Section of Endocrinology and Metabolism, Department of Medicine, Yale University School of Medicine, New Haven, Connecticut.
Division of Pharmacology, College of Korean Medicine, Semyung University, Jecheon, Republic of Korea.
Endocrinology. 2019 Aug 1;160(8):1797-1810. doi: 10.1210/en.2019-00230.
Prior studies have demonstrated that the calcium pump, plasma membrane calcium ATPase 2 (PMCA2), mediates calcium transport into milk and prevents mammary epithelial cell death during lactation. PMCA2 also regulates cell proliferation and cell death in breast cancer cells, in part by maintaining the receptor tyrosine kinase ErbB2/HER2 within specialized plasma membrane domains. Furthermore, the regulation of PMCA2 membrane localization and activity in breast cancer cells requires its interaction with the PDZ domain-containing scaffolding molecule sodium-hydrogen exchanger regulatory factor (NHERF) 1. In this study, we asked whether NHERF1 also interacts with PMCA2 in normal mammary epithelial cells during lactation. Our results demonstrate that NHERF1 expression is upregulated during lactation and that it interacts with PMCA2 at the apical membrane of secretory luminal epithelial cells. Similar to PMCA2, NHERF1 expression is rapidly reduced by milk stasis after weaning. Examining lactating NHERF1 knockout (KO) mice showed that NHERF1 contributes to the proper apical location of PMCA2, for proper apical-basal polarity in luminal epithelial cells, and that it participates in the suppression of Stat3 activation and the prevention of premature mammary gland involution. Additionally, we found that PMCA2 also interacts with the closely related scaffolding molecule, NHERF2, at the apical membrane, which likely maintains PMCA2 at the plasma membrane of mammary epithelial cells in lactating NHERF1KO mice. Based on these data, we conclude that, during lactation, NHERF1 is required for the proper expression and apical localization of PMCA2, which, in turn, contributes to preventing the premature activation of Stat3 and the lysosome-mediated cell death pathway that usually occur only early in mammary involution.
先前的研究表明,钙泵,质膜钙 ATP 酶 2(PMCA2)介导钙向乳汁中的转运,并防止哺乳期乳腺上皮细胞死亡。PMCA2 还调节乳腺癌细胞的增殖和细胞死亡,部分是通过维持受体酪氨酸激酶 ErbB2/HER2 位于特殊的质膜域内。此外,乳腺癌细胞中 PMCA2 膜定位和活性的调节需要其与 PDZ 结构域含有支架分子钠氢交换调节因子(NHERF)1 相互作用。在这项研究中,我们询问 NHERF1 是否也在哺乳期的正常乳腺上皮细胞中与 PMCA2 相互作用。我们的结果表明,NHERF1 的表达在哺乳期上调,并且它在分泌腔上皮细胞的顶膜上与 PMCA2 相互作用。与 PMCA2 相似,在断奶后乳汁停滞时,NHERF1 的表达迅速降低。检查哺乳期 NHERF1 敲除(KO)小鼠表明,NHERF1 有助于 PMCA2 在腔上皮细胞中的适当顶端位置,用于腔上皮细胞的适当顶端-基底极性,并且它参与抑制 Stat3 激活和防止乳腺过早退化。此外,我们发现 PMCA2 还与紧密相关的支架分子 NHERF2 在顶膜相互作用,这可能使 PMCA2 在哺乳期 NHERF1KO 小鼠的乳腺上皮细胞的质膜上保持稳定。基于这些数据,我们得出结论,在哺乳期,NHERF1 是 PMCA2 适当表达和顶端定位所必需的,这反过来又有助于防止 Stat3 的过早激活和溶酶体介导的细胞死亡途径,这些途径通常仅在乳腺退化的早期发生。