Sandhoff’s Disease: Studies on the Enzyme Defect in Homozygotes and Detection of Heterozygotes

  • Edwin H. Kolodny
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 19)


Three varieties of GM2-gangliosidosis have been described. These can be distinguished by: their clinical presentation; the nature of lipid storage; and the nature of the enzyme deficiency. In Tay-Sachs disease, the most common form of GM2 -gangliosidosis, GM2 ganglioside accumulates within the nervous system and there is a deficiency of hexosaminidase A (1,2). In the United States, most of the children afflicted with this disease have been of Jewish parentage. A much rarer type of GM2-gangliosidosis known as Juvenile GM2-gangliosidosis (3,4,5) has in common with Tay-Sachs disease central nervous system accumulation of GM2 ganglioside and deficiency of hexosaminidase A. However, these biochemical abnormalities are less severe than in Tay-Sachs disease.


Enzyme Defect Metachromatic Leukodystrophy Sandhoff Disease Neutral Glycolipid Cellulose Acetate Electrophoresis 


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  1. 1.
    Okada, S. and O’Brien, J. Science 165, 698 (1969).PubMedCrossRefGoogle Scholar
  2. 2.
    Sandhoff, K. FEBS Letters 4, 351 (1969).PubMedCrossRefGoogle Scholar
  3. 3.
    Volk, B. W., Adachi, M., Schneck, L., Saifer, A. and Kleinberg, W. Arch. Path. 87, 393 (1969).PubMedGoogle Scholar
  4. 4.
    Suzuki, K., Suzuki, K., Rapin, I., Suzuki, Y., and Ishii, N. Neurology 20, 190 (1970).PubMedCrossRefGoogle Scholar
  5. 5.
    Menkes, J. H., O’Brien, J. S., Okada, S., Grippo, J., Andrews, J. M., and Cancilla, P. A. Arch. Neurol. 25, 14 (1971).PubMedCrossRefGoogle Scholar
  6. 6.
    Sandhoff, K., Andreae, U., and Jatzkewitz, H. Life Sciences I 283 (1968).CrossRefGoogle Scholar
  7. 7.
    Pilz, H., Muller, D., Sandhoff, K. and ter Meulen, V. Deutsch. Med. Wochschr. 39, 1833 (1968).Google Scholar
  8. 8.
    Suzuki, Y., Jacob, J. C., Suzuki, K., Kutty, K. M. and Suzuki, K. Neurology 21, 313 (1971).PubMedCrossRefGoogle Scholar
  9. 9.
    Strecker, G. and Montrevil, J. Clin. Chem. Acta 33, 395 (1971)CrossRefGoogle Scholar
  10. 10.
    O’Brien, J. S. Lancet ii, 805 (1969).Google Scholar
  11. 11.
    Raine, D. N. Lancet ii, 959 (1969).Google Scholar
  12. 12.
    Okada, S., Veath, M. L., Leroy, J. and O’Brien, J. S. Am. J. Hum. Genet. 23, 55 (1971).Google Scholar
  13. 13.
    Desnick, R. J., Sharp, H. L. and Krivit, W. Abs. Intl Cong. Human Genetics. p. 57 (1971).Google Scholar
  14. 14.
    Tateson, R. and Bain, A. D. Lancet ii, 612 (1971).Google Scholar
  15. 15.
    Folch, J. Lees, M. and Sloane Stanley, G. H. J. Biol. Chem. 226, 497 (1957).Google Scholar
  16. 16.
    Lees, M. Unpublished.Google Scholar
  17. 17.
    Lowry, 0. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. J. Biol. Chem. 193, 265 (1951).Google Scholar
  18. 18.
