Carbohydrate sulfotransferase 2 (CHST2)

Carbohydrate sulfotransferase 2 (CHST2) is a Golgi-localized type II transmembrane enzyme that catalyzes the transfer of sulfate from the donor molecule 3'-phospho-5'-adenylyl sulfate (PAPS) to the 6-position of non-reducing N-acetylglucosamine (GlcNAc) residues in glycan chains, especially within keratan sulfate and mucin-associated glycans[1][2][3][8]. CHST2 is essential for biosynthesis of the 6-sulfosialyl Lewis X antigen, a critical ligand for selectin-mediated lymphocyte homing and trafficking, particularly in high endothelial venules[1][2]. Active in a range of tissues, CHST2 plays vital roles in immune cell homing and inflammation; its activity creates glycans recognized by the MECA79 antibody, important for immune surveillance[2]. Overexpression of CHST2 has been shown to enhance tumor cell migration and metastasis, especially in breast cancer, indicating a role in cancer progression via modulation of cell surface glycan structures involved in cell–cell interactions and metastatic dissemination[2]. No specific drugs targeting CHST2 are currently identified, but inhibition of its enzymatic activity can impact glycan sulfation patterns, with downstream effects on immune and tumor cell behavior[2][4].

Other names

GN6STGST-2GlcNAc6ST-1Gn6ST-1C6STGalactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2N-acetylglucosamine 6-O-sulfotransferase 1HEL-S-75GST2AI428561AW121776C130041E03RIKglcNAc6STcarbohydrate sulphotransferase 2Chts2LOC100044297

Inhibition of sulfotransferase activity to block cell surface glycan sulfation; Potential modulation of selectin ligand functionality