Synopsis
the early stages of Wallerian degeneration in peripheral nerves are accompanied by loss of a trypanophilic, trypsin-digestible basic protein from myelin. This loss of basic protein is ascribed to the activity of proteolytic enzymes. The reduced trypanophilia in degenerating nerves could not be attributed to loss of lipid. Likewise, the tryptophan-rich trypsin-resistant neurokeratin component of peripheral nerve myelin showed no change in the first week of degeneration. Loss of basic protein has been observed in and surrounding plaques of multiple sclerosis. We infer that digestion of basic protein would lead to the release of the encephalitogenic antigen contained therein.
Similar content being viewed by others
References
Adams, C. W. M. (1957). Ap-dimethylaminobenzaldehyde-nitrite method for the histochemical demonstration of tryptophan and related compounds.J. clin. Path. 10, 56–62.
Adams, C. W. M. (1958). The application of histochemical methods for protein identification in the study of certain pathological problems.Proc. Roy. Soc. Med. 51, 339–43.
Adams, C. W. M. (1968). The histochemistry of proteolytic enzymes and lipoproteins inthe normal and diseased nervous system. InMacromolecules and the function of the neuron (eds. Z. Lodin and S. P. R. Rose), p. 111, Amsterdam: Excerpta Medica Foundation.
Adams, C. W. M. &Bayliss, O. B. (1968a). Histochemistry of myelin. V. Trypsin-digestible and trypsin-resistant proteins.J. Histochem. Cytochem. 16, 110–14.
Adams, C. W. M. &Bayliss, O. B. (1968b). Histochemistry of myelin. VII. Analysis of lipid-protein relationships and the absence of acid mucopolysaccharide.J. Histochem. Cytochem. 16, 119–27.
Adams, C. W. M. &Davison, A. N. (1965). The myelin sheath. InNeurohistochemistry (ed. C. W. M. Adams), p. 332. Amsterdam: Elsevier.
Adams, C. W. M. & Hallpike, J. F. (1969). Lipid-protein relationships in normal and degenerating myelin. InProc. Int. Symp. Biochem. Histochem. of Myelin and Demyelination. Poznan (1968),Neuropat. Pol. 7, 217–24.
Adams, C. W. M. &Tu qan, N. A. (1961). Histochemistry of myelin. II. Proteins, lipidprotein dissociation and proteinase activity in Wallerian degeneration.J. Neurochem. 6 334–41.
Ansell, G. B. &Richter, D. (1954a). The proteolytic activity of brain tissue.Biochim. bïophys. Acta 13, 87–91.
Ansell, G. B. &Richter, D. (1954b). Evidence for a neutral proteinase in brain tissue.Biochim. biophys. Acta 13, 92–7.
Chao, L. P. &Einstein, E. R. (1968). Isolation and characterization of an active fragment from enzymatic degradation of encephalitogenic protein.J. biol. Chem. 243, 6050–5.
Einstein, E. R., Csejtey, J. &Marks, N. (1968). Degradation of encephalitogen by purified brain acid proteinase.FEBS Let. 1, 191–5.
Guroff, G. (1964). A neutral calcium-activated proteinase from the soluble fraction of rat brain.J. biol. Chem. 239, 149–55.
Hallpike, J. F. & Adams, C. W. M. (1969). Proteolytic enzymes in myelin breakdown. InProc. Int. Symp. Biochem. Histochem. of Myelin and Demyelination. Poznan (1968), in press.
Hallpike, J. F., Adams, C. W. M. &Bayliss, O. B. (1970a). Histochemistry of myelin. VIII. Proteolytic activity around multiple sclerosis plaques.Histochem. J. 2, 199–208.
Hallpike, J. F., Adams, C. W. M. &Bayliss, O. B. (1970b). Histochemistry of myelin. IX. Neutral and acid proteinases in early Wallerian degeneration.Histochem. J. 2, 209–18.
Hallpike, J. F., Adams, C. W. M. &Bayliss, O. B. (1970c). Histochemistry of myelin. X. Proteolysis of normal myelin and release of lipid by extracts of degenerating nerve.Histochem. J. 2, 315–21.
Johnson, A. D., McNabb, A. R. &Rossiter, R. J. (1950). Chemistry of Wallerian degeneration. A review of recent studies.Arch. Neurol. Psychiat. (Chicago) 64, 105–21.
Kirs, M. W., Murphy, J. B. &Alvord, E. C. (1961). Studies on the encephalitogenic factor in guinea pig CNS. InChemical Pathology of the Nervous System (ed. J. Folch-Pi), p. 197. Oxford: Pergamon Press.
Lumsden, C. E., Robertson, D. M. &Blight, R. (1966). Chemical studies on experimental allergic encephalomyelitis. Peptide as the common denominator in all encephalitogenic antigens.J. Neurochem. 13, 127–62.
Marks, N. &Lajtha, A. (1963). Protein breakdown in the brain. Subcellular distribution and properties of neutral and acid proteinases.Biochem. J. 89, 438–47.
Marks, N. &Lajtha, A. (1965). Separation of acid and neutral proteinases of brain.Biochem. J. 97, 74–83.
Nakao A., Davis, W. J. &Einstein, E. R. (1966a). Basic proteins from the acidic extract of bovine spinal cord. I. Isolation and characterization.Biochim. biophys. Acta 130, 162–70.
Nakao, A., Davis, W. J. &Einstein, E. R. (1966b). Basic proteins from the acidic extract of bovine spinal cord. II. Encephalitogenic, immunologic and structural inter-relationships.Biochim. biophys. Acta 13, 171–9.
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.
Porcellati, G. &Curti, B. (1960). Proteinase activity during Wallerian degeneration.J. Neurochem. 5, 277–82.
Riekkinen, P. J. &Rinne, U. K. (1968). A new neutral proteinase from the rat brain.Brain Res. (Amst.) 9, 126–35.
Rossiter, R. J. (1955). Biochemistry of demyelination. InNeurochemistry (eds. K. A. C. Elliott, I. H. Page and J. H. Quastel), 1st Ed., p. 696. Springfield, Ill.: Thomas.
Tuqan, N. A. &Adams, C. W. M. (1961). Histochemistry of myelin. I. Protein and lipid-protein complexes in the normal sheath.J. Neurochem. 6, 327–33.
Wolfgram, F. &Rose, A. S. (1961). A study of some component proteins of central and peripheral nerve myelin.J. Neurochem. 8, 161–8.
Wolman, M. &Hestrin-Lerner, S (1960). A histochemical contribution to the study of the molecular morphology of myelin sheath.J. Neurochem. 5, 114–20.
Author information
Authors and Affiliations
Additional information
Research Associate supported by the British Multiple Sclerosis Society.
Rights and permissions
About this article
Cite this article
Hallpike, J.F., Adams, C.W.M. & Bayliss, O.B. Histochemistry of myelin. XI. Loss of basic protein in early myelin breakdown and multiple sclerosis plaques. Histochem J 2, 323–328 (1970). https://doi.org/10.1007/BF01005000
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01005000