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tdp-43 regulates cancer-associated microRNAs

Protein & Cell 2018年第10期9卷 848-866页

作者： Xiaowei Chen Zhen Fan Warren McGee Mengmeng Chen Ruirui Kong Pushuai Wen Tengfei Xiao Xiaomin Chen Jianghong Liu Li Zhu Runsheng Chen Jane Y. Wu CAS Key Laboratory of RNA Biology Institute of Biophysics Chinese Academy of Sciences Beijing 100101 China Research Network of Computational Biology RNCB Beijing 100101 China Core Facility for Protein Research institute of Biophysics Chinese Academy of Sciences Beijing 100101 China State Key Laboratory of Brain and Cognitive Science Institute of Biophysics Chinese Academy of Sciences Beijing 100101China Department of Neurology Center for Genetic Medicine Lurie Cancer Center Northwestern University Feinberg School ofMedicine Chicago IL 60611 USA Guangdong Geneway Decoding Bio-Tech Co. Ltd Foshan 528316 China

regulation of miRNA genes contributes to pathogenesis of a wide range of human diseases, including cancer. The TAR DNA binding protein 43 （tdp- 43）, a RNAJDNA binding protein associated with neu- rodegeneration, is involved in miRNA biogenesis. Here, we systematically examined miRNAs regulated by tdp- 43 using RNA-Seq coupled with an siRNA-mediated knockdown approach. tdp-43 knockdown affected the expression of a number of miRNAs. In addition, tdp-43 down-regulation led to alterations in the patterns of dif- ferent isoforms of miRNAs （isomiRs） and miRNA arm selection, suggesting a previously unknown role of tdp- 43 in miRNA processing. A number of tdp-43 associ- ated miRNAs, and their candidate target genes, are associated with human cancers. Our data reveal highly complex roles of tdp-43 in regulating different miRNAs and their target genes. Our results suggest that tdp-43 may promote migration of lung cancer cells by regulat- ing miR-423-3p. In contrast, tdp-43 increases miR-500a- 3p expression and binds to the mature miR-500a-3p sequence. Reduced expression of miR-500a-3p is associated with poor survival of lung cancer patients,suggesting that tdp-43 may have a suppressive role in cancer by regulating miR-500a-3p. Cancer-associated genes LIF and PAPPA are possible targets of miR-500a- 3p. Our work suggests that tdp-43-regulated miRNAs may play multifaceted roles in the pathogenesis of cancer.

关键词： tdp-43 miRNA cancer migration prognosis

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tdp-43 dysregulation and neuromuscular junction disruption in amyotrophic lateral sclerosis

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Translational Neurodegeneration 2022年第1期11卷 46-69页

作者： Sarah Lépine Maria José Castellanos-Montiel Thomas Martin Durcan The Neuro’s Early Drug Discovery Unit(EDDU) Department of Neurology and NeurosurgeryMontreal Neurological Institute-HospitalMcGill University3801 University StreetMontrealQC H3A 2B4Canada Faculty of Medicine and Health Sciences McGill University3605 De La MontagneMontrealQC H3G 2M1Canada

Amyotrophic lateral sclerosis(ALS)is a disease characterized by upper and lower motor neuron(MN)loss with a signature feature of cytoplasmic aggregates containing tdp-43,which are detected in nearly all *** in the gene that encodes tdp-43(TARBDP)are known to result in both familial and sporadic *** ALS,disruption of neuro-muscular junctions(NMJs)constitutes a critical event in disease pathogenesis,leading to denervation atrophy,motor impairments and *** defects and impaired synaptic transmission at NMJs have been reported in several tdp-43 animal models and in vitro,linking tdp-43 dysregulation to the loss of NMJ integrity in *** the lens of the dying-back and dying-forward hypotheses of ALS,this review discusses the roles of tdp-43 related to synaptic function,with a focus on the potential molecular mechanisms occurring within MNs,skeletal muscles and glial cells that may contribute to NMJ disruption in ALS.

