Neuraminidase 4 (NEU4)

Neuraminidase 4 (NEU4) is a member of the sialidase (neuraminidase) family of enzymes that catalyze the hydrolytic removal of terminal sialic acid (N-acetylneuraminic acid) residues from glycoproteins, glycolipids, oligosaccharides, and gangliosides[1][3][6]. NEU4 exists in at least two forms (long and short) differing in their subcellular localization: the long form associates with the outer mitochondrial membrane, while the short form is mainly bound to the endoplasmic reticulum[4]. NEU4 is involved in important biological processes such as the degradation of polysialic acids on neural cell adhesion molecule (NCAM), regulation of neurite outgrowth, modulation of cell adhesion, and potentially regulating immune responses in microglia[6][7]. Abnormal NEU4 activity or expression has been associated with neurodevelopmental and neurodegenerative diseases, certain cancers, and inherited glycan storage disorders such as glycoproteinosis and GM2-gangliosidosis AB variant[1][6]. No specific drugs are currently known to target NEU4, and its clinical utility as a biomarker or therapeutic target remains under investigation.

Other names

Sialidase-4LP5125N-acetyl-alpha-neuraminidase 4neuraminidase 4 (sialidase)

Enzymatic cleavage of terminal sialic acid residues from glycoproteins, glycolipids, oligosaccharides, and gangliosides; Catabolism of poly-alpha-(2->8)-sialylated neural cell adhesion molecule (NCAM1)