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Gene Review

NEU1  -  sialidase 1 (lysosomal sialidase)

Homo sapiens

Synonyms: Acetylneuraminyl hydrolase, G9 sialidase, Lysosomal sialidase, N-acetyl-alpha-neuraminidase 1, NANH, ...
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Disease relevance of NEU1


Psychiatry related information on NEU1


High impact information on NEU1


Biological context of NEU1

  • Mutations in the sialidase gene NEU1, located on chromosome 6p21.3, result in autosomal recessive disorder, sialidosis, which is characterized by the progressive lysosomal storage of sialylated glycopeptides and oligosaccharides [11].
  • Thus, the differentiation of monocytes into macrophages is associated with regulation of the expression of at least three distinct cellular sialidases, with specific up-regulation of the enzyme activity of only Neu1 [12].
  • We report a Turkish family with parental consanguinity and at risk for sialidosis type II, an inherited autosomal recessive disorder caused by lysosomal alpha-N-acetyl-neuraminidase (sialidase, NEU1) deficiency [13].
  • DNA analysis showed that the siblings had a homozygous missense point mutation c.544A-->G (Ser182Gly) in the exon 3 of the alpha-N-acetyl-neuraminidase (NEU1) gene [14].
  • Lysosomal sialidase activity in homozygotes was absent, and that in heterozygotes was significantly decreased to 70% of control level [10].

Anatomical context of NEU1

  • The purpose of this study is to determine effects of GLB1, PPCA and NEU1 gene mutations on elastogenesis in skin fibroblasts [15].
  • In contrast to Neu1, Neu4 is targeted to lysosomes by the mannose 6-phosphate receptor and does not require association with other proteins for enzymatic activity [1].
  • The detection method for the abnormal sialylglycoproteins in cultured cells involving MAM lectin was demonstrated to be useful not only for biochemical and diagnostic analyses of NEU1 deficiencies but also for therapeutic evaluation of these conditions [16].
  • Activation of lymphocytes by exposure to anti-CD3 and anti-CD28 IgG resulted in a ninefold increase in Neu1-specific activity after growth of cells in culture for 5 days [17].
  • Neu1 was present on the surface of freshly isolated and activated CD4 and CD8 T lymphocytes, as determined by staining intact cells with anti-Neu1 IgG and analysis by flow cytometry and by Western blot analysis of biotin-labeled cell surface proteins [17].

Associations of NEU1 with chemical compounds

  • The carcinogenicity of N-nitroso-N-methylurea (NMU) and N-nitroso-N-ethylurea (NEU) has been determined in adult male Syrian golden hamsters following a single i.p. injection or two-thirds of the acute 50% lethal dose, or 30 and 60 mg/kg, respectively [18].
  • Lysosomal sialidase, encoded by neu1, is required for the removal of terminal sialic acid residues from a variety of sialoglycoconjugates [19].
  • DNA analysis of the family showed that both the proband and the third sibling had a novel homozygous nonsense point mutation at nucleotide 87 in exon 1 of the alpha-N-acetyl-neuraminidase (neu1) gene causing a substitution of tryptophan at codon 29 by a termination codon (W29X) [13].

Physical interactions of NEU1

  • Galactosialidosis, a clinically similar disorder, is caused by the secondary Neu1 deficiency because of genetic defects in cathepsin A that form a complex with Neu1 and activate it [1].
  • Our results also suggest that lysosomal sialidase activation may be required for the acquisition of the HA-binding form of CD44 in LPS- and TNF-alpha-stimulated monocytic cells [20].

Other interactions of NEU1

  • This protein forms a high-molecular-weight complex with the hydrolases beta-galactosidase (GLB1) and neuraminidase (NEU1) [21].
  • Western blot analysis using specific antibodies showed that the amount of Neu1 and Neu3 proteins increased during monocyte differentiation [12].
  • Cell surface Neu1 was found tightly associated with a subunit of protective protein/cathepsin A (PPCA) [17].

