ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 (ST6GALNAC5)

ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 (commonly abbreviated as ST6GALNAC5) is a Golgi-localized type II transmembrane sialyltransferase enzyme that catalyzes the transfer of sialic acid in an alpha-2,6 linkage to N-acetylgalactosaminide-containing glycolipids and glycoproteins[1]. ST6GALNAC5 plays a predominant role in the biosynthesis of α-series gangliosides, especially converting GM1b to GD1alpha, which is a compound involved in neural cell communication and adhesion within brain tissue[2][1]. The gene is normally expressed in the brain but is aberrantly upregulated in certain cancers, such as breast cancer, where its expression has been linked to enhanced capacity of cancer cells to transmigrate the blood–brain barrier and establish brain metastases[2]. Mutations in ST6GALNAC5 have also been implicated in rare familial cases of coronary artery disease[3]. Its broader expression and activity influence cell–cell interactions, mainly through sialylation of glycosphingolipids and the modulation of cell surface carbohydrate structures[1][2]. As of now, there are no approved drugs targeting ST6GALNAC5, but it remains a molecule of interest for therapeutic intervention in cancer metastasis and potentially in cardiovascular or neurological diseases.

Other names

Sialyltransferase 7ESIAT7EST6GalNAc VGD1 alpha synthaseGalNAc alpha-2,6-sialyltransferase VSialyltransferase 7 (alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase Ealpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5MGC3184SIAT7-EST6GalNAcV

Null