Neuraminidase-1 (NEU1)

Neuraminidase-1 (NEU1) is a lysosomal sialidase enzyme responsible for hydrolyzing terminal sialic acid residues from glycoproteins and glycolipids, thus regulating the structure and function of a variety of cell surface and lysosomal molecules[2][3][5][6]. NEU1 is most abundant in lysosomes, but also exists on the plasma membrane, where it modulates multiple physiological processes, including receptor activation, immune cell signaling, elastin fiber assembly, and metabolic regulation[1][3][4][5]. Dysfunction or genetic deficiency of NEU1 is implicated in lysosomal storage diseases such as sialidosis and galactosialidosis, as well as in certain cardiovascular, neurodegenerative, and oncological diseases[1][4][5]. The enzyme’s activation, stability, and correct cellular localization critically depend on its interaction with protective protein cathepsin A (PPCA) and β-galactosidase, forming a multi-enzyme complex essential for full NEU1 activity[1][5]. The ability of NEU1 to remodel cell surface glycosylation directly impacts immune and signaling pathways and has made it an emerging therapeutic target for a variety of diseases, including inflammation and neurodegeneration[1][4][5].

Other names

Sialidase-1NANHAcetylneuraminyl hydrolaseG9 sialidaseLysosomal sialidaseN-acetyl-alpha-neuraminidase 1SIAL1exo-alpha-sialidase

Inhibition of sialidase/neuraminidase activity, Modulation of cell-surface and lysosomal sialic acid removal, Alteration of receptor desialylation and downstream signaling