ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 6 (ST8SIA6)

ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 6 (ST8SIA6) is a member of the glycosyltransferase 29 protein family and functions as an enzyme that specifically catalyzes the transfer of sialic acid residues to form α2,8-linked disialic acids on glycoconjugates. ST8SIA6 is unique among the six α2,8-sialyltransferases in that it generates disialic acids as terminal structures, and is responsible for producing ligands recognized by immune-inhibitory Siglec receptors, including murine Siglec-E and human Siglec-7 and -9. Overexpression of ST8SIA6 in tumors leads to increased formation of these glycans, altering macrophage polarization toward suppressive M2 phenotypes and inhibiting antitumor immune responses, thereby promoting tumor growth and correlating with decreased patient survival in several cancers. Alternative splicing results in multiple transcript variants, and the gene product is mainly localized intracellularly with diverse expression across tissues. No clinically approved drugs are currently known to selectively target ST8SIA6, but its role in immune evasion and tumorigenesis makes it a candidate for future therapeutic intervention[1][3][5].

Other names

ST8SIA6Alpha-2,8-sialyltransferase 8FSIAT8FSIAT8-FST8SiaVISialyltransferase 8FSialyltransferase St8Sia VIST8Sia VISIA8FST8SIA-VIsialyltransferase 8F (alpha-2,8-sialyltransferase)sialyltransferase St8Sia VI

No approved drugs directly targeting ST8SIA6; mechanisms could include inhibition of sialylation to enhance antitumor immunity (inferred from biology and enzyme function)