Advertisement

Introduction and Comments

  • Elizabeth Roboz Einstein
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 100)

Abstract

As the first speaker at the Symposium, I take the opportunity to thank the organizers of that meeting, and especially Dr. J. Palo and Mrs. L.-M. Palo for all the arrangements they made. I am sure that all the participants share my sentiments when I say that it was a privilege to meet in the historically significant and architecturally magnificent Finlandia Hall.

Keywords

Multiple Sclerosis Proteolytic Enzyme Myelin Basic Protein Basic Protein Experimental Allergic Encephalomyelitis 
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. 1.
    Adams, C. W. M., Research on Multiple Sclerosis, C. Thomas, Springfield, Ill. (1971).Google Scholar
  2. 2.
    Alvord, E. C., Shaw, C. M., Hruby, S. and Kies, M.W., Encephali togen induced inhibition of experimental allergic encephalo-myelitis: prevention, suppression and therapy, Ann. N. Y. Acad. Sci. 122 (1965) 333 - 345.PubMedCrossRefGoogle Scholar
  3. 3.
    Barret, A. J., Lysosomal and related proteinases, in Proteases and Biological Control (E. Reich, D.B. Riffkin and E. Shaw, eds.) Cold Spring Harbor Conferences on Cell Proliferation, vol. 2 (1975) pp. 467-801.Google Scholar
  4. 4.
    Benetato, G. E., Gabrielescu, E. and Boros, I., The biochemistry of cerebral proteases in experimental allergic encephalo-myelitis, Rev. Roumaine. Physiol. 2 (1965) 379 - 384.Google Scholar
  5. 5.
    Bergstrand, H., Localization of antigenic determinants on bovine encephalitogenic protein, Eur. J. Biochem. 27 (1972) 126.PubMedCrossRefGoogle Scholar
  6. 6.
    Bergstrand, H., Encephalitogenic activity in rabbits of the C terminal region of bovine basic myelin protein. Localization to two different regions. FEBS Letts. 3 (1975) 195 - 198.Google Scholar
  7. 7.
    Buletza, G.F. and Smith, M.E., Enzymic hydrolysis of myelin basic protein and other proteins in CNS and lymphoid tissue from normal and demyelinating rats, Biochem. J. 156 (1976) 627 - 633.Google Scholar
  8. 8.
    Carnegie, P. R. and Dunkley, P. R., Basic proteins of central and peripheral nervous system myelin, Adv. Neurochem. 1 (1975) 95 - 135.Google Scholar
  9. 9.
    Chao, L. P. and Einstein, E. R., Isolation and characterization of an active fragment from enzymatic degradation of encephali togenic protein, J. Biol. Chem. 243 (1968) 6050 - 6058.PubMedGoogle Scholar
  10. 10.
    Chao, L. P. and Einstein, E. R., Localization of the active site through chemical modification of the encephalitogenic protein, J. Biol. Chem. 245 (1970) 6397 - 6403.PubMedGoogle Scholar
  11. 11.
    Chao, L. P. and Einstein, E. R., Physical properties of the encephalitogenic protein: molecular weight and conformation, J. Neurochem. 17 (1970) 1121 - 1132.PubMedCrossRefGoogle Scholar
  12. 12.
    Cohen, S. R., Herndon, R. M. and McKhann, G.M., Radioimmunoassay of myelin basic protein in spinal fluid, New Engl. J. Med. 293 (1976) 1455 - 1457.Google Scholar
  13. 13.
    Driscoll, B. F., Kies, M. W. and Alvord, E.C., Successful treatment of experimental allergic encephalomyelitis (EAE) in guinea pigs with homologous myelin basic protein, J. Immunol. 112 (1974) 392 - 397.PubMedGoogle Scholar
  14. 14.
    Einstein, E. R., Acid proteinase activity in multiple sclerotic brain in multiple sclerosis, in Multiple Sclerosis: Progress in Research ( E.J. Field, T.M. Bell and P.R. Carnegie, eds.) Academic Press, New York (1972) pp. 105 - 110.Google Scholar
  15. 15.
    Einstein, E. R., Chao, L. P. and Csejtey, J., Suppression of EAE by chemically modified encephalitogen, Immunochemistry 9 (1972) 1013 - 1019.PubMedCrossRefGoogle Scholar
  16. Einstein, E. R., Chao, L. P., Csejtey, J., Kibler, R.F. and Shapira, R., Species specificity in response to tryptophan modified encephalitogen, Immun. Chem. 9 (1972) 73 - 84.Google Scholar
