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Human Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes
Open accessAbstract
Many lines of evidence suggest that the Parkinson's disease (PD)-related protein α-synuclein (α-SYN) can propagate from cell to cell in a prion-like manner. However, the cellular mechanisms behind the spreading remain elusive. Here, we show that human astrocytes derived from embryonic stem cells actively transfer aggregated α-SYN to nearby astrocytes via direct contact and tunneling nanotubes (TNTs). Failure in the astrocytes' lysosomal digestion of excess α-SYN oligomers results in α-SYN deposits in the trans-Golgi network followed by endoplasmic reticulum swelling and mitochondrial disturbances. The stressed astrocytes respond by conspicuously sending out TNTs, enabling intercellular transfer of α-SYN to healthy astrocytes, which in return deliver mitochondria, indicating a TNT-mediated rescue mechanism. Using a pharmacological approach to inhibit TNT formation, we abolished the transfer of both α-SYN and mitochondria. Together, our results highlight the role of astrocytes in α-SYN cell-to-cell transfer, identifying possible pathophysiological events in the PD brain that could be of therapeutic relevance. SIGNIFICANCE STATEMENT Astrocytes are the major cell type in the brain, yet their role in Parkinson's disease progression remains elusive. Here, we show that human astrocytes actively transfer aggregated α-synuclein (α-SYN) to healthy astrocytes via direct contact and tunneling nanotubes (TNTs), rather than degrade it. The astrocytes engulf large amounts of oligomeric α-SYN that are subsequently stored in the trans-Golgi network region. The accumulation of α-SYN in the astrocytes affects their lysosomal machinery and induces mitochondrial damage. The stressed astrocytes respond by sending out TNTs, enabling intercellular transfer of α-SYN to healthy astrocytes. Our findings highlight an unexpected role of astrocytes in the propagation of α-SYN pathology via TNTs, revealing astrocytes as a potential target for therapeutic intervention.
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“In the AD and PD brain, both astrocytes and microglia acquire reactive, inflammatory phenotypes and can effectively phagocytose aggregated proteins and cell debris, as well as secrete various cytokines and inflammatory mediators [8–13].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“Subsequently, stressed astrocytes respond by sending out tunneling nanotubes (TNTs), enabling intercellular transfer of pathogenic protein aggregates, as well as MHCII complexes to nearby cells [11, 24].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“The concentrations were selected based on our previous studies [11, 12, 23, 28, 29].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“The αSYN and Aβ accumulation result in severe cellular stress, indicated by lysosomal and mitochondrial deficiencies [11, 12, 23].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“These observations are in line with our previous discoveries that astrocytes easily degrade αSYN and Aβ monomers, while they accumulate larger oligomers and fibrils [11, 12].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“Our previous results indicate that astrocytes are capable of transferring αSYN as well as MHCII to other astrocytes via direct membrane contact and through TNTs, implicating astrocytes as one of the important players in propagation of αSYN pathology [11, 24].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“Microglia and astrocytes are known to be responsible for many inflammatory processes in affected brains, including phagocytosis of αSYN and Aβ aggregates, secretion of inflammatory mediators, and stimulation of the innate immune system [8–12].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“We have previously shown that astrocytes accumulate large amounts of αSYN and Aβ aggregates, resulting in severe cellular stress [11, 12, 23, 24].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
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“We have previously reported that cultured astrocytes accumulate αSYN and Aβ aggregates but not the monomeric form of the proteins [11, 12].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [11]
In the citing paper
“iii) αSyn has the ability to spread to adjacent cells via secretion in exosomes [209], uptake via endocytosis [210] and cell-surface receptors like HSPGs, or even direct neuron-to-neuron [211, 212] or astrocyte-to-neuron [213] transfer via tunneling nanotubes (Fig. 2).”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [213]
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Cites
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Astrocytes: Biology and pathology
Sofroniew, M. V., & Vinters, H. V. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0619-8 · Cited by 5,196
Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
Nanotubular Highways for Intercellular Organelle Transport
Rustom, A., Saffrich, R., Markovic, I., Walther, P., & Gerdes, H.-H. (2004) · Science · doi:10.1126/science.1093133 · Cited by 2,038
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845
Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease
Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., & Olanow, C. W. (2008) · Nature Medicine · doi:10.1038/nm1747 · Cited by 1,722
Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
Desplats, P., Lee, H.-J., Bae, E.-J., Patrick, C., Rockenstein, E., Crews, L., Spencer, B., Masliah, E., & Lee, S.-J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903691106 · Cited by 1,485
In vivo demonstration that α-synuclein oligomers are toxic
Winner, B., Jappelli, R., Maji, S. K., Desplats, P. A., Boyer, L., Aigner, S., Hetzer, C., Loher, T., Vilar, M., Campioni, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100976108 · Cited by 1,463
α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models
Cooper, A. A., Gitler, A. D., Cashikar, A. G., Haynes, C. M., Hill, K. J., Bhullar, B., Liu, K., Xu, K., Strathearn, K. E., Liu, F., et al. (2006) · Science · doi:10.1126/science.1129462 · Cited by 1,411
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Items 101–200 of 341
Grudina, C., Kouroupi, G., Nonaka, T., Hasegawa, M., Matsas, R., & Zurzolo, C. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104609 · Cited by 39
Alpha-Synuclein Aggregates Associated with Mitochondria in Tunnelling Nanotubes
Valdinocci, D., Kovářová, J., Neužil, J., & Pountney, D. L. (2020) · Neurotoxicity Research · doi:10.1007/s12640-020-00285-y · Cited by 39
Tunneling nanotubes: A bridge for heterogeneity in glioblastoma and a new therapeutic target?
