Beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6) (ST3GAL6)

Beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6) is a Golgi-localized enzyme belonging to the sialyltransferase family, which catalyzes the transfer of sialic acid from CMP-sialic acid to the terminal galactose of type II disaccharides [UniProt: Q9Y274]. This enzymatic activity is essential for the biosynthesis of sialyl Lewis X (sLeX) epitopes, which serve as critical ligands for E-selectin-mediated cell adhesion [Harduin-Lepers et al., Glycobiology, 2001]. In clinical oncology, ST3GAL6 is significantly upregulated in multiple myeloma, where it promotes the homing of malignant plasma cells to the bone marrow and contributes to environment-mediated drug resistance [Glavey et al., Blood, 2014]. Beyond hematologic malignancies, its expression is linked to metastatic potential in breast and gastrointestinal cancers by facilitating tumor cell intravasation and extravasation [NCBI Gene: 10402]. The enzyme also plays a role in inflammatory responses by modulating the rolling and recruitment of leukocytes to sites of injury. Currently, there are no FDA-approved drugs that specifically target ST3GAL6, although it is a subject of research for the development of small-molecule glycomimetics and antisense oligonucleotides. Targeting ST3GAL6 represents a promising strategy to disrupt the interaction between cancer cells and the vascular endothelium, potentially overcoming chemoresistance and limiting metastatic spread. Its specific expression patterns also make it a potential biomarker for disease progression and therapeutic response.

Other names

ST3Gal VISIAT10Gal-beta-1,4-GlcNAc-alpha-2,3-sialyltransferase 6

Inhibition of the enzymatic transfer of sialic acid to galactose-containing substrates to prevent the formation of E-selectin ligands [Glavey et al., Blood, 2014].