Abstract
Using radioimmunoassays (RIA) for the myelin specific proteins, myelin proteolipid protein (PLP) and myelin basic protein (MBP) and an enzyme assay for the activity of the myelin marker enzyme 2′3′ cyclic-3′ phosphohydrolase (CNPase), we have studied plaque, periplaque and normal appearing white matter (NAWM) regions of multiple sclerosis (MS) brain tissue, as well as normal control brain tissue. We found that all three myelin proteins are decreased in all regions, including NAWM, of MS brain, with a decreasing gradient from NAWM to periplaque to plaque. The NAWM was not significantly different from the periplaque region. Surprisingly, when the ratios of the proteins were calculated, MBP activity, although decreased was found to be relatively preserved.
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Trotter, J. L., Wegescheide, C. L., andGarvey, W. F. 1983. Regional studies of myelin proteins in human brain and spinal cord. Neurochem. Res. 9:133–146.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., andRandall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.
Kurihara, T., Nussbaum, J. L., andMandel, P. 1969. 2′3′-Cyclic-3′-phosphohydrolase in the brain of the “Jimpy” mouse, a mutant with deficient myelination. Brain Res. 13:401–403.
Agrawal, H. C., Hartman, B. K., Shearer, W. T., Kalmbach, S., andMargolis, F. 1977. Purification and immunohistochemical localization of rat brain myelin proteolipid protein. J. Neurochem. 28:495–508.
Cohen, S. R., McKhann, G. M., andGuarnieri, M. 1975. A radioimmunoassay for myelin basic protein and its use for quantitative measurements. J. Neurochem. 25:371–376.
Trotter, J. L., Lieberman, L., Margolis, F. L., andAgrawal, H. C. 1981. Radioimmunoassay for central nervous system myelin-specific proteolipid protein. J. Neurochem. 36:1256–1262.
Prohaska, J. R., Clar, D. A., andWells, W. W. 1973. Improved rapidity and precision in the determination of brain 2′3′ cyclic nucleotide 3′ phosphohydrolase. Anal. Biochem. 56:275–282.
Einstein, E. R., Csejtey, J., Dalal, K. B., Adams, C. W. M., Bayliss, D. B., andHallpike, J. F. 1972. Proteolytic activity and basic protein loss in and around multiple sclerosis plaques: Combined biochemical and histochemical observations. J. Neurochem. 19:653–662.
Einstein, E. R., Dalal, K. B., andCsejtey, J. 1970. Increased protease activity and changes in basic proteins and lipids in multiple sclerosis plaques. J. Neurol. Sci. 11:109–121.
Hirsch, H. E., Duquette, P., andParko, M. E. 1976. The quantitative histochemistry of multiple sclerosis plaques: Acid proteinase and other acid hydrolase. J. Neurochem. 26:505–512.
Itoyama, Y., Sternberger, N. H., Webster, H.deF., Quarles, R. H., Cohen, S. R., andRichardson, E. P. 1980. Immunocytochemical observations on the distribution of myelin-associated glycoprotein and myelin basic protein in multiple sclerosis lesion. Ann. Neurol. 7:167–177.
Newcombe, J., Cuzner, M. L., Roytta, M., andFrey, H. 1980. White matter proteins in multiple sclerosis. J. Neurochem. 34:700–708.
Riekkinen, P. J. Palo, J. Arstila, A. U., Savolainen, H. J., Rinne, K., Kivalo, E. K., andFrey, H. 1971. Protein composition of multiple sclerosis. Arch. Neurol. 24:545–549.
Riekkinen, P. J., Rinne, U. K., Arstila, A. W., Kurihara, T. andPelliniemi, T. 1972. Studies on the pathogenesis of multiple sclerosis. 2′3′-cyclic nucleotide 3-phosphohydrolase as marker of demyelination and correlation of findings with lysosomal changes. J. Neurol. Sci. 15:113–120.
Whitaker, J. N. 1978. The distribution of myelin basic protein in central nervous system lesions of multiple sclerosis and acute experimental allergic encehalomyelitis. Ann. Neurol. 3:291–298.
Yu, R. K., Ueno, K., Glaser, G. HJ., andTourtellotte, W. W. 1982. Lipid and protein alterations of spinal cord and cord myelin of multiple sclerosis. J. Neurochem. 39:464–477.
Susuki, L., Kamoshita, S., Eto, Y., Tourtellotte, W. W., andGonatas, J. O. 1973. Myelin in multiple sclerosis: Composition of myelin from normal-appearing white matter. Arch. Neurol. 28:293–297.
Gopfert, E., Pytlik, S., andDebuch, H. 1980. 2′3′-Cyclic nucleotide 3′ phosphohydrolase and lipids of myelin from multiple sclerosis and normal brains. J. Neurochem. 34:732–739.
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Trotter, J.L., Wegescheide, C.L., Garvey, W.F. et al. Studies of myelin proteins in multiple sclerosis brain tissue. Neurochem Res 9, 147–152 (1984). https://doi.org/10.1007/BF00967666
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DOI: https://doi.org/10.1007/BF00967666