Inborn Errors of Complex Carbohydrate Catabolism

  • Glyn Dawson
  • Larry W. Hancock

Abstract

Complex carbohydrates of the nervous system are degraded in lysosomes by the sequential action of a group of exoglycosidases known collectively as the lysosomal hydrolases. Inherited defects in the synthesis, assembly, or turnover of these hydrolases lead to storage diseases in humans (Spranger, 1987) and a variety of domestic animals. Those involving the nervous system result in spectacular neuropathology and provide the best evidence for the types of glycoconjugates synthesized by nervous tissue, as well as their rate of turnover. For example, in Tay—Sachs disease, storage material (GM2 ganglioside) predominates in nervous tissue, especially motor neurons, and is virtually absent from visceral tissue. The variable level of accumulation of GM2 in different brain regions (identified morphologically as multilamellar cytosomes) can be related to different levels of synthesis and degradation. This clearly manifests itself in patients with partial hexosaminidase (HexA) deficiencies, who exhibit symptoms of motor neuron disease, or spinocerebellar degeneration with other neuronal function (such as vision and intelligence) relatively intact. The absence of GM2 storage outside the CNS reflects the lack of GM2 synthesis in nonneural tissue. However, since lysosomal hydrolases are synthesized constitutively in all tissues, GM2 can be fed to fibroblasts from HexA-deficient patients, and its steady accumulation observed. Thus, storage patterns in patients with inherited enzyme defects can be used to give an accurate reflection of glycoconjugate content of the CNS versus nonneural tissue and this will be emphasized on an enzyme/disease, case-by-case basis.

Keywords

Heparan Sulfate Fabry Disease Storage Disease Inborn Error Neuronal Ceroid Lipofuscinosis 
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. Akasaki, M., Sugahara, K., Funakoshi, I., Aula, P., and Yamashina, I., 1976, Characterization of a mannose-containing glycoasparagine isolated from urine of a patient with aspartylglycosaminuria, FEBS Leu. 69: 191.CrossRefGoogle Scholar
  2. Autio, S., 1972, Aspartylglucosaminuria: Analysis of thirty-four patients, J. Ment. Def. Res. Monogr. Ser. 1: 1–93.Google Scholar
  3. Bach, G., Friedman, R., Weismann, B., and Neufeld, E. F., 1972, The defect in the Hurler and Scheie syndrome: Deficiency of a-L-iduronidase, Proc. Natl. Acad. Sci. USA 69: 2048–2051.PubMedCrossRefGoogle Scholar
  4. Bach, G., Eisenberg, F., Cantz, M., and Neufeld, E. F., 1973, The defect in Hunter’s disease: Deficiency of sulfoiduronate sulfatase, Proc. Natl. Acad. Sci. USA 70: 2134–2138.PubMedCrossRefGoogle Scholar
  5. Baum, K. J., and Rome, L. H., 1986, Genetic evidence for transmembrane acetylation by lysosomes, Science 233: 1087–1089.CrossRefGoogle Scholar
  6. Baumkotter, J., Cantz, M., Mendla, K., Baumann, W., Friebolin, H., Gehler, J., and Spranger, J., 1985, N-acetylneuraminic acid storage disease, Hum. Genet. 71: 155–159.PubMedCrossRefGoogle Scholar
  7. Beck, M., Bender, S. W., Reiter, H. L., Otto, W., Bassler, R., Dancygier, H., and Gehler, J., 1984, Neuraminidase deficiency presenting as non-immune hydrops, Eur. J. Pediat. 143: 135–139.CrossRefGoogle Scholar
  8. Bell, C. E., Jr., Sly, W. S., and Brot, F. E., 1977, Human p-glucuronidase deficiency mucopolysac-charidosis, J. Clin. Invest. 598: 97–105.CrossRefGoogle Scholar
  9. Ben-Yoseph, Y., Pack, B. A., Mitchell, D. A., Elwell, D. G., Potior, M., Melancon, S. B., and Nadler, H. L., 1986, Characterization of the mutant N-acetylglucosaminyl-phosphotransferase in I-cell disease and pseudohurler polydystrophy: Complementation analysis and kinetic studies, Enzymology 35: 106–116.Google Scholar
  10. Bolhuis, P. A., Oonk, J. G. W., Kamp, P. E., Ris, A. J., Michalski, J. C., Overdijk, B., and Reuser, A. J. J., 1987, Ganglioside storage, hexosaminidase lability and urinary oligosaccharides in adult Sandhoff’s disease, Neurology 37: 75–81.PubMedCrossRefGoogle Scholar
  11. Borrone, C., Gatti, R., Trias, X., and Durand, P., 1974, Fucosidosis: Clinical, biochemical, immunologic and genetic studies in two new cases, J. Pediatr. 84: 727–730.PubMedCrossRefGoogle Scholar
  12. Cantz, M., Gehler, J., and Spranger, J., 1977, Mucolipidosis I: Increased sialic acid content and deficiency of an a-N-acetylneuraminidase in cultured fibroblasts, Biochem. Biophys. Res. Commun. 74: 732–738.PubMedCrossRefGoogle Scholar
