The Effects of 2,5-Hexanedione on Cholinesterase in the Rat

  • Barbara F. Bass
  • Alan M. Goldberg


Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are two enzymes that are important because of the role they play in neurotransmission and metabolism of exogenous and endogenous substrates. While both enzymes hydrolyze acetylcholine (ACh), they do so at significantly different rates, AChE being approximately 10X faster (Main, 1976). Both are glycoproteins and exist in homologous sets of six molecular forms, three globular and three asymmetric (Massoulie and Bon, 1982; Vigny et al., 1978). The globular forms consist of the catalytic subunit as a monomer (G1), a dimer (G2), and tetramer (G4). The asymmetric forms are composed of one (A4), two (A8), and three (A12) tetramers attached to a collagen tail. The composition of the molecular forms varies from tissue to tissue as well as from species to species.


Soleus Muscle AChE Activity Axonal Transport Molecular Form Tibial Nerve 


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  1. Cangiano, A., Lutzemberger, L., Rizzuto, N., Simomati, A., Rossi, A., and Toschi, G. (1980) Neurotoxic effects of 2,5-hexanedione in rats: early morphological and functional changes in nerve fibres and neuromuscular junctions. Neurotoxicology 2: 25–32.Google Scholar
  2. Carter, J.L., and Brimijoin, S. (1981) Effects of acute and chronic denervation on release of acetylcholinesterase and its molecular forms in rat diaphragms. J. Neurochem. 36: 1018–1025.CrossRefGoogle Scholar
  3. Close, R. I. (1972) Dynamic properties of mammalian skeletal muscles. Physiol. Rev. 52: 129–197.PubMedGoogle Scholar
  4. Couraud, J. Y., and Di Giamberardino, L. (1980) Axonal transport of the molecular forms of acetylcholinesterase in chick sciatic nerve. J. Neurochem. 35: 1053–1066.PubMedCrossRefGoogle Scholar
  5. Couraud, J. Y., Di Giamberardino, L., Chretien, M., Souyri, F., and Fardeau, M. (1982) Acrylamide neuropathy and changes in the axonal transport and muscular content of the molecular forms of acetylcholinesterase. Muscle and Nerve 5: 302–312.PubMedCrossRefGoogle Scholar
  6. Davey, B., and Younkin, S. G. (1978) Effect of nerve stump length on Cholinesterase in denervated rat diaphragm. Exp. Neurol. 59: 168–175.PubMedCrossRefGoogle Scholar
  7. Dettbarn, W.-D. (1981) A distinct difference between slow and fast muscle in acetylcholinesterase recovery after reinnervation in the rat. Exp. Neurol. 74: 35–50.CrossRefGoogle Scholar
  8. Di Giamberardino, L., and Couraud, J. Y. (1978) Rapid accumulation of high molecular weight acetylcholinesterase in transected sciatic nerve. Nature 271: 170–172.PubMedCrossRefGoogle Scholar
  9. Di Giamberardino, L., and Couraud, J. Y. (1981) Acetylcholinesterase and butyrylcholinesterase: similarities in normal and denervated muscles, differences in axonal transport. In: “Cholinergic Mechanisms”. (Eds.) Pepue, G., and Ladinsky, H. Plenum Press, New York, pp. 387–392.Google Scholar
  10. Drachman, D. B. (1972) Neurotrophic regulation of muscle cholinesterase: effects of botulinum toxin and denervation. J. Physiol. 226: 619–627.PubMedGoogle Scholar
  11. Drachman, D. B. (1976) Trophic interactions between nerves and muscles: the role of cholinergic transmission (including usage) and other factors. In: “Biology of Cholinergic Function”. (Eds.) Goldberg, A. M., and Hanin, I. Raven Press, New York, pp. 161–186.Google Scholar
  12. Edgerton, V. R., Gerchman, L., and Carrow, R. (1969) Histochemical changes in rat skeletal muscle after exercise. Exp. Neurol. 24: 110–123.PubMedCrossRefGoogle Scholar
