Carbohydrate sulfotransferase 7 (CHST7)

Carbohydrate sulfotransferase 7 (CHST7) is a member of the sulfotransferase enzyme family responsible for catalyzing the 6-O-sulfation of N-acetylgalactosamine (GalNAc) residues in chondroitin, a vital step in the biosynthesis of chondroitin sulfate glycosaminoglycans (GAGs). CHST7 acts within the Golgi apparatus, utilizing 3'-phospho-5'-adenylyl sulfate (PAPS) as a sulfate donor, and can also catalyze 6-O-sulfation of certain N-acetylglucosamine (GlcNAc) substrates. This regulated sulfation generates structural diversity among chondroitin sulfate chains, influencing key biological processes such as extracellular matrix assembly, cell–cell interactions, tissue repair, and immune response. Dysregulation of CHST7 expression or methylation is associated with various pathologies, including cancer metastasis (especially in colorectal and pituitary tumors), connective tissue diseases, and neurodevelopmental disorders (such as Waisman syndrome and spondyloepiphyseal dysplasia). CHST7’s role in biosynthetic regulation, tissue homeostasis, and disease indicates potential for future diagnostic and therapeutic targeting.

Other names

C6ST-2GST-5Chondroitin 6-sulfotransferase 2Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5N-acetylglucosamine 6-O-sulfotransferase 4GlcNAc6ST-4Gn6st-4C6ST2carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7chondroitin 6-sulfotransferase-2

Not established for drug interactions; theoretically, inhibitors or modulators would alter GAG sulfation, affecting cell signaling, extracellular matrix properties, and tissue homeostasis.