  13. Carroll, M., Dance, N., Masson, P. K., Robinson, D., and Winchester, B. G., 1972, Human mannosidosis—The enzymic defect, Biochem. Biophys. Res. Commun. 49: 579–583.PubMedCrossRefGoogle Scholar
  14. Cashman, N. R., Antel, J. P., Hancock, L. W., Dawson, G., Horwitz, A. L., Johnson, W. G., Huttenlocher, P. R., and Wolhnan, R. L., 1986, N-acetyl- 3-hexosaminidase 13-locus defect and juvenile motor neuron disease: A case study, Ann. Neurol. 19: 568–572.PubMedCrossRefGoogle Scholar
  15. Chen, W. W., Moser, A. B., and Moser, H. W., 1981, Role of lysosomal acid ceramidase in the metabolism of ceramide in human fibroblasts, Arch. Biochem. Biophys. 208: 444–455.PubMedCrossRefGoogle Scholar
  16. Christomanou, H., and Beyer, D., 1983, Absence of alpha fucosidase activity in two sisters showing a different phenotype, Eur. J. Pediatr. 140: 27–29.PubMedCrossRefGoogle Scholar
  17. Conary, J. P., Lorkowski, G., Schmidt, B., Pohlmann, R., Nagel, G., Meyer, H. E., Krentler, C., Cully, J., Hasilik, A., and von Figura, K., 1987, Genetic heterogeneity of steroid sulfatase deficiency revealed with cDNA for human steroid sulfatase, Biochem. Biophys. Res. Commun. 144: 1010–1017.PubMedCrossRefGoogle Scholar
  18. Cooper, A., Sardharwalla, I. B., and Roberts, M. M., 1986, Human ß-mannosidosis, N . Engl. J. Med. 315: 1231.PubMedCrossRefGoogle Scholar
  19. Crandall, B. F., Philippart, M., Brown, W. J., and Bluestone, D. A., 1982, Mucolipidosis IV, Am. J. Med. Genet. 12: 301–308.PubMedCrossRefGoogle Scholar
  20. Dawson, G., 1982, Evidence for two distinct forms of mammalian ß-mannosidase, J . Biol. Chem. 257: 3369–3371.PubMedGoogle Scholar
  21. Dawson, G., and Glaser, P., 1987, Abnormal cathepsin B deficiency in neuronal ceroid lipofuscinosis can be explained by peroxide inhibition, Biochem. Biophys. Res. Commun. 147: 267–274.PubMedCrossRefGoogle Scholar
  22. Dawson, G., Matalon, R., and Dorfman, A., 1972, Glycosphingolipids in cultured human skin fibroblasts from patients with inborn errors of glycosphingolipid and mucopolysaccharide metabolism, J. Biol. Chem. 247: 5951–5958.PubMedGoogle Scholar
  23. Dawson, G., McCabe, N., Hancock, L. W., and Johnson, K., 1988, Molecular biology of oligosaccharide storage disease, Trans. Am. Soc. Neurochem. 19: 296.Google Scholar
  24. Dekaban, A. S., and Patton, V. M., 1971, Hurler’s and Sanfilippo’s variants of mucopolysaccharidosis; cerebral pathology and lipid chemistry, Arch. Pathol. 91: 434–449.PubMedGoogle Scholar
  25. Dewji, N. N., Wenger, D. A., and O’Brien, J. S., 1987, Nucleotide sequence of cloned cDNA for human sphingolipid activator protein 1 precursor, Proc. Natl. Acad. Sci. USA 84: 8652–8656.PubMedCrossRefGoogle Scholar
  26. Dorfman, A., and Matalon, R., 1972, The mucopolysaccharidoses, in: The Metabolic Basis of Inherited Disease ( J. B. Stanbury, J. B. Wyngaarden, and D. S. Fredrickson, eds.), pp. 1218–1272, McGraw-Hill, New York.Google Scholar
  27. Dorfman, A., Matalon, R., Cifonelli, J. A., Thompson, J., and Dawson, G., 1972, The degradation of acid mucopolysaccharides and the mucopolysaccharidoses, in: Sphingolipidoses and Allied Disorders ( B. W. Volk and S. M. Aronson, eds.), pp. 195–210, Plenum Press, New York.CrossRefGoogle Scholar
  28. Durand, P., Borrone, C., and Della Cella, G., 1969, Fucosidosis, J. Pediatr. 75: 665–674.CrossRefGoogle Scholar
  29. Durand, P., Gatti, R., Cavalieri, S., Borrone, C., Tondeur, M., Michalski, J.-C., and Strecker, G., 1977, Sialidosis (mucolipidoses I), Heiv. Paediatr. Acta 32: 391–400.Google Scholar
  30. Eto, Y., Tahara, T., Tokoro, T., and Maekawa, K., 1983, Various sulfatase activities in leukocytes and cultured skin fibroblasts from heterozygotes for the multiple sulfatase deficiency (mucosulfatidosis), Pediatr. Res. 17: 97–100.PubMedCrossRefGoogle Scholar
  31. Fois, A., Balestri, P., Farnetani, G. M. S., Mancini, P., Borgogni, M. A., Margollicci, M. A., Molinelli, M., Alessandrini, C., and Gerli, R., 1987, Free sialic acid storage disease: A new Italian case, Eur. J. Pediatr. 146: 195–198.PubMedCrossRefGoogle Scholar
  32. Fontaine, G., Biserte, G., Montreuil, J., DuPont, A., and Farriaux, J. P., 1968, La sialurie: un trouble metabolique original, HeIv. Paediatr. Acta 23 (Suppl. XVII): 3–32.Google Scholar
  33. Galjaard, H., Hoogeveen, A., Keijzer, W., DeWit-Verbeek, H. A., Reusor, A. J. J., Ho, M. W., and Robinson, D., 1975, Genetic heterogeneity in GMr-gangliosidosis, Nature 257: 60–62.PubMedCrossRefGoogle Scholar
