All-trans retinoic acid increases expression of aquaporin-5 and plasma membrane water permeability via transactivation of Sp1 in mouse lung epithelial cells
All-trans retinoic acid increases expression of aquaporin-5 and plasma membrane water permeability via transactivation of Sp1 in mouse lung epithelial cells
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DOI：
10.1016/j.bbrc.2006.10.159
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发表时间：
2006-12-29
影响因子：
3.1
通讯作者：
Isohama, Yoichiro
中科院分区：
文献类型：
--
作者：
Nomura, Johji;Horie, Ichiro;Isohama, Yoichiro
水通道蛋白5 （Aquaporin-5, AQP5）是一种水选择性通道蛋白，表达于泪腺、唾液腺和远端。肺。一些使用AQP5敲除小鼠的研究表明，AQP5在维持肺水稳态中起重要作用。我们在这里报道了全反式维甲酸（atRA）增加MLE-12细胞的质膜透水性、AQP5 mRNA和蛋白表达以及AQP5启动子活性。Sp1/Sp3结合元件（SBE）的突变降低了atRA诱导的启动子激活，表明SBE介导了atRA的作用。此外，atRA增加了Sp1与SBE的结合，但没有改变细胞核中Sp1的水平。综上所述，我们的数据表明，atRA通过Sp1的反激活增加AQP5的表达，导致质膜透水性增加。(c) 2006爱思唯尔公司版权所有。
Aquaporin-5 (AQP5) is a water-selective channel protein that is expressed in lacrimal glands, salivary glands, and distal. lung. Several studies using AQP5 knockout mice have revealed that AQP5 plays an important role in maintaining water homeostasis in the lung. We report here that all-trans retinoic acid (atRA) increases plasma membrane water permeability, AQP5 mRNA and protein expression, and AQP5 promoter activity in MLE-12 cells. The promoter activation induced by atRA was diminished by mutation at the Sp1/Sp3 binding element (SBE), suggesting that the SBE mediates the effects of atRA. In addition, atRA increased the binding of Sp1 to the SBE without changing the levels of Sp1 in the nucleus. Taken together, our data indicate that atRA increases AQP5 expression through transactivation of Sp1, leading to an increase in plasma membrane water permeability. (c) 2006 Elsevier Inc. All rights reserved.