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

ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) is a key glycosyltransferase enzyme that catalyzes the transfer of sialic acid in an α2,3 linkage onto galactose residues of O-glycans, specifically forming sialoglycan structures on glycoproteins and glycolipids[1][3][5]. This modification has wide-ranging effects on cellular recognition, migration, and immune modulation. ST3GAL1 expression is tightly regulated in hematopoietic differentiation and is upregulated in several cancers, including ovarian cancer where it contributes to cell migration, invasion, and resistance to chemotherapy (e.g., paclitaxel)[2][4]. Functional disruption of ST3GAL1 alters cell surface glycosylation, thereby influencing biological processes like immune cell contraction, dendritic cell function, and platelet formation. Variants in ST3GAL1 are also implicated in neuropsychiatric and inflammatory conditions[1][5]. As both a molecular biomarker and potential therapeutic target, ST3GAL1 represents an important locus for drug development and disease monitoring.

Other names

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1SIAT4SIAT4AAlpha 2,3-ST 1Beta-galactoside alpha-2,3-sialyltransferase 1ST3GalISIAT4-AST3OSIATFLST3GalA.1Gal-NAc6SGal-beta-1,3-GalNAc-alpha-2,3-sialyltransferaseMonosialoganglioside sialyltransferaseSialyltransferase 4AST3Gal IA

Inhibition of ST3GAL1 reduces sialylation, disrupting glycan structures that support cancer cell migration and chemoresistance. Modulation of ST3GAL1 may alter immune cell glycosylation and affect cell proliferation and differentiation.