ArticlePloS one2016
Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Ferroptosis, a therapeutic target for cardiovascular diseases, neurodegenerative diseases and cancer.Journal of translational medicine · 2024Review
- A charged tail on anti-α-Synuclein antibodies does not enhance their affinity to α-Synuclein fibrils.PloS one · 2024Article
- The yeast guanine nucleotide exchange factor Sec7 is a bottleneck in spatial protein quality control and detoxifies neurological disease proteins.Scientific reports · 2023Article
- Aggregation of alpha-synuclein in enteric neurons does not impact function in vitro.Scientific reports · 2022Article
- Amelioration of pathologic α-synuclein-induced Parkinson's disease by irisin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Molecular mechanisms of amyloid formation in living systems.Chemical science · 2022Review
- Transcellular propagation of fibrillar α-synuclein from enteroendocrine to neuronal cells requires cell-to-cell contact and is Rab35-dependent.Scientific reports · 2022Article
- A Palette of Fluorescent AInternational journal of molecular sciences · 2022Article
- T cells, α-synuclein and Parkinson disease.Handbook of clinical neurology · 2022Review
- Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells.Communications biology · 2021Article
- Activation of α7-nAChRs Promotes the Clearance of α-Synuclein and Protects Against Apoptotic Cell Death Induced by Exogenous α-Synuclein Fibrils.Frontiers in cell and developmental biology · 2021Article
- Particle Detection and Characterization for Biopharmaceutical Applications: Current Principles of Established and Alternative Techniques.Pharmaceutics · 2020Review
- Transmission of α-synuclein seeds in neurodegenerative disease: recent developments.Laboratory investigation; a journal of technical methods and pathology · 2019Review
- AFM-STED correlative nanoscopy reveals a dark side in fluorescence microscopy imaging.Science advances · 2019Article
- Propagation of α-Synuclein Strains within Human Reconstructed Neuronal Network.Stem cell reports · 2019Article
- Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.Chembiochem : a European journal of chemical biology · 2018Article
- Import and Export of Misfolded α-Synuclein.Frontiers in neuroscience · 2018Review
- Polarized super-resolution structural imaging inside amyloid fibrils using Thioflavine T.Scientific reports · 2017Article
- Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies.The Journal of biological chemistry · 2017Article
- Quantitative computational models of molecular self-assembly in systems biology.Physical biology · 2017Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of α-synuclein has been linked to both familial and sporadic Parkinson's disease. Recent studies suggest that α-synuclein aggregates may spread from cell to cell and raise questions about the propagation of neurodegeneration. While continuous progress has been made characterizing α-synuclein aggregates in vitro, there is a lack of information regarding the structure of these species inside the cells. Here, we use confocal fluorescence microscopy in combination with direct stochastic optical reconstruction microscopy, dSTORM, to investigate α-synuclein uptake when added exogenously to SH-SY5Y neuroblastoma cells, and to probe in situ morphological features of α-synuclein aggregates with near nanometer resolution. We demonstrate that using dSTORM, it is possible to follow noninvasively the uptake of extracellularly added α-synuclein aggregates by the cells. Once the aggregates are internalized, they move through the endosomal pathway and accumulate in lysosomes to be degraded. Our dSTORM data show that α-synuclein aggregates remain assembled after internalization and they are shortened as they move through the endosomal pathway. No further aggregation was observed inside the lysosomes as speculated in the literature, nor in the cytoplasm of the cells. Our study thus highlights the super-resolution capability of dSTORM to follow directly the endocytotic uptake of extracellularly added amyloid aggregates and to probe the morphology of in situ protein aggregates even when they accumulate in small vesicular compartments.
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