  34. Gatti, R., Borrone, C., Durand, P., DeVirtilis, S., Sanna, G., Cao, A., von Figura, K., Kresse, H., and Paschke, E., 1982, Sanfilippo Type D disease, Eur. J. Pediatr. 138: 168–171.PubMedCrossRefGoogle Scholar
  35. Gilbert, E. F., Dawson, G., zu Rhein, G. M., Opitz, J. M., and Spranger, J. W., 1973, I-cell disease: Mucolipidosis II, Z. Kinderheilkd. 114: 259–292.PubMedCrossRefGoogle Scholar
  36. Gilles, F. H., and Deuel, R. K., 1971, Neuronal cytoplasmic globules in the brain in Morquio’s syndrome, Arch. Neurol. 25: 393–403.PubMedCrossRefGoogle Scholar
  37. Gonzalex-Noreiga, A., Grubb, J. H., Talkud, V., and Sly, W. S., 1980, Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling, J. Cell Biol. 85: 839–852.CrossRefGoogle Scholar
  38. Graves, P. N., Grabowski, G. A., Ludman, M. D., Palese, P., and Smith, F. I., 1986, Human acid ßglucosidase: Northern blot and SI nuclease analysis of mRNA from HeLa cells and normal and Gaucher disease fibroblasts, Am. J. Hum. Genet. 39: 763–774.PubMedGoogle Scholar
  39. Hall, C. W., Cantz, M., and Neufeld, E. F., 1973, A ß-glucuronidase deficiency mucopolysaccharidosis: Studies in cultured fibroblasts, Arch. Biochem. Biophys. 155: 32–38.PubMedCrossRefGoogle Scholar
  40. Hall, C. W., Liebaers, I., DiNatale, P., and Neufeld, E. F., 1978, Enzymatic diagnosis of the genetic mucopolysaccharide storage diseases, Methods Enzymol. 50: 439–455.PubMedCrossRefGoogle Scholar
  41. Hancock, L. W., 1987, Impaired processing of lysosomal enzymes in generalized N-acetylneuraminic acid storage disease, J. Cell Biol. 105: 249a.Google Scholar
  42. Hancock, L. W., Thaler, M. M., Horwitz, A. L., and Dawson, G., 1982, Generalized N-acetylneuraminic acid storage disease, J. Neurochem. 38: 803–809.PubMedCrossRefGoogle Scholar
  43. Hancock, L. W., Horwitz, A. L., and Dawson, G., 1983, N-acetylneuraminic acid and sialoglycoconjugate metabolism in cultured fibroblasts from a patient with generalized N-acetylneuraminic acid storage disease, Biochim. Biophys. Acta 760: 42–52.PubMedCrossRefGoogle Scholar
  44. Hancock, L. W., Horwitz, A. L., Cashman, N. R., Antel, J. P., and Dawson, G., 1985, N-acetyl-ßhexosaminidase B deficiency in cultured fibroblasts from a patient with progressive motor neuron disease, Biochem. Biophys. Res. Commun. 130: 1185–1192.PubMedCrossRefGoogle Scholar
  45. Hancock, L. W., Ricketts, J. P., and Hildreth, J., 1988, Impaired proteolytic processing of lysosomal Nacetyl-ß-hexosaminidase in cultured fibroblasts from patients with infantile generalized N-acetylneuraminic acid storage disease, Biochem. Biophys. Res. Commun. 152: 83–92.PubMedCrossRefGoogle Scholar
  46. Hannun, Y. A., and Bell, R. A., 1987, Lysoglycosphingolipids in lipid storage diseases, Science 235: 670–674.PubMedCrossRefGoogle Scholar
  47. Hasilik, A., and Neufeld, E. F., 1980, Biosynthesis of lysosomal enzymes in fibroblasts: Synthesis as precursors of higher molecular weights, J. Biol. Chem. 255: 4937–4945.PubMedGoogle Scholar
  48. Hasilik, A., Waheed, A., and von Figura, K., 1981, Lysosomal hydrolase synthesis and processing, Biochem. Biophys. Res. Commun. 98: 761–767.PubMedCrossRefGoogle Scholar
  49. Hildreth, J., Sachs, L., and Hancock, L. W., 1986, N-Acetylneuraminic acid accumulation in a buoyant lysosomal fraction of cultured fibroblasts from patients with infantile generalized N-acetylneuraminic acid storage disease, Biochem. Biophys. Res. Commun. 139: 838–844.PubMedCrossRefGoogle Scholar
  50. Hill, D. F., Bullock, P. N., Chiappelli, F., and Rome, L. H., 1985, Binding and internalization of lysosomal enzymes by primary cultures of rat glia, J. Neurosci. Res. 14: 35–47.PubMedCrossRefGoogle Scholar
  51. Horwitz, A. L., 1979, Genetic complementation studies of multiple sulfatase deficiency, Proc. Natl. Acad. Sci. USA 76: 6496–6498.PubMedCrossRefGoogle Scholar
  52. Horwitz, A. L., and Dorfman, A., 1978, The enzymic defect in Morquio’s disease: The specificities of Nacetylhexosamine sulfatases, Biochem. Biophys. Res. Commun. 80: 819–825.PubMedCrossRefGoogle Scholar
  53. Horwitz, A. L., Warshawsky, L., King, J., and Burns, G., 1986, Rapid degradation of steroid sulfatase in multiple sulfatase deficiency, Biochem. Biophys. Res. Commun. 135: 389–396.PubMedCrossRefGoogle Scholar
  54. Ivy, G. O., Schotter, F., Wenzel, J., Baudry, M., and Lynch, G., 1984, Inhibition of lysosomal enzymes produces a rapid and massive accumulation of lipofuscin-like dense bodies in the CNS, Science 226: 985–987.PubMedCrossRefGoogle Scholar
