Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, Jinan 250012, China.
Cell Death Dis. 2013 Aug 8;4(8):e761. doi: 10.1038/cddis.2013.285.
We previously reported that marchantin M (Mar) is an active agent to induce apoptosis in human prostate cancer (PCa), but the molecular mechanisms of action remain largely unknown. Here, we demonstrate that Mar potently inhibited chymotrypsin-like and peptidyl-glutamyl peptide-hydrolyzing activities of 20S proteasome both in in vitro and intracellular systems and significantly induced the accumulation of polyubiquitinated proteins in PCa cells. The computational modeling analysis suggested that Mar non-covalently bound to active sites of proteasome β5 and β1 subunits, resulting in a non-competitive inhibition. Proteasome inhibition by Mar subsequently resulted in endoplasmic reticulum (ER) stress, as evidenced by elevated glucose-regulated protein 78 and CHOP, increased phospho-eukaryotic translation initiation factor 2α (eIF(2α)), splicing of X-box-binding protein-1 and dilation of the ER. However, Mar-mediated cell death was not completely impaired by a pan inhibitor of caspases. Further studies revealed that the Mar-induced cell death was greatly associated with the activation of autophagy, as indicated by the significant induction of microtubule-associated protein-1 light chain-3 beta (LC3B) expression and conversion. Electron microscopic and green fluorescent protein-tagged LC3B analyses further demonstrated the ability of autophagy induction by Mar. Time kinetic studies revealed that Mar induced a rapid and highly sustained processing of LC3B in treated cells and simultaneously decreased the expression of p62/SQSTM1. Pharmacological blockade or knockdown of LC3B and Atg5 attenuated Mar-mediated cell death. The autophagic response triggered by Mar required the activation of RNA-dependent protein kinase-like ER kinase/eIF(2α) and suppression of the phosphatidylinositol-3 kinase/Akt/mammalian target of rapamycin axis via preventing activation and expression of Akt. Our results identified a novel mechanism for the cytotoxic effect of Mar, which strengthens it as a potential agent in cancer chemotherapy.
我们之前报道过,马钱亭 M(Mar)是一种能够诱导人前列腺癌(PCa)细胞凋亡的有效试剂,但作用的分子机制仍知之甚少。在此,我们证明了 Mar 能够强烈抑制 20S 蛋白酶体的糜蛋白酶样和肽基-谷氨酰肽水解活性,无论是在体外还是细胞内系统中,并显著诱导 PCa 细胞中多泛素化蛋白的积累。计算建模分析表明,Mar 非共价结合到蛋白酶体β5 和β1 亚基的活性部位,导致非竞争性抑制。Mar 对蛋白酶体的抑制随后导致内质网(ER)应激,这表现为葡萄糖调节蛋白 78 和 CHOP 升高,磷酸化真核翻译起始因子 2α(eIF(2α))增加,X 盒结合蛋白-1 的剪接和内质网扩张。然而,Mar 介导的细胞死亡并没有被 caspase 的泛抑制剂完全阻断。进一步的研究表明,Mar 诱导的细胞死亡与自噬的激活密切相关,这表现为微管相关蛋白-1 轻链-3β(LC3B)表达和转化的显著诱导。电子显微镜和绿色荧光蛋白标记的 LC3B 分析进一步证明了 Mar 诱导自噬的能力。时动力学研究表明,Mar 在处理的细胞中快速且高度持续地处理 LC3B,并同时降低 p62/SQSTM1 的表达。LC3B 和 Atg5 的药理学阻断或敲低减弱了 Mar 介导的细胞死亡。Mar 触发的自噬反应需要 RNA 依赖的蛋白激酶样内质网激酶/eIF(2α)的激活和通过阻止 Akt 的激活和表达来抑制磷脂酰肌醇-3 激酶/Akt/雷帕霉素靶蛋白(mTOR)轴。我们的结果确定了 Mar 的细胞毒性作用的新机制,这使其成为癌症化疗的潜在试剂。