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To identify the CYP isoforms involved in the production of 2-hydroxyestradiol 17-sulfate (2-OH-ES), which we assume to be an antioxidant in vivo, the 2-hydroxylation reaction of estradiol 17-sulfate (ES) by human liver microsome was investigated. As a result, it was estimated that CYP2C8 and 2C9 were largely involved in the production of 2-OH-ES. Therefore, the 2-hydroxylation kinetic analysis of ES was performed for both CYPs, and the metabolic clearance V max /K m (µL/nmol CYP/min) was determined. On comparing the results of ES with those of estradiol (E2), it was found that CYP2C8 was about 2.5 times higher and CYP2C9 was about 3 times higher, and ES was more likely to be a substrate for the 2-hydroxylation reaction by both CYPs. The CYP isoforms involved in A-ring hydroxylation of E2 and ES differed. From this, it was speculated that 2-OH-ES plays a different role to 2-hydroxyestradiol (2-OH-E2), which is recognized as an antioxidant in the body.

Comparison on Metabolism of Estradiol and Its 17-Sulfate by Recombinant Human CYP Isoforms