Trihydrophobin 1相互作用蛋白以及Trihydrophobin 1与乳腺癌细胞化疗药物敏感性之间关系的研究
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摘要
第一部分人类乳头瘤病毒E6相关蛋白(E6-AP)介导Trihydrophobin 1的泛素-蛋白酶体降解
人类乳头瘤病毒E6相关蛋白E6-AP是泛素连接酶的一种，它能够介导细胞内一系列蛋白质的泛素化降解。我们的研究发现TH1，作为一个负性转录延长调节因子复合体(NELF complex)中必不可少的组分之一，能够与E6-AP相互作用，并且可以作为E6-AP调节的泛素化降解的新的底物。研究发现，细胞内过表达E6-AP可以产生表达剂量依赖的TH1蛋白水平的降低，同时采用RNA干扰技术，降低细胞内源性E6-AP的表达能够增加细胞内TH1的蛋白水平。与对照组比较，过表达E6-AP的细胞株中TH1蛋白降解加快同时半衰期明显缩短。野生型的E6-AP可以明显的促进TH1蛋白的泛素化降解，而E6-AP蛋白HECT结构域点突变产生的泛素连接酶活性缺失的突变体却不能泛素化TH1蛋白。体外泛素化实验进一步说明了E6-AP在体外重组的泛素化系统中，同样可以促进TH1蛋白的泛素化，并且在此系统中加入蛋白酶体抑制剂MG132可以阻断E6-AP对TH1蛋白的这种泛素化降解。因此，我们的实验证实TH1蛋白的确是E6-AP这个经典的泛素连接酶的新的特异性底物。
第二部分Trihydrophobin 1促进雄激素受体降解进而抑制雄激素信号传导的研究
在前列腺癌细胞的生长和分化过程中，雄激素受体的转录调控起极其重要的作用。而对雄激素受体转录活性起到调控作用的目前研究较多的是众多的转录促进因子和抑制因子。在对雄激素受体转录活性的调控过程中，主要集中在对转录促进因子的研究，而对转录抑制因子的研究相对较少。我们的研究发现TH1蛋白能够抑制雄激素受体调控的转录，进而说明TH1蛋白是雄激素受体这个转录因子的抑制分子。TH1蛋白对雄激素受体转录活性的这种抑制作用的发挥，依赖于TH1蛋白与雄激素受体的相互作用。TH1 N末端第119到123位氨基酸的特异性的LXXLL结构域对于TH1蛋白与雄激素受体相互作用发挥了至关重要的作用。在运用RNA干扰技术，抑制细胞内源性TH1蛋白表达后，我们发现雄激素受体的转录活性有了明显的增高。这进一步说明TH1蛋白在体内的确能够抑制雄激素受体的转录活性。前列腺特异性抗原PSA是雄激素受体调控的最重要的基因，在前列腺癌LNCaP细胞中，过表达TH1蛋白能够抑制前列腺特异性抗原的表达。进一步的研究发现，TH1蛋白能够分别与激素受体N末端的转录激活结构域(TAD)和C末端的配体结合结构域(LBD)相互作用。我们知道雄激素受体在发挥转录活性的时候，会通过N末端和C末端的相互作用形成同源二聚体，TH1蛋白的这种相互作用特点抑制了雄激素受体同源二聚体的形成，进而抑制了雄激素受体的转录活性。同时，由于雄激素受体不能形成稳定的同源二聚体形式，稳定性下降，更易于通过泛素-蛋白酶体系统降解。进一步通过染色质免疫共沉淀的方法我们证实，在雄激素活化雄激素受体转录活性的同时，TH1蛋白会伴随着雄激素受体一起结合到LNCaP细胞中PSA基因的启动子和增强子上，伴随雄激素受体一起调控下游基因的表达。以上的实验结果提示我们，在雄激素受体转录活性发挥重要作用的组织的发育过程、生理以及病理状态下，TH1蛋白很可能作为一个新的不为人知的调控分子。
第三部分干扰TH1基IN表达促进乳腺癌细胞化疗药物敏感性的研究
当细胞增殖和细胞死亡之间的平衡被打破，细胞出现无控制的过度增殖就会形成肿瘤。为了研究TH1基因与细胞凋亡的关系，我们采用RNA干扰技术降低乳腺癌细胞内TH1蛋白水平后，用化疗药物诱导细胞株凋亡时，我们发现，由于RNA干扰而低表达TH1蛋白的细胞株与对照组细胞相比表现出更强的凋亡敏感性。乳腺癌细胞株T47D(雌激素敏感，雌激素受体表达)和MDA-MB 231(雌激素受体不敏感，雌激素受体不表达)稳定转染TH1 RNA干扰质粒后，发生细胞周期G2／M期阻滞，同时细胞生长收到抑制，增殖减缓，说明TH1的这种作用并不依赖雌激素受体的作用。将TH1 RNA干扰质粒稳定表达的MDA-MB 231细胞株接种裸鼠皮下，观察肿瘤生长情况发现，稳定表达TH1 RNA干扰质粒的细胞株接种后形成的肿瘤体积和重量明显小于对照细胞形成的肿瘤。为进一步研究上述现象发生的机制，我们检测了细胞周期和凋亡相关分子在两组细胞株之间的表达差异，发现T47D细胞和MDA-MB-231细胞中，降低内源性TH1蛋白的表达后，p21的蛋白水平明显增高。荧光素酶报告基因活性检测结果显示，过表达TH1蛋白后，p21启动子的活性明显受到抑制。综上所述，我们的结果说明TH1能够通过调节乳腺癌细胞中p21的表达进而影响细胞周期和细胞凋亡。
Human Papilloma virus E6-associated protein (E6-AP), which is known as an E3ubiquitin ligase, mediates ubiquitination and subsequent degradation of a series of cellularproteins. In this paper, we identify here tfihydrophobin 1 (TH1), an integral subunit of thehuman negative transcription elongation factor (NELF) complex, as a novel E6-APinteraction protein and a target of E6-APmediated degradation. Overexpression of E6-APresults in degradation of TH1 in a dose-dependent manner, whereas knock-down ofendogenous E6-AP elevates the TH1 protein level. TH1 protein turnover is substantiallyfaster, compared to controls, in cells that overexpressed E6-AP. Wild-type E6-APpromotes the ubiquitination of TH1, while a catalytically inactive point mutant of E6-APabolishes its ubiquitination. Furthermore, in vitro ubiquitination assay also demonstratesthat TH1 can be ubiquitinated by E6-AP. The degradation is blocked by treatment withproteasome inhibitor MG132. Herein, we provide strong evidence that TH1 is a specificsubstrate that is targeted for degradation through E6-AP-catalyzed polyubiquitination.
