Laboratory of Cytobiochemistry, Biotechnology Faculty, University of Wroclaw, 50-383 Wroclaw, Poland.
Department of Minimally Invasive Surgery and Proctology, Wroclaw Medical University, 50-556 Wroclaw, Poland.
Int J Mol Sci. 2021 Feb 9;22(4):1716. doi: 10.3390/ijms22041716.
Inhibition of the protein neddylation process by the small-molecule inhibitor MLN4924 has been recently indicated as a promising direction for cancer treatment. However, the knowledge of all biological consequences of MLN4924 for cancer cells is still incomplete. Here, we report that MLN4924 inhibits tumor necrosis factor-alpha (TNF-α)-induced matrix metalloproteinase 9 (MMP9)-driven cell migration. Using real-time polymerase chain reaction (PCR) and gelatin zymography, we found that MLN4924 inhibited expression and activity of MMP9 at the messenger RNA (mRNA) and protein levels in both resting cells and cells stimulated with TNF-α, and this inhibition was closely related to impaired cell migration. We also revealed that MLN4924, similar to TNF-α, induced phosphorylation of inhibitor of nuclear factor kappa B-alpha (IκB-α). However, contrary to TNF-α, MLN4924 did not induce IκB-α degradation in treated cells. In coimmunoprecipitation experiments, nuclear IκB-α which formed complexes with nuclear factor kappa B p65 subunit (NFκB/p65) was found to be highly phosphorylated at Ser32 in the cells treated with MLN4924, but not in the cells treated with TNF-α alone. Moreover, in the presence of MLN4924, nuclear NFκB/p65 complexes were found to be enriched in c-Jun and cyclin dependent kinase inhibitor 1 A (CDKN1A/p21) proteins. In these cells, NFκB/p65 was unable to bind to the MMP9 gene promoter, which was confirmed by the chromatin immunoprecipitation (ChIP) assay. Taken together, our findings identified MLN4924 as a suppressor of TNF-α-induced MMP9-driven cell migration in esophageal squamous cell carcinoma (ESCC), likely acting by affecting the nuclear ubiquitin-proteasome system that governs NFκB/p65 complex formation and its DNA binding activity in regard to the MMP9 promoter, suggesting that inhibition of neddylation might be a new therapeutic strategy to prevent invasion/metastasis in ESCC patients.
小分子抑制剂 MLN4924 抑制蛋白 neddylation 过程已被证明是癌症治疗的一个有前途的方向。然而,对于 MLN4924 对癌细胞的所有生物学后果的认识仍然不完整。在这里,我们报告 MLN4924 抑制肿瘤坏死因子-α(TNF-α)诱导的基质金属蛋白酶 9(MMP9)驱动的细胞迁移。通过实时聚合酶链反应(PCR)和明胶酶谱法,我们发现 MLN4924 在静止细胞和 TNF-α刺激的细胞中均抑制 MMP9 的信使 RNA(mRNA)和蛋白水平的表达和活性,并且这种抑制与细胞迁移受损密切相关。我们还揭示 MLN4924 与 TNF-α相似,诱导核因子 kappa B-α(IκB-α)抑制剂的磷酸化。然而,与 TNF-α相反,MLN4924 在处理的细胞中不诱导 IκB-α降解。在共免疫沉淀实验中,发现用 MLN4924 处理的细胞中,与核因子 kappa B p65 亚基(NFκB/p65)形成复合物的核 IκB-α在 Ser32 处高度磷酸化,但单独用 TNF-α处理的细胞中则没有。此外,在 MLN4924 的存在下,发现核 NFκB/p65 复合物富含 c-Jun 和细胞周期蛋白依赖性激酶抑制剂 1A(CDKN1A/p21)蛋白。在这些细胞中,NFκB/p65 无法与 MMP9 基因启动子结合,这通过染色质免疫沉淀(ChIP)实验得到证实。总之,我们的研究结果确定 MLN4924 是食管鳞状细胞癌(ESCC)中 TNF-α诱导的 MMP9 驱动的细胞迁移的抑制剂,可能通过影响核泛素-蛋白酶体系统来发挥作用,该系统控制 NFκB/p65 复合物的形成及其 DNA 结合活性与 MMP9 启动子有关,这表明抑制 neddylation 可能是预防 ESCC 患者侵袭/转移的新治疗策略。