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Dehydroepiandrosterone sulfotransferase (SULT2A1) is the principal enzyme responsible for converting dehydroepiandrosterone (DHEA) into its sulfated form, dehydroepiandrosterone sulfate (DHEA-S), in the adrenal cortex and peripheral tissues. DHEA-S is the most abundant circulating steroid in humans and serves as a reservoir for the more biologically active DHEA. The regulation of SULT2A1 expression and activity is critical in determining adrenal androgen output. Genetic polymorphisms in SULT2A1 can modulate DHEA-S levels and are implicated in disorders such as polycystic ovary syndrome. Other enzymes and factors, including CYP17, HSD3B2, cytochrome b5, and regulatory transcription factors (e.g., SF-1, GATA-6, ERRα), modulate the broader steroidogenic pathway but are not exclusive regulators of DHEA-S. No known selective drugs directly target SULT2A1 in clinical practice, but modulation of steroidogenesis can have marked effects on DHEA-S levels. Monitoring DHEA-S serves as a biomarker in various endocrine disorders. In summary, to properly refer to the molecular target of "DHEA-S regulation," use dehydroepiandrosterone sulfotransferase (SULT2A1), not the regulatory process or the hormone itself.
Sulfotransferase activity: catalyzes sulfation of DHEA to DHEA-S, affecting the relative circulating levels of these steroids
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