Sphingomyelinase of Human Tissues

  • Shuichi Yamaguchi
  • Kunihiko Suzuki
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 101)


Sphingomyelinase (sphingomyelin phosphodiesterase, E.C. 3.1.4. 12) catalyzes hydrolysis of sphingomyelin to ceramide and phosphorylcholine. A genetic deficiency of this enzyme characterizes at least two distinct clinical forms of Niemann-Pick disease (Crocker’s Type A and Type B (1)). Patients with the Type A disease exhibit severe neurological manifestations, while patients with the Type B disease are completely intact neurologically. The systemic accumulations of sphingomyelin are similar in the two types. The degree of the sphingomyelinase deficiency in the liver, spleen, leukocytes, or fibroblasts is similar in both of the clinical types and does not appear to explain the dramatic phenotypic difference (2). An alternative possibility would be that sphingomyelinase might be organ-specific in itself or in the distribution of isozymes and that different mutations can cause differential inactivation of the enzyme in different organs. In addition to the above sphingomyelinase with the acidic pH optimum, there is another enzyme which also hydrolyzes sphingomyelin but at neutral pH in the presence of magnesium ions (3–5). The relationship, if any, of this magnesium-dependent neutral sphingomyelinase to either the acidic sphingomyelinase or NiemannPick disease is not clear at the present time.


Magnesium Chloride Purification Factor Neutral Sphingomyelinase Sodium Chloride Gradient Sphingomyelin Phosphodiesterase 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Crocker, A. C. (1961), The cerebral defect in Tay-Sachs disease and Niemann-Pick disease. J. Neurochem. 7: 69–80.PubMedCrossRefGoogle Scholar
  2. 2.
    Fredrickson, D. S. and Sloan, H. R. (1972), Sphingomyelin lipidosis: Niemann-Pick disease, in The Metabolic Basis of Inherited Disease ( Stanbury, J. B., Wyngaarden, J. B. and Fredrickson, D. S., eds.), pp. 783–807, McGraw-Hill, New York.Google Scholar
  3. 3.
    Schneider, P. B. and Kennedy, E. P. (1967), Sphingomyelinase in normal human spleens and in spleen from subjects with NiemannPick disease. J. Lipid Res. 8: 202–209.PubMedGoogle Scholar
  4. 4.
    Rao, B. G. and Spence, M. W. (1976), Sphingomyelinase activity at pH 7.4 in human brain and a comparison to activity at pH 5.0. J. Lipid Res. 17: 506–514.PubMedGoogle Scholar
  5. 5.
    Gatt, S. (1976), Magnesium-dependent sphingomyelinase. Biochem. Biophys. Res. Commun. 68: 235–241.PubMedCrossRefGoogle Scholar
  6. 6.
    Barenholtz, Y., Roitman, A. and Gatt, S. (1966), Enzymatic hydrolysis of sphingolipids. II. Hydrolysis of sphingomyelin by an enzyme from rat brain. J. Biol. Chem. 241: 3731–3737.Google Scholar
  7. 7.
    Gatt, S. and Gottesdiner, T. (1976), Solubilization of sphingomyelinase by isotonic extraction of rat brain lysosomes, J. Neurochem. 26: 421–422.PubMedCrossRefGoogle Scholar
  8. 8.
    Kanfer, J. N., Young, O. M., Shapiro, D. and Brady, R. 0. (1966) The metabolism of sphingomyelin I. Purification and properties of a sphingomyelin-cleaving enzyme from rat liver tissue. J. Biol. Chem. 241: 1081–1084.Google Scholar
  9. 9.
    Heller, M. and Shapiro, B. (1966), Enzymatic hydrolysis of sphingomyelin by rat liver. Biochem. J. 98: 763–769.PubMedGoogle Scholar
  10. 10.
    Sloan, H. R. (1972), Sphingomyelinase from human liver (sphingomyelin choline-phosphodiesterase), in Methods in Enzymology,vol. 28B ( Ginsburg, V., ed.), pp. 874–879, Academic Press, New York.Google Scholar
  11. 11.
    Yamaguchi, S. and Suzuki, K. (1977), Purification and characterization of sphingomyelinase from human brain. J. Biol. Chem. 252: 3805–3813.PubMedGoogle Scholar
  12. 12.
    Yamaguchi, S. and Suzuki, K. (1977), Sphingomyelinase isozymes in human tissues: A hypothesis on enzymatic differentiation of the neuropathic and non-neuropathic forms of Niemann-Pick disease. Biochem. Biophys. Res. Commun., in press.Google Scholar
  13. 13.
    Lowry, 0. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. (1951), Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193: 265–275.PubMedGoogle Scholar
  14. 14.
    Bosmann, H. B. (1973), Synthesis of glycoproteins in brain: Identification, purification and properties of a synaptosomal sialyl transferase utilizing endogenous and exogenous acceptors. J. Neurochem. 20: 1037–1049.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Shuichi Yamaguchi
    • 1
    • 2
  • Kunihiko Suzuki
    • 2
    • 1
  1. 1.Department of NeuroscienceThe Saul R. Korey Department of NeurologyBronxUSA
  2. 2.Rose F. Kennedy Center for Research in Mental Retardation and Human DevelopmentAlbert Einstein College of MedicineBronxUSA

Personalised recommendations