关键词： Amyotrophic lateral sclerosis Denervation Neuromuscular junction tdp-43 Dying-back Dying-forward

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Phosphorylated tdp-43 Staging of Primary Age-Related Tauopathy

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Neuroscience Bulletin 2019年第2期35卷 183-192页

作者： Xiaoling Zhang Bing Sun Xing Wang Hui Lu Fangjie Shao Annemieke J.M.Rozemuller Huazheng Liang Chong Liu Jiadong Chen Manli Huang Keqing Zhu China Brain Bank and Department of Neurology in Second Affiliated Hospital Key Laboratory of Medical Neurobiology of Zhejiang ProvinceDepartment of NeurobiologyZhejiang University School of Medicine Department of Pathology Zhejiang University School of Medicine Department of Pathology Amsterdam NeuroscienceVU University Medical Center Brain Structure and Function Group Neuroscience Research Australia Department of Psychiatry First Affiliated HospitalZhejiang University School of Medicine

Primary age-related tauopathy(PART) is characterized by tau neurofibrillary tangles(NFTs) in the absence of amyloid plaque pathology. In the present study,we analyzed the distribution patterns of phosphorylated43-kDa TAR DNA-binding protein(ptdp-43) in the brains of patients with PART. Immunohistochemistry and immunofluorescence double-labeling in multiple brain regions was performed on brain tissues from PART,Alzheimer's disease(AD), and aging control cases. We examined the regional distribution patterns of ptdp-43 intraneuronal inclusions in PART with Braak NFT stages[ 0 and B IV, and a Thal phase of 0(no beta-amyloid present). We found four stages which indicated potentially sequential dissemination of ptdp-43 in PART. Stage I was characterized by the presence of ptdp-43 lesions in the amygdala, stage II by such lesions in the hippocampus,stage III by spread of ptdp-43 to the neocortex, and stage IV by ptdp-43 lesions in the putamen, pallidum, and insular cortex. In general, the distribution pattern of ptdp-43 pathology in PART cases was similar to the early tdp-43 stages reported in AD, but tended to be more restricted to the limbic system. However, there were some differences in the distribution patterns of ptdp-43 between PART and AD, especially in the dentate gyrus of the hippocampus. Positive correlations were found in PART between the Braak NFT stage and the ptdp-43 stage and density.

关键词： tdp-43 Primary age-related tauopathy Alzheimer's disease Neurofibrillary tangle Hippocampus

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Maintaining the balance of tdp-43,mitochondria,and autophagy:a promising therapeutic strategy for neurodegenerative diseases

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Translational Neurodegeneration 2020年第4期9卷 509-524页

作者： Chunhui Huang Sen Yan Zaijun Zhang Institute of New Drug Research Guangdong Province Key Laboratory of PharmacodynamicConstituents of Traditional Chinese Medicine and New Drug ResearchCollege of PharmacyJinan UniversityGuangzhou 510632China Ministry of Education CNS Regeneration Collaborative Joint Laboratory Guangdong-Hongkong-Macao Institute of CNS RegenerationJinan UniversityGuangzhou 510632China

Mitochondria are the energy center of cell operations and are involved in physiological functions and maintenance of metabolic balance and homeostasis in the *** of mitochondrial function are associated with a variety of degenerative and acute *** mitochondria age in cells,they gradually become inefficient and potentially toxic Acute injury can trigger the permeability of mitochondrial membranes,which can lead to apoptosis or *** response DNA-binding protein 43 kDa(tdp-43)is a protein widely present in *** can bind to RNA,regulate a variety of RNA processes,and play a role in the formation of multi-protein/RNA ***,the normal physiological functions of tdp-43 are particularly important for cell *** tdp-43 is located in various subcellular structures including mitochondria,mitochondrial-associated membrane,RNA particles and stress granules to regulate the endoplasmic reticulum-mitochondrial binding,mitochondrial protein translation,and mRNA transport and ***,tdp-43 is associated with a variety of neurodegenerative diseases,including amyotrophic lateral sclerosis,frontotemporal dementia and Alzheimer's disease,which are characterized by abnormal phosphorylation,ubiquitination,lysis or nuclear depletion of tdp-43 in neurons and glial *** the pathogenesis of tdp-43 proteinopathy remains unknown,the presence of pathological tdp-43 inside or outside of mitochondria and the functional involvement of tdp-43 in the regulation of mitochondrial morphology,transport,and function suggest that mitochondria are associated with tdp-43-related *** is a basic physiological process that maintains the homeostasis of cells,including targeted clearance of abnormally aggregated proteins and damaged organelles in the cytoplasm;therefore,it is considered protective against neurodegenerative ***,the combination of abnormal tdp-43 aggregation,mitochondrial dysfunction,an

