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.
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References
Ahlquist, J. and Andersson, L., Methyl green-pyronin staining: Effects of fixation: Use in routine pathology, Stain. Technol. 1 (1972) 17–22.
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.
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.
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.
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.
Einstein, E.R., Csejtey, J. and Marks, N., Degradation of encephalitogen by prifiari hrain acid proteinase. FEBS Letts. 1 (1968) 191–195.
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.
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.
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.
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.
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.
Link, H., Oligoclonal immunoglobulin G in multiple sclerosis brains, J. Neurol. Sci. 16 (1972) 103–114.
Lumsden, C.E., The neuropathology of multiple sclerosis, Clin. Neurol. 9 (1970) 217–309.
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.
Riekkinen, P.J. and Clausen, J., Proteinase activity of myelin, Brain Res. 15 (1969) 413–430.
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.
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.
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.
Röyttä, M., Frey, H., Riekkinen, P.J., Laaksonen, H. and Rinne, U.K., Myelin breakdown and basic protein, Exp. Neurol. 45 (1974) 174–185.
Suzuki, K., Kamoshita, S., Eto, Y., Tourtellotte, W.W. and Gonatas, J.O., Myelin in multiple sclerosis, Arch. Neurol. 28 (1973) 293–297.
Wolfgram, F., Wallace, W. and Tourtellotte,W., Amino acid composition of myelin in multiple sclerosis, Neurology 22 (1972) 1044–1046.
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.
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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
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DOI: https://doi.org/10.1007/978-1-4684-2514-7_42
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