ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3 (ST8SIA3)

ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3 (ST8SIA3) is a membrane-associated glycosyltransferase of the sialyltransferase family, catalyzing the addition of α2,8-linked sialic acids to glycoproteins and glycolipids, notably within the striatum. This enzyme modulates the distribution and interactions of crucial signaling proteins including dopamine and adenosine receptors, influencing motor function and neurochemical communication[1]. It forms disialylated and trisialylated glycotopes rather than long polysialic acid chains, which are the hallmark of other family members. Its emerging role in neurological diseases and potential as a cancer target is tied to its regulation of membrane microdomains and cell-cell interactions through glycosylation events[1][3]. While drugs targeting ST8SIA3 are not yet clinically validated, its modulatory role in systems biology and disease suggests it is a promising target for therapeutic intervention and research.

Other names

ST8SIA3SIAT8CST8SiaIIIAlpha-2,8-sialyltransferase 8CAlpha-2,8-sialyltransferase IIIhST8Sia IIISialyltransferase 8CSialyltransferase St8Sia IIIGanglioside GD3 synthase ST8SIA3Other variants as listed in query

Potential mechanisms would involve inhibition of sialylation, which alters membrane protein distribution, protein-protein interaction, and downstream signaling in relevant cell types[1][3].