Skip to main content
Log in

A unique acid phosphatase location: the transverse tubule of avian fast muscle

  • Papers
  • Published:
The Histochemical Journal Aims and scope Submit manuscript

Synopsis

Acid phosphatase activity was localized cytochemically in the posterior latissimus dorsi muscle of the chicken. Reaction product was observed in three distinct structures: T-tubules, sarcoplasmic reticulum and dense bodies. Examination of cross-and longitudinal sections confirmed that the reaction product was membrane-limited. Acid phosphatase activity was observed in sarcoplasmic reticulum adjacent to the A-I junction and the A-band, in intermyofibrillar dense bodies located along the length of the fibre and in the T-tubules but not in the surface caveolae or in the lateral sacs of the sarcoplasmic reticulum. The uniqueness of the T-tubular localization with respect to cytochemical localizations in other muscles is discussed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Barka, T. &Anderson, P. J. (1962). Histochemical methods for acid phosphatase using hexazonium pararosanilin as complex.J. Histochem. Cytochem. 10, 741–53.

    Google Scholar 

  • Canonico, P. G. &Bird, J. W. C. (1969). The use of acridine orange as a lysosomal marker in rat skeletal muscle.J. Cell Biol. 43, 367–71.

    Google Scholar 

  • Canonico, P. G. &Bird, J. W. C. (1970). Lysosomes in skeletal muscle: Zonal centrifugation evidence for multiple cellular sources.J. Cell. Biol. 45, 321–33.

    Google Scholar 

  • Christie, K. N. &Stoward, P. J. (1977). A cytochemical study of acid phosphatase in dystrophic hamster muscle.J. Ultrastruct. Res. 58, 219–34.

    Google Scholar 

  • Engel, A. G. &McDonald, R. D. (1970). Acid maltase deficiency in adult life: Morphologic and biochemical data in three cases of a syndrome simulating other myopathies, In:Muscle Disease (eds. J. N. Watson, N. Canal and G. Scarlato). pp. 236–245 Amsterdam: Excerpta Medica.

    Google Scholar 

  • Engel, A. G. (1970). Ultrasturctural reactions in muscle disease and their light microscopic correlates, InMuscle Diseases (eds. J. N. Watson, N. Canal and G. Scarlato). pp. 71–89. Amsterdam: Excerpta Medica.

    Google Scholar 

  • Farquhar, M. G. &Palade, G. E. (1964). Functional organization of amphibian skin.Proc. Nat. Acad. Sci, U.S.A. 51, 569–77.

    Google Scholar 

  • Frasca, J. &Parks, V. (1965). A routine technique for double-staining ultrathin sections using uranyl and lead stains.J. Cell Biol. 25, 157–61.

    Google Scholar 

  • Gordon, G. B., Price, H. N. &Blumberg, J. M. (1967). Electron microscopic localization of phosphatase activities within striated muscle fibers.Lab. Invest. 16, 422–35.

    Google Scholar 

  • Luft, J. M. (1961). Improvements in epoxy resin embedding methods.J. Biophys. Biochem. Cytol. 9, 409–14.

    Google Scholar 

  • Martinosi, A. (1972). Biochemical and clinical aspects of sarcoplasmic reticulum function. InCurrent Topics in Membranes and Transport. Vol. 3, pp. 83–197. New York: Academic Press.

    Google Scholar 

  • Page, S. G. (1969). Structure and some contractile properties of fast and slow muscles of the chicken.J. Physiol. 205, 131–45.

    Google Scholar 

  • Pearce, G. W. (1966). Electron microscopy in the study of muscle diseases.Ann. N. Y. Acad. Sci. 138 138–50.

    Google Scholar 

  • Rubio, R. &Sperelakis, N. (1972). Penetration of horseradish peroxidase into the terminal cisternae of skeletal muscle fibers and blockade of caffeine contracture by Ca++ depletion.Z. Zellforsch. 124, 57–71.

    Google Scholar 

  • Seiden, D. (1973). Effects of colchicine on myofilament arrangement and the lysosomal system in skeletal muscle.Z. Zellforsch. 144, 467–73.

    Google Scholar 

  • Sperelakis, N., Valle, R., Orozco, C., Martinez-Palomo, A. &Rubio, R. (1973). Electromechanical uncoupling of frog skeletal muscle by possible change in sarcoplasmic reticulum content.Am. J. Physiol. 225, 793–800.

    Google Scholar 

  • Stauber, W. T. &Schottelius, B. A. (1975). Biochemical and physiological differences between avian ALD and PLD muscle subcellular fractions.Cytobios 14, 87–100.

    Google Scholar 

  • Trout, J. J., Stauber, W. T. &Schottelius, B. A. (1979). Cytochemical observations of two distinct acid phosphatase reactive structures in anterior latissimus dorsi muscles of the chicken.Histochem. J. 11, 223–30.

    Google Scholar 

  • Venable, J. H. &Coggeshall, R. (1965). A simplified lead citrate stain for use in electron microscopy.J. Cell Biol. 25, 407–8.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Trout, J.J., Stauber, W.T. & Schottelius, B.A. A unique acid phosphatase location: the transverse tubule of avian fast muscle. Histochem J 11, 417–423 (1979). https://doi.org/10.1007/BF01002769

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01002769

Keywords

Navigation