Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4 (CHST4)

Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4 (CHST4) is a Golgi-resident enzyme that catalyzes the transfer of sulfate groups to the 6-hydroxyl position of N-acetylglucosamine residues on glycoproteins, particularly O-linked mucin-type glycans. This post-translational modification is critical for the biosynthesis of specific sulfated carbohydrate ligands, such as sialyl 6-sulfo Lewis X, serving as binding domains for selectins, especially L-selectin, and thereby enabling lymphocyte homing and trafficking through high endothelial venules. CHST4 is regulated by inflammatory cytokines and its altered expression is implicated in cancer progression, inflammation, immunological diseases, and mucosal barrier function. It serves as both a functional enzyme in glycan biology and a potential disease biomarker, especially in cancer and immune-related disorders. No targeted therapeutics are currently approved for CHST4, but its roles in immunology and oncology continue to make it of interest for translational research

Other names

CHST4GST-3HEC-GlcNAc6STLSSTGlcNAc6ST-2Gn6st-2High endothelial cells N-acetylglucosamine 6-O-sulfotransferaseL-selectin ligand sulfotransferaseGalactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3GLCNAC6ST2HECGLCNAC6STGST3GlcNAc6ST2carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4carbohydrate sulfotransferase 4galactose/N-acetylglucosamine/N-acetylgalactosamine 6-O-sulfotransferase 3

No approved drugs directly target CHST4. Hypothetical approaches might include enzyme inhibition or modulation affecting glycan sulfation, but this is not documented in a clinical context.