Sialidase-3 (NEU3)

Sialidase-3 (NEU3) is a membrane-associated sialidase that catalyzes the removal of terminal sialic acid residues from glycolipids and glycoproteins, with a high specificity for gangliosides[4][2][5]. It is primarily localized to the plasma membrane and endosomal compartments, where it regulates the composition of membrane gangliosides and modulates transmembrane signaling by directly interacting with receptors such as EGFR[1][4]. NEU3 activity influences processes such as cell adhesion, migration, differentiation, apoptosis, and cancer progression, and is implicated in several pathophysiological conditions, including cancer and neurodegenerative diseases[1][2][4]. The enzyme can be pharmacologically inhibited by competitive neuraminidase inhibitors, which impact its role in cellular signaling and disease[2][3].

Other names

Neuraminidase 3SIAL3ganglioside sialidasemembrane sialidaseN-acetyl-alpha-neuraminidase 3

Inhibition of sialidase/neuraminidase activity (by competitive inhibitors such as DANA); Modulation of ganglioside metabolism and downstream signaling pathways