Analytical, diagnostic and therapeutic context of NEU1


  1. Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells. Seyrantepe, V., Landry, K., Trudel, S., Hassan, J.A., Morales, C.R., Pshezhetsky, A.V. J. Biol. Chem. (2004) [Pubmed]
  2. Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression. Kakugawa, Y., Wada, T., Yamaguchi, K., Yamanami, H., Ouchi, K., Sato, I., Miyagi, T. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Splice donor site mutation in the lysosomal neuraminidase gene causing exon skipping and complete loss of enzyme activity in a sialidosis patient. Penzel, R., Uhl, J., Kopitz, J., Beck, M., Otto, H.F., Cantz, M. FEBS Lett. (2001) [Pubmed]
  4. Role of plasma membrane ganglioside sialidase of human neuroblastoma cells in growth control and differentiation. Kopitz, J., von Reitzenstein, C., Mühl, C., Cantz, M. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  5. Cell proliferation in intracranial tumours: selective silver staining of nucleolar organizer regions (AgNORs). Application to surgical and experimental neuro-oncology. Plate, K.H., Rüschoff, J., Mennel, H.D. Neuropathol. Appl. Neurobiol. (1991) [Pubmed]
  6. Identification of a CTL4/Neu1 fusion transcript in a sialidosis patient. Uhl, J., Penzel, R., Sergi, C., Kopitz, J., Otto, H.F., Cantz, M. FEBS Lett. (2002) [Pubmed]
  7. Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis. Pshezhetsky, A.V., Richard, C., Michaud, L., Igdoura, S., Wang, S., Elsliger, M.A., Qu, J., Leclerc, D., Gravel, R., Dallaire, L., Potier, M. Nat. Genet. (1997) [Pubmed]
  8. Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A. van der Spoel, A., Bonten, E., d'Azzo, A. EMBO J. (1998) [Pubmed]
  9. Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex. Lukong, K.E., Elsliger, M.A., Chang, Y., Richard, C., Thomas, G., Carey, W., Tylki-Szymanska, A., Czartoryska, B., Buchholz, T., Criado, G.R., Palmeri, S., Pshezhetsky, A.V. Hum. Mol. Genet. (2000) [Pubmed]
  10. Carrier detection of sialidosis with partial beta-galactosidase deficiency by the assay of lysosomal sialidase in lymphocytes. Tsuji, S., Yamada, T., Ariga, T., Toyoshima, I., Yamaguchi, H., Kitahara, Y., Miyatake, T., Yamakawa, T. Ann. Neurol. (1984) [Pubmed]
  11. Molecular pathology of NEU1 gene in sialidosis. Seyrantepe, V., Poupetova, H., Froissart, R., Zabot, M.T., Maire, I., Pshezhetsky, A.V. Hum. Mutat. (2003) [Pubmed]
  12. Differential expression of endogenous sialidases of human monocytes during cellular differentiation into macrophages. Stamatos, N.M., Liang, F., Nan, X., Landry, K., Cross, A.S., Wang, L.X., Pshezhetsky, A.V. FEBS J. (2005) [Pubmed]
  13. Prenatal diagnosis and fetal pathology in a Turkish family harboring a novel nonsense mutation in the lysosomal alpha-N-acetyl-neuraminidase (sialidase) gene. Sergi, C., Penzel, R., Uhl, J., Zoubaa, S., Dietrich, H., Decker, N., Rieger, P., Kopitz, J., Otto, H.F., Kiessling, M., Cantz, M. Hum. Genet. (2001) [Pubmed]
  14. First report of two Taiwanese siblings with sialidosis type I: a 10-year follow-up study. Chen, C.M., Lai, S.C., Chen, I.C., Hsu, K.C., Lyu, R.K., Ro, L.S., Chang, H.S. J. Neurol. Sci. (2006) [Pubmed]
  15. Elastogenesis in cultured dermal fibroblasts from patients with lysosomal beta-galactosidase, protective protein/cathepsin A and neuraminidase-1 deficiencies. Tatano, Y., Takeuchi, N., Kuwahara, J., Sakuraba, H., Takahashi, T., Takada, G., Itoh, K. J. Med. Invest. (2006) [Pubmed]
  16. Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement. Oheda, Y., Kotani, M., Murata, M., Sakuraba, H., Kadota, Y., Tatano, Y., Kuwahara, J., Itoh, K. Glycobiology (2006) [Pubmed]
  17. Sialidase expression in activated human T lymphocytes influences production of IFN-{gamma}. Nan, X., Carubelli, I., Stamatos, N.M. J. Leukoc. Biol. (2007) [Pubmed]
  18. Carcinogenicity of single doses of N-nitroso-N-methylurea and N-nitroso-N-ethylurea in Syrian golden hamsters and the persistence of alkylated purines in the DNA of various tissues. Likhachev, A.J., Ivanov, M.N., Brésil, H., Planche-Martel, G., Montesano, R., Margison, G.P. Cancer Res. (1983) [Pubmed]
  19. Overexpression of MyoD-inducible lysosomal sialidase (neu1) inhibits myogenesis in C2C12 cells. Champigny, M.J., Perry, R., Rudnicki, M., Igdoura, S.A. Exp. Cell Res. (2005) [Pubmed]
  20. Tumor necrosis factor-alpha induces functionally active hyaluronan-adhesive CD44 by activating sialidase through p38 mitogen-activated protein kinase in lipopolysaccharide-stimulated human monocytic cells. Gee, K., Kozlowski, M., Kumar, A. J. Biol. Chem. (2003) [Pubmed]
  21. New mutations in the PPBG gene lead to loss of PPCA protein which affects the level of the beta-galactosidase/neuraminidase complex and the EBP-receptor. Malvagia, S., Morrone, A., Caciotti, A., Bardelli, T., d'Azzo, A., Ancora, G., Zammarchi, E., Donati, M.A. Mol. Genet. Metab. (2004) [Pubmed]
  22. Mucolipidosis I: studies of sialidase activity and a prenatal diagnosis. Mueller, O.T., Wenger, D.A. Clin. Chim. Acta (1981) [Pubmed]
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