Acta Neuropathologica

, Volume 58, Issue 3, pp 210–214 | Cite as

Selective loss of Purkinje cells from the rat cerebellum caused by acrylamide and the responses ofβ-glucuronidase andβ-galactosidase

  • J. B. Cavanagh
  • C. C. Nolan
Original Works


Acrylamide (30mg/kg) given daily to rats five times each week for 3 weeks leads to progressive loss of Purkinje cells. The necrotic cells begin to be visible from the third day and their numbers reach a peak at the time when the dosing ceases at 18 days. They are less frequent thereafter, but are still visible almost 3 weeks later in small numbers. The density of Purkinje cells per millimeter falls to about 70% of normal at the 7th day, and a similar degree of reduction of the neuronal marker enzyme, β-galactosidase, is found over the same time scale. By contrast, while there is a brisk macrophage/microglial response in the molecular layer to the loss of the Purkinje cell dendrites, the increase in β-glucuronidase activity is relatively minor and is not significantly different from normal until after the 21st day. These responses are discussed in the context of the use of lysosomal enzyme activities in the assay of certain neurotoxic lesions.

Key words

Purkinje Cells Selective loss Rat cerebellum Acrylamide β-Glucuronidase β-Galactosidase 


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  1. Brown, AW, Brierley JB (1968) The nature, distribution and earliest stages of anoxic-ischaemic nerve cell damage in the rat brain as defined by the optical microscope. Br J Exp Pathol 49:87–106Google Scholar
  2. Cammermeyer J (1960) The postmortem origin and mechanism of neuronal hyperchromatosis and nuclear pyknosis. Exp Neurol 2:379–405Google Scholar
  3. Cavanagh JB (1982) The pathokinetics of acrylamide intoxication: a reappraisal of the problem. Neuropathol Appl Neurobiol 8:315–336Google Scholar
  4. Dewar AJ, Moffett BJ (1979) Biochemical methods for detecting neurotoxicity—a short review. Pharmacol Therap 5:545–562Google Scholar
  5. Gipon L, Schotman P, Jennekens FGI, Gispen WH (1977) Polyneuropathies and CNS protein metabolism. I. Description of the acrylamide syndrome in rats. Neuropathol Appl Neurobiol 3:115–123Google Scholar
  6. Kaplan ML, Murphy SD (1972) Effect of acrylamide on rotarod performance and sciatic nerve β-glucuronidase activity of rats. Toxicol Appl Pharmacol 22:259–268Google Scholar
  7. Kuperman AS (1958) Effects of acrylamide on the central nervous system of the cat. J Pharmacol Exp Therap 123:180–192Google Scholar
  8. McCaman RE, Robins, E (1959) Quantitation of biochemical studies on Wallerian degeneration in the peripheral and central nervous systems. II. Twelve enzymes J Neurochemistry 5:32–42Google Scholar
  9. Robins E (1961) β-Glycosidases in the nervous system. In: Kety SS, Elkes J (eds) Neurochemistry: the regional chemistry, physiology and pharmacology of the nervous system. Pergamon Press, New YorkGoogle Scholar
  10. Robins E, Hirsch HE (1968) Glycosidases in the nervous system II. Localisation of β-galactosidase, β-glucuronidase, and β-glucosidase in individual nerve cell bodies. J Biol. Chemistry 243:4253–4257Google Scholar
  11. Robins E, Hirsch HE, Eamons SG (1968) Glycosidases in the nervous system. I. Assay, some properties and distribution of β-galactosidase, β-glucuronidase and β-glucosidase. J Biol Chemistry 243:4246–4252Google Scholar
  12. Sinha AK, Rose SPR (1972) Compartmentation of lysosomes in neurones and neuropil and a new neuronal marker. Brain Res 39:181–196Google Scholar

Copyright information

© Springer-Verlag 1982

Authors and Affiliations

  • J. B. Cavanagh
    • 1
  • C. C. Nolan
    • 1
  1. 1.Institute of NeurologyLondonUK

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