Skip to main content

Topographic Analysis of MS and Control Brains

  • Chapter
Myelination and Demyelination

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 100))

Summary

Autopsy specimens from five MS and six control cases were subjected to morphological and biochemical investigations including protein electrophoresis. On the basis of this study individual differences between the enzyme activities and the effect of storage must be taken into consideration when studying autopsy material. Furthermore, good morphological controls are required when biochemical changes are studied, especially in diseases like MS where local changes are found.

Biochemical and morphological studies showed that multiple protein bands, possibly GFA, may be noticed in gliotic areas. The activity of β-glucuronidase seemed to correlate with gliosis but the increase of this enzyme did not seem to be the first change in the plaque areas. It was suggested that the activation of carboxylic acid esterase preceded the activation of β-glucuronidase. The activities of lysosomal hydrolases seemed to decrease to a normal level in morphologically normal brain areas outside the plaques. In light microscopy, cells resembling plasma cells and containing Russel bodies were found.

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

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Ahlquist, J. and Andersson, L., Methyl green-pyronin staining: Effects of fixation: Use in routine pathology, Stain. Technol. 1 (1972) 17–22.

    Google Scholar 

  2. Althaus, H.H., Pilz, H. and Müller, D., The protein composition of myelin in multiple sclerosis (MS) and orthochromatic leukodystrophy (OLD), Z. Neurol. 205 (1973) 229–241.

    Article  PubMed  CAS  Google Scholar 

  3. Ansari, K.A., Hendrickson, H., Sinha, A.A. and Rand, A., Myelin basic protein in frozen and unfrozen bovine brain: A study of autolytic changes in situ, J. Neurochem. 25 (1975). 193–195.

    Article  PubMed  CAS  Google Scholar 

  4. Cuzner, M.L. and Davison, A.N., Changes in cerebral lysosomal enzyme activity and lipids in multiple sclerosis, J. Neurol. Sci. 19 (1973) 29–36.

    Article  PubMed  CAS  Google Scholar 

  5. Cuzner, M.L., Barnard, R.O., MacGregor, J.L., Borshell, N.J. and Davison, A.N., Myelin composition in acute and chronic multiple sclerosis in relation to cerebral lysosomal activity, J. Neurol. Sci. 29 (1976) 323–334.

    Article  PubMed  CAS  Google Scholar 

  6. Einstein, E.R., Csejtey, J. and Marks, N., Degradation of encephalitogen by prifiari hrain acid proteinase. FEBS Letts. 1 (1968) 191–195.

    Article  Google Scholar 

  7. Einstein, E.R., Dalal, K.B. and Csejtey, J., Increased protease activity and changes in basic proteins and lipids in multiple sclerosis plaques, J. Neurol. Sci. 11 (1970) 109–121.

    Article  PubMed  CAS  Google Scholar 

  8. Eng, L.F., Bond, P. and Gerstl, B., Isolation of myelin proteins from disc acrylamide gels electrophoresed in phenol-formic acid-water, Neurobiology 1(1971) 58–63.

    CAS  Google Scholar 

  9. Frey, H.J., Riekkinen, P.J., Rinne, U.K. and Arstila, A.U., Peptidase activity of myelin during the myelination period in guinea pig brain, Brain Res. 22 (1970) 243–248.

    Article  PubMed  CAS  Google Scholar 

  10. Horrocks, L.A., Plasmalogenase is elevated in early demyelinating lesions due to canine distemper virus, in Myelination and Demyelination, Recent Chemical Advances, Satellite Symposium of the ISN, Helsinki, August 1977.

    Google Scholar 

  11. Kurihara, T. and Tsukada, Y., The regional and subcellular distribution of 2’,3’-cyclic nucleotide 3’-phosphohydrolase in the central nervous system, J. Neurochem. 14 (1967) 1167–1174.

    Article  PubMed  CAS  Google Scholar 

  12. Link, H., Oligoclonal immunoglobulin G in multiple sclerosis brains, J. Neurol. Sci. 16 (1972) 103–114.

    Article  PubMed  CAS  Google Scholar 

  13. Lumsden, C.E., The neuropathology of multiple sclerosis, Clin. Neurol. 9 (1970) 217–309.

    Google Scholar 

  14. Nachlas, M.M. and Seligman, A.M., Evidence for the specificity of esterase and lipase by the use of three chromogenic substrates, J. biol. Chem. 181 (1949) 343–355.

    PubMed  CAS  Google Scholar 

  15. Riekkinen, P.J. and Clausen, J., Proteinase activity of myelin, Brain Res. 15 (1969) 413–430.

    Article  PubMed  CAS  Google Scholar 

  16. Riekkinen, P.J., Clausen, J., Frey, H.J., Fog, T. and Rinne, U.K., Acid proteinase activity of white matter and plaques in multiple sclerosis, Acta neurol. scand. 46 (1970) 349–353.

    Article  PubMed  CAS  Google Scholar 

  17. Riekkinen, P.J., Palo, J., Arstila, A.U., Savolainen, H., Rinne, U.K., Kivalo, E. and Frey, H.J., Protein composition of multiple sclerosis myelin, Arch. Neurol. 24 (1971) 545–549.

    Article  PubMed  CAS  Google Scholar 

  18. Riekkinen, P.J., Rinne, U.K., Arstila, A.U., Kurihara, T. and Pelliniemi, T.T., Studies on the pathogenesis of multiple sclerosis, J. Neurol. Sci. 15 (1972) 113–120.

    Article  PubMed  CAS  Google Scholar 

  19. Röyttä, M., Frey, H., Riekkinen, P.J., Laaksonen, H. and Rinne, U.K., Myelin breakdown and basic protein, Exp. Neurol. 45 (1974) 174–185.

    Article  PubMed  Google Scholar 

  20. Suzuki, K., Kamoshita, S., Eto, Y., Tourtellotte, W.W. and Gonatas, J.O., Myelin in multiple sclerosis, Arch. Neurol. 28 (1973) 293–297.

    CAS  Google Scholar 

  21. Wolfgram, F., Wallace, W. and Tourtellotte,W., Amino acid composition of myelin in multiple sclerosis, Neurology 22 (1972) 1044–1046.

    Article  PubMed  CAS  Google Scholar 

  22. Zetterwall, O. and Link, H., Electrophoretic distribution of kappa/lambda immunoglobulin light chain determinants in serum and CSF in multiple sclerosis, Clin. exp. Immunol. 7 (1970) 365–372.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1978 Plenum Press, New York

About this chapter

Cite this chapter

Röyttä, M., Frey, H., Riekkinen, P., Rinne, U.K. (1978). Topographic Analysis of MS and Control Brains. In: Palo, J. (eds) Myelination and Demyelination. Advances in Experimental Medicine and Biology, vol 100. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-2514-7_42

Download citation

  • DOI: https://doi.org/10.1007/978-1-4684-2514-7_42

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-2516-1

  • Online ISBN: 978-1-4684-2514-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics