ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) (ST3GAL1)

ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) is a Golgi-resident enzyme that catalyzes the transfer of sialic acid from CMP-sialic acid to the Gal-beta-1,3-GalNAc (Core 1) structure of O-linked glycans (UniProt P11738). This enzyme plays a pivotal role in the terminal sialylation of glycoproteins, which influences cell-cell recognition, adhesion, and signaling (NCBI Gene ID: 6482). In oncology, ST3GAL1 is frequently upregulated and is associated with the synthesis of the sialyl-T antigen, a carbohydrate structure linked to increased tumor malignancy, metastasis, and poor prognosis in breast, ovarian, and gastric cancers (PubMed: 28652377, 30217934). Research indicates that ST3GAL1 promotes the epithelial-mesenchymal transition (EMT) and helps tumor cells evade immune detection by masking surface antigens (PubMed: 31434674). While no FDA-approved drugs specifically target ST3GAL1, experimental approaches including siRNA-mediated knockdown and antisense oligonucleotides (ASOs) are being explored to reduce its expression and inhibit tumor progression (PubMed: 25670301). Additionally, small molecule inhibitors like soyasaponin I have been used in research to study the effects of sialyltransferase inhibition, though achieving high specificity for the ST3GAL1 isoform remains a significant challenge in drug development.

Other names

SIAT4AST3GalIGal-beta-1,3-GalNAc-alpha-2,3-sialyltransferaseCMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1Alpha 2,3-ST 1Sialyltransferase 4A

Inhibition of sialyltransferase enzymatic activity or RNA-interference mediated knockdown of mRNA transcripts to prevent the formation of sialylated O-glycans and disrupt oncogenic signaling.