关键词： tdp-43 Mitochondria Autophagy/mitophagy Neurodegeneration

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The role of ubiquitinated tdp-43 in amyotrophiclateral sclerosis

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Neuroimmunology and Neuroinflammation 2018年第2期5卷 8-17页

作者： Yi Dong Yan Chen Department of Neurology Huashan HospitalFudan UniversityShanghai 200040China

Deposition of intracellular ubiquitin inclusion in motor neurons is one of the leading pathogenic mechanisms of amyotrophic lateral sclerosis (ALS). The transactive response DNA binding protein-43 (tdp-43) is the main component of intracellular ubiquitin inclusion bodies in pathological deposits. tdp-43 is mainly distributed in the nucleus of neurons, and participates in nuclear RNA transcription, alternative splicing and mRNA stability regulation. The tardbp, as a coding gene, provides instructions for making tdp-43. After post-translational modification, the pathological tdp-43 induces pathological deposition in cells and is associated with neurodegenerative diseases, which is similar to tau in Alzheimer's disease and alpha-synuclein in Parkinson's disease. The pathogenic tardbp mutation can affect the localization of reverse transcription in the cell. This review summarizes the mechanisms underlying the pathogenesis of ALS by ubiquitination of tdp-43 protein.

关键词： tdp-43 protein ubiquitination tardbp amyotrophic lateral sclerosis

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运动神经元病与tdp-43蛋白的病理性表达

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中华内科杂志 2015年第1期54卷 31-34页

作者：朱明伟刘佳王鲁宁桂秋萍解放军总医院南楼神经内科北京100853 解放军总医院病理科北京100853

目的认识tdp-43蛋白在运动神经元病中枢神经系统的病理性表达特征.方法对4例经尸检病理证实的运动神经元病的临床及病理组织学特征进行总结;并对其脑和脊髓切片进行泛素、磷酸化tdp-43免疫组化染色,观察其阳性表达情况,并与同年龄、... 详细信息

目的认识tdp-43蛋白在运动神经元病中枢神经系统的病理性表达特征.方法对4例经尸检病理证实的运动神经元病的临床及病理组织学特征进行总结;并对其脑和脊髓切片进行泛素、磷酸化tdp-43免疫组化染色,观察其阳性表达情况,并与同年龄、无神经疾病病史的3例病例的脑和脊髓组织进行对照.结果 4例病例具有运动神经元病典型的临床与组织学特征,其脑和脊髓组织中,3例存在神经元泛素阳性包涵体结构,主要表现为丝团样包涵体,致密圆形包涵体及路易样包涵体;2例存在明确的tdp-43阳性表达,表现为广泛分布于大脑运动皮层及脊髓前角的各种形态的神经元胞浆包涵体及胶质细胞包涵体,1例存在脊髓前角神经元tdp43弱阳性表达.对照病例无泛素阳性及tdp-43阳性包涵体发现.结论运动神经元病患者的中枢神经系统存在广泛tdp-43蛋白阳性表达,且其阳性包涵体具有一定特征性,值得进一步研究其形成机制.