  13. Fernandez, H. L., Duell, M. J., and Festoff, B. W. (1979) Neurotrophic control of 16S acetylcholinesterase at the vertebrate neuromuscular junction. J. Neurobiol. 10: 441–454.PubMedCrossRefGoogle Scholar
  14. Groswald, D. E., and Dettbarn, W.-D. (1983) Nerve crush induced change in molecular forms of acetylcholinesterase in soleus and extensor digitorum muscles. Exp. Neurol. 79: 519–531.PubMedCrossRefGoogle Scholar
  15. Guth, L. (1968) “Trophic” influences of nerve on muscle. Physiol. Rev. 48:645–687.PubMedGoogle Scholar
  16. Hall, Z. W. (1973) Multiple forms of acetylcholinesterase and their distribution of endplate and non-endplate regions of rat diaphragm muscle. J. Neurobiol. 4: 343–361.PubMedCrossRefGoogle Scholar
  17. Inestrosa, N. C., Ramirez, B. U., and Fernandez, H. L. (1977) Effect of denervation and of axoplasmic transport blockage on the in vitro release of muscle endplate acetylcholinesterase. J. Neurochem. 28: 941–945.PubMedCrossRefGoogle Scholar
  18. Johnson, C. D., and Russell, R. L. (1975) A rapid, simple radiometric assay for cholinesterase, suitable for multiple determinations. Anal. Biochem. 64: 229–238.PubMedCrossRefGoogle Scholar
  19. Kugelberg, E. (1976) Adaptive transformation of rat soleus motor units during growth. J. Neurol. Sci. 27: 269–289.PubMedCrossRefGoogle Scholar
  20. Main, A. R. (1976) Structure and inhibitors of cholinesterase. In: “Biology of Cholinergic Function”. (Eds.) Goldberg, A. M. and Hanin, I. Raven Press, New York, pp. 269–353.Google Scholar
  21. Massoulie, J., and Bon, S. (1982) The molecular forms of cholinesterase and acetylcholinesterase in vertebrates. Ann. Rev. Neurosci. 5: 57–106.PubMedCrossRefGoogle Scholar
  22. McLaughlin, J., and Bosmann, H. B. (1976) Molecular species in acetylcholinesterase in denervated rat skeletal muscle. Exp. Neurol. 52: 263–271.PubMedCrossRefGoogle Scholar
  23. Ranish, N. A., Kiauta, T., and Dettbarn, W.-D. (1979) Axotomy induced changes in cholinergic enzymes in rat nerve and muscles. J. Neurochem. 32: 1157–1164.PubMedCrossRefGoogle Scholar
  24. Silman, I., Di Giamberardino, L., Lyles, J., Couraud, J. Y., and Barnard, E. A. (1979) Parallel regulation of acetylcholinesterase and pseudocholinesterase in normal, denervated and dystrophic chicken skeletal muscle. Nature 280: 160–162.PubMedCrossRefGoogle Scholar
  25. Spencer, P. S., and Schaumburg, H. H. (1977) Ultrastructural studies of the dying-back process. IV. Differential vulnerability of PNS and CNS fibers in experimental central-peripheral distal axonopathies. J. Neuropathol. Exp. Neurol. 36: 300–320.PubMedCrossRefGoogle Scholar
  26. Spencer, P. S., and Schaumburg, H. H. (1978) Pathobiology of neurotoxic axonal degeneration. In: “Physiology and Pathobiology of Axons”. (Ed.) Waxman, S. G. Raven Press, New York, pp. 265–282.Google Scholar
  27. Vigny, M., Gisiger, V., and Massoulie, J. (1978) Nonspecific cholin-esterase and acetylcholinesterase in rat tissues: Molecular forms, structural and catalytic properties, and significance of the two enzyme systems. Proc. Natl. Acad. Sci. 75: 2588–2592.PubMedCrossRefGoogle Scholar
  28. Vigny, M., Koenig, J., and Rieger, F. (1976) The motor endplate specific form of acetylcholinesterase: appearance during embryogenesis and reinnervation of rat muscle. J. Neurochem. 27: 1347–1353.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Barbara F. Bass
    • 1
  • Alan M. Goldberg
    • 1
  1. 1.The Johns Hopkins School of Hygiene and Public HealthBaltimoreUSA

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