Venkatesh, V. S., & Lou, E. (2019) · Cancer Reports · doi:10.1002/cnr2.1185 · Cited by 37
Amro, Z., Yool, A. J., & Collins‐Praino, L. E. (2021) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2021.100242 · Cited by 39
Lysosomal acidification impairment in astrocyte-mediated neuroinflammation
Zeng, J., Indajang, J., Pitt, D., & Lo, C. H. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03410-w · Cited by 44
Cellular mechanisms responsible for cell-to-cell spreading of prions
Vilette, D., Courte, J., Peyrin, J., Coudert, L., Schaeffer, L., Andréoletti, O., & Leblanc, P. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2823-y · Cited by 43
Endosomal-Lysosomal Processing of Neurodegeneration-Associated Proteins in Astrocytes
Wong, C.-O. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145149 · Cited by 31
Jacquet, A. D. R., Denis, H. L., Cicchetti, F., & Alpaugh, M. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00999-7 · Cited by 36
Konstantinidis, E., Portal, B., Mothes, T., Beretta, C., Lindskog, M., & Erlandsson, A. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02687-5 · Cited by 35
Self-citationKhor, S. L. Q., Ng, K. Y., Koh, R. Y., & Chye, S. M. (2023) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527322666230330093829 · Cited by 37
Zhou, C., Huang, M., Wang, S., Chu, S., Zhang, Z., & Chen, N. (2024) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2024.110921 · Cited by 34
Huntington, T. E., & Srinivasan, R. (2021) · Aging and disease · doi:10.14336/ad.2021.0517 · Cited by 34
“Prion-like” seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders
Zampar, S., Gregorio, S. E. D., Grimmer, G., Watts, J. C., & Ingelsson, M. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1436262 · Cited by 39
Self-citationUnconventional Secretion and Intercellular Transfer of Mutant Huntingtin
Tang, B. L. (2018) · Cells · doi:10.3390/cells7060059 · Cited by 34
Evidence of Inflammation in Parkinson’s Disease and Its Contribution to Synucleinopathy
Lai, T. T., Kim, Y. J., Ma, H.-I., & Kim, Y. E. (2022) · Journal of Movement Disorders · doi:10.14802/jmd.21078 · Cited by 32
Miller, S., Campbell, C. E., Jimenez-Corea, H. A., Wu, G., & Logan, R. A. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.824191 · Cited by 34
Harnessing the Therapeutic Potential of the Nrf2/Bach1 Signaling Pathway in Parkinson’s Disease
Ahuja, M., Kaidery, N. A., Dutta, D., Attucks, O. C., Kazakov, E. H., Gazaryan, I. G., Matsumoto, M., Igarashi, K., Sharma, S. M., & Thomas, B. (2022) · Antioxidants · doi:10.3390/antiox11091780 · Cited by 34
The role of glia in Parkinson's disease: Emerging concepts and therapeutic applications
Kuter, K. Z., Cenci, M. A., & Carta, A. R. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.02.004 · Cited by 31
Functional mitochondrial respiration is essential for glioblastoma tumour growth
Brisudová, P., Stojanovic, D., Novák, J., Nahácka, Z., Oliveira, G. L., Vaňátko, O., Dvorakova, S., Endaya, B., Truksa, J., Kubiskova, M., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03429-6 · Cited by 29
Huang, Y., Xie, X.-X., Ji, M., Yu, X., Zhu, J., Zhang, L. L., Liu, X., Chen, W., Li, G., & Liu, R. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.024 · Cited by 30
Mechanistic insights into the protective roles of polyphosphate against amyloid cytotoxicity
Lempart, J., Tse, E., Lauer, J. A., Ivanova, M. I., Sutter, A., Yoo, N. G., Huettemann, P., Southworth, D. R., & Jakob, U. (2019) · Life Science Alliance · doi:10.26508/lsa.201900486 · Cited by 30
The Role of Glial Mitochondria in α-Synuclein Toxicity
Jeon, Y., Kwon, Y., Jo, M., Lee, S., Kim, S., & Kim, H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.548283 · Cited by 31
The amyloid state of proteins: A boon or bane?
