Laboratory of Metabolism, National Cancer Institute, Bethesda, Maryland 20892, USA.
Mol Pharmacol. 2012 Nov;82(5):814-23. doi: 10.1124/mol.112.080820. Epub 2012 Jul 31.
Several basic leucine zipper (B-ZIP) transcription factors have been implicated in cancer, substance abuse, and other pathological conditions. We previously identified arylstibonic acids that bind to B-ZIP proteins and inhibit their interaction with DNA. In this study, we used electrophoretic mobility shift assay to analyze 46 arylstibonic acids for their activity to disrupt the DNA binding of three B-ZIP [CCAAT/enhancer-binding protein α, cyclic AMP-response element-binding protein (CREB), and vitellogenin gene-binding protein (VBP)] and two basic helix-loop-helix leucine zipper (B-HLH-ZIP) [USF (upstream stimulating factor) and Mitf] proteins. Twenty-five arylstibonic acids showed activity at micromolar concentrations. The most active compound, P6981 [2-(3-stibonophenyl)malonic acid], had half-maximal inhibition at ~5 nM for CREB. Circular dichroism thermal denaturation studies indicated that P6981 binds both the B-ZIP domain and the leucine zipper. The crystal structure of an arylstibonic acid, NSC13778, bound to the VBP leucine zipper identified electrostatic interactions between both the stibonic and carboxylic acid groups of NSC13778 [(E)-3-(3-stibonophenyl)acrylic acid] and arginine side chains of VBP, which is also involved in interhelical salt bridges in the leucine zipper. P6981 induced GFP-B-ZIP chimeric proteins to partially localize to the cytoplasm, demonstrating that it is active in cells. P6981 inhibited the growth of a patient-derived clear cell sarcoma cell line whose oncogenic potential is driven by a chimeric protein EWS-ATF1 (Ewing's sarcoma protein-activating transcription factor 1), which contains the DNA binding domain of ATF1, a B-ZIP protein. NSC13778 inhibited the growth of xenografted clear cell sarcoma, and no toxicity was observed. These experiments suggest that antimony containing arylstibonic acids are promising leads for suppression of DNA binding activities of B-ZIP and B-HLH-ZIP transcription factors.
几种基本亮氨酸拉链(B-ZIP)转录因子已被牵涉到癌症、物质滥用和其他病理状况中。我们之前发现了芳基膦酸酯可以与 B-ZIP 蛋白结合并抑制其与 DNA 的相互作用。在这项研究中,我们使用电泳迁移率变动分析来分析 46 种芳基膦酸酯,以研究它们是否能破坏三种 B-ZIP [CCAAT/增强子结合蛋白α、环 AMP 反应元件结合蛋白(CREB)和卵黄蛋白原结合蛋白(VBP)]和两种碱性螺旋-环-螺旋亮氨酸拉链(B-HLH-ZIP)[USF(上游刺激因子)和 Mitf]蛋白的 DNA 结合。25 种芳基膦酸酯在微摩尔浓度下表现出活性。最活跃的化合物 P6981 [2-(3-膦酰苯基)丙二酸]对 CREB 的半数最大抑制浓度约为 5 nM。圆二色性热变性研究表明 P6981 结合 B-ZIP 结构域和亮氨酸拉链。芳基膦酸酯 NSC13778 的晶体结构与 VBP 亮氨酸拉链结合,确定了 NSC13778 [(E)-3-(3-膦酰苯基)丙烯酸]的膦酸和羧酸基团与 VBP 的精氨酸侧链之间的静电相互作用,VBP 也参与亮氨酸拉链中的螺旋间盐桥。P6981 诱导 GFP-B-ZIP 嵌合蛋白部分定位于细胞质中,表明它在细胞中是活跃的。P6981 抑制了由嵌合蛋白 EWS-ATF1(Ewing 肉瘤蛋白激活转录因子 1)驱动的患者来源的透明细胞肉瘤细胞系的生长,该蛋白包含 ATF1 的 DNA 结合结构域,是一种 B-ZIP 蛋白。NSC13778 抑制了异种移植的透明细胞肉瘤的生长,并且没有观察到毒性。这些实验表明,含锑的芳基膦酸酯是抑制 B-ZIP 和 B-HLH-ZIP 转录因子的 DNA 结合活性的有前途的先导化合物。