TY - JOUR
T1 - Bisphenol A-induced apoptosis of cultured rat Sertoli cells
AU - Iida, Hiroshi
AU - Maehara, Kazue
AU - Doiguchi, Masamichi
AU - Mõri, Takayuki
AU - Yamada, Fumio
N1 - Funding Information:
This work was supported by Grants for ‘Integrated research program on effects of endocrine disrupters on agriculture, forestry and fisheries and their mechanisms of action on domestic animals and fishes’ and by Takeda Science Foundation.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2003
Y1 - 2003
N2 - Bisphenol A (BPA) was examined for its effects on cultured Sertoli cells established from 18-day-old rat testes. We demonstrated that exposure of cultured Sertoli cells to BPA decreased the cell viability in a dose- and a time-dependent manner and that exposure to BPA brought about morphologic changes of the cells, such as membrane blebs, cell rounding, cytoskeletal collapse, and chromatin condensation or fragmentation, all of which conform to the morphologic criteria for apoptosis. Immunocytochemistry showed that active caspase-3, a major execution caspase, was expressed in round Sertoli cells positively labeled by the TUNEL method. Co-localization of active caspase-3 and aggregated actin fragments was also observed in the round Sertoli cells. Theses results suggest that BPA induces cell death of Sertoli cells by promoting apoptosis. Apoptosis-inducing cell death was observed in cells exposed to 150-200 μM BPA, while BPA at < 100 μM had only slight cytotoxic effects on the cells.
AB - Bisphenol A (BPA) was examined for its effects on cultured Sertoli cells established from 18-day-old rat testes. We demonstrated that exposure of cultured Sertoli cells to BPA decreased the cell viability in a dose- and a time-dependent manner and that exposure to BPA brought about morphologic changes of the cells, such as membrane blebs, cell rounding, cytoskeletal collapse, and chromatin condensation or fragmentation, all of which conform to the morphologic criteria for apoptosis. Immunocytochemistry showed that active caspase-3, a major execution caspase, was expressed in round Sertoli cells positively labeled by the TUNEL method. Co-localization of active caspase-3 and aggregated actin fragments was also observed in the round Sertoli cells. Theses results suggest that BPA induces cell death of Sertoli cells by promoting apoptosis. Apoptosis-inducing cell death was observed in cells exposed to 150-200 μM BPA, while BPA at < 100 μM had only slight cytotoxic effects on the cells.
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U2 - 10.1016/S0890-6238(03)00034-0
DO - 10.1016/S0890-6238(03)00034-0
M3 - Article
C2 - 12849858
AN - SCOPUS:0038442153
VL - 17
SP - 457
EP - 464
JO - Reproductigve Toxicoloy
JF - Reproductigve Toxicoloy
SN - 0890-6238
IS - 4
ER -