Molecular changes induced by bisphenol-A in rat Sertoli cell culture

Bisphenol-A (BPA) is an industrial chemical and is known to act as an endocrine disrupter. This study was designed to evaluate how BPA regulates Sertoli cell (SC) signal molecules. Purified rat SCs were cultured and treated with BPA (200 mu mol/l) at various time points. Western blot analysis was used to determine the activation of extracellular signal-related kinases 1 and 2 (ERK1/2), c-Jun N-terminal kinase (JNK), p38 mitogen activated protein kinase (MAPK), nuclear factor kappa B (NF-kappa B), cyclooxygenase-1,2 (COX-1, 2), estrogen receptor-alpha (ER-alpha), and androgen receptor (AR). The levels of transferrin (TF), prostaglandin E(2) (PGE(2)), and prostaglandin F(2 alpha) (PGF(2 alpha)) in culture medium were quantified by ELISA. Interleukin (IL)-1 beta and IL-6 mRNAs were measured by quantitative real-time PCR (QRT-PCR). Compared with the control, BPA activated the phosphorylation of ERK1/2 (p-ERK1/2) through 30 min to 6 h. TF was down-regulated at 6 and 24 h. Furthermore, IL-1 beta was up-regulated at 30 min and IL-6 was up-regulated at 1 and 24 h. ERK activity inhibitor (PD98059, 10 mu mol/l) inhibited these molecular changes. These results reveal the possibility that BPA may have adverse effects on spermatogenesis via ERK1/2.