The inhibition of steroid and phenol sulfotransferase activities in human liver cytosol by a wide range of commonly used drugs was studied. Dehydroepiandrosterone (DHEA) and estrone sulfotransferase activities were strongly inhibited by a number of compounds, with IC50values ranging between 440 pM and 147 μM. For DHEA sulfotransferase, clomiphene, testosterone, danazol and spironolactone were the best inhibitors, with IC50values less than 5 μM, wherease for estrone sulfotransferase cyclizine, ibuprofen, chlorpheniramine and dimenhydrinate resulted in the strongest inhibition, again with IC50values of less majority of the drugs which inhibited steroid ST activities strongly were either synthetic steroids, antisteroidals or were tertiary amine drugs such as tricyclic antidepressants and antihistamines, many of which exhibit adverse side effects manifesting particularly as sexual dysfunction and disruption of hormone action in clinical use. The importance of these findings for our understanding of the molecular basis of adverse drug reactions is discussed. © 1992.
Bamforth, K. J., Dalgliesh, K., & Coughtrie, M. W. H. (1992). Inhibition of human liver steroid sulfotransferase activities by drugs: a novel mechanism of drug toxicity? European Journal of Pharmacology: Environmental Toxicology And, 228(1), 15–21. https://doi.org/10.1016/0926-6917(92)90006-X