Abstract

In human, previous pharmacokinetic studies have shown the metabolism of 17α‐ethinylestradiol (EE2) through sulfation, with estrogen sulfotransferase (SULT1E1). Since SULT1E1 is a major responsible enzyme that mediates the biotransformation of endogenous estrogens and estrogen‐like drugs, genetic polymorphisms of SULT1E1 may significantly impact the 17α‐ethinylestradiol‐sulfating activity by SULT1E1. Subsequently, this study was performed to investigate the implications of SULT1E1 genetic polymorphisms in the sulfation of 17α‐ethinylestradiol. By using the site directed mutagenesis technique, five selected recombinant SULT1E1 allozymes were generated, expressed and purified. Compared with the wild‐type SULT1E1, purified allozymes of SULT1E1 were shown to exhibit significantly distinct sulfating activity with 17α‐Ethinylestradiol as a substrate. In summary, the obtained results provide evidence related to differential metabolism of 17α‐ethinylestradiol in individuals with different SULT1E1 genotypes, which may be useful for further in‐vivo study contributed to the therapeutic‐ as well as adverse effects of 17α‐ethinylestradiol through sulfation.Support or Funding InformationThe College of Pharmacy, University of ToledoThis abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.

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