ST3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6)

ST3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6) is a glycosyltransferase enzyme responsible for catalyzing the transfer of sialic acid in an α2-3 linkage to terminal β-galactoside residues on glycoproteins and glycolipids, influencing the synthesis of selectin ligands such as sialyl Lewis X. This modification plays a critical role in mediating cell–cell and cell–matrix interactions, particularly those involving cell adhesion, migration, and trafficking in both physiological and pathological contexts. In cancer, especially multiple myeloma and lung adenocarcinoma, altered expression or activity of ST3GAL6 affects tumor cell homing, metastasis, and survival, making it a potential biomarker and therapeutic target. Its inhibition reduces surface α2-3 sialylation and impairs cancer cell adhesion and migration, but could also have consequences for normal cellular and immune functions due to its central role in glycosylation.

Other names

Type 2 lactosamine alpha-2,3-sialyltransferaseSIAT10ST3GalVIST3GALVICMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VISialyltransferase 10alpha2,3-sialyltransferase ST3Gal VIsialyltransferase 10 (alpha-2,3-sialyltransferase VI)

Sialyltransferase inhibitors would block the enzymatic transfer of sialic acid, potentially disrupting selectin ligand formation and thereby affecting cell adhesion, migration, and metastatic potential.