    Vance, D. E. and Sweeley, C. C. J. Lipid Res. 8, 621 (1967).PubMedGoogle Scholar
  19. 19.
    Franey, R. and Amador, E. Clin. Chem. Acta 21, 255 (1968).CrossRefGoogle Scholar
  20. 20.
    Bartlett, G. R. J. Biol. Chem. 234, 466 (1959).Google Scholar
  21. 21.
    Hakomori, S. and Strycharz, G. D. Biochemistry 7, 1279 (1968).CrossRefGoogle Scholar
  22. 22.
    Nomenclature is that of Svennerhilm, L. J. Neurochem. 10, 613 (1963).CrossRefGoogle Scholar
  23. 23.
    Kolodny, E. H., Kanfer, J., Quirk, J. M., and Brady, R. O. J. Biol. Chem. 246, 1426 (1971).Google Scholar
  24. 24.
    Kanfer, J. N., in J. Lowenstein (editor), Methods in Enzymol-ogy, Vol. 14, Academic Press, New York, p. 660 (1969).Google Scholar
  25. 25.
    Penick, R. J., Meisler, M. H., and McCluer, R. H. Biochim. Biophys. Acta 116, 279 (1966).CrossRefGoogle Scholar
  26. 26.
    Folch, J. and Greaney, J. Unpublished.Google Scholar
  27. 27.
    Aminoff, D. Biochem. J. 81, 384 (1961).PubMedGoogle Scholar
  28. 28.
    Young, E., Ellis, E., Lake, B. and Patrick, A. FEBS Letters 9, 1 (1970).CrossRefGoogle Scholar
  29. 29.
    Kolodny, E. H., Brady, R. 0. and Volk, B. W. Biochem. Biophys. Res. Comm. 37, 526 (1969).Google Scholar
  30. 30.
    Morgan, W. T. J. and Elson, L. A. Biochem. J. 28, 988 (1934).PubMedGoogle Scholar
  31. 31.
    O’Brien, J. S., Okada, S., Chen, A. and Fillerup, D. New Engl. J. Med. 283, 15 (1970).Google Scholar
  32. 32.
    Kampine, J. P., Brady, R. O., Kanfer, J. N., Feld, M., and Shapiro, D. Science 155, 86 (1967).PubMedCrossRefGoogle Scholar
  33. 33.
    Turban. Thesis. Freiburg (1944).Google Scholar
  34. 34.
    Norman, R. M., Urich, H., Tingey, A. H. and Goodbody, R. A. J. Path. Bac. 78, 409 (1959).CrossRefGoogle Scholar
  35. 35.
    Sandhoff, K. FEBS Letters 11, 342 (1970).PubMedCrossRefGoogle Scholar
  36. 36.
    Kolodny, E. H. Unpublished.Google Scholar
  37. 37.
    Stumpf, D. and Austin, J. Arch. Neurol. 24, 117 (1971).PubMedCrossRefGoogle Scholar
  38. 38.
    Pinsky, L., Powell, E. and Callahan, J. Nature 228, 1093 (1970).PubMedCrossRefGoogle Scholar
  39. 39.
    Robinson, D. and Stirling, J. L. Biochem. J. 107, 321 (1965).Google Scholar
  40. 40.
    Ho, M. W., and O’Brien, J. S. Science 165, 611 (1969).Google Scholar
  41. 41.
    Murphy, J. V., Wolfe, H. J., Balazs, E. A., and Moser, H. W., in J. Bernsohn and H. Grossman (Editors), Lipid Storage Diseases, Academic Press, New York, p. 67 (1971).Google Scholar
  42. 42.
    Kolodny, E. H., Jacobson, C. and Uhlendorf, W. Unpublished.Google Scholar

Copyright information

© Springer Science+Business Media New York 1972

Authors and Affiliations

  • Edwin H. Kolodny
    • 1
    • 2
  1. 1.Walter E. Fernald State SchoolEunice Kennedy Shriver Center for Mental Retardation, Inc.WalthamUSA
  2. 2.J.P. Kennedy Memorial LaboratoriesMassachusetts General HospitalBostonUSA

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