Skip to main content
Log in

Microphotometric determination of enzyme activities in type-grouped fibres of reinnervated rat muscle

  • Published:
Histochemistry Aims and scope Submit manuscript

Summary

Activities of succinate dehydrogenase (SDH), glycerolphosphate oxidase (GP-OX), cytochrome oxidase (CYT-OX) and lactate dehydrogenase (LDH) were determined microphotometrically in single, actomyosin-ATPase typed (Guth and Samaha 1970) fibres within cross-sections of normal and reinnervated rat tibialis anterior muscles. SDH and GP-OX activities displayed pronounced scattering and large overlaps existed between α-, αβ-, and β-fibres of normal muscle. Coefficients of variation were in the range of 16–40% for GP-OX and SDH in the different fibre populations. Enzyme activity determinations in typegrouped α-, αβ-, and β-fibres of reinnervated muscle showed much less scattering than in normally distributed α-, αβ-, and β-fibres of control muscles. Coefficients of variation were in the range of 10–13% for SDH, GP-OX, CYT-OX and LDH. The experimental error of the kinetic microphotometric measurement of enzyme activities in situ is in the range of 10% (Reichmann and Pette 1982). Our results therefore suggest a high degree of metabolic similarity or homogeneity of typed-grouped muscle fibres and thus support the assumption that type-groped fibres are homogeneous and correspond to regularly assembled motor units.

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

  • Ballantyne B, Bright JE (1979) Comparison of kinetic and endpoint microdensitometry for the direct quantitative histochemical assessment of cytochrome oxidase activity. Histochem J 11:173–186

    Google Scholar 

  • Burke RE, Levine DN, Zajac III FE, Tsairis P, Engel WK (1971) Mammalian motor units: Physiological-histochemical, correlation in three types in cat gastrocnemius. Science 174:709–712

    Google Scholar 

  • Burke RE, Levine DN, Tsairis P, Zajac III FE (1973) Physiological types and histochemical profiles in motor units of the cat gastrocnemius. J Physiol (Lond) 234:723–748

    Google Scholar 

  • Burke RE, Levine DN, Salcman M, Tsairis P (1974) Motor units in cat soleusmuscle: Physiological, histochemical and morphological characteristics. J. Physiol (Lond) 238:503–514

    Google Scholar 

  • Dubowitz V, Brooke MH (1973) Muscle biopsy: A modern approach. WB Saunders, London Philadelphia Toronto

    Google Scholar 

  • Edström L, Kugelberg E (1968) Histochemical composition, distribution of fibres and fatiguability of single motor units. J Neurol Neurosurg Psychiat 31:424–433

    Google Scholar 

  • Green HJ, Reichmann H, Pette D (1982) A comparison of two ATPase based schemes for histochemical muscle fibre typing in various mammals. Histochemistry 76:21–31

    Google Scholar 

  • Guth L, Samaha FJ (1970) Procedure for the histochemical demonstration of actomyosin ATPase. Exp Neurol 28:365–367

    Google Scholar 

  • Hintz CS Lowry CV, Kaiser KK, McKee D, Lowry OH (1980) Enzyme levels in individual rat muscle fibers. Am J Physiol (Cell Physiol 8) 239:C58-C65

    Google Scholar 

  • Karpati G, Engel WK (1968) “Type grouping”. in skeletal muscles after experimental reinnervation. Neurology (Minneap) 18:447–455

    Google Scholar 

  • Kugelberg E, Edström L (1968) Differential histochemical effects of muscle contractions on phosphorylase and glycogen in various types of fibres: relation to fatigue. J Neurol Neurosurg Psychiat 31:415–423

    Google Scholar 

  • Kugelberg E, Lindegren B (1979) Transmission and contraction fatigue of rat motor units in relation to succinate dehydrogenase activity of motor unit fibres. J Physiol (Lond) 288:285–300

