메뉴 건너뛰기




Volumn 6, Issue 27, 2015, Pages 24178-24191

Exposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure

Author keywords

ALS; Exosomes; FTD; TDP 43; Tunneling nanotubes

Indexed keywords

TAR DNA BINDING PROTEIN; DNA BINDING PROTEIN; NANOTUBE; PRION;

EID: 84943414298     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.4680     Document Type: Article
Times cited : (123)

References (58)
  • 1
    • 37349041489 scopus 로고    scopus 로고
    • Motor neuron disease and frontotemporal lobar degeneration:a tale of two disorders linked to TDP-43
    • Elman LB, McCluskey L and Grossman M. Motor neuron disease and frontotemporal lobar degeneration:a tale of two disorders linked to TDP-43. Neuro-Signals. 2008; 16:85-90.
    • (2008) Neuro-Signals , vol.16 , pp. 85-90
    • Elman, L.B.1    McCluskey, L.2    Grossman, M.3
  • 2
    • 78651268247 scopus 로고    scopus 로고
    • A morphometric study of the spatial patterns of TDP-43 immunoreactive neuronal inclusions in frontotemporal lobar degeneration (FTLD) with progranulin (GRN) mutation
    • Armstrong RA and Cairns NJ. A morphometric study of the spatial patterns of TDP-43 immunoreactive neuronal inclusions in frontotemporal lobar degeneration (FTLD) with progranulin (GRN) mutation. Histology and histopathology. 2011;26:185-190.
    • (2011) Histology and histopathology , vol.26 , pp. 185-190
    • Armstrong, R.A.1    Cairns, N.J.2
  • 3
    • 84870993605 scopus 로고    scopus 로고
    • The RNA-binding motif 45 (RBM45) protein accumulates in inclusion bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients
    • Collins M, Riascos D, Kovalik T, An J, Krupa K, Hood BL, Conrads TP, Renton AE, Traynor BJ and Bowser R. The RNA-binding motif 45 (RBM45) protein accumulates in inclusion bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients. Acta neuropathologica. 2012; 124:717-732.
    • (2012) Acta neuropathologica , vol.124 , pp. 717-732
    • Collins, M.1    Riascos, D.2    Kovalik, T.3    An, J.4    Krupa, K.5    Hood, B.L.6    Conrads, T.P.7    Renton, A.E.8    Traynor, B.J.9    Bowser, R.10
  • 4
    • 84866490231 scopus 로고    scopus 로고
    • The molecular basis of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum
    • van Langenhove T, van der Zee J and van Broeckhoven C. The molecular basis of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum. Annals of medicine. 2012;44:817-28.
    • (2012) Annals of medicine , vol.44 , pp. 817-828
    • van Langenhove, T.1    van der Zee, J.2    van Broeckhoven, C.3
  • 5
    • 80052967905 scopus 로고    scopus 로고
    • TDP-43:the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Baloh RH. TDP-43:the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. The FEBS journal. 2011;278:3539-3549.
    • (2011) The FEBS journal , vol.278 , pp. 3539-3549
    • Baloh, R.H.1
  • 7
    • 80755153025 scopus 로고    scopus 로고
    • TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
    • Cohen TJ, Lee VM and Trojanowski JQ. TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies. Trends in molecular medicine. 2011; 17:659-667.
    • (2011) Trends in molecular medicine , vol.17 , pp. 659-667
    • Cohen, T.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 8
    • 84866251985 scopus 로고    scopus 로고
    • RNA-Binding Proteins in Amyotrophic Lateral Sclerosis and Neurodegeneration
    • Ugras SE and Shorter J. RNA-Binding Proteins in Amyotrophic Lateral Sclerosis and Neurodegeneration. Neurology research international. 2012;2012:432780.
    • (2012) Neurology research international , vol.2012
    • Ugras, S.E.1    Shorter, J.2
  • 9
    • 84861841901 scopus 로고    scopus 로고
    • Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation?
    • Kanouchi T, Ohkubo T and Yokota T. Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation? Journal of neurology, neurosurgery, and psychiatry. 2012;83:739-45.
    • (2012) Journal of neurology, neurosurgery, and psychiatry , vol.83 , pp. 739-745
    • Kanouchi, T.1    Ohkubo, T.2    Yokota, T.3
  • 11
    • 33750012281 scopus 로고    scopus 로고
    • Classical and atypical clinical features in amyotrophic lateral sclerosis [Article in French]
    • Spec No 2
