Rajhans Rajib, Nair Hareesh B, Nair Sujit S, Cortez Valerie, Ikuko Kijima, Kirma Nameer B, Zhou Dujin, Holden Alan E, Brann Darrell W, Chen Shiuan, Tekmal Rajeshwar Rao, Vadlamudi Ratna K
Department of Obstetrics and Gynecology, University of Texas Health Science Center, Floyd Curl Drive, San Antonio, Texas 78229-3900, USA.
Mol Endocrinol. 2008 Mar;22(3):649-64. doi: 10.1210/me.2007-0350. Epub 2007 Dec 13.
In situ estrogen synthesis is implicated in tumor cell proliferation through autocrine or paracrine mechanisms especially in postmenopausal women. Several recent studies demonstrated activity of aromatase, an enzyme that plays a critical role in estrogen synthesis in breast tumors. Proline-, glutamic acid-, and leucine-rich protein-1 (PELP1/MNAR) is an estrogen receptor (ER) coregulator, and its expression is deregulated in breast tumors. In this study, we examined whether PELP1 promotes tumor growth by promoting local estrogen synthesis using breast cancer cells (MCF7) that stably overexpress PELP1. Immunohistochemistry revealed increased aromatase expression in MCF7-PELP1-induced xenograft tumors. Real-time PCR analysis showed enhanced activation of the aromatase promoter in MCF7-PELP1 clones compared with MCF7 cells. Using a tritiated-water release assay, we demonstrated that MCF7-PELP1 clones exhibit increased aromatase activity compared with control MCF-7 cells. PELP1 deregulation uniquely up-regulated aromatase expression via activation of aromatase promoter I.3/II, and growth factor signaling enhanced PELP1 activation of aromatase. PELP1-mediated induction of aromatase requires functional Src and phosphatidylinositol-3-kinase pathways. Mechanistic studies revealed that PELP1 interactions with ER-related receptor-alpha and proline-rich nuclear receptor coregulatory protein 2 lead to activation of aromatase. Immunohistochemistry analysis of breast tumor array showed increased expression of aromatase in ductal carcinoma in situ and node-positive tumors compared with no or weak expression in normal breast tissue. Fifty-four percent (n = 79) of PELP1-overexpressing tumors also overexpressed aromatase compared with 36% (n = 47) in PELP1 low-expressing tumors. Our results suggest that PELP1 regulation of aromatase represents a novel mechanism for in situ estrogen synthesis leading to tumor proliferation by autocrine loop and open a new avenue for ablating local aromatase activity in breast tumors.
原位雌激素合成通过自分泌或旁分泌机制与肿瘤细胞增殖相关,尤其在绝经后女性中。最近的几项研究证实了芳香化酶的活性,该酶在乳腺肿瘤雌激素合成中起关键作用。富含脯氨酸、谷氨酸和亮氨酸的蛋白-1(PELP1/MNAR)是一种雌激素受体(ER)共调节因子,其表达在乳腺肿瘤中失调。在本研究中,我们使用稳定过表达PELP1的乳腺癌细胞(MCF7),研究PELP1是否通过促进局部雌激素合成来促进肿瘤生长。免疫组织化学显示,在MCF7-PELP1诱导的异种移植肿瘤中芳香化酶表达增加。实时PCR分析表明,与MCF7细胞相比,MCF7-PELP1克隆中芳香化酶启动子的激活增强。使用氚水释放试验,我们证明与对照MCF-7细胞相比,MCF7-PELP1克隆表现出更高的芳香化酶活性。PELP1失调通过激活芳香化酶启动子I.3/II独特地上调芳香化酶表达,并且生长因子信号增强了PELP1对芳香化酶的激活。PELP1介导的芳香化酶诱导需要功能性Src和磷脂酰肌醇-3-激酶途径。机制研究表明,PELP1与ER相关受体-α和富含脯氨酸的核受体共调节蛋白2的相互作用导致芳香化酶的激活。乳腺肿瘤阵列的免疫组织化学分析显示,与正常乳腺组织中无或弱表达相比,原位导管癌和淋巴结阳性肿瘤中芳香化酶表达增加。与PELP1低表达肿瘤中的36%(n = 47)相比,54%(n = 79)的PELP1过表达肿瘤也过表达芳香化酶。我们的结果表明,PELP1对芳香化酶的调节代表了原位雌激素合成导致肿瘤通过自分泌环增殖的一种新机制,并为消除乳腺肿瘤中局部芳香化酶活性开辟了一条新途径。