  55. Jenner, F. A., and Pollitt, R. J., 1967, Large quantities of 2-acetamido-1-(13-L-aspartamido)-1,2-dideoxyglucose in the urine of mentally retarded siblings, Biochem. J. 103: 48–49.Google Scholar
  56. Johnson, K., and Dawson, G., 1985, Molecular defect in processing alpha-fucosidase in fucosidosis, Biochem. Biophys. Res. Commun. 133: 90–97PubMedCrossRefGoogle Scholar
  57. Jolly, R. D., Winchester, B. G., Gehler, J., Dorling, P. R., and Dawson, G., 1981, Mannosidosis: A comparative review of biochemical and related clinicopathological aspects of three forms of the disease, J. Appl. Biochem. 3: 273–291.Google Scholar
  58. Jonas, A. J., 1986, Studies of lysosomal sialic acid metabolism: Retention of sialic acid by Salla disease lysosomes, Biochem. Biophys. Res. Commun. 137: 175–181.PubMedCrossRefGoogle Scholar
  59. Jones, M. Z., and Dawson, G., 1981, Caprine ß-mannosidosis: Inherited deficiency of 13-D-mannosidase, J. Biol. Chem. 256: 5185–5188.PubMedGoogle Scholar
  60. Jones, M. Z., and Laine, R. A., 1981, Caprine 3-mannosidosis: Identification of the trisaccharide storage material, J. Biol. Chem. 256: 5181–5184.PubMedGoogle Scholar
  61. Jones, M. Z., Cunningham, J. G., Dade, A. W., Dawson, G., Laine, R. A., Williams, C. S. F., Alessi, D. M., Mostoskey, U. V., and Votro, J. R., 1982, Caprine 3-annosidosis, in: Animal Models of Inherited Metabolic Diseases (R. F. Desnick, D. F. Patterson, and D. G. Scarpelli, eds.), pp. 165–176, Liss, New York.Google Scholar
  62. Kaplan, A., Fischer, D., Achord, D., and Sly, W., 1977, Phosphohexosyl recognition is a general characteristic of pinocytosis of lysosomal glycosidases by human fibroblasts, J. Clin. Invest. 60: 1088–1093.PubMedCrossRefGoogle Scholar
  63. Kelly, T. E., and Graetz, G., 1977, Isolated acid neuraminidase deficiency: A distinct lysosomal storage disease, Am. J. Med. Genet. 1: 31–46.PubMedCrossRefGoogle Scholar
  64. Kint, J. A., Dacrement, G., Carton, D., Orye, E., and Hooft, C., 1973, Mucopolysaccharidosis: Secondarily induced abnormal distribution of lysosomal isoenzymes, Science 181: 352–354.PubMedCrossRefGoogle Scholar
  65. Kolodny, E. H., and Raghavan, S. S., 1983, GM2-gangliosidosis—ß-hexosaminidase mutants, Trends Neurosci. 6: 16–20.CrossRefGoogle Scholar
  66. Kornfeld, S., 1987, Trafficking of lysosomal enzymes, FASEB J. 1: 462–468.PubMedGoogle Scholar
  67. Koster, J. F., Nieremeijer, M. F., Loonen, M. C. B., and Galjaard, H., 1976, ß-Galactosidase deficiency in an adult: A biochemical and somatic cell genetic study on a variant of GMl-gangliosidosis, Clin. Genet. 9: 427.PubMedCrossRefGoogle Scholar
  68. Koto, A., Horwitz, A. L., Suzuki, K., Tiffany, C. W., and Suzuki, K., 1978, The Morquio syndrome: Neuropathology and biochemistry, Ann. Neurol. 4: 26–36.PubMedCrossRefGoogle Scholar
  69. Kresse, H., Paschke, E., von Figura, K., Gilberg, W., and Fuchs, W., 1980, Biochemical defect in Sanfilippo D, Proc. Natl. Acad. Sci. USA 77: 6822–6826.PubMedCrossRefGoogle Scholar
  70. Laney, P. A., Rattazzi, M. C., and Shows, T. B., 1974, Human 3-D-N-acetylhexosaminidases A and B: Expression and linkage relationships in somatic cell hybrids, Proc. Natl. Acad. Sci. USA 71: 1569–1573.CrossRefGoogle Scholar
  71. Laver, J., Fried, K., Beer, S. I., Ianci, T. C., Heyman, E., and Bach, G., 1983, Infantile lethal neuraminidase deficiency (sialidosis), Clin. Genet. 23: 97–101.PubMedCrossRefGoogle Scholar
  72. Ledeen, R., Salsman, K., Gonatas, J., and Taghavy, A., 1965, Structure comparisons of the major monosialogangliosides from brains of normal humans, gargoylism and late infantile systemic lipidosis, Part 1, J. Neuropathol. Exp. Neurol. 24: 341–351.PubMedCrossRefGoogle Scholar
  73. Lemansky, P., Bishop, D. F., Desnick, R. J., Hasilik, A., and von Figura, K., 1987, Synthesis and processing of a-galactosidase A in human fibroblasts: Evidence for different mutations in Fabry disease, J. Biol. Chem. 262: 2062–2065.PubMedGoogle Scholar
  74. Leroy, J. G., Ho, M. W., MacBrinn, M. C., Zielke, K., Jacob, J., and O’Brien, J. S., 1972, I-cell disease: Biochemical studies, Pediatr. Res. 6: 752–757.PubMedCrossRefGoogle Scholar
  75. Little, L. E., Mueller, Q. T., Honey, N. K., Shows, T. B., and Miller, A. L., 1986, Heterogeneity of Nacetyl-glucosamine-l-phosphotransferase within mucolipidosis III, J. Biol. Chem. 261: 733–738.PubMedGoogle Scholar
