Advertisement

The Histochemical Journal

, Volume 2, Issue 3, pp 209–218 | Cite as

Histochemistry of myelin. IX. Neutral and acid proteinases in early Wallerian degeneration

  • J. F. Hallpike
  • C. W. M. Adams
  • O. B. Bayliss
Papers

Synopsis

Acid and neutral proteinases, ‘leucine aminopeptidase’ (l-leucyl-β-naphthylamidase) and acid phosphatase were studied in rat sciatic nerves undergoing Wallerian degeneration. Biochemical evidence indicated that increased activity of both proteases and acid phosphatase occurred by 12 hr after nerve section. Histochemical changes in these three enzymes were apparent after three days. Biochemical estimation of neutral ‘leucine aminopeptidase’ (an enzyme predominantly located in myelin in the normal peripheral nerve) showed increased activity near the of the first week of degeneration. During the second week after nerve section all the enzymes studied became markedly more active. The parallel increase in activity of acid proteinase and acid phosphatase and the similarities in their histochemical distribution suggest that the acid proteinase is of lysosomal origin. Such changes in early Wallerian degeneration appear to precede macrophage invasion of the nerve and to arise mainly from the degenerating axon, the Schwann cell, or both. In spite of the delayed increase in ‘leucine aminopeptidase’ it seems possible that some proteinase activity also arises from myelin.