The transcriptional activity of the androgen receptor (AR) modulated by positive ornegative regulators plays critical roles in controlling the growth and survival of prostatecancer cells. In this study, we report that TH1 is a potent transcriptional repressor tosuppress AR activity. Knock-down of TH1 expression augment AR transcriptionalactivation. The attenuation of AR activity by TH1 is in a physical interaction dependentmanner, and TH1 N-terminal LXXLL motif is indispensable. TH1 can interact with bothtransactivation domain and Ligand binding domain of AR, and interferes withintramolecular interaction, hence decreases the stability of AR. Using chromatinimmunoprecipitation (ChIP) analyses, we show that TH1 dynamically associates with ARat the active androgen-responsive prostate-specific antigen (PSA) promoter in LNCaPcells. In agreement with these findings, TH1 overexpression blocks the PSA geneexpression in LNCaP cells. Taken together, these results indicate that TH1 is a novelregulator to control the duration and magnitude of AR transcriptional activation, and maybe directly involved in AR-related developmental, physiological, and pathologicalprocesses.
Cancer develops when the balance between cell proliferation and cell death isdisrupted, and the ensuing aberrant proliferation leads to tumor growth. We report in thispaper that depletion of TH1 by small hairpin RNA sensitizes the breast cancer cell lines tochemotherapy drugs induced apoptosis. Furthermore, knock-down of TH1 expression cancause cell cycle G2/M phase arrest, inhibit the proliferation of two human breast cancercell lines: estrogen-dependent, ER-positive T47D and estrogen-independent, ER-negativeMDA-MB-231. We also determined the phenotypic effects of TH1 knock-downT47D-derived tumors and control T47D-derived tumors in nude mice. TH1 knock-downT47D-derived tumors showed 60% and 70% reduction in tumor volume and weightrespectively. As a proliferation inhibitor, p21 expression is elevated in TH1 knock-downversus parental control cells. Further study indicates that over-expression of TH1 proteininhibits the promoter activity of p21, hence reduce both mRNA and protein level of p21.Knock-down of p21 expression using siRNA in TH1 knock-down cells counteracts cellcycle G2/M phase arrest and the chemotherapy drugs induced apoptosis. These resultssuggest that TH1 may functions as a novel regulator in chemotherapy drugs inducedapoptosis by regulating the expression of p21 in breast cancer cell lines.
