ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2 (ST8SIA2)

ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2 (ST8SIA2) is a type II membrane-bound glycosyltransferase enzyme responsible for catalyzing the transfer of sialic acid residues from CMP-sialic acid onto glycoproteins and N-linked oligosaccharides, playing a crucial role in the formation of polysialic acid chains[1][7]. Its key biological function is to add polysialic acid to neural cell adhesion molecule 1 (NCAM1), thereby regulating cell adhesion, neuronal migration, synaptic plasticity, and neural network formation during development[1][4][5][7]. Genetic variants or expression changes in ST8SIA2 are associated with an increased risk for neurodevelopmental and neuropsychiatric disorders, including schizophrenia, autism spectrum disorder, and epilepsy[4][5][7]. The enzyme is primarily expressed in the brain and is vital for proper nervous system development and function, with critical implications for cognition, behavior, and potentially cardiac physiology[1][2][4][5][7]. There are currently no known therapeutics that directly target ST8SIA2, though its pathway is modulated by certain psychiatric drugs and through genetic manipulation in research models[4]. Safety concerns center on its essential developmental role—alterations can result in significant neurodevelopmental abnormalities[4][5].

Other names

Alpha-2,8-sialyltransferase 8BSIAT8BST8SIA-IISTXSialyltransferase 8BSialyltransferase XSialyltransferase St8Sia II

Drugs can indirectly modulate the expression of polysialylated NCAM via altering ST8SIA2 expression (e.g., some antipsychotics in animal studies modulate PSA-NCAM levels). Genetic interventions (e.g., knockout or gene editing) in research settings. Not a direct pharmacological target as of current knowledge.