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Gene Review

NAGLU  -  N-acetylglucosaminidase, alpha

Homo sapiens

Synonyms: Alpha-N-acetylglucosaminidase, MPS-IIIB, MPS3B, N-acetyl-alpha-glucosaminidase, NAG, ...
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Disease relevance of NAGLU


Psychiatry related information on NAGLU

  • In MPS IIIB, there is a deficiency in the enzyme alpha-N-acetylglucosaminidase (NAGLU) and early clinical symptoms include aggressive behaviour and hyperactivity followed by progressive mental retardation [4].

High impact information on NAGLU


Chemical compound and disease context of NAGLU


Biological context of NAGLU

  • Most of the identified mutations in the SGSH and NAGLU genes are associated with severe clinical phenotypes [9].
  • Direct metabolic labeling experiments with Na(2) (32)PO(4) confirmed that the specific phosphorylation of recombinant NAGLU secreted from transfected CHO cells is significantly lower when compared with a control lysosomal enzyme [2].
  • Two isoforms of recombinant NAGLU with apparent molecular weights of 89 and 79 kDa were purified and shown to differ in their glycosylation pattern [2].
  • It was observed that the emu NAGLU gene is structurally similar to that of human and mouse, but the introns are considerably shorter [10].
  • Transient transfection of COS cells, by DNA mutagenized with NAGLU mutations, produced enzymatic molecules without activity, demonstrating the deleterious nature of the defects [8].

Anatomical context of NAGLU

  • Many of the missense, nonsense, and insertion/deletion mutations have been expressed in mammalian cell lines to permit the characterization of their effects on SGSH and NAGLU activity and intracellular processing and trafficking [9].
  • However, compared to other recombinant lysosomal enzymes expressed from CHO-K1 cells, the mannose-6-phosphate receptor mediated uptake of the secreted form of recombinant NAGLU into cultured skin fibroblasts was considerably reduced [2].
  • NAGLU is involved in the degradation of the glycosaminoglycan (GAG) heparan sulphate, and a deficiency results in the accumulation of partially degraded GAGs inside lysosomes [11].
  • Insofar as p47(phox), p67(phox), and gp91(phox) are all components of the phagocyte NADPH oxidase, our results suggest the possible involvement of the reactive oxygen species in the genesis of neurodegeneration in MPS IIIB disease [12].
  • The value of bone marrow transplantation in the mucopolysaccharidoses, especially in MPS IIIB, is discussed with a wide review of the literature [13].

Associations of NAGLU with chemical compounds


Analytical, diagnostic and therapeutic context of NAGLU

  • To characterize this enzyme further and evaluate its potential for enzyme replacement studies we expressed the NAGLU-encoding cDNA in Chinese hamster ovary cells (CHO-K1 cells) and purified the recombinant enzyme from the medium of stably transfected cells by a two-step affinity chromatography [2].
  • Mutation screening using SSCP/heteroduplex analysis on genomic DNA fragments was performed in five Turkish MPS IIIA and eight Turkish MPS IIIB patients [15].


  1. NAGLU mutations underlying Sanfilippo syndrome type B. Schmidtchen, A., Greenberg, D., Zhao, H.G., Li, H.H., Huang, Y., Tieu, P., Zhao, H.Z., Cheng, S., Zhao, Z., Whitley, C.B., Di Natale, P., Neufeld, E.F. Am. J. Hum. Genet. (1998) [Pubmed]
  2. Expression and characterization of human recombinant and alpha-N-acetylglucosaminidase. Weber, B., Hopwood, J.J., Yogalingam, G. Protein Expr. Purif. (2001) [Pubmed]
  3. MR imaging of the brain in patients with mucopolysaccharidosis. Murata, R., Nakajima, S., Tanaka, A., Miyagi, N., Matsuoka, O., Kogame, S., Inoue, Y. AJNR. American journal of neuroradiology. (1989) [Pubmed]
  4. Identification of 12 novel mutations in the alpha-N-acetylglucosaminidase gene in 14 patients with Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB). Beesley, C.E., Young, E.P., Vellodi, A., Winchester, B.G. J. Med. Genet. (1998) [Pubmed]
  5. Genotype-phenotype correspondence in Sanfilippo syndrome type B. Zhao, H.G., Aronovich, E.L., Whitley, C.B. Am. J. Hum. Genet. (1998) [Pubmed]
  6. The molecular basis of Sanfilippo syndrome type B. Zhao, H.G., Li, H.H., Bach, G., Schmidtchen, A., Neufeld, E.F. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  7. Neurological correction of lysosomal storage in a mucopolysaccharidosis IIIB mouse model by adeno-associated virus-mediated gene delivery. Fu, H., Samulski, R.J., McCown, T.J., Picornell, Y.J., Fletcher, D., Muenzer, J. Mol. Ther. (2002) [Pubmed]
  8. Molecular defects in the alpha-N-acetylglucosaminidase gene in Italian Sanfilippo type B patients. Tessitore, A., Villani, G.R., Di Domenico, C., Filocamo, M., Gatti, R., Di Natale, P. Hum. Genet. (2000) [Pubmed]
  9. Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications. Yogalingam, G., Hopwood, J.J. Hum. Mutat. (2001) [Pubmed]
  10. Molecular basis of mucopolysaccharidosis type IIIB in emu (Dromaius novaehollandiae): an avian model of Sanfilippo syndrome type B. Aronovich, E.L., Johnston, J.M., Wang, P., Giger, U., Whitley, C.B. Genomics (2001) [Pubmed]
  11. Molecular defects in Sanfilippo syndrome type B (mucopolysaccharidosis IIIB). Beesley, C.E., Jackson, M., Young, E.P., Vellodi, A., Winchester, B.G. J. Inherit. Metab. Dis. (2005) [Pubmed]
  12. Cytokines, neurotrophins, and oxidative stress in brain disease from mucopolysaccharidosis IIIB. Villani, G.R., Gargiulo, N., Faraonio, R., Castaldo, S., Gonzalez Y Reyero, E., Di Natale, P. J. Neurosci. Res. (2007) [Pubmed]
  13. Sanfilippo disease type B. A case report and review of the literature on recent advances in bone marrow transplantation. Güngör, N., Tunçbilek, E. Turk. J. Pediatr. (1995) [Pubmed]
  14. Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer. Villani, G.R., Follenzi, A., Vanacore, B., Di Domenico, C., Naldini, L., Di Natale, P. Biochem. J. (2002) [Pubmed]
  15. Sanfilippo syndrome in Turkey: Identification of novel mutations in subtypes A and B. Emre, S., Terzioglu, M., Tokatli, A., Coskun, T., Ozalp, I., Weber, B., Hopwood, J.J. Hum. Mutat. (2002) [Pubmed]
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