Abstract
Niemann-Pick disease (NPD) is the name given to a group of genetic disorders in which the common feature is a varying degree of sphingomyelin storage in certain tissues. The wide range of clinical heterogeneity led Crocker to suggest in 1961 a classification into four types, A to D, which is still widely used. Schematically, type A refers to cases similar to the original description of Albert Niemann, i.e. an infantile severe neurovisceral form. Patients presenting with a heavy visceral involvement but no neurological symptoms are assigned to type B. In those two types, a severe and generalized deficiency of sphingomyelinase activity has been desmonstrated (for review, see Brady, 1983). There is more confusion for classification of a third group of patients with neurovisceral involvement but a protracted neurological onset, originally subdivided by Crocker into types C and D, and also described in the litterature under other names, among which juvenile NPD, juvenile dystonic lipidosis, neurovisceral disease with vertical supranuclear ophtalmoplegia. In this group, the nature of the primary biochemical lesion remains unknown. None of the postulated defects, lack of a specific sphingomyelinase isoenzyme (Callahan et al., 1974) or of an activator (Christomanou, 1980) has to-date received general acceptance, and it is not even clear at present if such patients belong to a single nosological entity or not. For the sake of simplification, the name NPD type C will be used throughout the present report for designation of the group as a whole.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Albouz, S., Hauw, J.J., Berwald-Netter, Y., Boutry, J.M., Bourdon, R.,and Baumann, N., 1981, Tricyclic antidepressants induce sphingomyelinase deficiency in fibroblasts and neuroblastoma cell cultures, Biomedicine, 35: 218–220.
Basu, A. and Glew, R.H., 1984, Characterization of the phospholipid re- quirement of a rat liver β-glucosidase, Biochem.J., 224: 515–524.
Beaudet, A.L. and Manschrek, A.A., 1982, Metabolism of sphingomyelin by intact cultured fibroblasts. Differentiation of Niemann-Pick disease type A and B, Biochem.Biophys.Res.Commun., 105: 1419.
Berent, S.L. and Radin, N.S., 1981, β-Glucosidase activator protein from bovine spleen (coglucosidase), Arch.Biochem.Biophys., 208: 248–260.
Besley, G.T.N., Hoogeboom, A.J.M., Hoogeven, A., Kleijer, W.J. and Galjaard, H., 1980, Somatic cell hybridization studies showing different gene mutations in Niemann-Pick disease variants, Hum.Genet., 54: 409–412.
Brady, R.O., 1983, Sphingomyelin lipidoses: Niemann-Pick disease. In “The Metabolic Basis of Inherited Disease,” J.B. Stanbury, J.B. Wyngaarden, D.S. Fredrickson, J.L. Goldstein, M.S. Brown, eds., Mc Graw Hill, New York, pp. 831–841.
Callahan, J.W., Khalil, M., Gerrie, J., 1974, Isoenzymes of sphingomyelinase and the genetic defect in Niemann-Pick disease, Biochem.Biophys.Res.Commun., 58: 384–390.
Christomanou, H., 1980, Niemann-Pick disease type C: evidence for the deficiency of an activating factor stimulating sphingomyelin and glucocerebroside, Hoppe Seyler’s Z.phys.Chem., 361: 1489–1502.
Christomanou, H. and Kleinschmidt, T., 1985, Isolation of two forms of an activator protein for the enzymic sphingomyelin degradation from human Gaucher spleen, Biol.Chem.Hoppe-Seyler, 346: 245–256.
Dale, G.L., Villacorte, D.G. and Beutler, E., 1976, Solubilization of glucocerebrosidase from human placenta and demonstration of a phospholipid requirement for its catalytic activity, Biochem.Biophys.Res. Commun., 71: 1048–1053.
Fujibayashi, S. and Wenger, D.A., 1985, Studies on a sphingolipid activator protein (SAP-2) in fibroblasts from patients with lysosomal storage diseases, including Niemann-Pick disease type C, Clin.Chim.Acta, 146: 147–156.
Gatt, S., Herzl, A. and Barenholz, Y., 1973, Hydrolysis of sphingomyelin liposomes by sphingomyelinase, Febs Lett., 30: 281–285.
Hanada, E. and Suzuki, K., 1979, Activation of human brain galactosylceramidase by phosphatidylserine, Biochim.Biophys.Acta, 575: 410–420.
