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Uronyl 2-sulfotransferase (UST) is an enzyme responsible for transferring sulfate groups to the 2-position of uronyl residues in glycosaminoglycans, such as iduronyl in dermatan sulfate and glucuronyl in chondroitin sulfate[3][7]. This sulfation is crucial for producing structurally diverse and functionally important domains within the extracellular matrix, especially within proteoglycans. UST activity alters cellular signaling by modifying the interaction of growth factors like FGF2 with their glycosaminoglycan co-receptors, thereby influencing processes such as cell migration and extracellular matrix dynamics[1]. Diseases and functional changes involving UST are suggested in certain neoplastic (e.g., breast fibroadenoma) and degenerative contexts, likely through disruption of glycosaminoglycan-mediated cellular activities[3][5][6]. There are currently no known drugs that specifically target UST, nor established biomarkers or significant safety concerns uniquely attributed to direct modulation of this enzyme.
Not established for drugs; general mechanism is enzymatic transfer of sulfate to sugar residues in glycosaminoglycans
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