Heparan sulfate-glucosamine 3-O-sulfotransferase 3A1 (HS3ST3A1)

Heparan sulfate-glucosamine 3-O-sulfotransferase 3A1 (HS3ST3A1) is a type II integral membrane enzyme that catalyzes the transfer of a sulfo group from the sulfate donor PAPS (3'-phosphoadenosine-5'-phosphosulfate) to the 3-O position of glucosamine residues within heparan sulfate chains. This modification leads to the generation of specific, highly sulfated domains in heparan sulfate, which regulate protein interactions vital for cell signaling, morphogenesis, and viral infection. HS3ST3A1 is widely expressed, with higher abundance in liver and placenta, and shows functional redundancy with related sulfotransferases. Loss of HS3ST3A1 in animal models affects epithelial tissue morphogenesis, growth factor signaling (notably FGF pathways), and can result in subtle secretory phenotypes such as glandular hypofunction. An established biological role includes contributing to cell-surface receptor function for Herpes simplex virus-1, facilitating viral entry. Direct drug targeting is not yet established, and systemic inhibition may have broad and complex effects due to this enzyme's central role in cellular and tissue biology.

Other names

Heparan sulfate glucosaminyl 3-O-sulfotransferase 3A13-O-sulfotransferase 3A13OST3A1HS3ST3AHeparin-glucosamine 3-O-sulfotransferaseh3-OST-3AHS3SAHeparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1

Not applicable for drugs, as there are no approved drugs known to target this enzyme directly. Experimental inhibition or genetic knockout leads to altered heparan sulfate sulfation patterns, affecting binding to viral proteins and growth factors.