Histochemistry

, Volume 47, Issue 1, pp 43–57 | Cite as

Intrafusal fibre types in rat limb muscle spindles

Morphological and histochemical characteristics
  • Tomáš Soukup
Article

Summary

Morphological, histochemical and ultrastructural characteristics of intrafusal fibre types were studied in rat muscle spindles. The existence of three intrafusal fibre types, namely the typical bag, the intermediate bag and the chain fibres was confirmed. Intrafusal fibres differ in diameter, length and number of nuclei in the equatorial zone. Histochemically, typical bag fibres exhibit both alkali-and acid-stable ATPase activity and low SDH activity. Intermediate bag fibres possess low alkali-stable ATPase activity; after acid-preincubation, however, they have low activity only in the juxtaequatorial region, whereas in the polar zones they exhibit high acid-stable ATPase activity. The SDH activity varies from moderate to high. The chain fibres exhibit high alkali-stable and low acid-stable ATPase and high SDH activity in the extensor digitorum longus muscle, whereas in the soleus muscle the acid-stable ATPase activity varies from a low one to a high one, either among individual chain fibres in one spindle, and/or repeatedly along the fibre length.

Since there are regional differences in morphological characteristics and in staining properties of intrafusal fibres, a reliable identification of intrafusal fibre types can only be achieved by an analysis of serial sections.

