyHC isoform. Phenotypic differences in contractile, metabolic and morphological properties seen between fibre types were related to MyHC content. All canine skeletal muscle fibre types had a relatively high histochemical SDH activity but significant differences existed in the order IIA>I>IIX. Mean GPDH was ranked according to fibre type such that I<IIA<IIX. Type IIA fibres were the smallest, type IIX fibres the largest and type I of intermediate size. Capillary and nuclear density decreased in the order IIA>I>IIX. Hybrid fibres, which represented nearly one third of the whole pool of skeletal muscle fibres analysed, had mean values intermediate between their respective pure phenotypes. Slow fibres expressed the slow SERCA isoform and PLB, whereas type II fibres expressed the fast SERCA isoform. Discrimination of myofibres according to their MyHC content was possible on the basis of their contractile, metabolic and morphological features. These intrafibre interrelationships suggest that myofibres of control dogs exhibit a high degree of co-ordination in their physiological, biochemical and morphological characteristics. This study demonstrates that canine skeletal muscle fibres have been misclassified in numerous previous studies and offers useful baseline data and new prospects for future work on muscle-fibre-typing in canine experimental studies.
Luz M Acevedo; José-Luis L Rivero
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Publication Detail:
Type:  Journal Article     Date:  2005-09-15
Journal Detail:
Title:  Cell and tissue research     Volume:  323     ISSN:  0302-766X     ISO Abbreviation:  Cell Tissue Res.     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-01-17     Completed Date:  2006-06-27     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0417625     Medline TA:  Cell Tissue Res     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  283-303     Citation Subset:  IM    
Laboratory of Muscular Biopathology, Department of Comparative Anatomy and Pathological Anatomy, Faculty of Veterinary Sciences, University of Cordoba, 14071 Cordoba, Spain.
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MeSH Terms
Adenosine Triphosphatases / analysis,  metabolism
Calcium-Binding Proteins / analysis,  metabolism
Calcium-Transporting ATPases / metabolism
Glycerolphosphate Dehydrogenase / analysis,  metabolism
Glycogen / analysis,  metabolism
Image Processing, Computer-Assisted
Muscle Contraction / physiology
Muscle Fibers, Skeletal / chemistry,  classification*,  metabolism*
Muscle, Skeletal / cytology,  metabolism*
Myofibrils / enzymology
Myosin Heavy Chains / analysis,  metabolism*
Protein Isoforms
Sarcoplasmic Reticulum Calcium-Transporting ATPases
Succinate Dehydrogenase / analysis,  metabolism
Reg. No./Substance:
0/Calcium-Binding Proteins; 0/Myosin Heavy Chains; 0/Protein Isoforms; 0/phospholamban; 9005-79-2/Glycogen; EC 1.1.-/Glycerolphosphate Dehydrogenase; EC Dehydrogenase; EC 3.6.1.-/Adenosine Triphosphatases; EC ATPases; EC Reticulum Calcium-Transporting ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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