Carbohydrate sulfotransferase 8 (CHST8)

Carbohydrate sulfotransferase 8 (CHST8) is a Golgi-resident enzyme responsible for catalyzing the transfer of sulfate to the 4-position of non-reducing terminal N-acetylgalactosamine (GalNAc) residues present in both N-glycans and O-glycans. It is primarily expressed in the pituitary gland and is crucial for the appropriate sulfation of glycoprotein hormones, particularly lutropin (luteinizing hormone, LH) and thyrotropin (TSH), which is required for their biologic activity. CHST8-mediated sulfation also has important roles in cell–cell signaling, extracellular matrix maintenance, and immune response modulation. Genetic alterations in CHST8 are implicated in rare congenital skin disorders and recent studies suggest a role in the tumor immune microenvironment—especially in breast cancer, where CHST8 activity influences immune cell infiltration and response to immune checkpoint blockade therapies. CHST8 thus constitutes a potential biomarker and emerging therapeutic target in oncology and immunology

Other names

GalNAc-4-O-sulfotransferase 1GalNAc4ST-1N-acetylgalactosamine-4-O-sulfotransferase 1carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 8PSS3GALNAC4ST-1GalNAc-4-ST1GALNAC4ST1GalNAc4STgalNAc4ST-1

Inhibition or modulation of glycan sulfation on hormones and cell surface proteins Potential immune modulation via altered sulfation of PD-L1 and related immune checkpoint proteins, affecting T cell activation and macrophage polarization in tumors