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ST6 beta-galactoside alpha-2,6-sialyltransferase 2 (ST6GAL2) is a type II transmembrane sialyltransferase enzyme primarily involved in the transfer of sialic acid from CMP-sialic acid to galactose-containing acceptors (particularly those with Gal-β-1,4-GlcNAc termini), producing alpha-2,6-linked sialylated oligosaccharides. ST6GAL2 is a member of the glycosyltransferase family 29 and displays a tissue-restricted expression pattern, being preferentially expressed in the human brain, especially in specific cerebral cortical regions, and to a lesser extent in other tissues. Unlike the broadly expressed ST6GAL1, ST6GAL2 has distinct substrate preference, favoring free disaccharides over protein-linked glycoconjugates and appears to play specialized roles in brain function and cell signaling during intestinal host-pathogen interactions. Genetic variants in ST6GAL2 have been associated with variability in response to antipsychotic treatment in schizophrenia, suggesting potential utility as a pharmacogenomic biomarker.
Drugs such as risperidone may have differential efficacy or side effect profiles in patients with specific ST6GAL2 polymorphisms; mechanism relates to impact on downstream glycosylation and cell signaling
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