5α-Reduction of Epitestosterone Is Catalyzed by Human SRD5A1 and SRD5A2 and Increases Androgen Receptor Transactivation

    Lina Schiffer, Wiebke Arlt, Karl‐Heinz Storbeck
    Studysummary This study found that epitestosterone, a stereoisomer of testosterone, is metabolized to 5α-dihydroepitestosterone by human 5α-reductase enzymes, which enhances its androgenic activity and reduces its antagonistic effect on testosterone-driven androgen receptor signaling.
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    Research cited in this study 4

    1. Intracrine Androgen Biosynthesis, Metabolism, and Action Revisited Molecular and Cellular Endocrinology · 2017
    2. Epitestosterone: Regulatory Roles in Androgen-Dependent Processes Journal of steroid biochemistry and molecular biology/˜The œJournal of steroid biochemistry and molecular biology · 2003
    3. Four-Amino Acid Segment in Steroid 5 Alpha-Reductase 1 Confers Sensitivity to Finasteride, a Competitive Inhibitor Journal of Biological Chemistry · 1992
    4. Epitestosterone—An Endogenous Antiandrogen? Journal of steroid biochemistry/Journal of Steroid Biochemistry · 1989

    Related research 1

    1. 5α-Reduction of Epitestosterone Is Catalyzed by Human SRD5A1 and SRD5A2 and Increases Androgen Receptor Transactivation The Journal of Steroid Biochemistry and Molecular Biology · 2024