  17. 17.
    Einstein, E. R., Csejtey, J., Dalai, K. B., Adams, C.W.M., Bayliss, O.B. and Hallpike, J.F., Proteolytic activity and basic protein loss in and around multiple sclerosis plaques. Combined biochemical and histochemical observations, J. Neurochem. 19 (1972) 653 - 662.PubMedCrossRefGoogle Scholar
  18. 18.
    Einstein, E. R., Csejtey, J., Davis, W. J., Lajtha, A. and Marks, N., Enzymatic degradation of encephalitogenic protein, Int. Arch. Allergy 36 (1969) 363 - 375.PubMedGoogle Scholar
  19. 19.
    Einstein, E. R., Csejtey, J., Davis, W. J. and Rauch, H. C., Protective action of the encephalitogen and other basic proteins in experimental allergic encephalomyelitis, Immunochemistry 5 (1968) 567 - 575.PubMedCrossRefGoogle Scholar
  20. 20.
    Einstein, E. R., Csejtey, J. and Marks, N., Degradation of en cephalitogen by purified acid proteinase, FEBS Letts. 1 (1968) 191 - 195.CrossRefGoogle Scholar
  21. 21.
    Einstein, E. R., Richard, K. A. and Kwa, G. B., Determination of gamma globulin in the cerebrospinal fluid by quantitative chromatography, J. Lab. Clin. Med. 68 (1966) 120 - 130.PubMedGoogle Scholar
  22. 22.
    Eng, L. F., Lee, Y. L. and Miles, L.E. M., 2-site immunoradiometric assay for glial fibrillary acidic protein in human cerebral spinal fluid, Fifth International Meeting of the ISN, Barcelona (1975) p. 302.Google Scholar
  23. 23.
    Eng, L. F., Vanderhaegen, J. J., Bignami, A. and Gerstl, B., An acidic protein isolated from fibrous astrocytes, Brain Res. 28 (1971) 351 - 354.PubMedCrossRefGoogle Scholar
  24. 24.
    Eylar, E. H., Experimental allergic encephalomyelitis and mul tiple sclerosis, in Multiple Sclerosis Immunology, Virology and Ultrastructure ( F. Wofgram, G.E. Ellison, J.G. Stevens and J.M. Andrews, eds.) Academic Press, New York (1972) pp. 449 - 486.Google Scholar
  25. 25.
    Eylar, E. H., Discussion to Experimental allergic encephalo myelitis and multiple sclerosis, in Multiple Sclerosis Immunology, Virology and Ultrastructure ( F. Wolfgram, G. E. Ellison, J. G. Stevens and J. M. Andrews, eds.) Academic Press, New York (1972) p. 480.Google Scholar
  26. 26.
    Eylar, E. H. and Thompson, M., Allergic encephalomyelitis: the physiochemical properties of the basic protein encephalitogen from bovine spinal cord, Arch. Biochem. Biophys. 129 (1969) 468 - 479.CrossRefGoogle Scholar
  27. 27.
    Felgenhauer, K. and Hagedorn, D., Evaluation of CSF proteins by two-dimensional mapping technique, Sixth International Meeting of the ISN, Copenhagen (1977) p. 338.Google Scholar
  28. 28.
    Felgenhauer, K. and Pak, S.J., Detection of ampholine patterns, Ann. N.Y. Acad. Sci. 209 (1973) 147 - 153.PubMedCrossRefGoogle Scholar
  29. 29.
    Felgenhauer, K., Schliep, G. and Rapic, N., Evaluation of the blood-CSF barrier by protein gradients and the humoral immune response within the central nervous system, J. Neurol. Sci. 30 (1976) 113 - 128.PubMedCrossRefGoogle Scholar
  30. 30.
    Goettlich-Riemann, W., Young, J. O. and Tappel, A. G., Cathepsin D, A and B and the effect of pH in the pathway of protein hydrolysis, Biochim. Biophys. Acta 243 (1971) 137.Google Scholar
  31. 31.
    Govindarajan, K. R., Rauch, H. C., Clausen, J. and Einstein, E. R., Changes in cathepsins B-1 and D-1, neutral proteinase and 2',3'-cyclic nucleotide 3'-phosphohydrolase activities in monkey brain with experimental allergic encephalomyelitis, J. Neurol. Sci. 23 (1974) 295 - 306.PubMedCrossRefGoogle Scholar
  32. 32.
    Kerekes, M. F., Feszt, T. and Kovacs, A., Catheptic activity in the cerebral tissue of the rabbit during EAE, Experientia 21 (1965) 42 - 46.PubMedCrossRefGoogle Scholar
  33. 33.
    Link, H., Oligoclonal immunoglobulin G in multiple sclerosis brain, J. Neurol. Sci. 16 (1972) 103 - 114.PubMedCrossRefGoogle Scholar