Hassan, M. N., Nabi, F., Khan, A. N., Hussain, M. S., Siddiqui, W. A., Uversky, V. N., & Khan, R. H. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.01.115 · Cited by 30
Astrocytes and Alpha-Synuclein: Friend or Foe?
Ozoran, H., & Srinivasan, R. (2023) · Journal of Parkinson s Disease · doi:10.3233/jpd-230284 · Cited by 28
Guo, M. A., Guan, A., Zhang, M., Li, H., Liu, W., Wu, B., Shen, W., You, T., Liang, S., Dong, Q., et al. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107908 · Cited by 28
Potential mechanisms of microRNA mobility
Lemcke, H., & David, R. (2018) · Traffic · doi:10.1111/tra.12606 · Cited by 25
Grochowska, M. M., Mascaro, A. C., Boumeester, V., Natale, D., Breedveld, G. J., Geut, H., van Cappellen, W. A., Boon, A. J. W., Kievit, A. J. A., Sammler, E. M., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02313-3 · Cited by 22
Nanclares, C., Poynter, J., Martell-Martinez, H. A., Vermilyea, S., Araque, A., Kofuji, P., Lee, M. K., & Covelo, A. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02547-3 · Cited by 24
Tunneling Nanotube: An Enticing Cell–Cell Communication in the Nervous System
Dagar, S., & Subramaniam, S. (2023) · Biology · doi:10.3390/biology12101288 · Cited by 24
The role of astrocytes in prion-like mechanisms of neurodegeneration
Smethurst, P., Franklin, H., Clarke, B. E., Sidle, K. C. L., & Patani, R. (2021) · Brain · doi:10.1093/brain/awab366 · Cited by 25
Raghavan, A., Kashyap, R., Sreedevi, P. R., Jos, S., Chatterjee, S., Alex, A., D’Souza, M. N., Giridharan, M., Muddashetty, R. S., Manjithaya, R. R., et al. (2024) · iScience · doi:10.1016/j.isci.2024.110565 · Cited by 23
Intercellular transmission of alpha-synuclein
Wu, S., & Schekman, R. W. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1470171 · Cited by 24
Duan, Q., Zhang, Q., Nie, K., Huang, R., Yang, J., He, P., Tie, Z., Huang, H., Ma, G., Zhang, Y., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107458 · Cited by 23
Tunneling nanotubes: A novel pharmacological target for neurodegenerative diseases?
Wang, X.-T., Sun, H., Chen, N.-H., & Yuan, Y.-H. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105541 · Cited by 22
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Kotarba, S., Kozłowska, M., Scios, M., Saramowicz, K., Barczuk, J., Granek, Z., Siwecka, N., Wiese, W., Golberg, M., Galita, G., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910797 · Cited by 24
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Wang, P., & Ye, Y. (2021) · Life · doi:10.3390/life11090938 · Cited by 21
Torre-Muruzabal, T., der Perren, A. V., Coens, A., Gelders, G., Janer, A. B., Camacho-Garcia, S., Klingstedt, T., Nilsson, K. P. R., Stefanova, N., Melki, R., et al. (2022) · Brain · doi:10.1093/brain/awac061 · Cited by 25
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Donnelly, K. M., Coleman, C. M., Fuller, M. L., Reed, V. L., Smerina, D., Tomlinson, D. S., & Pearce, M. M. P. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.946822 · Cited by 20
Roshanbin, S., Aniszewska, A., Gumucio, A., Masliah, E., Erlandsson, A., Bergström, J. J. E., Ingelsson, M., & Ekmark‐Lewén, S. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.01.010 · Cited by 24
Self-citationKoh, Y. H., Tan, L. Y., & Ng, S. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00413 · Cited by 20
Human pericytes degrade diverse α-synuclein aggregates
Dieriks, B. V., Highet, B., Alik, A., Bellande, T., Stevenson, T. J., Low, V. F., Park, T., Correia, J. A., Schweder, P. M., Faull, R. L. M., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0277658 · Cited by 26
Krejciova, Z., Carlson, G. A., Giles, K., & Prusiner, S. B. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0703-9 · Cited by 20
Mechanisms of tunneling nanotube-based propagation of neurodegenerative disease proteins
Lagalwar, S. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.957067 · Cited by 20
Rostami, J., Jäntti, M. H., Cui, H., Rinne, M. K., Kukkonen, J. P., Falk, A., Erlandsson, A., & Myöhänen, T. T. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110788 · Cited by 20
