|
|
||||||||
Department of Zoology, La Trobe University, Bundoora, Melbourne, Victoria, Australia.
1. Contractile activation properties of various types of normal and dystrophic (Duchenne muscular dystrophy, DMD) human muscle fibres were investigated using mechanically skinned fibres activated in Ca2(+)- and Sr2(+)-buffered solutions at room temperature (21-25 degrees C). 2. The majority of the normal human muscle fibres (18/22; 82%) could be classified according to the Ca2(+)- and Sr2(+)-activation characteristics in the same three major groups as other mammalian skeletal muscle fibres studied previously: slow-twitch (8/22; 36%), fast-twitch (3/22; 14%) and fast-twitch intermediate (7/22; 32%), which correspond to the three major histological fibre types I, II B and IIA respectively. 3. Of these three major groups only the slow-twitch (type I; 14/24; 58%) and the fast-twitch intermediate (type IIA; 3/24; 13%) fibres were found in the DMD muscle, indicating that fast-twitch fibres of type IIB were in very low proportion in DMD muscle. 4. The DMD muscle contained a new group of fibres (4/24; 17%) with different Ca2(+)- and Sr2(+)-activation characteristics from the three major histological types. This group of fibres is likely to be of embryonic type. 5. The maximum tension development ability of DMD fibres was less than 20% of that in normal fibres with the exception of some slow-twitch fibres which could produce near normal tension. 6. A significant proportion of normal (4/22; 18%) and DMD (3/24; 13%) fibres were found to have a mixture of Ca2(+)- and Sr2(+)-activation characteristics. This can be explained by co-existence of various myofibrillar protein isoforms in different proportions with regulatory functions in the same individual fibre. 7. The results demonstrate that DMD leads to marked diminution in the ability of most individual skeletal muscle fibres to develop tension, and causes changes in the overall fibre-type distribution in afflicted muscles.
This article has been cited by other articles:
![]() |
G. D'Antona, L. Brocca, O. Pansarasa, C. Rinaldi, R. Tupler, and R. Bottinelli Structural and functional alterations of muscle fibres in the novel mouse model of facioscapulohumeral muscular dystrophy J. Physiol., November 1, 2007; 584(3): 997 - 1009. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. M. Duke, P. M. Hopkins, P. J. Halsall, and D. S. Steele Mg2+ dependence of Ca2+ release from the sarcoplasmic reticulum induced by sevoflurane or halothane in skeletal muscle from humans susceptible to malignant hyperthermia Br. J. Anaesth., September 1, 2006; 97(3): 320 - 328. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. E Woods, D. Novo, M. DiFranco, J. Capote, and J. L Vergara Propagation in the transverse tubular system and voltage dependence of calcium release in normal and mdx mouse muscle fibres J. Physiol., November 1, 2005; 568(3): 867 - 880. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. E. Woods, D. Novo, M. DiFranco, and J. L. Vergara The action potential-evoked sarcoplasmic reticulum calcium release is impaired in mdx mouse muscle fibres J. Physiol., May 15, 2004; 557(1): 59 - 75. [Abstract] [Full Text] [PDF] |
||||
![]() |
O. Friedrich, M. Both, J. M. Gillis, J. S. Chamberlain, and R. H. A. Fink Mini-dystrophin restores L-type calcium currents in skeletal muscle of transgenic mdx mice J. Physiol., February 15, 2004; 555(1): 251 - 265. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Most, A. Remppis, C. Weber, J. Bernotat, P. Ehlermann, S. T. Pleger, W. Kirsch, M. Weber, D. Uttenweiler, G. L. Smith, et al. The C Terminus (Amino Acids 75-94) and the Linker Region (Amino Acids 42-54) of the Ca2+-binding Protein S100A1 Differentially Enhance Sarcoplasmic Ca2+ Release in Murine Skinned Skeletal Muscle Fibers J. Biol. Chem., July 11, 2003; 278(29): 26356 - 26364. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. A. Woolley, M. F. Patterson, G. M. Stephenson, and D. G. Stephenson The ilio-marsupialis muscle in the dasyurid marsupial Sminthopsis douglasi: form, function and fibre-type profiles in females with and without suckling young J. Exp. Biol., December 15, 2002; 205(24): 3775 - 3781. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. K. Bortolotto, M. Cellini, D. G. Stephenson, and G. M. M. Stephenson MHC isoform composition and Ca2+- or Sr2+-activation properties of rat skeletal muscle fibers Am J Physiol Cell Physiol, November 1, 2000; 279(5): C1564 - C1577. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. W. Berchtold, H. Brinkmeier, and M. Muntener Calcium Ion in Skeletal Muscle: Its Crucial Role for Muscle Function, Plasticity, and Disease Physiol Rev, July 1, 2000; 80(3): 1215 - 1265. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. Kunst, K. R. Kress, M. Gruen, D. Uttenweiler, M. Gautel, and R. H. A. Fink Myosin Binding Protein C, a Phosphorylation-Dependent Force Regulator in Muscle That Controls the Attachment of Myosin Heads by Its Interaction With Myosin S2 Circ. Res., January 7, 2000; 86(1): 51 - 58. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |