Kavarthapu Raghuveer, Dufau Maria L
Section on Molecular Endocrinology, Eunice Kennedy Schriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-4510, USA.
Oncotarget. 2017 Apr 18;8(16):27353-27363. doi: 10.18632/oncotarget.16040.
Our early studies have shown that Estradiol (E2)/Estrogen Receptor α (ER) in a non-DNA dependent manner through complex formation with C/EBPβ/SP1 induced transcriptional activation of the generic hPIII promoter and expression of the Prolactin Receptor (PRLR) receptor in MCF-7 cells. Subsequent studies demonstrated effects of unliganded ERα with requisite participation of endogenous PRL on the activation of PRLR transcription. Also, EGF/ERBB1 in the absence of PRL and E2 effectively induced upregulation of the PRLR. In this study we have delineated the transcriptional mechanism of upregulation of PRLR receptor induced by E2 incorporating knowledge of the various transcriptional upregulation modalities from our previous studies. Here, we demonstrate an essential requirement of STAT5a induced by PRL via PRLR receptor which associates at the promoter and its interaction with phoshoERα S118. Knock-down of PRL by siRNA significantly reduced E2-induced PRLR promoter activity, mRNA and protein expression, recruitment of ERα to the complex at promoter, C/EBPβ association to its DNA site and productive complex formation at hPIII promoter. The specific CDK7 inhibitor (THZ1) that attenuates E2-induced ERα phosphorylation at S118 abrogated E2-induced PRLR promoter activation. Further studies demonstrated that E2 induced cell migration was inhibited by PRL siRNA and THZ1 indicating its dependence on PRL/PRLR and CDK7, respectively. Our studies have demonstrated the essential role of endogenous PRL and CDK7 in the upregulation of PRLR by E2 and provide insights for therapeutic approaches that will mitigate the transcription/expression of PRLR and its participation in breast cancer progression fueled by E2 and PRL via their cognate receptors.
我们早期的研究表明,雌二醇(E2)/雌激素受体α(ER)以非DNA依赖的方式,通过与C/EBPβ/SP1形成复合物,诱导MCF-7细胞中通用hPIII启动子的转录激活和催乳素受体(PRLR)的表达。随后的研究表明,未结合配体的ERα在内源性催乳素的必要参与下,对PRLR转录的激活有影响。此外,在没有催乳素和E2的情况下,表皮生长因子/表皮生长因子受体1(EGF/ERBB1)能有效诱导PRLR的上调。在本研究中,我们结合之前研究中各种转录上调模式的知识,阐述了E2诱导PRLR受体上调的转录机制。在这里,我们证明了催乳素通过PRLR受体诱导的信号转导和转录激活因子5a(STAT5a)的重要需求,该受体在启动子处结合,并与磷酸化的ERα S118相互作用。通过小干扰RNA(siRNA)敲低催乳素可显著降低E2诱导的PRLR启动子活性、mRNA和蛋白表达,ERα募集到启动子复合物、C/EBPβ与其DNA位点的结合以及hPIII启动子处有效复合物的形成。特异性细胞周期蛋白依赖性激酶7(CDK7)抑制剂(THZ1)可减弱E2诱导的ERα在S118位点的磷酸化,从而消除E2诱导的PRLR启动子激活。进一步的研究表明,E2诱导的细胞迁移分别被催乳素siRNA和THZ1抑制,表明其分别依赖于催乳素/PRLR和CDK7。我们的研究证明了内源性催乳素和CDK7在E2上调PRLR中的重要作用,并为治疗方法提供了思路,这些方法将减轻PRLR的转录/表达及其通过同源受体参与E2和催乳素驱动的乳腺癌进展。