  76. Lowden, J. A., Callahan, J. W., Norman, M. G., Thain, M., and Pritchard, J. S., 1974, Juvenile GM! gangliosidosis, Arch. Neurol. 31: 20–24.CrossRefGoogle Scholar
  77. Mancini, G. M. S., Verheijen, F. W., and Galjaard, H., 1986, Free N-acetylneuraminic acid (NANA) storage disorders: Evidence for defective NANA transport across the lysosomal membrane, Hum. Genet. 73: 214–217.PubMedCrossRefGoogle Scholar
  78. Maroteaux, P., Humbel, R., Strecker, G., Michalski, J. C., and Mande, R., 1978, Un nouveau type de sialidose avec attiente renale: La nephrosialidose, Arch. Fr. Pediatr. 35: 819–829.PubMedGoogle Scholar
  79. Martiniuk, F., Mehler, M., Pellicer, A., Tzall, S., LaBadie, G., Hobart, C., Ellenbogen, A., and Hirschhorn, R., 1986, Isolation of a cDNA for human acid a-glucosidase and detection of genetic heterogeneity for mRNA in three a-glucosidase-deficient patients, Proc. Natl. Acad. Sci. USA 83: 9641–9644.PubMedCrossRefGoogle Scholar
  80. Matalon, R., and Dorfman, A., 1972, Hurler’s syndrome: An a-t-iduronidase deficiency, Biochem. Biophys. Res. Commun. 47: 959–966.PubMedCrossRefGoogle Scholar
  81. Matalon, R., and Dorfman, A., 1974, Sanfilippo A syndrome: Sulfamidase deficiency in cultured skin fibroblasts and liver, J. Clin. Invest. 54: 907–912.PubMedCrossRefGoogle Scholar
  82. Matalon, R., Cifonelli, J. A., Zellweger, H., and Dorfman, A., 1968, Lipid abnormalities in a variant of the Hurler syndrome, Proc. Natl. Acad. Sci. USA, 59: 1097–1102.PubMedCrossRefGoogle Scholar
  83. Matalon, R., Arbogast, B., Justice, P., Brandt, I. K., and Dorfman, A., 1974a, Morquio’s syndrome: Deficiency of a chondroitin sulfate N-acetyl-hexosamine sulfate sulfatase, Biochem. Biophys. Res. Commun. 61: 759.PubMedCrossRefGoogle Scholar
  84. Matalon, R., Arbogast, B., and Dorfman, A., 1974b, Deficiency of chondroitin sulfate N-acetyl-galactosamine-4-sulfate sulfatase in Maroteaux—Lamy syndrome, Biochem. Biophys. Res. Commun. 61: 1450–1457.PubMedCrossRefGoogle Scholar
  85. Moser, H. W., Prensky, A. L., Wolfe, H. J., and Rosman, N. P., 1969, Farber’s lipogranulomatosis: Report of a case and demonstration of an excess of free ceramide and ganglioside, Am. J. Med. 47: 869–890.PubMedCrossRefGoogle Scholar
  86. Myerowitz, R., and Hogikyan, N. D., 1986, Different mutations in Ashkenazi Jewish and non-Jewish French Canadians with Tay–Sachs disease, Science 232: 1646–1648.PubMedCrossRefGoogle Scholar
  87. Myerowitz, R., and Proia, R. L., 1984, A cDNA clone for the a-chain of human ß-hexosaminidase; deficiency of the a-chain in mRNA in Ashkenazi Tay–Sachs fibroblasts, Proc. Natl. Acad. Sci. USA 81: 5396–5398.CrossRefGoogle Scholar
  88. Nakagawa, F., Schulte, B. A., and Spicer, S. S., 1986, Selective cytochemical demonstration of glycoconjugate containing terminal N-acetylgalactosamine on some brain neurons, J. Comp. Neurol. 243: 280–290.PubMedCrossRefGoogle Scholar
  89. Navon, R., Argov, Z., and Frisch, A., 1986, Hexosaminidase A deficiency in adults, Am. J. Med. Genet. 24: 179–196.PubMedCrossRefGoogle Scholar
  90. Norden, N. E., Lundblad, A., Svensson, S., and Autio, S., 1974, Characterization of two mannosecontaining oligosaccharides isolated from the urine of patients with mannosidosis, Biochemistry 13: 871–874.PubMedCrossRefGoogle Scholar
  91. O’Brien, J. S., 1972a, Sanfilippo syndrome: Profound deficiency of alpha-acetylglucosaminidase activity in organs and skin from type B patients, Proc. Natl. Acad. Sci. USA 69: 1720–1722.PubMedCrossRefGoogle Scholar
  92. O’Brien, J. S., 1972b, Gag-gangliosidosis, in: The Metabolic Basis of Inherited Disease ( J. B. Stanbury, J. B. Wyngaarden, and D. S. Fredrickson, eds.), pp. 639–662, McGraw-Hill, New York.Google Scholar
  93. O’Brien, J. S., 1977, Neuraminidase deficiency in the cherry red spot-myoclonus syndrome, Biochem. Biophys. Res. Commun. 79: 1136–1141.PubMedCrossRefGoogle Scholar
  94. O’Brien, J. S., Willems, P. J., Fukushima, H., deWet, J. R., Darby, J. K., DiCioccio, R., Fowler, M. L., and Shows, T. B., 1987, Molecular biology of the alpha-L-fucosidase gene and fucosidosis, Enzyme 38: 45–53.PubMedGoogle Scholar
  95. O’Dowd, B., Quan, F., Willard, H. F., Lamhonwah, A. M., Komeluk, R. G., Lowden, J. A., Gravel, R. A., and Mahuran, D., 1985, Isolation of cDNA clones encoding the 3-hexosaminidase gene, Proc. Natl. Acad. Sci. USA 82: 1184–1188.PubMedCrossRefGoogle Scholar
