Myosin phenotype and SDH enzyme variability among motor unit fibers.
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 (approximately 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.
Sieck
G C
GC
Department of Anesthesiology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Fournier
M
M
Prakash
Y S
YS
Blanco
C E
CE
D000818:Animals; D002415:Cats; D003964:Diaphragm / Q000502:physiology*; D006003:Glycogen / Q000378:metabolism; D007150:Immunohistochemistry; D009046:Motor Neurons / Q000502:physiology*; D018485:Muscle Fibers, Skeletal / Q000378:metabolism; D018995:Myosin Heavy Chains / Q000378:metabolism*; D013385:Succinate Dehydrogenase / Q000378:metabolism*
D006003:Glycogen; D013385:Succinate Dehydrogenase; D018995:Myosin Heavy Chains