Keywords

Leucine Sciatic Nerve Schwann Cell Acid Phosphatase Proteinase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adams, C. W. M. (1959). A histochemical method for the demonstration of normal and degenerating myelin.J. Path. Bact. 77, 648–50.Google Scholar
  2. Adams, C. W. M. (1960). Osmium tetroxide and the Marchi reaction; reactions with polar and non-polar lipids, protein and polysaccharide.J. Histochem. Cytochem. 8, 262–7.Google Scholar
  3. Adams, C. W. M., Abdulla, Y. H., Turner, D. R. &Bayliss, O. B. (1968). Subcellular preparation of peripheral nerve myelin.Nature, Lond. 220, 171–3.Google Scholar
  4. Adams, C. W. M. &Bayliss, O. B. (1961). Histochemistry of myelin. III. Peripheral nerve cathepsin.J. Histochem. Cytochem. 9, 473–6.Google Scholar
  5. Adams, C. W. M., Davison, A. N. &Gregson, N. A. (1963). Enzyme inactivity of myelin: histochemical and biochemical evidence.J. Neurochem. 10, 383–445.Google Scholar
  6. Adams, C. W. M. &Glenner, G. G. (1962). Histochemistry of myelin. IV. Aminopeptidase activity in CNS and PNS.J. Neurochem. 9, 233–9.Google Scholar
  7. Adams, C. W. M., Ibrahim, M. Z. M. &Leibowitz, S. (1965). Demyelination. InNeurohistochemistry (ed.C. W. M. Adams), p. 437. Amsterdam: Elsevier.Google Scholar
  8. Adams, C. W. M. &Tuqan, N. A. (1961a). Histochemistry of myelin. II. Proteins, lipid-protein dissociation and proteinase activity in Wallerian degeneration.J. Neurochem. 6, 334–41.Google Scholar
  9. Adams, C. W. M. &Tuqan, N. A. (1961b). The histochemical demonstration of protease by a gelatinsilver film substrate.J. Histochem. Cytochem. 9, 469–72.Google Scholar
  10. Barka, T. &Anderson, P. J. (1962). Histochemical methods for acid phosphatase using hexazonium pararosaniline as coupler.J. Histochem. Cytochem. 10, 741.Google Scholar
  11. Bubis, J. J. &Wolman, M. (1965). Hydrolytic enzymes in Wallerian degeneration.Israel. J. Med. Sci. 1, 410–14.Google Scholar
  12. Davis, B. J. &Ornstein, L. (1959). High resolution enzyme localization with a new diazo reagent, “Hexazonium Pararosaniline”.J. Histochem. Cytochem. 7, 297–8.Google Scholar
  13. De Ouve, C. &Wattiaux, R. (1966). Functions of lysosomes.A. Rev. Physiol. 28, 435–92.Google Scholar
  14. Fishman, W. H. &Goldman, S. S. (1965). A postcoupling technique for β-glucuronidase employing the substrate, naphthol AS-BI-β-D-glucosiduronic acid.J. Histochem. Cytochem. 13, 441–7.Google Scholar
  15. Gomori, G. (1952).Microscopic Histochemistry. Chicago University Press.Google Scholar
  16. Gould, R. P. & Holt, S. J. (1961). Observations on acid phosphatase and esterases in the rat sciatic nerve undergoing Wallerian degeneration.Proc. Anat. Soc., 45–8.Google Scholar
  17. Hallpike, J. F. & Adams, C. W. M. (1969a). Proteolytic enzymes in myelin breakdown. InProc. Internat. Symp. Biochemistry and Histochemistry of Myelin and Demyelination, Poznan 1968.Neuropat. Pol. 7, 225–31.Google Scholar
  18. Hallpike, J. F. &Adams, C. W. M. (1969b). Proteolysis and myelin breakdown: a review of recent histochemical and biochemical studies.Histochem. J. 1, 559–78.Google Scholar
  19. Hallpike, J. F., Adams, C. W. M. &Bayliss, O. B. (1970a). Histochemistry of myelin. VIII. proteolytic activity around multiple sclerosis plaques.Histochem. J. 2, 559–78.Google Scholar
  20. Hallpike, J. F., Adams, C. W. M. & Bayliss, O. B. (1970b). Histochemistry of myelin. X. Proteolysis of normal myelin and release of lipid by extracts of degenerating nerve.Histochem. J. 2,in press.Google Scholar
  21. Hallpike, J. F., Adams, C. W. M. & Bayliss, O. B. (1970c). Histochemistry of myelin. XI. Loss of basic protein in early myelin breakdown and multiple sclerosis plaques.Histochem. J. 2,in press.Google Scholar
  22. Hallpike, J. F., Adams, C. W. M. & Bayliss, O. B. (1970d). Observations to be published.Google Scholar
  23. Heinzen, B. (1947). Acid phosphatase activity in transected sciatic nerves.Anat. Rec. 98, 193–205.Google Scholar
  24. Hoit, S. J. (1959). Factors governing the validity of staining methods for enzymes and their bearing upon the Gomeri acid phosphatase technique.Expl. Cell Res. Suppl. 7, 1–27.Google Scholar
  25. Holtzman, E. &Novikoff, A. B. (1965). Lysosomes in the rat sciatic nerve following crush.J. Cell Biol. 27, 651–69.Google Scholar
  26. Johnson, A. C., McNabb, A. R. &Rossiter, R. J. (1950). Chemistry of Wallerian degeneration. A review of recent studies.Arch. Neurol. Psychiat. 64, 105.Google Scholar
  27. Kunitz, M. (1946–7). Crystalline soybean trypsin inhibitor. II. General properties.J. Gen. Physiol. 30, 291–310.Google Scholar
  28. Lumsden, C. E. (1952). Quantitative studies on lipolytic enzyme activity in degenerating and regenerating nerve.Q. Jl exp. Physiol. 37, 45–57.Google Scholar
  29. Marks, N. &Lajtha, A. (1963). Protein breakdown in the brain. Subcellular distribution and properties of neutral and acid proteinases.Biochem. J. 89, 438–47.Google Scholar
  30. Matthews, D. M., Muir, G. G. &Baron, D. N. (1964). Estimation of alpha-amino nitrogen in plasma and urine by the colorimetric ninhydrin reaction.J. clin. Path. 17, 150–3.Google Scholar
  31. Montanini, I. &Porcellati, G. (1964). Protein metabolism of peripheral nerves during demyelination by organophosphorous compounds.Ital. J. Biochem. 13, 230–9.Google Scholar
  32. Pearse, A. G. E. (1960).Histochemistry: theoretical and applied. 2nd Ed. pp. 881–2. London: Churchill.Google Scholar
  33. Porcellati, G. (1964–5). Alcuna aspetti del metabolismo proteico del sistema nervoso centrale e periferico.Progr. Biochem. 2, 1–20.Google Scholar
  34. Porcellati, G. (1966). Biochemical aspects of protein metabolism during nerve degeneration and regeneration. InProtides of the biological fluids (ed. H. Peeters), p. 115. Amsterdam: Elsevier.Google Scholar
  35. Porcellati, G. &Curti, B. (1960). Proteinase activity of peripheral nerves during Wallerian degeneration.J. Neurochem. 5, 277–82.Google Scholar
  36. Porcellati, G., Millo, A. &Manocchio, I. (1961). Proteinase activity of nervous tissues in organophosphorous compound poisoning.J. Neurochem. 7, 313–20.Google Scholar
  37. Porcellati, G. &Thompson, R. H. S. (1959). The effect of nerve section on the free aminoacids of nervous tissue.J. Neurochem. 1, 340–7.Google Scholar
  38. Rossiter, R. J. (1955). The biochemistry of demyelination. InNeurochemistry (eds. K. A. C. Elliott. I. H. Page and J. H. Quastel), 1st Ed., p. 696. Springfield, Illinois: Thomas.Google Scholar
  39. Weller, R. O. (1965). Diphtheritic neuropathy in the chicken: an electron-microscopic study.J. Path. Bact. 89, 591–8.Google Scholar
  40. Weller, R. O. &Mellick, R. S. (1966). Acid phosphatase and lysosome activity in diphtheritic neuropathy and Wallerian degeneration.Br. J. exp. Path. 47, 425–34.Google Scholar
  41. Wolfgram, F. &Rose, A. S. (1960). The histochemistry of neurokeratin in normal and degenerating sciatic nerve.Neurology (Minneap) 10, 365–71.Google Scholar
  42. Wootton, I. D. P. (1964).Micro-analysis in medical biochemistry, p. 103. London: Churchill.Google Scholar

Copyright information

© Chapman and Hall Ltd 1970

Authors and Affiliations

  • J. F. Hallpike
    • 1
  • C. W. M. Adams
    • 1
  • O. B. Bayliss
    • 1
  1. 1.Department of PathologyGuy's Hospital Medical School (London University)London

Personalised recommendations