Immunohistochemical identification of spindle fibre types in mammalian muscle using type-specific antibodies to isoforms of myosin

  • A. Rowlerson
  • L. Gorza
  • S. Schiaffino


Recent work has shown that the various extrafusal muscle fibre types distinguishable by means of their histochemical myosin-based properties all contain structurally slightly different forms (isoforms) of myosin. In nearly all cases a different histochemical profile is associated with the presence of a single distinct myosin isoform (Gauthier & Lowey, 1977; Pierobon-Bormioli et al., 1981; Rowlerson et al., 1981), but for IIC fibres there as biochemical and immunohistochemical evidence (Billeter et al., 1980 & 1981) that two myosin isoforms co-exist in the same fibres. Futhermore, in fibres which transform from one histochemical type to another there is a corresponding switch from one form of myosin to another (e.g. Rubinstein et al., 1978). In addition to histochemical methods for ATPase activity (e.g. Brooke & Kaiser, 1970) the various myosin isoforms can be detected immunohistochemically using type (isoform)-specific antibodies to myosin.


Myosin ATPase Activity Propagate Action Potential Chain Fibre Intrafusal Muscle Fibre Tonic Fibre 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Barany, M. (1967). ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol., 50, 197–216.Google Scholar
  2. Barker, D., Bessou, P., Jankowska, E., Pages, P. & Stacey, M.J. (1975). Distribution of static and dynamic axons to cat intrafusal muscle fibres. J. Anat. 119, 199–200.Google Scholar
  3. Bessou, P. & Pages, B. (1972). Intracellular potentials from intrafusal muscle fibres evoked by stimulation of static and dynamic fusimotor axons in the cat. J. Phvsiol.. 227. 709–727.Google Scholar
  4. Bessou, P. & Pages, B. (1975). Cinematographic analysis of contractile events produced in intrafusal muscle fibres by stimulation of static and dynamic fusimotor axons in the cat. J. Physiol., 252, 397–427.Google Scholar
  5. Billeter, R., Weber, H., Lutz, H., Howald, H., Eppenberger, H.M. & Jenny, E. (1980). Myosin types in human skeletal muscle fibres. Histochemistry, 65, 249–259.Google Scholar
  6. Billeter, R., Heizmann, C.W., Howald, H. & Jenny, E. (1981). Analysis of myosin light and heavy chain types in single human skeletal muscle fibres. Eur. J. Biochem. 116, 389–395.Google Scholar
  7. Boyd, I.A. (1976). The response of fast and slow nuclear bag fibres and nuclear chain fibres in isolated cat muscle spindles to fusimotor stimulation, and the effect of intrafusal contraction on the sensory endings. Quart. J. Exp. Physiol., 61. 203–254.Google Scholar
  8. Boyd, I.A., Gladden, M., McWilliam, P.N. & Ward, J (1977). Control of dynamic and static nuclear bag fibres by gamma and beta axons in isolated cat muscle spindles. J. Physiol., 265, 133–162.Google Scholar
  9. Brooke, M.H. & Kaiser, K.K. (1970). Muscle fiber types: how many and what kind? Archs. Neurol., 23, 369–379.Google Scholar
  10. Close, R. (1965). The relationship between intrinsic speed of shortening and duration of the active state in muscle. J. Physiol., 180, 542–549.Google Scholar
  11. Gauthier, G.F. & Lowey, S. (1977). Polymorphism of myosin among skeletal muscle fiber types. J. Cell Biol. 74, 760–779.Google Scholar
  12. Gladden, M. (1976). Structural features relative to the function of intrafusal muscle fibres in the cat. Prog. Brain Res. 44, 51–59.Google Scholar
  13. Kronnie, G., Donselaar, Y., Soukup, T. & van Raamsdonk, W. (1981). Immunohistochemical differences in myosin composition among intrafusal muscle fibres. Histochemistry. 73. 65–74.Google Scholar
  14. Ovalle, W.K. & Smith, R.S. (1972). Histochemical identification of three types of intrafusal muscle fibres in the cat and monkey based on the myosin ATPase reaction. Can. J. Physiol. Pharmacol., 50, 195–202.Google Scholar
  15. Pierobon-Bormioli, S., Sartore, S., Vitadello, M. & Schiaffino, S. (1980). “Slow” myosins in vertebrate skeletal muscle. An immuno -fluorescence study. J. Cell Biol., 85, 672–681.Google Scholar
  16. Pierobon-Bormioli, S., Sartore, S., Dalla Libera, L., Vitadello, M. & Schiaffino, S. (1981). “Fast” isomyosins and fiber types in mammalian skeletal muscle. J. Histochem. Cytochem., 29, 1179–1188.Google Scholar
  17. Rowlerson, A., Pope, B., Murray, J., Whalen, R.B. & Weeds, A.G. (1981). A novel myosin present in cat jaw-closing muscles. J. Mus. Res. Cell Motil., 2, 415–438.Google Scholar
  18. Rubinstein, N., Mabuchi, K., Pepe, F., Salmons, S., Gergely, J. & Sreter, F.A. (1978). Use of type-specific antimyosins to demonstrate the transformation of individual fibres in chronically stimulated rabbit fast muscles. J. Cell Biol., 79, 252–261.Google Scholar
  19. Sartore, S., Gorza, L. & Schiaffino, S. (1982). Fetal myosin heavy chains in regenerating muscle. Nature 298, 294–296.Google Scholar
  20. Whalen, R.G., Sell, S.M., Butler-Browne, G.S., Schwarz, K., Bouveret, P. & Pinset-Harstrom, I. (1981). Three myosin heavy chain isozymes appear sequentially in rat muscle development. Nature, 292, 805–809.Google Scholar

Copyright information

© I. A. Boyd and M. H. Gladden 1985

Authors and Affiliations

  • A. Rowlerson
  • L. Gorza
  • S. Schiaffino

There are no affiliations available

Personalised recommendations