Wu Juanjuan, Williams Devin, Walter Grant A, Thompson Winston E, Sidell Neil
Department of Gynecology & Obstetrics, Emory University School of Medicine, 101 Woodruff Circle, Suite 4211 WMB, Atlanta, GA 30322, United States.
Department of Obstetrics & Gynecology, Morehouse School of Medicine, Atlanta, GA 30310, United States.
Exp Cell Res. 2014 Nov 1;328(2):351-60. doi: 10.1016/j.yexcr.2014.08.030. Epub 2014 Aug 27.
The actions of the transcription factor Nuclear factor erythroid 2-related factor (Nrf2) in breast cancer have been shown to include both pro-oncogenic and anti-oncogenic activities which is influenced, at least in part, by the hormonal environment. However, direct regulation of Nrf2 by steroid hormones (estrogen and progesterone) has received only scant attention. Nrf2 is known to be regulated by its cytosolic binding protein, Kelch-like ECH-associated protein 1 (Keap1), and by a Keap1-independent mechanism involving a series of phosphorylation steps mediated by phosphatidylinositol 3-kinase (PI3K) and glycogen synthase kinase 3 beta (GSK3β). Here, we report that estrogen (E2) increases Nrf2 activity in MCF7 breast cancer cells through activation of the PI3K/GSK3β pathway. Utilizing antioxidant response element (ARE)-containing luciferase reporter constructs as read-outs for Nrf2 activity, our data indicated that E2 increased ARE activity >14-fold and enhanced the action of the Nrf2 activators, tertiary butylhydroquinone (tBHQ) and sulforaphane (Sul) 4 to 9 fold compared with cells treated with tBHQ or Sul as single agents. This activity was shown to be an estrogen receptor-mediated phenomenon and was antagonized by progesterone. In addition to its action on the reporter constructs, mRNA and protein levels of heme oxygenase 1, an endogenous target gene of Nrf2, was markedly upregulated by E2 both alone and in combination with tBHQ. Importantly, E2-induced Nrf2 activation was completely suppressed by the PI3K inhibitors LY294002 and Wortmannin while the GSK3β inhibitor CT99021 upregulated Nrf2 activity. Confirmation that E2 was, at least partly, acting through the PI3K/GSK3β pathway was indicated by our finding that E2 increased the phosphorylation status of both GSK3β and Akt, a well-characterized downstream target of PI3K. Together, these results demonstrate a novel mechanism by which E2 can regulate Nrf2 activity in estrogen receptor-positive breast cancer cells and suggest that patients׳ hormonal status through this activity may play a significant role in some therapeutic outcomes.
转录因子核因子红细胞2相关因子(Nrf2)在乳腺癌中的作用已被证明兼具促癌和抗癌活性,这至少部分受激素环境的影响。然而,类固醇激素(雌激素和孕激素)对Nrf2的直接调控却很少受到关注。已知Nrf2受其胞质结合蛋白kelch样ECH相关蛋白1(Keap1)调控,同时也通过一种不依赖Keap1的机制进行调控,该机制涉及由磷脂酰肌醇3激酶(PI3K)和糖原合酶激酶3β(GSK3β)介导的一系列磷酸化步骤。在此,我们报告雌激素(E2)通过激活PI3K/GSK3β途径增加MCF7乳腺癌细胞中的Nrf2活性。利用含抗氧化反应元件(ARE)的荧光素酶报告基因构建体作为Nrf2活性的读出指标,我们的数据表明,与单独用叔丁基对苯二酚(tBHQ)或萝卜硫素(Sul)处理的细胞相比,E2使ARE活性增加了14倍以上,并使Nrf2激活剂tBHQ和Sul的作用增强了4至9倍。这种活性被证明是一种雌激素受体介导的现象,并受到孕激素的拮抗。除了对报告基因构建体的作用外,Nrf2的内源性靶基因血红素加氧酶1的mRNA和蛋白水平在E2单独作用以及与tBHQ联合作用时均显著上调。重要的是,PI3K抑制剂LY294002和渥曼青霉素完全抑制了E2诱导的Nrf2激活,而GSK3β抑制剂CT99021上调了Nrf2活性。我们发现E2增加了GSK3β和Akt的磷酸化状态,Akt是PI3K一个特征明确的下游靶点,这表明E2至少部分是通过PI3K/GSK3β途径发挥作用。总之,这些结果证明了一种新机制,即E2可在雌激素受体阳性乳腺癌细胞中调节Nrf2活性,并表明患者的激素状态通过这种活性可能在某些治疗结果中发挥重要作用。
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