ST3 beta-galactoside alpha-2,3-sialyltransferase 2 (ST3GAL2)

ST3 beta-galactoside alpha-2,3-sialyltransferase 2 (ST3GAL2) is a type II membrane-bound glycosyltransferase primarily located in the Golgi apparatus. It catalyzes the transfer of sialic acid from the donor substrate CMP-neuraminic acid to galactose-containing acceptors on glycoproteins and glycolipids, creating α2,3-glycosidic linkages. ST3GAL2 is essential for terminal sialylation of ganglio and globo series glycolipids (such as GD1a and GT1b), and it also modifies cell surface glycoproteins and glycolipids, impacting key antigens like SSEA4. The enzyme’s activity is critical for the composition of cell surface glycans that regulate cell migration, immune evasion, chemoresistance, and neuronal stability. Overexpression of ST3GAL2 has been linked to tumor progression, metastatic phenotype, and poor clinical prognosis, especially in kidney, breast, and brain cancers. No approved drugs currently target this enzyme, but it represents a potential therapeutic target due to its central role in cancer biology and neurological disease.

Other names

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2SIAT4BAlpha 2,3-ST 2Beta-galactoside alpha-2,3-sialyltransferase 2ST3GalIIST3GALIIST3GalA.2Gal-NAc6SMonosialoganglioside sialyltransferaseSialyltransferase 4BGal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase

If targeted, drugs would typically act as enzyme inhibitors to block glycan sialylation, potentially impacting cell surface antigenicity and cancer-related pathways. Modulation of immune recognition (via ganglioside sialylation, impacting Siglec signaling)