{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T22:14:59Z","timestamp":1791670499403,"version":"4.3.4"},"reference-count":67,"publisher":"American Chemical Society (ACS)","issue":"3","license":[{"start":{"date-parts":[[2017,12,29]],"date-time":"2017-12-29T00:00:00Z","timestamp":1514505600000},"content-version":"vor","delay-in-days":1807,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Background: Bisphenol A (BPA) is a well-known endocrine disruptor that imperfectly mimics the effects of physiologic estrogens via membrane-bound estrogen receptors (mER\u03b1, mER\u03b2, and GPER\/GPR30), thereby initiating nongenomic signaling. Bisphenol S (BPS) is an alternative to BPA in plastic consumer products and thermal paper.<\/jats:p>\n                  <jats:p>Objective: To characterize the nongenomic activities of BPS, we examined signaling pathways it evoked in GH3\/B6\/F10 rat pituitary cells alone and together with the physiologic estrogen estradiol (E2). Extracellular signal-regulated kinase (ERK)\u2013 and c-Jun-N-terminal kinase (JNK)\u2013specific phosphorylations were examined for their correlation to three functional responses: proliferation, caspase activation, and prolactin (PRL) release.<\/jats:p>\n                  <jats:p>Methods: We detected ERK and JNK phosphorylations by fixed-cell immunoassays, identified the predominant mER initiating the signaling with selective inhibitors, estimated cell numbers by crystal violet assays, measured caspase activity by cleavage of fluorescent caspase substrates, and measured PRL release by radioimmunoassay.<\/jats:p>\n                  <jats:p>Results: BPS phosphoactivated ERK within 2.5 min in a nonmonotonic dose-dependent manner (10\u201315 to 10\u20137 M). When combined with 10\u20139 M E2, the physiologic estrogen\u2019s ERK response was attenuated. BPS could not activate JNK, but it greatly enhanced E2-induced JNK activity. BPS induced cell proliferation at low concentrations (femtomolar to nanomolar), similar to E2. Combinations of both estrogens reduced cell numbers below those of the vehicle control and also activated caspases. Earlier activation of caspase 8 versus caspase 9 demonstrated that BPS initiates apoptosis via the extrinsic pathway, consistent with activation via a membrane receptor. BPS also inhibited rapid (\u2264 1 min) E2-induced PRL release.<\/jats:p>\n                  <jats:p>Conclusion: BPS, once considered a safe substitute for BPA, disrupts membrane-initiated E2-induced cell signaling, leading to altered cell proliferation, cell death, and PRL release.<\/jats:p>","DOI":"10.1289\/ehp.1205826","type":"journal-article","created":{"date-parts":[[2013,1,17]],"date-time":"2013-01-17T08:50:01Z","timestamp":1358412601000},"page":"352-358","source":"Crossref","is-referenced-by-count":209,"title":["Bisphenol S Disrupts Estradiol-Induced Nongenomic Signaling in a Rat Pituitary Cell Line: Effects on Cell Functions"],"prefix":"10.1021","volume":"121","author":[{"given":"Ren\u00e9","family":"Vi\u00f1as","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Texas Medical Branch Galveston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cheryl S.","family":"Watson","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Texas Medical Branch Galveston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2013,1,17]]},"reference":[{"key":"2026080505053463600_micit1","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/0269-7491(93)90096-7","article-title":"Bioaccumulation of the lipophilic metabolites of nonionic surfactants in freshwater organisms.","volume":"79","author":"Ahel","year":"1993","journal-title":"Environ Pollut"},{"key":"2026080505053463600_micit2","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.molcel.2007.03.019","article-title":"Phosphorylation of caspase-9 by CDK1\/cyclin B1 protects mitotic cells against apoptosis.","volume":"26","author":"Allan","year":"2007","journal-title":"Mol Cell"},{"key":"2026080505053463600_micit3","doi-asserted-by":"crossref","first-page":"6063","DOI":"10.1111\/j.1742-4658.2009.07330.x","article-title":"Apoptosis and autophagy: regulation of caspase-9 by phosphorylation.","volume":"276","author":"Allan","year":"2009","journal-title":"FEBS J"},{"key":"2026080505053463600_micit4","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1038\/ncb1005","article-title":"Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK.","volume":"5","author":"Allan","year":"2003","journal-title":"Nat Cell Biol"},{"key":"2026080505053463600_micit5","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1289\/ehp.1001993","article-title":"Bisphenol A exposure during pregnancy disrupts glucose homeostasis in mothers and adult male offspring.","volume":"118","author":"Alonso-Magdalena","year":"2010","journal-title":"Environ Health Perspect"},{"issue":"4","key":"2026080505053463600_micit6","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1111\/j.1471-4159.2008.05491.x","article-title":"The roles of membrane estrogen receptor subtypes in modulating dopamine transporters in PC-12 cells.","volume":"106","author":"Alyea","year":"2008","journal-title":"J Neurochem"},{"key":"2026080505053463600_micit7","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1186\/1471-2202-10-59","article-title":"Nongenomic mechanisms of physiological estrogen-mediated dopamine efflux.","volume":"16","author":"Alyea","year":"2009","journal-title":"BMC Neurosci"},{"key":"2026080505053463600_micit8","unstructured":"Bisphenol A Global Industry Group\n          . 2002. 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