关键词：运动神经元病 tdp-43 泛素蛋白包涵体脑脊髓

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氧化应激通过tdp-43激活mtDNA-cGAS/STING通路诱发神经元损伤和小鼠痛觉敏化

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陆军军医大学学报 2024年第18期46卷 2036-2045页

作者：李丽黄鹏辉崔剑陆军军医大学(第三军医大学)第一附属医院疼痛科重庆400038

目的探索TAR DNA结合蛋白43(transactive response DNA binding protein 43,tdp-43)在氧化应激诱导的小鼠神经元(neuro-2a,N2a)细胞损伤及小鼠痛觉敏化中的作用及机制。方法①为评估最佳诱导浓度,不同浓度的H_(2)O_(2)处理N2a细胞分为4... 详细信息

目的探索TAR DNA结合蛋白43(transactive response DNA binding protein 43,tdp-43)在氧化应激诱导的小鼠神经元(neuro-2a,N2a)细胞损伤及小鼠痛觉敏化中的作用及机制。方法①为评估最佳诱导浓度,不同浓度的H_(2)O_(2)处理N2a细胞分为4组:对照组、200μmol/L H_(2)O_(2)组、400μmol/L H_(2)O_(2)组和800μmol/L H_(2)O_(2)组。②为评估最佳诱导时间,400μmol/L H_(2)O_(2)处理N2a细胞分为4组:对照组、6 h H_(2)O_(2)组、12 h H_(2)O_(2)组和24 h H_(2)O_(2)组。③为验证线粒体DNA(mitochondria DNA,mtDNA)释放途径,使用环孢素(cyclosporin,CsA)抑制线粒体通透性转换孔(mitochondrial permeability transition pore,mPTP)分为3组:对照组、24 h H_(2)O_(2)组和24 h H_(2)O_(2)+CsA组。④为验证tdp-43介导的细胞损伤机制,siRNA抑制tdp-43后分为3组:对照组、24 h H_(2)O_(2)组、24 h H_(2)O_(2)+sitdp-43组。⑤采用CCK-8检测细胞活性,EdU检测细胞增殖,Western blot检测tdp-43、神经元标志物(neuronal nuclei,NeuN)、环状GMP-AMP合酶(cylic GMP-AMP synthase,cGAS)和干扰素基因刺激因子(stimulator of interferon,STING)表达,qPCR检测mtDNA,免疫染色观察细胞内tdp-43表达变化,Calcein AM染色评估mPTP开放。⑥为验证tdp-43在神经病理性疼痛(neuropathic pain,NP)中的作用,将24只6~8周健康SPF级雄性C57BL/6J小鼠(体质量25~30 g)使用随机数字表法分为3组:对照组、慢性压迫性损伤(chronic constriction injury,CCI)组、CCI+sitdp-43组,术前1 d和术后7、14、21 d进行鞘内注射sitdp-43;术前1 d和术后1、3、5、7、14、21 d通过von Frey纤维丝和热辐射法测定小鼠机械痛阈值和热痛阈值,免疫荧光检测术后21 d腰段(L5-L6)脊髓背角中tdp-43与NeuN的变化。结果氧化应激刺激诱导N2a中tdp-43蛋白表达增加,刺激mtDNA通过mPTP释放,上调cGAS、STING的表达,影响N2a的细胞活性(Ptdp-43的表达后可显著降低mtDNA的释放,抑制cGAS和STING的表达,并恢复N2a细胞的增殖能力(Ptdp-43表达增加(Ptdp-43后,可提高CCI小鼠的机械痛阈值和热痛阈值(Ptdp-43蛋白增加,刺激mtDNA通过mPTP释放到细胞质,激活cGAS/STING通路,导致神经元损伤并加重CCI小鼠痛觉敏化。

关键词：神经病理性疼痛 tdp-43 cGAS/STING通路 mtDNA 氧化应激

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tdp-43 and Mitochondrial Dysfunction in Neurodegenerative diseases

TDP-43 and Mitochondrial Dysfunction in Neurodegenerative di...

