Sult1d1, a member of the sulfotransferase superfamily, plays a crucial role in the inactivation of endogenous dopamine-derived compounds, including catecholamines. It is involved in detoxification processes and may be associated with stress response and metabolic regulation pathways. Genetically modified mouse models have been valuable for studying its functions [1,2,3,4].

In mice, Sult1d1 is directly induced by glucocorticoids. Dexamethasone treatment in wild-type mice significantly increases Sult1d1 mRNA levels in the liver and kidney within 6 hours, and this induction is blocked by the GR antagonist RU-486. Sult1d1 mRNA localizes to renal collecting ducts and its enzymatic activity is induced in vivo after dexamethasone treatment. Knockout of Sult1d1 in mice leads to a 99% decrease in renal activation of 1-hydroxymethylpyrene, a genotoxicant, and reduces plasma 1-sulfooxymethylpyrene levels as well as DNA adduct formation in some tissues. In the context of 4-aminobiphenyl (ABP), a human bladder carcinogen, knocking out both Sult1a1 and Sult1d1 almost totally eliminates the gender gap in bladder susceptibility to ABP in mice, accompanied by a dramatic decrease in ABP genotoxicity in the liver [1,2,3,4].

In conclusion, Sult1d1 is essential for the inactivation of catecholamines and is responsive to glucocorticoids. Gene-knockout mouse models have revealed its role in the metabolic activation of genotoxicants and in the gender-related susceptibility to bladder carcinogens. These findings contribute to understanding the biological functions of Sult1d1 and its implications in disease-related metabolic processes.