Polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2)

Polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) is an enzyme of the glycosyltransferase family that initiates mucin-type O-linked glycosylation, catalyzing the transfer of N-acetylgalactosamine to serine or threonine residues of proteins in the Golgi apparatus[1][2][6]. This process is crucial for the production and function of many glycoproteins, including those involved in lipid metabolism and receptor signaling. Genetic and epigenetic variations in GALNT2 influence plasma lipoprotein profiles, impacting high-density lipoprotein (HDL) cholesterol and triglyceride levels, and thereby modulating cardiovascular disease risk[1][4]. GALNT2 also regulates the glycosylation and signaling of growth factor receptors such as EGFR and MET, influencing cell proliferation, migration, and malignancy in specific cancers. Its altered expression or activity is implicated in a range of diseases including cardiovascular disease, cancer, type 2 diabetes, and immune-mediated disorders[1][4]. GALNT2 is essential for metabolic and inflammatory homeostasis, with its mutations or dysregulation contributing to disease susceptibility and progression[1].

Other names

Polypeptide N-acetylgalactosaminyltransferase 2GalNAc-T2pp-GaNTase 2polypeptide GalNAc transferase 2protein-UDP acetylgalactosaminyltransferase 2UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2CDG2T

Not applicable; enzymes like GALNT2 are not typical direct drug targets, but inhibitors would likely act as enzyme inhibitors of glycosyltransferase activity.