    • Pradat PF and Bruneteau G. Classical and atypical clinical features in amyotrophic lateral sclerosis [Article in French]. Revue neurologique. 2006;162 Spec No 2:4S17-14S24.
    • (2006) Revue neurologique , vol.162 , pp. 4S17-14S24
    • Pradat, P.F.1    Bruneteau, G.2
  • 13
    • 84931042760 scopus 로고    scopus 로고
    • Chronic exposure to cerebrospinal fluid of multiple system atrophy in neuroblastoma and glioblastoma cells induces cytotoxicity via ER stress and autophagy activation
    • Wang X, Ma M, Teng J, Zhang J, Zhou S, Zhang Y, Wu E and Ding X. Chronic exposure to cerebrospinal fluid of multiple system atrophy in neuroblastoma and glioblastoma cells induces cytotoxicity via ER stress and autophagy activation. Oncotarget. 2015;6:13278-13294.
    • (2015) Oncotarget , vol.6 , pp. 13278-13294
    • Wang, X.1    Ma, M.2    Teng, J.3    Zhang, J.4    Zhou, S.5    Zhang, Y.6    Wu, E.7    Ding, X.8
  • 15
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert M, Clavaguera F and Tolnay M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends in neurosciences. 2010;33:317-325.
    • (2010) Trends in neurosciences , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 16
    • 84921424656 scopus 로고    scopus 로고
    • Extracellular vesicles including exosomes are mediators of signal transduction:Are they protective or pathogenic?
    • Gangoda L, Boukouris S, Liem M, Kalra H and Mathivanan S. Extracellular vesicles including exosomes are mediators of signal transduction:Are they protective or pathogenic? Proteomics. 2014;15:260-271.
    • (2014) Proteomics , vol.15 , pp. 260-271
    • Gangoda, L.1    Boukouris, S.2    Liem, M.3    Kalra, H.4    Mathivanan, S.5
  • 17
    • 79953855830 scopus 로고    scopus 로고
    • TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage
    • Suzuki H, Lee K and Matsuoka M. TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage. The Journal of biological chemistry. 2011;286:13171-13183.
    • (2011) The Journal of biological chemistry , vol.286 , pp. 13171-13183
    • Suzuki, H.1    Lee, K.2    Matsuoka, M.3
  • 19
    • 79251484992 scopus 로고    scopus 로고
    • The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominantnegative mechanism
    • Yang C, Tan W, Whittle C, Qiu L, Cao L, Akbarian S and Xu Z. The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominantnegative mechanism. PloS one. 2010;5:e15878.
    • (2010) PloS one , vol.5
    • Yang, C.1    Tan, W.2    Whittle, C.3    Qiu, L.4    Cao, L.5    Akbarian, S.6    Xu, Z.7
  • 21
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration:prion-like spreading in ALS
    • Polymenidou M and Cleveland DW. The seeds of neurodegeneration:prion-like spreading in ALS. Cell. 2011; 147:498-508.
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 24
    • 84878373738 scopus 로고    scopus 로고
    • Different molecular pathologies result in similar spatial patterns of cellular inclusions in neurodegenerative disease:a comparative study of eight disorders
    • Armstrong RA and Cairns NJ. Different molecular pathologies result in similar spatial patterns of cellular inclusions in neurodegenerative disease:a comparative study of eight disorders. Journal of Neural Transmission. 2012;119:1551-1560.
    • (2012) Journal of Neural Transmission , vol.119 , pp. 1551-1560
    • Armstrong, R.A.1    Cairns, N.J.2
  • 30
    • 80055078948 scopus 로고    scopus 로고
    • CSF from amyotrophic lateral sclerosis patients produces glutamate independent death of rat motor brain cortical neurons:protection by resveratrol but not riluzole
    • Yanez M, Galan L, Matias-Guiu J, Vela A, Guerrero A and Garcia AG. CSF from amyotrophic lateral sclerosis patients produces glutamate independent death of rat motor brain cortical neurons:protection by resveratrol but not riluzole. Brain research. 2011;1423:77-86.
    • (2011) Brain research , vol.1423 , pp. 77-86
    • Yanez, M.1    Galan, L.2    Matias-Guiu, J.3    Vela, A.4    Guerrero, A.5    Garcia, A.G.6
  • 32
    • 79956194152 scopus 로고    scopus 로고
    • Down regulation of trophic factors in neonatal rat spinal cord after administration of cerebrospinal fluid from sporadic amyotrophic lateral sclerosis patients
