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Gene Review

NEU2  -  sialidase 2 (cytosolic sialidase)

Homo sapiens

Synonyms: Cytosolic sialidase, N-acetyl-alpha-neuraminidase 2, SIAL2, Sialidase-2
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Disease relevance of NEU2


High impact information on NEU2


Biological context of NEU2

  • Predicted structures and the experimental protein-ligand complex of NEU2 were compared to identify similarities and differences among the active sites [7].
  • Using a sequence homology-based approach, we previously identified a human gene, named NEU2, mapping to chromosome 2q37 [8].
  • In addition, based on the detectable similarities between the NEU2 amino acid sequence and bacterial sialidases, a prediction of the three-dimensional structure of the enzyme was carried out using a protein homology modeling approach [8].
  • Neu2 expression was strictly correlated with IGF-1 signaling also in C2 myoblasts overexpressing the insulin-like growth factor 1 binding protein 5 and therefore not responding to endogenously produced insulin-like growth factor 1 [2].
  • Indeed, the hypertrophy induced by transfection of a constitutively activated form of AKT was able to induce high Neu2 activity in C2C12 cells, whereas the transfection of a kinase-inactive form of AKT prevented myotube formation, triggering Neu2 downregulation [2].

Anatomical context of NEU2


Associations of NEU2 with chemical compounds

  • NEU2 encoded protein is a polypeptide of 380 amino acids with two Asp block consensuses and the YRIP sequence in the amino terminal part of the primary structure [8].

Other interactions of NEU2


Analytical, diagnostic and therapeutic context of NEU2


  1. Properties of recombinant human cytosolic sialidase HsNEU2. The enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules. Tringali, C., Papini, N., Fusi, P., Croci, G., Borsani, G., Preti, A., Tortora, P., Tettamanti, G., Venerando, B., Monti, E. J. Biol. Chem. (2004) [Pubmed]
  2. Insulin-like growth factor 1 signaling regulates cytosolic sialidase Neu2 expression during myoblast differentiation and hypertrophy. Fanzani, A., Colombo, F., Giuliani, R., Preti, A., Marchesini, S. FEBS J. (2006) [Pubmed]
  3. Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition. Chavas, L.M., Tringali, C., Fusi, P., Venerando, B., Tettamanti, G., Kato, R., Monti, E., Wakatsuki, S. J. Biol. Chem. (2005) [Pubmed]
  4. Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase. Miyagi, T., Konno, K., Emori, Y., Kawasaki, H., Suzuki, K., Yasui, A., Tsuik, S. J. Biol. Chem. (1993) [Pubmed]
  5. Dependence of neurotrophic factor activation of Trk tyrosine kinase receptors on cellular sialidase. Woronowicz, A., Amith, S.R., De Vusser, K., Laroy, W., Contreras, R., Basta, S., Szewczuk, M.R. Glycobiology (2007) [Pubmed]
  6. Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family. Monti, E., Bassi, M.T., Bresciani, R., Civini, S., Croci, G.L., Papini, N., Riboni, M., Zanchetti, G., Ballabio, A., Preti, A., Tettamanti, G., Venerando, B., Borsani, G. Genomics (2004) [Pubmed]
  7. Homology modeling of human sialidase enzymes NEU1, NEU3 and NEU4 based on the crystal structure of NEU2: Hints for the design of selective NEU3 inhibitors. Magesh, S., Suzuki, T., Miyagi, T., Ishida, H., Kiso, M. J. Mol. Graph. Model. (2006) [Pubmed]
  8. Expression of a novel human sialidase encoded by the NEU2 gene. Monti, E., Preti, A., Nesti, C., Ballabio, A., Borsani, G. Glycobiology (1999) [Pubmed]
  9. Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases. Monti, E., Preti, A., Rossi, E., Ballabio, A., Borsani, G. Genomics (1999) [Pubmed]
  10. 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]
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