Center for Kidney Disease, Second Affiliated Hospital, Nanjing Medical University, Nanjing, Jiangsu, China.
J Cell Mol Med. 2018 Mar;22(3):1684-1695. doi: 10.1111/jcmm.13446. Epub 2017 Nov 29.
β-Catenin signalling plays an important role in regulating tubular epithelial-to-mesenchymal transition (EMT), an indispensable programme for driving renal fibrosis. As an adapter protein, four and a half LIM domain protein 2 (FHL2) acts as a coregulator of β-catenin in several other cell types. To determine whether FHL2 affects β-catenin signalling and thus is involved in tubular EMT, we examined its expression and function in the process of TGF-β1-induced EMT. FHL2 mRNA and protein were induced by TGF-β1 in rat tubular epithelial cells (NRK-52E), an effect that intracellular Smad signalling was required. Ectopic expression of FHL2 inhibited E-cadherin and enhanced α-smooth muscle actin (α-SMA) and fibronectin expression, whereas knockdown of FHL2 partially restored E-cadherin and reduced α-SMA and fibronectin induction stimulated by TGF-β1. Overexpression of FHL2 increased β-catenin dephosphorylation (Ser37/Thr41), nuclear translocation and β-catenin-mediated transcription and up-regulated expression of β-catenin target, EMT-related genes, such as Snail, Twist, vimentin, plasminogen activator inhibitor-1 and matrix metalloproteinase-7. Conversely, knockdown of FHL2 increased β-catenin phosphorylation (Ser33/37/Thr41), decreased its nuclear translocation and inhibited β-catenin-mediated transcription and target genes expression. TGF-β1 induced a FHL2/β-catenin interaction in NRK-52E cells, especially in the nuclei. In a mouse model of obstructive nephropathy, FHL2 mRNA and protein were induced in a time-dependent fashion, and the extent and pattern of renal β-catenin activation were positively correlated with FHL2 induction. Collectively, this study suggests that FHL2, via modulating β-catenin signalling, may implicate in regulation of TGF-β1-mediated tubular EMT and could be a potential therapeutic target for fibrotic kidney disease.
β-连环蛋白信号在调节肾小管上皮-间充质转化(EMT)中起着重要作用,EMT 是驱动肾纤维化的必不可少的程序。作为衔接蛋白,四个半 LIM 结构域蛋白 2(FHL2)在其他几种细胞类型中作为β-连环蛋白的共调节剂发挥作用。为了确定 FHL2 是否影响β-连环蛋白信号转导,从而参与肾小管 EMT,我们研究了其在 TGF-β1 诱导的 EMT 过程中的表达和功能。FHL2 mRNA 和蛋白被 TGF-β1 在大鼠肾小管上皮细胞(NRK-52E)中诱导,该作用需要细胞内 Smad 信号转导。FHL2 的异位表达抑制了 E-钙粘蛋白,增强了α-平滑肌肌动蛋白(α-SMA)和纤连蛋白的表达,而 FHL2 的敲低部分恢复了 E-钙粘蛋白,并减少了 TGF-β1 刺激的α-SMA 和纤连蛋白诱导。FHL2 的过表达增加了β-连环蛋白去磷酸化(Ser37/Thr41)、核易位和β-连环蛋白介导的转录,并上调了β-连环蛋白靶标,如 EMT 相关基因,如 Snail、Twist、波形蛋白、纤溶酶原激活物抑制剂-1 和基质金属蛋白酶-7。相反,FHL2 的敲低增加了β-连环蛋白磷酸化(Ser33/37/Thr41),减少了其核易位,并抑制了β-连环蛋白介导的转录和靶基因表达。TGF-β1 在 NRK-52E 细胞中诱导 FHL2/β-连环蛋白相互作用,尤其是在核内。在梗阻性肾病的小鼠模型中,FHL2 mRNA 和蛋白呈时间依赖性诱导,肾β-连环蛋白激活的程度和模式与 FHL2 诱导呈正相关。总之,这项研究表明,FHL2 通过调节β-连环蛋白信号转导,可能参与调节 TGF-β1 介导的肾小管 EMT,并且可能是纤维化肾病的潜在治疗靶点。