Myosin phenotype and SDH enzyme variability among motor unit fibers

Gary C. Sieck, Mario Fournier, Y. S. Prakash, Cesar E. Blanco

Research output: Contribution to journalArticlepeer-review

63 Scopus citations


Motor units in cat diaphragm and tibialis posterior muscles were classified physiologically as slow-twitch, fast-twitch fatigue-resistant, fast-twitch fatigue-intermediate, or fast-twitch fatigable. Motor unit fibers were then identified by glycogen depletion and classified as type I, IIa, IIb, or IIx on the basis of myofibrillar adenosinetriphosphatase-staining profiles and immunoreactivity for myosin heavy-chain (MHC) isoforms. In both muscles, slow-twitch and fast-twitch fatigue-resistant units comprised type I and IIa fibers expressing MHC-slow and MHC-2A isoforms, respectively. Fast- twitch fatigue-intermediate and fast-twitch fatigable units comprised type IIx fibers expressing the MHC-2X isoform. Some fast-twitch fatigue- intermediate units had a mixed composition with a few fibers (~10%) expressing the MHC-2A isoform. Motor unit fiber succinate dehydrogenase (SDH) activity was quantified, and variability was estimated by the interquartile range, which was lower among motor unit fibers than in adjacent fibers of the same histochemical type but comparable to that along the length of individual fibers. We conclude that, despite the mixed-MHC phenotype of some diaphragm and tibialis posterior motor units, SDH activity is relatively uniform. This supports the hypothesis that motoneurons exert a predominant influence on muscle fiber SDH activity.

Original languageEnglish (US)
Pages (from-to)2179-2189
Number of pages11
JournalJournal of applied physiology
Issue number6
StatePublished - Jun 1996


  • diaphragm muscle
  • immunohistochemistry
  • myosin heavy chain
  • quantitative histochemistry

ASJC Scopus subject areas

  • Physiology
  • Physiology (medical)


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