β-1,3-GalNAc-T2 Activators

Beta-1,3-N-acetylgalactosaminyltransferase 2 (B3GALNT2) is an enzyme responsible for initiating the synthesis of mucin-type O-glycans in glycoproteins. This enzyme catalyzes the transfer of N-acetylgalactosamine (GalNAc) to serine or threonine residues on proteins, a fundamental step in the biosynthesis of the glycan moiety of proteoglycans. B3GALNT2's activity is crucial for the proper function of mucin-type O-glycans, which are involved in numerous biological processes, including cell adhesion, protein stability, and the immune response.O-glycosylation, the type of enzymatic activity carried out by B3GALNT2, is a post-translational modification that adds carbohydrate structures to proteins, dramatically altering their properties and interactions. This modification is diverse and complex, leading to a multitude of glycan structures with various functions. B3GALNT2 specifically contributes to the formation of core 1 structures, commonly known as T-antigens, which are precursors for more complex glycan branches.

The regulation of B3GALNT2 is vital, as aberrant O-glycosylation can lead to diseases such as cancer and congenital disorders of glycosylation. It is expressed in various tissues, with significant roles in muscle and brain development. Mutations in the B3GALNT2 gene have been linked to muscular dystrophy-dystroglycanopathy, underscoring the enzyme's importance in muscle function and development.