    • Deepa P, Shahani N, Alladi PA, Vijayalakshmi K, Sathyaprabha TN, Nalini A, Ravi V and Raju TR. Down regulation of trophic factors in neonatal rat spinal cord after administration of cerebrospinal fluid from sporadic amyotrophic lateral sclerosis patients. Journal of Neural Transmission. 2011;118:531-538.
    • (2011) Journal of Neural Transmission , vol.118 , pp. 531-538
    • Deepa, P.1    Shahani, N.2    Alladi, P.A.3    Vijayalakshmi, K.4    Sathyaprabha, T.N.5    Nalini, A.6    Ravi, V.7    Raju, T.R.8
  • 37
    • 84875271402 scopus 로고    scopus 로고
    • The molecular basis of induction and formation of tunneling nanotubes
    • Kimura S, Hase K and Ohno H. The molecular basis of induction and formation of tunneling nanotubes. Cell and tissue research. 2013;352:67-76.
    • (2013) Cell and tissue research , vol.352 , pp. 67-76
    • Kimura, S.1    Hase, K.2    Ohno, H.3
  • 38
    • 84866318324 scopus 로고    scopus 로고
    • Tunneling-nanotube:A new way of cell-cell communication
    • Zhang Y. Tunneling-nanotube:A new way of cell-cell communication. Communicative & integrative biology. 2011;4:324-325.
    • (2011) Communicative & integrative biology , vol.4 , pp. 324-325
    • Zhang, Y.1
  • 39
    • 79952619322 scopus 로고    scopus 로고
    • Tunneling-nanotube development in astrocytes depends on p53 activation
    • Wang Y, Cui J, Sun X and Zhang Y. Tunneling-nanotube development in astrocytes depends on p53 activation. Cell death and differentiation. 2011;18:732-742.
    • (2011) Cell death and differentiation , vol.18 , pp. 732-742
    • Wang, Y.1    Cui, J.2    Sun, X.3    Zhang, Y.4
  • 41
    • 23844523232 scopus 로고    scopus 로고
    • Frontotemporal dementia with co-occurrence of astrocytic plaques and tufted astrocytes, and severe degeneration of the cerebral white matter:a variant of corticobasal degeneration?
    • Tan CF, Piao YS, Kakita A, Yamada M, Takano H, Tanaka M, Mano A, Makino K, Nishizawa M, Wakabayashi K and Takahashi H. Frontotemporal dementia with co-occurrence of astrocytic plaques and tufted astrocytes, and severe degeneration of the cerebral white matter:a variant of corticobasal degeneration? Acta neuropathologica. 2005; 109:329-338.
    • (2005) Acta neuropathologica , vol.109 , pp. 329-338
    • Tan, C.F.1    Piao, Y.S.2    Kakita, A.3    Yamada, M.4    Takano, H.5    Tanaka, M.6    Mano, A.7    Makino, K.8    Nishizawa, M.9    Wakabayashi, K.10    Takahashi, H.11
  • 42
    • 0035115604 scopus 로고    scopus 로고
    • Astrocytes degenerate in frontotemporal dementia:possible relation to hypoperfusion
    • Martin JA, Craft DK, Su JH, Kim RC and Cotman CW. Astrocytes degenerate in frontotemporal dementia:possible relation to hypoperfusion. Neurobiology of aging. 2001; 22:195-207.
    • (2001) Neurobiology of aging , vol.22 , pp. 195-207
    • Martin, J.A.1    Craft, D.K.2    Su, J.H.3    Kim, R.C.4    Cotman, C.W.5
  • 44
    • 84907092601 scopus 로고    scopus 로고
    • The non-cell-autonomous component of ALS: new in vitro models and future challenges
    • Ferraiuolo L. The non-cell-autonomous component of ALS: new in vitro models and future challenges. Biochemical Society transactions. 2014;42:1270-1274.
    • (2014) Biochemical Society transactions , vol.42 , pp. 1270-1274
    • Ferraiuolo, L.1
  • 46
    • 84920106094 scopus 로고    scopus 로고
    • TDP-43 modification in the hSOD1 amyotrophic lateral sclerosis mouse model
    • Cai M, Lee KW, Choi SM and Yang EJ. TDP-43 modification in the hSOD1 amyotrophic lateral sclerosis mouse model. Neurological research. 2014;37:253-262.
    • (2014) Neurological research , vol.37 , pp. 253-262
    • Cai, M.1    Lee, K.W.2    Choi, S.M.3    Yang, E.J.4
  • 47
    • 84906829145 scopus 로고    scopus 로고
    • Familial and sporadic ALS astrocytes activate necroptosis in motor neurons [Article in French]
    • Le Verche V. Familial and sporadic ALS astrocytes activate necroptosis in motor neurons [Article in French]. Medecine sciences. 2014;30:748-750.
    • (2014) Medecine sciences , vol.30 , pp. 748-750
    • Le Verche, V.1
  • 48
    • 84973855590 scopus 로고    scopus 로고
    • Role of transcription factor yin yang 1 in manganeseinduced reduction of astrocytic glutamate transporters: Putative mechanism for manganese-induced neurotoxicity
    • S0197-0186(14)00185-5
