Heparan sulfate 6-O-sulfotransferase 3 (HS6ST3)

Heparan sulfate 6-O-sulfotransferase 3 (HS6ST3) is an enzyme that catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the 6-O position of the N-sulfoglucosamine residues in heparan sulfate glycosaminoglycans[3]. Through this enzymatic activity, HS6ST3 generates distinct sulfation patterns on heparan sulfate chains, which are critical for specific interactions with growth factors, cytokines, adhesion molecules, and structural proteins[3]. These interactions regulate diverse biological processes, including cell proliferation, differentiation, adhesion, migration, blood coagulation, and inflammation[3][4]. Genetic variation or dysregulation of HS6ST3 has been implicated in developmental disorders such as omodysplasia and idiopathic generalized epilepsy[3], and could theoretically contribute to other diseases through disruption of heparan sulfate–mediated cell signaling. While HS6ST3 is recognized as a member of a gene family (including HS6ST1 and HS6ST2), it possesses distinct substrate specificities and tissue expression patterns[2][3]. At present, there are no approved drugs specifically targeting HS6ST3, but its central role in heparan sulfate biosynthesis marks it as a potential therapeutic target for modifying extracellular matrix interactions or signaling pathways in regenerative medicine, oncology, and other fields[4].

Other names

HS6ST3Heparan-sulfate 6-O-sulfotransferase 3HS6ST-3

For potential future drugs: Inhibition or modulation of sulfotransferase activity, altering the sulfation pattern of heparan sulfate, and thereby modifying cellular functions or disease phenotypes[3]