Carbohydrate sulfotransferase 9 (CHST9)

Carbohydrate sulfotransferase 9 (CHST9) is a Golgi-localized membrane-associated enzyme responsible for catalyzing the transfer of sulfate to the 4-position of non-reducing N-acetylgalactosamine (GalNAc) residues on N- and O-linked glycans[1][3][5]. This sulfation is crucial for the functional diversification of glycoproteins, glycolipids, and proteoglycans, thereby affecting processes such as cell-cell interaction, signal transduction, and embryonic development[1][3][5]. CHST9 plays a specific role in the biosynthesis of glycoprotein hormones in the pituitary gland, including lutropin and thyrotropin, by modifying their carbohydrate structures[1][5]. CHST9 is considered a molecular marker for a unique subpopulation of striatal medium spiny neurons, indicating restricted expression and potential utility in neuroscience research[2]. Dysfunction or altered expression of CHST9 and related sulfotransferases have been associated with cancer, connective tissue diseases, and other pathologies related to extracellular matrix composition and hormone biosynthesis[5].

Other names

GalNAc-4-O-sulfotransferase 2GalNAc-4-ST2GalNAc4ST-2N-acetylgalactosamine-4-O-sulfotransferase 2carbohydrate (N-acetylgalactosamine 4-O) sulfotransferase 9UNQ2549/PRO6175

Inhibitors would suppress sulfation of N-acetylgalactosamine residues, affecting glycoprotein hormone biosynthesis and extracellular matrix modifications[5].