Premium
Bisphenol A stimulates steroidogenic acute regulatory protein expression via an unknown mechanism in adrenal cortical cells
Author(s) -
Medwid Samantha,
Guan Haiyan,
Yang Kaiping
Publication year - 2019
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.27574
Subject(s) - steroidogenic acute regulatory protein , medicine , endocrinology , cholesterol side chain cleavage enzyme , biology , messenger rna , antagonist , estrogen receptor , endocrine disruptor , receptor , endocrine system , chemistry , hormone , gene , cytochrome p450 , biochemistry , metabolism , breast cancer , cancer
Bisphenol A (BPA) is one of the most widespread endocrine disrupting chemicals in the environment. Exposure to BPA is known to be associated with disruption of steroidogenesis in reproductive tissues, but little is known about its effects on the adrenal gland. We previously showed that prenatal BPA exposure resulted in elevated plasma corticosterone levels concomitant with increased adrenal levels of steroidogenic acute regulatory protein (StAR), the rate‐limiting step in steroidogenesis, in adult female mouse offspring. However, the molecular mechanisms underlying the BPA‐induced StAR protein expression in the adrenal gland remain unknown. Therefore, the current study was designed to address this important question using the human cortical cell line, H295A cells, as an in vitro model system. We found that: (1) BPA increased StAR protein levels in a dose‐dependent manner; (2) both estrogen receptor alpha (ERα)‐ and ERβ‐specific agonists mimicked while the ER antagonist ICI abrogated the stimulatory effects of BPA on StAR protein levels; and (3) BPA did not alter StAR messenger RNA, 37kDa preprotein or protein half‐life. Taken together, these findings demonstrate that BPA increases StAR protein levels through an unknown mechanism independent of StAR gene transcription, translation, and protein half‐life. Furthermore, such effects are likely mediated by ERα and/or ERβ.