人类乳头瘤病毒E6相关蛋白E6-AP是泛素连接酶的一种，它能够介导细胞内一系列蛋白质的泛素化降解。我们的研究发现TH1，作为一个负性转录延长调节因子复合体(NELF complex)中必不可少的组分之一，能够与E6-AP相互作用，并且可以作为E6-AP调节的泛素化降解的新的底物。研究发现，细胞内过表达E6-AP可以产生表达剂量依赖的TH1蛋白水平的降低，同时采用RNA干扰技术，降低细胞内源性E6-AP的表达能够增加细胞内TH1的蛋白水平。与对照组比较，过表达E6-AP的细胞株中TH1蛋白降解加快同时半衰期明显缩短。野生型的E6-AP可以明显的促进TH1蛋白的泛素化降解，而E6-AP蛋白HECT结构域点突变产生的泛素连接酶活性缺失的突变体却不能泛素化TH1蛋白。体外泛素化实验进一步说明了E6-AP在体外重组的泛素化系统中，同样可以促进TH1蛋白的泛素化，并且在此系统中加入蛋白酶体抑制剂MG132可以阻断E6-AP对TH1蛋白的这种泛素化降解。因此，我们的实验证实TH1蛋白的确是E6-AP这个经典的泛素连接酶的新的特异性底物。
第二部分Trihydrophobin 1促进雄激素受体降解进而抑制雄激素信号传导的研究
在前列腺癌细胞的生长和分化过程中，雄激素受体的转录调控起极其重要的作用。而对雄激素受体转录活性起到调控作用的目前研究较多的是众多的转录促进因子和抑制因子。在对雄激素受体转录活性的调控过程中，主要集中在对转录促进因子的研究，而对转录抑制因子的研究相对较少。我们的研究发现TH1蛋白能够抑制雄激素受体调控的转录，进而说明TH1蛋白是雄激素受体这个转录因子的抑制分子。TH1蛋白对雄激素受体转录活性的这种抑制作用的发挥，依赖于TH1蛋白与雄激素受体的相互作用。TH1 N末端第119到123位氨基酸的特异性的LXXLL结构域对于TH1蛋白与雄激素受体相互作用发挥了至关重要的作用。在运用RNA干扰技术，抑制细胞内源性TH1蛋白表达后，我们发现雄激素受体的转录活性有了明显的增高。这进一步说明TH1蛋白在体内的确能够抑制雄激素受体的转录活性。前列腺特异性抗原PSA是雄激素受体调控的最重要的基因，在前列腺癌LNCaP细胞中，过表达TH1蛋白能够抑制前列腺特异性抗原的表达。进一步的研究发现，TH1蛋白能够分别与激素受体N末端的转录激活结构域(TAD)和C末端的配体结合结构域(LBD)相互作用。我们知道雄激素受体在发挥转录活性的时候，会通过N末端和C末端的相互作用形成同源二聚体，TH1蛋白的这种相互作用特点抑制了雄激素受体同源二聚体的形成，进而抑制了雄激素受体的转录活性。同时，由于雄激素受体不能形成稳定的同源二聚体形式，稳定性下降，更易于通过泛素-蛋白酶体系统降解。进一步通过染色质免疫共沉淀的方法我们证实，在雄激素活化雄激素受体转录活性的同时，TH1蛋白会伴随着雄激素受体一起结合到LNCaP细胞中PSA基因的启动子和增强子上，伴随雄激素受体一起调控下游基因的表达。以上的实验结果提示我们，在雄激素受体转录活性发挥重要作用的组织的发育过程、生理以及病理状态下，TH1蛋白很可能作为一个新的不为人知的调控分子。
第三部分干扰TH1基IN表达促进乳腺癌细胞化疗药物敏感性的研究
当细胞增殖和细胞死亡之间的平衡被打破，细胞出现无控制的过度增殖就会形成肿瘤。为了研究TH1基因与细胞凋亡的关系，我们采用RNA干扰技术降低乳腺癌细胞内TH1蛋白水平后，用化疗药物诱导细胞株凋亡时，我们发现，由于RNA干扰而低表达TH1蛋白的细胞株与对照组细胞相比表现出更强的凋亡敏感性。乳腺癌细胞株T47D(雌激素敏感，雌激素受体表达)和MDA-MB 231(雌激素受体不敏感，雌激素受体不表达)稳定转染TH1 RNA干扰质粒后，发生细胞周期G2／M期阻滞，同时细胞生长收到抑制，增殖减缓，说明TH1的这种作用并不依赖雌激素受体的作用。将TH1 RNA干扰质粒稳定表达的MDA-MB 231细胞株接种裸鼠皮下，观察肿瘤生长情况发现，稳定表达TH1 RNA干扰质粒的细胞株接种后形成的肿瘤体积和重量明显小于对照细胞形成的肿瘤。为进一步研究上述现象发生的机制，我们检测了细胞周期和凋亡相关分子在两组细胞株之间的表达差异，发现T47D细胞和MDA-MB-231细胞中，降低内源性TH1蛋白的表达后，p21的蛋白水平明显增高。荧光素酶报告基因活性检测结果显示，过表达TH1蛋白后，p21启动子的活性明显受到抑制。综上所述，我们的结果说明TH1能够通过调节乳腺癌细胞中p21的表达进而影响细胞周期和细胞凋亡。
Human Papilloma virus E6-associated protein (E6-AP), which is known as an E3ubiquitin ligase, mediates ubiquitination and subsequent degradation of a series of cellularproteins. In this paper, we identify here tfihydrophobin 1 (TH1), an integral subunit of thehuman negative transcription elongation factor (NELF) complex, as a novel E6-APinteraction protein and a target of E6-APmediated degradation. Overexpression of E6-APresults in degradation of TH1 in a dose-dependent manner, whereas knock-down ofendogenous E6-AP elevates the TH1 protein level. TH1 protein turnover is substantiallyfaster, compared to controls, in cells that overexpressed E6-AP. Wild-type E6-APpromotes the ubiquitination of TH1, while a catalytically inactive point mutant of E6-APabolishes its ubiquitination. Furthermore, in vitro ubiquitination assay also demonstratesthat TH1 can be ubiquitinated by E6-AP. The degradation is blocked by treatment withproteasome inhibitor MG132. Herein, we provide strong evidence that TH1 is a specificsubstrate that is targeted for degradation through E6-AP-catalyzed polyubiquitination.