  34. 34.
    London, Y. and Vossenberg, F. G. A., Specific interaction of central nervous system myelin basic protein With lipids, Biochim. Biophys. Acta 478 (1973) 478 - 490.Google Scholar
  35. 35.
    Marks, N., Grynbaum, A. and Lajtha, A., The breakdown on myelin-bound protein by intra and extracellular proteases, Neurochem. Res. 1 (1976) 93 - 111.Google Scholar
  36. 36.
    Marks, N., Grynbaum, A. and Levine, S., Proteolytic enzymes in ordinary, hyperacute, monocytic and passive transfer forms of experimental allergic encephalomyelitis, Brain Res. 123 (1977) 147 - 157.CrossRefGoogle Scholar
  37. 37.
    Murazio, M., Massaro, A. and Michetti, F., A brain specific protein (S-100) in cerebrospinal fluid of multiple sclerosis patients, Proc. Int. Soc. Neurochem. 6 (1977) 324.Google Scholar
  38. 38.
    Nakao, A., Einstein, E. R. and Dharmaraksa, S., Relationship between experimental allergic encephalomyelitis and rabies postvaccinal encephalomyelitis, First Asian and Oceanian Congress of Neurology, Tokyo, Japan (1962) p. 129.Google Scholar
  39. 39.
    Oehmichen, M., Cerebrospinal Fluid Cytology, W. B. Saunders, Philadelphia (1976).Google Scholar
  40. 40.
    Olsson, J. E. and Link, H., Immunoglobulin abnormalities in multiple sclerosis. Relation to clinical parameters. Exacerbations and remissions. Arch. Neurol. 28 (1973) 392.PubMedCrossRefGoogle Scholar
  41. 41.
    Paterson, P. Y., Transfer of allergic encephalomyelitis in rats by means of lymph node cells, J. Exp. Med. 111 (1960) 119.PubMedCrossRefGoogle Scholar
  42. 42.
    Rauch, H. C. and Einstein, E. R., Induction and suppression of experimental allergic encephalomyelitis in the non-human primate, J. Neurol. Sci. 23 (1974) 99 - 116.PubMedCrossRefGoogle Scholar
  43. 43.
    Rauch, H. C. and Einstein, E. R., Specific brain proteins: A biochemical and immunological review, in Reviews of Neuroscience, vol. 5 ( S. Ehrenpreis and I.J. Kopin, eds.) Raven Press, New York (1974) pp. 283 - 343.Google Scholar
  44. 44.
    Rauch, H. C., Einstein, E. R. and Csejtey, J., Enzymatic degradation of myelin basic protein in central nervous system lesions of monkeys with experimental allergic encephalomyelitis, Neuro-biology 3 (1973) 195 - 205.Google Scholar
  45. 45.
    Ruchel, R., Mesecke et al., Microelectrophoresis in continuous polyacrylamide gradient gels, Hoppe-Seyler’s Z. Physiol. Chem. 355 (1974) 997 - 1020.CrossRefGoogle Scholar
  46. 46.
    Sammeck, R. and Brady, R. O., Studies of the catabolism of myelin basic proteins of the rat in situ and in vitro, Brain Res. 42 (1972) 441 - 453.PubMedCrossRefGoogle Scholar
  47. 47.
    Shiraki, H. and Otani, S., Clinical and pathologic features of rabies postvaccinal encephalomyelitis in man, in Allergic Encephalomyelitis ( M.W. Kies and E.C. Alvord, eds.) C. Thomas, Springfield, Ill. (1965).Google Scholar
  48. 48.
    Smith, M. E. and Rauch, H. C., Metabolic activity of CNS proteins in rats and monkeys with experimental allergic encephalomyelitis, J. Neurochem. 23 (1974) 775 - 785.PubMedCrossRefGoogle Scholar
  49. 49.
    Smith, M. E., Sedgewick, M. and Tagg, J. S., Proteolytic enzymes and experimental demyelination in the rat and the monkey, J. Neurochem. 23 (1974) 465 - 471.CrossRefGoogle Scholar
  50. 50.
    Stibler, H., Crossed immunoelectrofocusing for identification of normal and abnormal CSF proteins, J. Neurol. Sci. 32 (1977) 331 - 336.PubMedCrossRefGoogle Scholar
  51. 51.
    Svet-Moldayskaja, I. A. and Svet-Moldayskij, G. J., Acquired resistance to experimental allergic encephalomyelitis, Nature 181 (1958) 1536 - 1537.CrossRefGoogle Scholar
  52. 52.
    Svet-Moldayskij, G. J., Andjaparidze, O. G., Unanov, S. S. et al. Allerginfree antirabies vaccine, Bull. W1d. Hlth. Org. 32 (1965) 47 - 57.Google Scholar
