Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2022 Oct;39(5):677-683.
doi: 10.1007/s10719-022-10067-7. Epub 2022 Jun 8.

Sialidase NEU3 and its pathological significance

Taeko Miyagi  1 , Koji Yamamoto  2
Affiliations
Review

Sialidase NEU3 and its pathological significance

Taeko Miyagi et al. Glycoconj J. 2022 Oct.

Erratum in

Abstract

Sialidases (EC 3.2.1.18, also called neuraminidases) catalyze the removal of α-glycosidically linked sialic acid residues from glycoproteins and glycolipids; this is the initial step in the degradation of these glycoconjugates. Sialidases of mammalian origin have been implicated in not only lysosomal catabolism but also the modulation of functional molecules involved in many biological processes. To date, four types of mammalian sialidases have been cloned and designated as Neu1, Neu2, Neu3 and Neu4. These sialidases differ in their subcellular localization and enzymatic properties, as well as their chromosomal localization, and they are expressed in a tissue-specific manner. Among the sialidases, the plasma membrane-associated sialidase Neu3 appears to play particular roles in controlling transmembrane signaling through the modulation of gangliosides, and its aberrant expression is closely related to various pathogeneses, including that of cancer. Interestingly, the human orthologue NEU3 acts in two ways, catalytic hydrolysis of gangliosides and protein interactions with other signaling molecules. Aberrant NEU3 expression can induce various pathological conditions. This review briefly summarizes recent studies, focusing on the involvement of NEU3 in various pathological phenomena.

Keywords: Gangliosides; Hepatic steatosis; Pulmonary fibrosis; Sialidase; Transmembrane signaling; cancer.

PubMed Disclaimer

References

    1. Bonten, E., van der Spoel, A., Fornerod, M., Grosveld, G., d’Azzo, A.: Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis. Genes Dev. 10, 3156–3169 (1996) - PubMed
    1. Milner, C.M., Smith, S.V., Carrillo, M.B., Taylor, G.L., Hollinshead, M., Campbell, R.D.: Identification of a sialidase encoded in the human major histocompatibility complex. J. Biol. Chem. 272, 4549–4558 (1997) - PubMed
    1. Pshezhetsky, A.V., Richard, C., Michaud, L., Igdoura, S., Wang, S., Elsliger, M.A., Qu, J., Leclerc, D., Gravel, R., Dallaire, L., Potier, M.: Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis. Nat. Genet. 15, 316–320 (1997) - PubMed
    1. Carrillo, M.B., Milner, C.M., Ball, S.T., Snoek, M., Campbell, R.D.: Cloning and characterization of a sialidase from the murine histocompatibility-2 complex: low levels of mRNA and a single amino acid mutation are responsible for reduced sialidase activity in mice carrying the Neu1a allele. Glycobiology. 7, 975–986 (1997) - PubMed
    1. Miyagi, T., Konno, K., Emori, Y., Kawasaki, H., Suzuki, K., Yasui, A., Tsuik, S.: Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase. J. Biol. Chem. 268, 26435–26440 (1993) - PubMed

LinkOut - more resources