    Google Scholar 

  • Kugelberg E, Edström L, Abbruzzese M (1970) Mapping of motor units in experimentally reinnervated rat muscle. J Neurol Neurosurg Psychiat 33:319–329

    Google Scholar 

  • Lowry CV, Kimmey JS, Felder S, Chi MM-Y, Kaiser KK, Passonneau PN, Kirk KA, Lowry OH (1978) Enzyme patterns in single human muscle fibers. J Biol Chem 253:8269–8277

    Google Scholar 

  • Nemeth P, Pette D (1981) Succinate dehydrogenase activity in fibres classified by myosin ATPase in three hind limb muscles of rat. J Physiol (Lond) 320:73–80

    Google Scholar 

  • Nemeth PM, Pette D, Vrbová G (1981) Comparison of enzyme activities among single muscle fibres within defined motor units. J Physiol (Lond) 311:489–495

    Google Scholar 

  • Nolte J, Pette D (1972a) Microphotometric determination of enzyme activity in single cells in cryostat sections. I. Application of the gel film technique to microphotometry and studies on the intralobular distribution of succinate dehydrogenase activities in rat liver. J Histochem Cytochem 20:567–576

    Google Scholar 

  • Nolte J, Pette D (1972b) Microphotometric determination of enzyme activity in single cells in cryostat sections. II. Succinate dehydrogenase, lactate dehydrogenase and triosephosphate dehydrogenase activities in red, intermediate and white fibers of soleus and rectus femoris muscles of rat. J Histochem Cytochem 20:577–582

    Google Scholar 

  • Pette D (1981) Microphotometric measurement of initial maximum reaction rates in quantitative enzyme histochemistry in situ. Histochem J 13:319–327

    Google Scholar 

  • Pette D, Tyler KR (1983) Response of succinate dehydrogenase activity in fibres of rabbit tibialis anterior muscle to chronic nerve stimulation. J Physiol (Lond) 338:1–9

    Google Scholar 

  • Pette D, Wasmund H, Wimmer M (1979) Principle and method of kinetic microphotometric enzyme activity determination in situ. Histochemistry 64:1–10

    Google Scholar 

  • Pette D, Reichmann H, Vetter C (1983) Metabolic homogeneity of grouped fibres in reinnervated rat muscle. J Physiol (Lond) 343:104P

    Google Scholar 

  • Reichmann H, Pette D (1982) A comparative microphotometric study of succinate dehydrogenase activity levels in type I, IIA and IIB fibres of mammalian and human muscles. Histochemistry 74:27–41

    Google Scholar 

  • Romanul FCA (1971) Reversal of enzymatic profiles and capillary supply of muscle fibers in fast and slow muscles after crossinnervation. In: Pernow B, Saltin B (eds) Muscle metabolism during exercise. Plenum Press, New York, pp 21–32

    Google Scholar 

  • Romanul FCA, van der Meulen JP (1967) Slow and fast muscles after cross-innervation. Arch Neurol (Chicago) 17:387–402

    Google Scholar 

  • Spamer C, Pette D (1977) Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle. Histochemistry 52:201–216

    Google Scholar 

  • Spamer C, Pette D (1979) Activities of malate dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase and fructose-1,6-diphosphatase with regard to metabolic subpopulations of fast- and slowtwitch fibres in rabbit muscles. Histochemistry 60:9–19

    Google Scholar 

  • Spamer C, Pette D (1980) Metabolic suppopulations of rabbit skeletal muscle fibres. In: Pette D (ed) Plasticity of muscle. Walter de Gruyter, Berlin New York, pp 19–30

    Google Scholar 

  • Yellin H (1967) Neural regulation of enzymes in muscle fibers of red and white muscle. Exp Neurol 19:92–103

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Vetter, C., Reichmann, H. & Pette, D. Microphotometric determination of enzyme activities in type-grouped fibres of reinnervated rat muscle. Histochemistry 80, 347–351 (1984). https://doi.org/10.1007/BF00495415

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00495415

Keywords

Navigation