  53. 53.
    Swanborg, R. H., Antigen-induced inhibition of experimental allergic encephalomyelitis. I. Inhibition in guinea pigs in jected with non-encephalitogenic modified myelin basic protein, J. Immunol. 109 (1972) 540.PubMedGoogle Scholar
  54. 54.
    Swanborg, R. H., Antigen-induced inhibition of experimental allergic encephalomyelitis. Localization of an inhibitory site distinct from major encephalitogenic determinant of myelin basic protein, J. Immunol. 114 (1975) 191 - 194.PubMedGoogle Scholar
  55. 55.
    Swanborg, R. H., Maintenance of immunologic self tolerance by nonimmunogenic forms of antigen, Clin. Exp. Immunol. 26 (1976) 597 - 600.Google Scholar
  56. 56.
    Takuomi, H., Shoichkiro, K. et al., Changes of cerebrospinal fluid protein during course of demyelinating disease, Annual Report of the Ministry of Health and Welfare, Demyelinating Disease Research Committee, Japan 1976, p. 71.Google Scholar
  57. 57.
    Terletskaya, Ja., Belik, Ja. V., Kozulina, E. P. et al., Effectiveness of experimental allergic encephalomyelitis treatment in guinea pigs with myelin basic protein and encephali togenic synthetic peptide, Papers of the Ukrainian Academy of Sciences, Series "B" Geology, Geophysics, Chemistry and Biology, No. 10, Kiev, 1976.Google Scholar
  58. 58.
    Tourtellotte, W. W., On cerebrospinal immunoglobulin (IgG) quotients in MS and other diseases. A review and a new formula to estimate the amount of IgG synthesized per day by the CNS, J. Neurol. Sci. 10 (1970) 279 - 304.PubMedCrossRefGoogle Scholar
  59. 59.
    Umana, C. R., Protein degradation at neutral pH. Possible enzymic and control mechanisms. Proc. Soc. Exp. Biol. Med. 138 (1971) 31 - 38.PubMedGoogle Scholar
  60. 60.
    Unkeless, J. C., Gordon, S. and Reich, E., Secretion of plas minogen activator by stimulated macrophages, J. Exp. Med. 139 (1974) 834 - 850.PubMedCrossRefGoogle Scholar
  61. 61.
    Vesterberg, O., Isoelectric focusing of protein, in Methods in Enzymology, vol. 22 (J. Jacoby, ed.) Academic Press, New York (1971) pp. 389-412.Google Scholar
  62. 62.
    Vesterberg, O. and Svensson, H., Isoelectric fractionation, analysis and characterization of ampholyte in natural pH gradient, Acta Chem. Scand. 20 (1966) 820 - 834.CrossRefGoogle Scholar
  63. 63.
    Vinogradow, S. N., Lowenkron, S., Andonian, M. R. et al., Synthetic ampholytes for isoelectric focusing of proteins, Biochem. Biophys. Res. Commun. 54 (1973) 501 - 506.CrossRefGoogle Scholar
  64. 64.
    Westall, F. C., Robinson, A. B., Caccam, J., Jackson, J. and Eylar, E. H., Essentail chemical requirement for induction of allergic encephalomyelitis, Nature 229 (1971) 22 - 24.PubMedCrossRefGoogle Scholar
  65. 65.
    Westall, F. C. and Thompson, M., Encephalitogenic regions for the Lewis rat within the myelin basic protein, Immun. Commun. (1977) 13 - 21.Google Scholar
  66. 66.
    Westall, F. C. and Thompson, M., Further definition of the en cephalitogenic region for guinea pigs, Immun. Commun. 6 (1977) 23 - 31.Google Scholar
  67. 67.
    Whitaker, J., Myelin encephalitogenic protein fragments in cerebrospinal fluid of persons with multiple sclerosis, Neurology 27 (1977) 911 - 920.PubMedCrossRefGoogle Scholar
  68. 68.
    Wiener, E. and Curelaru, Z., The intracellular distribution of cathepsins and other acid hydrolases in mouse peritoneal macrophages, J. Reticuloendothel. Soc. 17 (1975) 319.PubMedGoogle Scholar
  69. 69.
    Woelk, H., Kanig, K. and Peiler-Ichikawa, Phospholipid metab olism in experimental allergic encephalomyelitis, J. Neurochem. 23 (1974) 745 - 750.Google Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Elizabeth Roboz Einstein
    • 1
  1. 1.Department of Physiology, Institute of Human DevelopmentUniversity of CaliforniaBerkeleyUSA

Personalised recommendations