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MeSH Review

Gangliosidoses

 
 
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Disease relevance of Gangliosidoses

 

High impact information on Gangliosidoses

  • Inactivation of GM1-ganglioside beta-galactosidase by a specific inhibitor: a model for ganglioside storage disease [6].
  • In addition to accumulating cholesterol, NPC1-deficient cells also accumulate gangliosides and other glycosphingolipids (GSLs), and neuropathological abnormalities in NPC disease closely resemble those seen in primary gangliosidoses [7].
  • Mutations in the HEXA gene, encoding the alpha-subunit of beta-hexosaminidase A (Hex A), that abolish Hex A enzyme activity cause Tay-Sachs disease (TSD), the fatal infantile form of G(M2) gangliosidosis, Type 1 [8].
  • In G(M2) gangliosidosis variant 0, a defect in the beta-subunit of lysosomal beta-N-acetylhexosaminidase (EC 3.2.1.52) causes abnormal accumulation of G(M2) ganglioside and severe neurodegeneration [3].
  • We have documented the presence of secondary ganglioside accumulation in mouse models of several MPS disorders (types I, IIIA, IIIB, and VII) and report that this storage is accompanied by sequestration of free cholesterol in a manner similar to that observed in primary gangliosidoses [9].
 

Chemical compound and disease context of Gangliosidoses

 

Biological context of Gangliosidoses

 

Gene context of Gangliosidoses

  • The G(M2) activator protein is a substrate specific cofactor for degradation of G(M2) ganglioside by lysosomal beta-hexosaminidase A. Mutations in the gene encoding the activator result in the AB-variant form of G(M2) gangliosidosis [14].

References

  1. Identification of candidate active site residues in lysosomal beta-hexosaminidase A. Fernandes, M.J., Yew, S., Leclerc, D., Henrissat, B., Vorgias, C.E., Gravel, R.A., Hechtman, P., Kaplan, F. J. Biol. Chem. (1997) [Pubmed]
  2. Degradation of blood group A glycolipid A-6-2 by normal and mutant human skin fibroblasts. Asfaw, B., Schindler, D., Ledvinová, J., Cerný, B., Smíd, F., Conzelmann, E. J. Lipid Res. (1998) [Pubmed]
  3. An inversion of 25 base pairs causes feline GM2 gangliosidosis variant. Martin, D.R., Krum, B.K., Varadarajan, G.S., Hathcock, T.L., Smith, B.F., Baker, H.J. Exp. Neurol. (2004) [Pubmed]
  4. Review: Metabolic cardiomyopathy and conduction system defects in children. Gilbert-Barness, E. Ann. Clin. Lab. Sci. (2004) [Pubmed]
  5. Lectin histochemical study of lipopigments: results with concanavalin A. Elleder, M., Goebel, H.H., Koppang, N. Adv. Exp. Med. Biol. (1989) [Pubmed]
  6. Inactivation of GM1-ganglioside beta-galactosidase by a specific inhibitor: a model for ganglioside storage disease. Singer, H.S., Tiemeyer, M., Slesinger, P.A., Sinnott, M.L. Ann. Neurol. (1987) [Pubmed]
  7. Critical role for glycosphingolipids in Niemann-Pick disease type C. Zervas, M., Somers, K.L., Thrall, M.A., Walkley, S.U. Curr. Biol. (2001) [Pubmed]
  8. W474C amino acid substitution affects early processing of the alpha-subunit of beta-hexosaminidase A and is associated with subacute G(M2) gangliosidosis. Petroulakis, E., Cao, Z., Clarke, J.T., Mahuran, D.J., Lee, G., Triggs-Raine, B. Hum. Mutat. (1998) [Pubmed]
  9. Differential subcellular localization of cholesterol, gangliosides, and glycosaminoglycans in murine models of mucopolysaccharide storage disorders. McGlynn, R., Dobrenis, K., Walkley, S.U. J. Comp. Neurol. (2004) [Pubmed]
  10. Ceroid-lipofuscinosis (Batten disease). Fluorescein angiography, electrophysiology, histopathology, ultrastructure, and a review of amaurotic familial idiocy. Hittner, H.M., Ziller, R.S. Arch. Ophthalmol. (1975) [Pubmed]
  11. Juvenile parkinsonism: a heterogeneous entity. Cardoso, F., Camargos, S. Eur. J. Neurol. (2000) [Pubmed]
  12. G(M2)-ganglioside metabolism in situ in mucolipidosis IV fibroblasts. Raghavan, S., Leshinsky, E., Kolodny, E.H. Neurochem. Res. (1999) [Pubmed]
  13. Structure of the glycopeptide storage material in GM 1 gangliosidosis. Sequence determination with specific endo- and exoglycosidases. Tsay, G.C., Dawson, G., Li Y-T, n.u.l.l. Biochim. Biophys. Acta (1975) [Pubmed]
  14. Characterization of the affinity of the G(M2) activator protein for glycolipids by a fluorescence dequenching assay. Smiljanic-Georgijev, N., Rigat, B., Xie, B., Wang, W., Mahuran, D.J. Biochim. Biophys. Acta (1997) [Pubmed]
 
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