  96. O’Dowd, B. F., Klavins, M. H., Willard, H. F., Gravel, R., Lowden, J. A., and Mahuran, D. J., 1986, Molecular heterogeneity in the infantile and juvenile forms of Sandhoff disease (O-variant GM2 gangliosidosis), J. Biol. Chem. 261: 12680–12685.PubMedGoogle Scholar
  97. Olmo, K., and Suzuki, K., 1988, Mutation in GM2-gangliosidosis B1 variant, J. Neurochem. 50:316–318. Okada, S., and O’Brien, J. S., 1968, Generalized gangliosidosis (ß-galactosidase deficiency), Science 160: 1002–1004.Google Scholar
  98. Okada, S., and O’Brien, J. S., 1969, Tay–Sachs disease: Generalized absence of a 13-D-acetylhexosaminidase component, Science 165: 698–700.PubMedCrossRefGoogle Scholar
  99. Palmeri, S., Hoogeveen, A. T., Verheijen, F. W., and Galjaard, H., 1986, Galactosidosis: Molecular heterogeneity among distinct clinical phenotypes, Am. J. Hum. Genet. 38: 137–148.PubMedGoogle Scholar
  100. Palo, J., Riekkinen, P., Arstila, A, Y., Autio, S., and Kivimaki, T., 1972, Aspartylglucosaminuria II: biochemical studies on brain, liver, kidney, and spleen, Acta Neuropathol. 20: 217–224.Google Scholar
  101. Palo, J., Pollitt, R. J., Pretty, K. M., and Savolainen, H., 1973, Glycoasparagine metabolites in patients with aspartylglycosaminuria: Comparison between English and Finnish patients with special reference to storage materials, Clin. Chim. Acta 47: 69–74.PubMedCrossRefGoogle Scholar
  102. Palo, J., Rauvala, H., Finne, J., Haltia, M., and Palmgren, K., 1985, Hyperexcretion of free N-acetylneuraminic acid—A novel type of sialuria, Clin. Chim. Acta 145: 237–242.PubMedCrossRefGoogle Scholar
  103. Paschke, E., Trinkl, G., Erwa, W., Pavelka, M., Mutz, I., and Roscher, A., 1986, Infantile type of sialic acid storage disease with sialuria, Clin. Genet. 29: 417–424.PubMedCrossRefGoogle Scholar
  104. Pentchev, P. G., Comly, M. E., Kruth, M. S., Tokoro, T., Butler, J., Sokol, J., Filling-Katz, M., Quirk, J. H., Marshall, D. C., Patel, S., Vanier, M. T., and Brady, R. O., 1987, Group C Niemann-Pick disease, FASEB J. 1: 40–45.PubMedGoogle Scholar
  105. Pullarkat, R. K., 1987, Dolichols and phosphodolichols in aging and in neurological disorders, Chem. Scr. 27: 85–88.Google Scholar
  106. Purpura, D., and Suzuki, K., 1976, Distortion of neuronal geometry and formation of aberrant synapses in neuronal storage disease, Brain Res. 116: 1–12.PubMedCrossRefGoogle Scholar
  107. Reitman, M. L., Varki, A. P., and Kornfeld, S., 1981, Lysosomal enzyme targetting, J. Clin. Invest. 67: 1574–1579.PubMedCrossRefGoogle Scholar
  108. Renlund, M., 1984, Clinical and laboratory diagnosis of Salla disease in infancy and childhood, J. Pediatr. 104: 232–236.PubMedCrossRefGoogle Scholar
  109. Renlund, M., Chester, M. A., Lundblad, A., Aula, P., Raivio, K. O., Autio, S., and Koskela, S.-L., 1979, Increased urinary excretion of free N-acetylneuraminic acid in thirteen patients with Salla disease, Eur. J. Biochem. 101: 245–250.PubMedCrossRefGoogle Scholar
  110. Renlund, M., Chester, M. A., Lundblad, A., Parkkinen, J., and Krusius, T., 1983a, Free N-acetylneuraminic acid in tissues in Salla disease and the enzymes involved in its metabolism, Eur. J. Biochem. 130: 39–45.PubMedCrossRefGoogle Scholar
  111. Renlund, M., Aula, P., Raivio, K. O., Autio, S., Sainio, K., Rapola, J., and Koskela, S. I., 1983b, Salla disease: A new lysosomal storage disorder with distributed sialic acid metabolism, Neurology 33: 5766.CrossRefGoogle Scholar
  112. Renlund, M., Kovanen, P. T., Raivio, K. O., Aula, P., Gahmberg, C. G., and Ehnholm, C., 1986a, Studies on the defect underlying the lysosomal storage of sialic acid in Salla disease, J. Clin. Invest. 77: 568–574.PubMedCrossRefGoogle Scholar
  113. Renlund, M., Tietze, F., and Gahl, W. A., 1986b, Defective sialic acid egress from isolated fibroblast lysosomes of patients with Salla disease, Science 232: 759–762.PubMedCrossRefGoogle Scholar
  114. Roubicek, M., Gehler, J., and Spranger, J., 1985, The clinical spectrum of alpha-iduronidase deficiency, Am. J. Med. Genet. 20: 471–481.PubMedCrossRefGoogle Scholar
  115. Rushton, A. R., and Dawson, G., 1977, The effect of glycosatninoglycans on the in vivo activity of human skin fibroblast glycosphingolipid ß-galactosidases and neuraminidases, Clin. Chim. Acta 80: 133–139.PubMedCrossRefGoogle Scholar
  116. Sandhoff, K., Harzer, K., Wassle, W., and Jatzkewitz, H., 1971, Enzyme alterations and lipid storage in three variants of Tay—Sachs disease, J. Neurochem. 18: 2469–2489.PubMedCrossRefGoogle Scholar