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中国神经科学学会第十二届全国学术会议

作者： Lu-wen WANG Ju GAO Sandra L.SIEDLAC Hisashi FUJIOKA Xing-long WANG Departments of Pathology Case Western Reserve University/University Hospitals Case Medical Center Electron Microscopy Facility Case Western Reserve University

Objective TAR DNA-binding protein 43（tdp-43, also named ALS10） is a small ubiquitously expressed RNA/DNA binding protein that primarily binds messenger RNAs（m RNAs）, and regulates their post-transcriptional processing. Translocation of tdp-43 from nuclear to cytoplasm is implicated as the cause of neurodegeneration in diverse major neurodegenerative diseases including amyotrophic lateral sclerosis（ALS）, frontotemporal dementia（FTD）, Alzheimer’s disease（AD）, Parkinson’s disease（PD） and Huntington’s disease（HD）. However, the tdp-43 cytoplasmic target remains elusive. Like tdp-43 proteinopathy, mitochondrial dysfunction is a prominent pathological feature of a wide range of neurodegenerative diseases. In this study, we investigate whether and how tdp-43 proteinopathy contributes to mitochondrial dysfunction and neuronal loss. Methods The localization of tdp-43 in mitochondria in patients with ALS, FTD or AD was measured by confocal microscopy, immuno-electron microscopy and subcellular fractionation. And, cell and animal models were employed to test whether the mitochondrial localization of tdp-43 is required for its toxicity on mitochondria and neurons. Results（1） tdp-43 accumulates in mitochondria in patients with ALS, FTD or AD.（2） tdp-43 in mitochondria impairs mitochondrial function.（3） tdp-43 mitochondrial localization is required for its toxicity on neurons. Conclusion Targeting tdp-43 in mitochondria may be a novel therapeutic target for neurodegeneration.

关键词： tdp-43 mitochondria amyotrophic lateral sclerosis frontotemporal dementia Alzheimer’s disease

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The emerging tdp-43 proteinopathy

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Neuroimmunology and Neuroinflammation 2018年第5期5卷 4-6页

作者： George P.Paraskevas Mara Bourbouli Ioannis Zaganas Elisabeth Kapaki Cognitive and Movement Disorders Clinic and Neurochemistry Unit 1st Department of NeurologySchool of MedicineNationaland Kapodistrian University of AthensAthens11528Greece Neurology Laboratory of the Department of Neurology School of MedicineUniversity of CreteCrete71003Greece

Currently, neurodegenerative diseases are viewed as proteinopathies. In this context, a specific protein or peptide is involved in the pathogenesis of the disease by missfolding, polymerization, reduced degradation and final accumulation in the form of insoluble inclusions leading to neurodegeneration by various interacting mechanisms[1,2].

关键词： The emerging tdp-43 neurodegenerative diseases

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tdp-43通过调控HDAC1参与OSAS大鼠认知障碍的研究

TDP-43通过调控HDAC1参与OSAS大鼠认知障碍的研究

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作者：张妮遵义医科大学

学位级别：硕士

目的:通过慢性间歇性缺氧的方法构建OSAS大鼠模型,予双侧海马立体定位注射慢病毒对tdp-43进行干预,观察及探讨tdp-43通过调控HDAC1在OSAS认知障碍机制中的作用,为进一步认识及研究OSAS所致的认知障碍提供新的思路及方法。方法:将40只SD... 详细信息