The transcriptional activity of the androgen receptor (AR) modulated by positive ornegative regulators plays critical roles in controlling the growth and survival of prostatecancer cells. In this study, we report that TH1 is a potent transcriptional repressor tosuppress AR activity. Knock-down of TH1 expression augment AR transcriptionalactivation. The attenuation of AR activity by TH1 is in a physical interaction dependentmanner, and TH1 N-terminal LXXLL motif is indispensable. TH1 can interact with bothtransactivation domain and Ligand binding domain of AR, and interferes withintramolecular interaction, hence decreases the stability of AR. Using chromatinimmunoprecipitation (ChIP) analyses, we show that TH1 dynamically associates with ARat the active androgen-responsive prostate-specific antigen (PSA) promoter in LNCaPcells. In agreement with these findings, TH1 overexpression blocks the PSA geneexpression in LNCaP cells. Taken together, these results indicate that TH1 is a novelregulator to control the duration and magnitude of AR transcriptional activation, and maybe directly involved in AR-related developmental, physiological, and pathologicalprocesses.
Cancer develops when the balance between cell proliferation and cell death isdisrupted, and the ensuing aberrant proliferation leads to tumor growth. We report in thispaper that depletion of TH1 by small hairpin RNA sensitizes the breast cancer cell lines tochemotherapy drugs induced apoptosis. Furthermore, knock-down of TH1 expression cancause cell cycle G2/M phase arrest, inhibit the proliferation of two human breast cancercell lines: estrogen-dependent, ER-positive T47D and estrogen-independent, ER-negativeMDA-MB-231. We also determined the phenotypic effects of TH1 knock-downT47D-derived tumors and control T47D-derived tumors in nude mice. TH1 knock-downT47D-derived tumors showed 60% and 70% reduction in tumor volume and weightrespectively. As a proliferation inhibitor, p21 expression is elevated in TH1 knock-downversus parental control cells. Further study indicates that over-expression of TH1 proteininhibits the promoter activity of p21, hence reduce both mRNA and protein level of p21.Knock-down of p21 expression using siRNA in TH1 knock-down cells counteracts cellcycle G2/M phase arrest and the chemotherapy drugs induced apoptosis. These resultssuggest that TH1 may functions as a novel regulator in chemotherapy drugs inducedapoptosis by regulating the expression of p21 in breast cancer cell lines.
引文
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