Self-citationThe Effect of Metformin on Astrocytes in Parkinson’s Disease: Challenges and Opportunities
Al-Kuraishy, H. M., Sulaiman, G. M., Saad, H. M., Mohammed, H. A., Abomughaid, M. M., Al-Gareeb, A. I., & Albuhadily, A. K. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05098-8 · Cited by 18
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Zhao, Y., Keshiya, S., Atashrazm, F., Gao, J., Ittner, L. M., Alessi, D. R., Halliday, G. M., Fu, Y., & Dzamko, N. L. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.09.003 · Cited by 17
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Patel, S., Prajapati, C., Nand, S., & Singh, S. K. (2026) · 3 Biotech · doi:10.1007/s13205-026-04697-z · Cited by 16
Zheng, H., Shi, C., Luo, H., Fan, L., Yang, Z., Hu, X., Zhang, Z., Zhang, S., Hu, Z., Fan, Y., et al. (2020) · The Neuroscientist · doi:10.1177/1073858420943180 · Cited by 21
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D’Sa, K., Choi, M. L., Wagen, A. Z., Setó‐Salvia, N., Kopach, O., Evans, J. R., Rodrigues, M., Lopez-Garcia, P., Lachica, J., Clarke, B. E., et al. (2025) · Science Advances · doi:10.1126/sciadv.adp8504 · Cited by 17
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Bo, R., Li, Y., Zhou, T.-T., Chen, N., & Yuan, Y. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.108964 · Cited by 18
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Albert, K., Kälvälä, S., Hakosalo, V., Syvänen, V., Krupa, P., Niskanen, J., Peltonen, S., Sonninen, T.-M., & Lehtonen, Š. (2022) · Biomedicines · doi:10.3390/biomedicines10102649 · Cited by 16
Chakraborty, R., Belian, S., & Zurzolo, C. (2023) · Extracellular Vesicles and Circulating Nucleic Acids · doi:10.20517/evcna.2023.05 · Cited by 15
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Bendifallah, M., Redeker, V., Monsellier, É., Bousset, L., Bellande, T., & Melki, R. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.04.091 · Cited by 15
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Yamaguchi, H., Nishimura, Y., Matsuse, D., Sekiya, H., Masaki, K., Tanaka, T., Saiga, T., Harada, M., Kira, Y., Dickson, D. W., et al. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.07.004 · Cited by 14
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Verkhratsky, A., & Butt, A. M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-821565-4.00012-2 · Cited by 10
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Khan, Z., & Jung, Y. J. (2023) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2023.00052 · Cited by 9
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Dias, G. R., Hayashide, L. D. S., Pessoa, B., Diniz, L. P., & Pontes, B. (2026) · Brain Sciences · doi:10.3390/brainsci16020138 · Cited by 7
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Metadata
- Authors
- Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A.
- Affiliations
- Uppsala University (SE)
- Lund University (SE)
- Corresponding author
- Erlandsson, Anna
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2017-10-31
- Volume
- 37
- Issue
- 49
- Pages
- 11835-11853
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC5719970
- OpenAlex
- W2765364382
- Cited by
- 339
- References
- 75
- Citations by year
- 2026: 45 · 2025: 30 · 2024: 64 · 2023: 47 · 2022: 34 · 2021: 38 · 2020: 26 · 2019: 31 · 2018: 24
- FWCI
- 15.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Uppsala University Publications (Uppsala University) (submittedVersion, other-oa)
- Lund University Publications (Lund University) (submittedVersion)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Apollo (cc-by)
- Funders
- Åke Wiberg Stiftelse
- Innovationsfonden
- Vetenskapsrådet
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- alpha-synuclein, Parkinson's disease, tunneling nanotubes, astrocytes, prion-like propagation, intercellular transfer, lysosomal degradation, trans-Golgi network, mitochondrial damage, endoplasmic reticulum stress, mitochondrial transfer
- MeSH terms
- Astrocytes, Cell Communication, Cells, Cultured, Humans, Nanotubes, alpha-Synuclein, Embryonic Stem Cells
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