Biology:Sialidase-1

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Sialidase-1, is a mammalian lysosomal neuraminidase enzyme which in humans is encoded by the NEU1 gene.

Function

The protein SIALIDASE-1 encoded by the NEU-1 gene encodes the lysosomal enzyme SIALIDASE-1, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis.

Clinical significance

Mutations in NEU1 leads to sialidosis, a rare lysosomal storage disease. Sialidase has also been shown to enhance recovery from spinal cord contusion injury when injected in rats.

Interactions

NEU1 has been shown to interact with Cathepsin A.

Further reading

• "The biochemistry and clinical features of galactosialidosis". Biochim. Biophys. Acta 1225 (3): 244–54. 1994. doi:10.1016/0925-4439(94)90002-7. PMID 8312369. 
• "Molecular pathology of NEU1 gene in sialidosis". Hum. Mutat. 22 (5): 343–52. 2004. doi:10.1002/humu.10268. PMID 14517945. 
• "Purification and partial characterization of lysosomal neuraminidase from human placenta". Eur. J. Biochem. 162 (1): 63–7. 1987. doi:10.1111/j.1432-1033.1987.tb10542.x. PMID 3102233. 
• "Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein". Eur. J. Biochem. 149 (2): 315–21. 1985. doi:10.1111/j.1432-1033.1985.tb08928.x. PMID 3922758. 
• "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface". J. Virol. 70 (11): 7462–70. 1996. doi:10.1128/JVI.70.11.7462-7470.1996. PMID 8892864. 
• "Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate". J. Biol. Chem. 271 (45): 28359–65. 1996. doi:10.1074/jbc.271.45.28359. PMID 8910459. 
• "Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis". Genes Dev. 10 (24): 3156–69. 1997. doi:10.1101/gad.10.24.3156. PMID 8985184.  * "Identification of a sialidase encoded in the human major histocompatibility complex". J. Biol. Chem. 272 (7): 4549–58. 1997. doi:10.1074/jbc.272.7.4549. PMID 9020182. 
• "Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis". Nat. Genet. 15 (3): 316–20. 1997. doi:10.1038/ng0397-316. PMID 9054950. 
• "Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation". Biochem. J. 330 ( Pt 2) (Pt 2): 641–50. 1998. doi:10.1042/bj3300641. PMID 9480870. 
• "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. 17 (6): 1588–97. 1998. doi:10.1093/emboj/17.6.1588. PMID 9501080. 
• "Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex". Hum. Mol. Genet. 9 (7): 1075–85. 2000. doi:10.1093/hmg/9.7.1075. PMID 10767332. 
• "Molecular and structural studies of Japanese patients with sialidosis type 1". J. Hum. Genet. 45 (4): 241–9. 2000. doi:10.1007/s100380070034. PMID 10944856. 
• "Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis". Hum. Mol. Genet. 9 (18): 2715–25. 2000. doi:10.1093/hmg/9.18.2715. PMID 11063730. 
• "Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex". J. Biol. Chem. 276 (20): 17286–90. 2001. doi:10.1074/jbc.M100460200. PMID 11279074. 
• "Splice donor site mutation in the lysosomal neuraminidase gene causing exon skipping and complete loss of enzyme activity in a sialidosis patient". FEBS Lett. 501 (2–3): 135–8. 2001. doi:10.1016/S0014-5793(01)02645-X. PMID 11470272.  * "Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail". J. Biol. Chem. 276 (49): 46172–81. 2002. doi:10.1074/jbc.M104547200. PMID 11571282. 
• "Prenatal diagnosis and fetal pathology in a Turkish family harboring a novel nonsense mutation in the lysosomal alpha-N-acetyl-neuraminidase (sialidase) gene". Hum. Genet. 109 (4): 421–8. 2001. doi:10.1007/s004390100592. PMID 11702224. 
• "Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes". J. Hum. Genet. 47 (1): 29–37. 2002. doi:10.1007/s10038-002-8652-7. PMID 11829139.