Ho, M.W. and Light, M, 1973, Glucocerebrosidase: reconstitution from macromolecular components depends on acidic phospholipids, Biochem.J., 136: 821–823.
Kudoh, T., Velkoff, M. and Wenger, D.A., 1983, Uptake and metabolism of radioactively labelled sphingomyelin in cultured skin fibroblasts from controls and patients with Niemann-Pick disease and other lysosomal diseases, Biochim.Biophys.Acta, 754: 82–92.
Pentchev, P.G., Gal, A.E., Boothe, A.D., Omodeo-Sale, F., Fouks, J., Neumeyer, B.A., Quirk, J.M., Dawson,G. and Brady, R.O., 1980, A lysosomal storage disorder in mice characterized by a dual deficiency of sphingomyelinase and glucocerebrosidase, Biochim.Biophys.Acta, 619: 669–679.
Pentchev, P.G., Boothe, A.D., Kruth, H.S., Weintroub, H., Stivers, J. and Brady, R.O., 1984, A genetic storage disorder in BALB/C mice with a metabolic block in esterification of exogeneous cholesterol, J.Biol.Chem., 259: 5784–5791.
Pentchev, P.G., Comly, M.E., Kruth, H.S., Vanier, M.T., Wenger, D.A., Patel, S. and Brady, R.O., 1985, A defect in cholesterol esterification in certain patients designated as Niemann-Pick disease type C. Proc. Nat.Acad.Sci.USA, in press.
Peters, S.P., Coyle, P., Coffee, C.J., Glew, R.H., Kuhlenschmidt, M.S., Rosenfeld, L. and Lee, Y.C., 1976, Purification and properties of a heat-stable glucocerebrosidase activating factor from control and Gaucher spleen. J.Biol.Chem., 252: 563–573.
Poulos, A., Shankaran, P., Jones, C.S. and Callahan, J.W., 1983, Enzymatic hydrolysis of sphingomyelin liposomes by normal tissues and tissues from patients with Niemann-Pick disease, Biochim.Biophys.Acta, 751: 428.
Poulos, A., Ranieri, E., Shankaran, P. and Callahan, J.W., 1984a, Studies on the activation of the enzymatic hydrolysis of sphingomyelin liposomes, Biochim.Biophys.Acta, 793: 141–148.
Poulos, A., Ranieri, E., Shankaran, P. and Callahan, J.W., 1984b, Studies on the activation of sphingomyelinase activity in Niemann-Pick type A, B and C fibroblasts. Enzymological differentiation of type A and B, Ped.Res., 18: 1088–1093.
Rousson, R., Vanier, M.T. and Louisot, P., 1983, Chromatofocusing of purified placental sphingomyelinase, Biochimie, 65: 115–120.
Vanier, M.T., 1983, Biochemical studies in Niemann-Pick disease.I-Major sphingolipids of liver and spleen, Biochim.Biophys.Acta, 750: 178. 184
Vanier, M.T. and Rousson, R., 1984, Niemann-Pick disease:a clinical and biochemical study, In “Recent Progress in Neurolipidoses and Allied Disorders,” M.T.Vanier, ed., Fondation Mérieux, Lyon, pp. 183–201.
Vanier, M.T., Revol, A. and Fichet, M., 1980, Sphingomyelinase activities of various human tissues in control subjects and in Niemann-Pick disease, Clin.Chim.Acta, 106: 257–267.
Vanier, M.T., Rousson, R., Garcia, I., Bailloud, G., Juge, M.C., Revol, A. and Louisot, P., 1985, Biochemical studies in Niemann-Pick disease.III-In vitro and in vivo assays of sphingomyelin degradation in cultured skin fibroblasts and amniotic fluid cells for the diagnosis of the various forms of the disease, Clin.Genet., 27: 20–32.
Wenger, D.A., Sattler, M. and Roth, S., 1982, A protein activator of galactosylceramide β-galactosidase, Biochim.Biophys.Acta, 712: 639–649.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1986 Plenum Press, New York
About this chapter
Cite this chapter
Vanier, M.T., Rousson, R., Zeitouni, R., Pentchev, P.G., Louisot, P. (1986). Sphingomyelinase and Niemann-Pick Disease. In: Freysz, L., Dreyfus, H., Massarelli, R., Gatt, S. (eds) Enzymes of Lipid Metabolism II. NATO ASI Series, vol 116. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5212-9_94
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5212-9_94
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5214-3
Online ISBN: 978-1-4684-5212-9
eBook Packages: Springer Book Archive