  117. Sando, G. N., Titus-Dillon, P., Hall, C. W., and Neufeld, E. F., 1979, Inhibition of receptor-mediated uptake of a lysosomal enzyme into fibroblasts by chloroquine, procaine and ammonia, Exp. Cell Res. 119: 359–364.PubMedCrossRefGoogle Scholar
  118. Scaravilli, F., and Suzuki, K., 1983, Enzyme replacement in grafted nerve of twitcher mouse, Nature 305: 713–715.PubMedCrossRefGoogle Scholar
  119. Schwarting, G. A., Williams, M. A., Evans, J. E., and McCluer, R. H., 1988, Characterization of SSEA-1 glycolipids in human fucosidosis brain, Trans. Am. Soc. Neurochem. 19: 349.Google Scholar
  120. Shinoda, H., Kobayashi, T., Katayama, M., Goto, I., and Nagara, H., 1987, Accumulation of galactosylsphingosine (psychosine) in the twitcher mouse: Determination by HPLC, J. Neurochem. 49: 9299.CrossRefGoogle Scholar
  121. Sjoberg, I., Fransson, L.-A., Matalon, R., and Dorfman, A., 1973, Hunter’s syndrome: A deficiency of Liduronosulfate sulfatase, Biochem. Biophys. Res. Commun. 54: 1125–1132.PubMedCrossRefGoogle Scholar
  122. Sly, W. S., Quinton, B. A., McAllister, W. H., and Rimoin, D. L., 1973, ß-Glucuronidase deficiency: Report of clinical, radiological and biochemical features of a new mucopolysaccharidosis, J. Pediatr. 82: 249–257.PubMedCrossRefGoogle Scholar
  123. Sorge, J., Kuhl, W., West, C., and Beutler, E., 1987, Complete correction of the enzymatic defect of type 1 Gaucher disease fibroblasts by retroviral-mediated gene transfer, Proc. Natl. Acad. Sci. USA 84: 906–909.PubMedCrossRefGoogle Scholar
  124. Spranger, J., 1987, Inborn errors of complex carbohydrates metabolism, Am. J. Med. Genet. 28: 489–499.PubMedCrossRefGoogle Scholar
  125. Stevenson, R. E., Lubinsky, M., Taylor, H. A., Wenger, D. A., Schroer, R. J., and Olmstead, P. M., 1983, Sialic acid storage disease with sialuria: Clinical and biochemical features in the severe infantile type, Pediatrics 72: 441–449.PubMedGoogle Scholar
  126. Strecker, G., Peers, M.-C., Michalski, J.-C., Hondi-Assah, T., Foumet, B., Spik, G., Montreuil, J., Farriaux, J.-P., Maroteaux, P., and Durand, P., 1977a, Structure of nine sialyl-oligosaccharides accumulated in urine of eleven patients with three different types of sialidosis, Eur. J. Biochem. 75: 391–403.PubMedCrossRefGoogle Scholar
  127. Strecker, G., Michalski, J. C., Herlant-Peers, M. C., Foumet, B., and Montreuil, J., 1977b, Structure of 40 oligosaccharides and glycopeptides accumulating in the urine from patients with catabolism defect of glycoconjugates (sialidosis, fucosidosis, mannosidosis and Sandhoffs disease), Proc. 4th Intl. Symp. Glycoconjugates, Woods Hole, Mass.Google Scholar
  128. Sugahara, K., Funakoshi, S., Funakoshi, I., Aula, P., and Yamashina, I., 1976, Characterization of one neutral and two acidic glycoasparagines isolated from the urine of patients with aspartylglucosaminuria (AGU), J. Biochem. 80: 195–201.PubMedGoogle Scholar
  129. Suzuki, Y., and Suzuki, K., 1970, Krabbe’s globoid cell leukodystrophy: Deficiency of galactocerebrosidase in serum leukocytes and fibroblasts, Science 171: 73–75.CrossRefGoogle Scholar
  130. Suzuki, Y., Sakubara, H., and Yamanaka, T., 1984, Galactosialidosis: A comparative study of clinical and biochemical data on 22 patients, in: The Developing Brain and Its Disorders (M. Arima, ed.), pp. 173–188, Tokyo University Press, Tokyo.Google Scholar
  131. Svennerholm, L., Vanier, M.-T., and Mansson, J. E., 1980, Krabbe disease: A galactosyisphingosine (psychosine) lipidosis, J. Lipid Res. 21: 53–64.PubMedGoogle Scholar
  132. Sweeley, C. C., and Klionsky, B., 1963, Fabry’s disease: Classification as a sphingolipidosis and partial characterization of a novel glycolipid, J. Biol. Chem. 238: 3148–3150.PubMedGoogle Scholar
  133. Sweeley, C. C., and Usuki, S., 1987, The effect of a sialidase inhibitor on the cell cycle of cultured human fibroblasts, J. Cell Biol. 105: 101a.Google Scholar
  134. Thomas, G. H., Reynolds, L. W., and Miller, C. S., 1985, Overproduction of Nacetylneuraminic acid (sialic acid) by sialuria fibroblasts, Pediatr. Res. 19: 451–455.PubMedCrossRefGoogle Scholar
  135. Thompson, J. N., Roden, L., and Reynertson, R., 1986, Oligosaccharide substrates for heparin sulfamidase, Anal. Biochem. 152: 412–422.PubMedCrossRefGoogle Scholar
  136. Tondeur, M., Libert, J., Vamos, E., Van Hoff, F., Thomas, G. H., and Strecker, G., 1982, Infantile forms of sialic acid storage disorder, Eur. J. Pediatr. 139: 142–147.PubMedCrossRefGoogle Scholar
