NEU2

NEU2, or neuraminidase 2, is a human gene that encodes an enzyme belonging to the sialidase (neuraminidase) family. Members of this family catalyze the hydrolysis of sialic acid residues from glycoproteins and glycolipids, thereby modulating the sialylation state of cellular surfaces and glycoconjugates.

NEU2 is described as a cytosolic sialidase, in contrast to the lysosomal neuraminidase NEU1 and the plasma membrane-associated NEU3. The encoded NEU2 enzyme possesses catalytic motifs common to sialidases and can remove terminal sialic acids from various substrates in vitro, potentially affecting protein stability, receptor interactions, and cell signaling through altered glycan patterns.

Expression studies have detected NEU2 transcripts and protein in multiple human tissues, with expression levels differing by tissue type and developmental context. The precise physiological roles of NEU2 in vivo are not fully characterized, but research suggests it participates in desialylation of cytosolic substrates and may influence signaling pathways and cellular interactions through changes in glycan composition.

Clinical and biomedical relevance remains an area of active investigation. Some studies have examined changes in NEU2 expression in cancer models and other disease contexts, but there is no widely established disease caused by NEU2 mutations or dysregulation. As part of the four-member human neuraminidase family (NEU1–NEU4), NEU2 contributes to the broader regulation of sialylation patterns important for cellular communication and metabolism.

In summary, NEU2 encodes a cytosolic sialidase distinct from other mammalian sialidases, contributing to the dynamic modulation of sialic acid residues on glycoconjugates with ongoing research to clarify its in vivo functions and clinical significance.