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References

  1. Asiedu, S., Shafiq, S. A.: Actomyosin ATPase activity of the anterior latissimus dorsi muscle of the chicken. Exp. Neurol. 35, 211–213 (1972)Google Scholar
  2. Banker, B. Q., Girvin, J. P.: The ultrastructural features of the mammalian muscle spindle. J. Neuropath. exp. Neurol. 30, 155–195 (1971)Google Scholar
  3. Banks, R. W.: Histochemical studies on rabbit intrafusal fibres. J. Anat. (Lond.) 108, 613–614 (1971)Google Scholar
  4. Barker, D.: The innervation of the muscle spindle. Quart. J. micr. Sci. 89, 143–186 (1948)Google Scholar
  5. Barker, D.: The structure and distribution of muscle receptors. In: Symposium on muscle receptors (D. Barker, ed.), pp. 227–240. Hong Kong University Press 1962Google Scholar
  6. Barker, D.: Morphology of muscle receptors. In: Muscle receptors (C. C. Hunt ed.), Vol. III, Pt. 2. Handbook of sensory physiology. Berlin-Heidelberg-New York: Springer 1974Google Scholar
  7. Barker, D., Harker, D. W., Stacey, M. J., Smith, C. R.: Fusimotor innervation. In: Research concepts in muscle development and the muscle spindle (Banker, B. Q. et al., eds.), pp. 227–250. Amsterdam: Excerpta Medica 1972Google Scholar
  8. Barker, D., Stacey, M. J.: Rabbit intrafusal fibres. J. Physiol. (Lond.) 210, 70–72 P (1970)Google Scholar
  9. Boyd, I. A.: The tenuissimus muscle of the cat. J. Physiol. (Lond.) 133, 35–36 P (1956)Google Scholar
  10. Boyd, I. A.: The diameter and distribution of the nuclear bag and nuclear chain muscle fibres in the muscle spindles of the cat. J. Physiol. (Lond.) 153, 23–24 P (1960)Google Scholar
  11. Boyd, I. A.: The structure and innervation of the nuclear bag muscle fibre system and the nuclear chain fibre system in mammalian muscle spindles. Phil. Trans. B 245, 81–136 (1962)Google Scholar
  12. Brooke, M. H., Kaiser, K. K.: Muscle fibre types. How many and what kind. Arch. Neurol. (Chic.) 23, 369–379 (1970)Google Scholar
  13. Cooper, S.: Muscle spindles and other muscle receptors. In: Structure and function of muscle (G. H. Bourne, ed.), vol. I, pp. 381–420. New York: Academic Press 1960Google Scholar
  14. Cooper, S., Daniel, P. M.: Human muscle spindles. J. Physiol. (Lond.) 133, 1–3 P (1956)Google Scholar
  15. Cooper, S., Daniel, P. M.: Muscle spindles in man; their morphology in the lumbricals and the deep muscles of the neck. Brain 86, 563–586 (1963)Google Scholar
  16. Farrell, P. R., Fedde, M. R.: Uniformity of structural characteristics throughout the length of skeletal muscle fibres. Anat. Rec. 164, 219–230 (1969)Google Scholar
  17. Guth, L.: Fact and artifact in the histochemical procedure for myofibrillar ATPase. Exp. Neurol. 41, 440–450 (1973)Google Scholar
  18. Guth, L., Samaha, F. J.: Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle. Exp. Neurol. 25, 138–152 (1969)Google Scholar
  19. Guth, L., Samaha, F. J.: Procedure for the histochemical demonstration of actomyosin ATPase. Exp. Neurol. 28, 365–367 (1970)Google Scholar
  20. Guth, L., Samaha, F. J.: Erroneous interpretations which may result from application of the “myofibrillar ATPase” histochemical procedure to developing muscle. Exp. Neurol. 34, 465–475 (1972)Google Scholar
  21. Harker, D. W.: The structure and innervation of sheep extraocular and foot muscles. Ph. D. Thesis, University of Durham (1973)Google Scholar
  22. Hess, A.: Vertebrate slow muscle fibres. Physiol. Rev. 50, 40–62 (1970)Google Scholar
  23. James, N. T.: The histochemical demonstration of three types of intrafusal fibre in rat muscle spindles. Histochem. J. 3, 457–462 (1971)Google Scholar
  24. Koenig, J., Fardeau, M.: Histochemical study of the normal, denervated, self and crossreinnervated anterior and posterior lat. dorsi muscles of the chicken. Arch. Anat. microscopique 62, 249–267 (1973)Google Scholar
  25. Milburn, A.: The early development of muscle spindles in the rat. J. Cell Sci. 12, 175–195 (1973a)Google Scholar
  26. Milburn, A.: The development of the muscle spindles in the rat. Ph. D. Thesis, University of Durham (1973b)Google Scholar
  27. Nachlas, M. M., Tsou, K. C., De Souza, E., Cheng C. S., Seligman, A. M.: Cytochemical demonstration of succinic dehydrogenase by the use of a new p-nitrophenyl substituted ditetrasolium. J. Histochem. Cytochem. 5, 420–436 (1957)Google Scholar
  28. Ogata, T., Mori, M.: Histochemical demonstration of the three types of intrafusal fibres of muscle spindles, a study on oxidative enzymes. Acta Med. Okyma 16, 347–350 (1962)Google Scholar
  29. Ogata, T., Mori, M.: Histochemical study of oxidative enzymes in vertebrate muscles. J. Histochem. Cytochem. 12, 171–182 (1964)Google Scholar
  30. Ovalle, W. K.: Fine structure of rat intrafusal muscle fibres. The polar region. J. Cell Biol. 51, 83–103 (1971)Google Scholar
  31. Ovalle, W. K.: Fine structure of rat intrafusal muscle fibres. The equatorial region. J. Cell Biol. 52, 382–396 (1972)Google Scholar
  32. Ovalle, W. K., Smith, R. S.: Histochemical identification of three types of intrafusal muscle fibres in the cat and monkey based on the myosin ATPase reaction. Canad. J. Physiol. Pharmacol. 50, 195–202 (1972)Google Scholar
  33. Padykula, H. A., Herman, E.: The specificity of the histochemical method for adenosine triphosphate. J. Histochem. Cytochem. 3, 170–195 (1955)Google Scholar
  34. Pearson, J., Sabarra, A.: A method for obtaining longitudinal cryostat sections of living muscle without contraction artifacts. Stain Technol. 49, 143–146 (1974)Google Scholar
  35. Peter, J. B.: Skeletal muscle: Diversity and mutability of its histochemical, electron microscopic, biochemical and physiologic properties. In: The striated muscle (Pearson, C. M. and Mostofi, F. K., eds.), pp. 1–18. Baltimore: Williams and Wilkins Co. 1973Google Scholar
  36. Reuck, J. de, van der Eecken, H., Roels, H.: Biometrical and histochemical comparison between extra- and intra-fusal muscle fibres in denervated and re-innervated rat muscle. Acta neuropath. (Berl.) 25, 249–258 (1973)Google Scholar
  37. Samaha, F. J., Yunis, E.: Quantitative and histochemical demonstration of a skeletal muscle calcium activated mitochondrial ATPase. Exp. Neurol. 41, 431–439 (1973)Google Scholar
  38. Saghal, V., Nayyar, R., Betts, H. B.: Histochemical profile of human intrafusal fibres. Excerpta Medica No. 237: II. International Congress on Muscle Disease, Vol. 5, pp. 2–3. Amsterdam: Excerpta Medica 1971Google Scholar
  39. Smith, R. S., Ovalle, W. K.: Structure and function of intrafusal muscle fibres. In: Muscle biology (R. G. Cassens, ed.), Vol. 1, pp. 147–227. New York: Marcel Deccer, Inc. 1972Google Scholar
  40. Spiro, A. J., Beilin, R. L.: Histochemical duality of rabbit intrafusal fibres. J. Histochem. Cytochem. 17, 348–349 (1969a)Google Scholar
  41. Spiro, A. J., Beilin, R. L.: Human muscle spindle histochemistry. Arch. Neurol. (Chic.) 20, 271–275 (1969b)Google Scholar
  42. Syrový, I., Zelená, J.: The onset and progress of transformation of avian slow into fast muscles under neural influence. Pflügers Arch. 360, 121–134 (1975)Google Scholar
  43. Tunik, B. D.: Cytochemical localization of myofibrillar adenosine trifosphatase activity in sarcomeres of glycerinated muscle by the calcium precipitation method. J. Histochem. Cytochem. 19, 75–84 (1971)Google Scholar
  44. Widemann, S. E., Magnusson, B. C., Heyden, G.: Enzyme histochemical studies of ATPase activities in longitudinal sections of striated muscle tissue in the rat. Histochem. J. 5, 265–269 (1973)Google Scholar
  45. Wirsen, C.: Histochemical heterogenity of muscle spindle fibres. J. Histochem. Cytochem. 12, 308–309 (1964)Google Scholar
  46. Yellin, H.: A histochemical study of muscle spindles and their relationship to extrafusal fibre types in the rat. Amer. J. Anat. 125, 31–46, (1969a)Google Scholar
  47. Yellin, H.: Unique intrafusal fibres exhibiting dual actomyosin ATPase activity. Exp. Neurol. 25, 153–163 (1969b)Google Scholar
  48. Yellin, H.: Regional differences in the contractile apparatus of intrafusal muscle fibres. Amer. J. Anat. 139, 147–152 (1974)Google Scholar
  49. Yellin, H.: Limitations to the neuroregulation of enzymes in mammalian skeletal muscle. Anat. Rec. 182, 479–498 (1975)Google Scholar
  50. Zelená, J., Soukup, T.: The differentiation of intrafusal fibre types in rat muscle spindles after motor denervation. Cell Tiss. Res. 153, 115–136 (1974)Google Scholar

Copyright information

© Springer-Verlag 1976

Authors and Affiliations

  • Tomáš Soukup
    • 1
  1. 1.Institute of PhysiologyCzechoslovak Academy of SciencesPrague 4-KrčCzechoslovakia

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