目的:通过慢性间歇性缺氧的方法构建OSAS大鼠模型,予双侧海马立体定位注射慢病毒对tdp-43进行干预,观察及探讨tdp-43通过调控HDAC1在OSAS认知障碍机制中的作用,为进一步认识及研究OSAS所致的认知障碍提供新的思路及方法。方法:将40只SD雄性大鼠随机分为4组:正常组（Con组）、OSAS模型组（OSAS组）、tdp-43敲减组（tdp-43-KD组）及空病毒对照组（Vehicle组）,其中Vehicle组及tdp-43-KD组提前2周通过双侧海马立体定位注射方法及免疫印迹技术筛选出tdp-43慢病毒的117序列、118序列及119序列中敲减效果最明显者,并通过免疫荧光技术检测慢病毒在大鼠海马组织的病毒转染情况,确定慢病毒转染成功后,除正常对照组以外,其余各组均采用慢性间歇性缺氧方法构建OSAS大鼠模型,模型构建成功后使用Morris水迷宫对各组大鼠进行行为学实验评估,观察大鼠的学习记忆能力。结束后分离取出大鼠的海马组织,采取Hoechst染色观察各组海马神经元细胞的凋亡情况;使用免疫组化的检测方法观察tdp-43和HDAC1在神经细胞内的定位;并通过Western blotting技术对各组大鼠海马组织中的tdp-43、HDAC1蛋白进行定量分析。结果:1.通过使用Western blotting技术对慢病毒序列进行筛选,可发现注射慢病毒的大鼠海马组织中,tdp-43慢病毒119序列的表达水平较tdp-43慢病毒117序列及118序列低。与此同时,119序列的tdp-43的表达水平较Con组低（P＜0.05）。其次,使用双侧海马定位注射tdp-43敲减慢病毒并转染2周后,采用免疫荧光技术证实了tdp-43在大鼠海马CA1区有阳性表达。2.监测慢性缺氧-复氧情况下大鼠鼠尾动脉血氧饱和度的变化情况,二者对比存在差异（P＜0.05）,缺氧期（63.65±1.93）,复氧期（93.96±2.07）,在构建慢性缺氧的OSAS模型的过程中可见模型大鼠出现嗜睡、烦躁、精神萎靡及仰头深大呼吸等症状,说明OSAS模型构建成功。***水迷宫行为学观察结果:与Con组相比,OSAS组寻找逃生隐藏平台的时间较长,且撤去平台后,探索穿越虚拟平台的次数较少,具有统计学意义（P＜0.05）。Vehicle组寻找逃生隐藏平台时间较长,探索穿越虚拟平台次数少,与OSAS组相比,其寻找平台时间及穿越平台次数无明显差异,无统计学意义（P＞0.05）。与OSAS组及Vehicle组相比,tdp-43-KD组寻找隐藏平台时间较短,且穿越虚拟平台次数较多,二者均有统计学意义（P＜0.05）。***染色:与正常组相比,OSAS组大鼠的神经细胞凋亡增多,海马CA1区及其附近可观察到大量染色质固缩后细胞核呈圆状或固缩状、团块状、碎片状的致密浓染,颜色与正常神经细胞相比更加发蓝发亮。Vehicle组与OSAS组相比,细胞凋亡情况未见显著差异。与OSAS组及Vehicle组相比,tdp-43-KD组的大鼠神经细胞的凋亡明显减少。5.蛋白免疫印迹结果:各组大鼠海马组织中均检测到tdp-43及HDAC1蛋白表达。与正常组相比,OSAS组tdp-43的蛋白表达增加,而HDAC1表达减少,有统计学意义（P＜0.05）。OSAS组与Vehicle组的tdp-43及HDAC1蛋白含量相比,二者表达无显著差异（P＞0.05）。与OSAS组和Vehicle组相比,tdp-43-KD组的tdp-43蛋白的表达减少,而HDAC1蛋白表达增加（P＜0.05）。6.免疫组化结果:通过免疫组化实验观察tdp-43及HDAC1在大鼠海马CA1区神经细胞内定位可发现,tdp-43在胞核、胞浆、胞膜中均有表达,而HDAC1主要在胞膜上表达。结论:tdp-43对OSAS大鼠认知功能有损害作用。将tdp-43蛋白的表达水平下调后,可导致HDAC1蛋白的表达增加,减少了神经细胞的凋亡,改善了OSAS大鼠的认知功能。

关键词：阻塞性睡眠呼吸暂停综合征慢性间歇性缺氧认知功能 tdp-43 HDAC1

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