  137. Tsay, G. C., and Dawson, G., 1976, Oligosaccharide storage in brains from patients with fucosidosis, GMtgangliosidosis and GM2-gangliosidosis (Sandhoffs disease), J. Neurochem. 27: 733–740.PubMedCrossRefGoogle Scholar
  138. Tsay, G. C.; Dawson, G., and Li, Y.-T., 1975, Structure of the glycopeptide storage material in GMlgangliosidosis: Sequence determination with specific endo and exoglycosidases, Biochim. Biophys. Acta 385: 305–311.PubMedCrossRefGoogle Scholar
  139. Tsay, G. C., Dawson, G., and Sung, J. S.-S., 1976, Structure of the accumulating oligosaccharide in fucosidosis, J. Biol. Chem. 251: 5852–5859.PubMedGoogle Scholar
  140. Tsuji, S., Choudary, P. V., Martin, B. H., Stubblefield, B. K., Mayor, J. A., Barranger, J. A., and Ginns, E. I., 1986, A mutation in the human glucocerebrosidase gene in neuronopathic Gaucher’s disease, N. Engl. J. Med. 316: 510–575.Google Scholar
  141. van Diggelen, O. P., Galjaard, H., Egge, H., Dabrowski, U., and Cantz, M., 1987, Lysosomal a-Nacetylgalactosantinidase deficiency: A new inherited metabolic disease, Lancet 2: 804.PubMedCrossRefGoogle Scholar
  142. van Kuijk, F. J. G. M., Sevanian, A., Handelman, G. J., and Dratz, E. A., 1987, A new role for phospholipase A2: Protection of membranes from lipid peroxidation damage, Trends Biochem. Sci. 12: 31–34.CrossRefGoogle Scholar
  143. Verheijen, F. W., Palmeri, S., and Galjaard, H., 1987, Purification and partial characterization of lysosomal neuraminidase from human placenta, Eur. J. Biochem. 162: 63–67.PubMedCrossRefGoogle Scholar
  144. Vestermark, S., Tonnesen, T., Schulz-Andersen, M., and Guttler, F., 1987, Neurological symptoms in a Maroteaux—Lamy patient, Clin. Genet. 31: 114–117.PubMedCrossRefGoogle Scholar
  145. von Figura, K., and Hasilik, A., 1986, Lysosomal enzymes and their receptors, Annu. Rev. Biochem. 55: 167–193.CrossRefGoogle Scholar
  146. Warner, T. G., DeKremer, R. D., Sjoberg, E. R., and Mock, A. K., 1985, Characterization and analysis of branched chain N-acetylglucosaminyl oligosaccharides accumulating in Sandhoff disease tissue: Evidence that biantennary-bisected oligosaccharides of glycoproteins are abundant substrates for lysosomes, J. Biol. Chem. 260: 6194–6199.PubMedGoogle Scholar
  147. Weismann, U., DiDonata, S., and Hershkowitz, N. N., 1975, Effect of chloroquine on culturd fibroblasts release of lysosomal hydrolases and inhibition of their uptake, Biochem. Biophys. Res. Commun. 66: 1338–1343.CrossRefGoogle Scholar
  148. Wenger, D. A., Sattler, M., Clark, C., Tanaka, H., Suzuki, K., and Dawson, G., 1975, Lactosyl ceramidosis: Normal activity for two lactosyl ceramide ß-galactosidases, Science 188: 1310–1312.PubMedCrossRefGoogle Scholar
  149. Wenger, D. A., Sattler, M., Mueller, T., Myers, G. G., Schneiman, R. S., and Nixon, G. W., 1980, Adult GMl gangliosidosis, Clin. Genet. 17: 323–334.PubMedCrossRefGoogle Scholar
  150. Wenger, D. A., Sujansky, E., Fennessey, P. V., and Thompson, J. N., 1986, Combined heparan sulfate sulfamidase and 3-mannosidase deficiency in a Sanfilippo phenotype, N. Engl. J. Med. 315: 1203–1206.CrossRefGoogle Scholar
  151. Wollburg-Buchholz, K., Schlote, W., Baumkotter, J., Cantz, M., Holder, H., and Harzer, K., 1985, Familial lysosomal storage disease with generalized vacuolization and sialic aciduria, Sporadic Salla disease, Neuropaediatrie 16: 67–75.CrossRefGoogle Scholar
  152. Wolfe, L. S., Senior, R. G., and Ng Ying Kin, N. M. K., 1974, The structure of oligosaccharides accumulating in the liver of GMl-gangIiosidosis type 1, J. Biol. Chem. 249: 1828–1838.PubMedGoogle Scholar
  153. Wolfe, L. S., Ivy, G. O., and Witkop, C. J., 1987, Dolichols: Lysosomal membrane turnover and relationships to the accumulation of ceroid and lipofuscin in inherited diseases, Alzheimer’s disease and aging, Chem. Scr. 27: 79–84.Google Scholar
  154. Ylitalo, V., Hagberg, B., Rapola, J., Mansson, J. E., Svennerholm, L., Sauner, G., and Tonnby, B., 1986, Salta disease variants, Neuropediatr. 17: 44–47.CrossRefGoogle Scholar
  155. Ziegler, M., and Bach, G., 1986, Internalization of exogenous gangliosides in cultured skin fibroblasts for the diagnosis of mucolipidosis IV, Clin. Chim. Acta 157: 183–190.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Glyn Dawson
    • 1
  • Larry W. Hancock
    • 1
  1. 1.Departments of Pediatrics and Biochemistry and Molecular BiologyUniversity of ChicagoChicagoUSA

Personalised recommendations