Carbohydrate sulfotransferase 12 (CHST12)

Carbohydrate sulfotransferase 12 (CHST12) is an enzyme localized in the Golgi apparatus that catalyzes the sulfation of the 4-position of N-acetylgalactosamine residues within chondroitin, a glycosaminoglycan component of the extracellular matrix. This modification is critical for the structural integrity and signaling functions of proteoglycans in tissues such as cartilage and may play a regulatory role in cell adhesion, migration, and extracellular signaling. CHST12 has emerged as a potential therapeutic target and biomarker in oncology, as its dysregulation contributes to enhanced tumor proliferation, migration, and immune microenvironment modulation, particularly in glioblastoma multiforme and pancreatic cancer. Its overexpression in tumors is associated with poorer clinical outcomes and may influence the efficacy of immunotherapy by affecting immune checkpoint molecule expression and immune cell infiltration[1][2][3][4].

Other names

CHST12UNQ500/PRO1017C4ST-2C4ST2C4S-2Chondroitin 4-O-sulfotransferase 2Chondroitin 4-sulfotransferase 2Sulfotransferase HloCarbohydrate (chondroitin 4) sulfotransferase 12

For research targeting CHST12 (e.g., in GBM): Inhibition or knockdown of CHST12 reduces tumor cell proliferation and mobility, likely by modifying the Wnt/β-catenin signaling pathway May affect immune cell infiltration and immune checkpoint expression, suggesting indirect modulation of tumor immune microenvironment