    • Karki P, Smith K, Johnson J, Jr., Aschner M and Lee E. Role of transcription factor yin yang 1 in manganeseinduced reduction of astrocytic glutamate transporters: Putative mechanism for manganese-induced neurotoxicity. Neurochemistry international. 2014;S0197-0186(14)00185-5.
    • (2014) Neurochemistry international
    • Karki, P.1    Smith, K.2    Johnson, J.3    Aschner, M.4    Lee, E.5
  • 49
    • 84904648362 scopus 로고    scopus 로고
    • Mitochondria-targeted catalase reverts the neurotoxicity of hSOD1G(9)(3)A astrocytes without extending the survival of ALS-linked mutant hSOD1 mice
    • Pehar M, Beeson G, Beeson CC, Johnson JA and Vargas MR. Mitochondria-targeted catalase reverts the neurotoxicity of hSOD1G(9)(3)A astrocytes without extending the survival of ALS-linked mutant hSOD1 mice. PloS one. 2014;9:e103438.
    • (2014) PloS one , vol.9
    • Pehar, M.1    Beeson, G.2    Beeson, C.C.3    Johnson, J.A.4    Vargas, M.R.5
  • 50
    • 84895447564 scopus 로고    scopus 로고
    • Motor neuron death in ALS:programmed by astrocytes?
    • Pirooznia SK, Dawson VL and Dawson TM. Motor neuron death in ALS:programmed by astrocytes? Neuron. 2014; 81:961-963.
    • (2014) Neuron , vol.81 , pp. 961-963
    • Pirooznia, S.K.1    Dawson, V.L.2    Dawson, T.M.3
  • 51
    • 84893574224 scopus 로고    scopus 로고
    • Astrocytes expressing mutant SOD1 and TDP43 trigger motoneuron death that is mediated via sodium channels and nitroxidative stress
    • Rojas F, Cortes N, Abarzua S, Dyrda A and van Zundert B. Astrocytes expressing mutant SOD1 and TDP43 trigger motoneuron death that is mediated via sodium channels and nitroxidative stress. Frontiers in cellular neuroscience. 2014;8:24.
    • (2014) Frontiers in cellular neuroscience , vol.8 , pp. 24
    • Rojas, F.1    Cortes, N.2    Abarzua, S.3    Dyrda, A.4    van Zundert, B.5
  • 52
    • 0030222037 scopus 로고    scopus 로고
    • Microglia:a sensor for pathological events in the CNS
    • Kreutzberg GW. Microglia:a sensor for pathological events in the CNS. Trends in neurosciences. 1996;19:312-318.
    • (1996) Trends in neurosciences , vol.19 , pp. 312-318
    • Kreutzberg, G.W.1
  • 54
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk VI, Menzies FM and Rubinsztein DC. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS letters. 2010; 584:1393-1398.
    • (2010) FEBS letters , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 55
    • 41449113885 scopus 로고    scopus 로고
    • Altered macroautophagy in the spinal cord of SOD1 mutant mice
    • Li L, Zhang X and Le W. Altered macroautophagy in the spinal cord of SOD1 mutant mice. Autophagy. 2008;4:290-293.
    • (2008) Autophagy , vol.4 , pp. 290-293
    • Li, L.1    Zhang, X.2    Le, W.3
  • 56
    • 79955522014 scopus 로고    scopus 로고
    • Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis
    • Sasaki S. Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis. Journal of neuropathology and experimental neurology. 2011;70:349-359.
    • (2011) Journal of neuropathology and experimental neurology , vol.70 , pp. 349-359
    • Sasaki, S.1
  • 57
    • 77956224840 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a converging point of multiple pathological pathways in amyotrophic lateral sclerosis
    • Shi P, Wei Y, Zhang J, Gal J and Zhu H. Mitochondrial dysfunction is a converging point of multiple pathological pathways in amyotrophic lateral sclerosis. Journal of Alzheimer's disease :JAD. 2010;20 Suppl 2:S311-324.
    • (2010) Journal of Alzheimer's disease :JAD , vol.20 , pp. S311-S324
    • Shi, P.1    Wei, Y.2    Zhang, J.3    Gal, J.4    Zhu, H.5
  • 58
    • 77957833643 scopus 로고    scopus 로고
    • Blocking the mitochondrial apoptotic pathway preserves motor neuron viability and function in a mouse model of amyotrophic lateral sclerosis
    • Reyes NA, Fisher JK, Austgen K, VandenBerg S, Huang EJ and Oakes SA. Blocking the mitochondrial apoptotic pathway preserves motor neuron viability and function in a mouse model of amyotrophic lateral sclerosis. The Journal of clinical investigation. 2010;120:3673-3679.
    • (2010) The Journal of clinical investigation , vol.120 , pp. 3673-3679
    • Reyes, N.A.1    Fisher, J.K.2    Austgen, K.3    VandenBerg, S.4    Huang, E.J.5    Oakes, S.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.