ArticleNeurotoxicity research2019
Abundance of Synaptic Vesicle-Related Proteins in Alpha-Synuclein-Containing Protein Inclusions Suggests a Targeted Formation Mechanism.
Article in Neurotoxicity research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Evaluation of cerebrospinal fluid levels of VAMP-2 and SNAP-25 in a dementia with Lewy bodies clinical cohort stratified by Alzheimer's pathophysiological biomarkers.Alzheimer's research & therapy · 2025Article
- Senataxin deficiency disrupts proteostasis through nucleolar ncRNA-driven protein aggregation.The Journal of cell biology · 2024Article
- Parkinson's disease-associated mutations in α-synuclein alters its lipid-bound state.Biophysical journal · 2024Article
- Neuropathology of Multiple System Atrophy, a Glioneuronal Degenerative Disease.Cerebellum (London, England) · 2024Article
- Increased palmitoylation improves estrogen receptor alpha-dependent hippocampal synaptic deficits in a mouse model of synucleinopathy.Science advances · 2023Article
- α-Synuclein fibril and synaptic vesicle interactions lead to vesicle destruction and increased lipid-associated fibril uptake into iPSC-derived neurons.Communications biology · 2023Article
- Spatial Transcriptome Profiling of Mouse Hippocampal Single Cell Microzone in Parkinson's Disease.International journal of molecular sciences · 2023Article
- Heterotypic Amyloid β interactions facilitate amyloid assembly and modify amyloid structure.The EMBO journal · 2022Article
- α-Synuclein Disrupts Vesicle Fusion by Two Mutant-Specific Mechanisms.Molecules and cells · 2022Article
- Exploring the Role of Ubiquitin-Proteasome System in Parkinson's Disease.Molecular neurobiology · 2022Review
- Article
- Dopaminergic Axons: Key Recitalists in Parkinson's Disease.Neurochemical research · 2022Review
- Fluid markers of synapse degeneration in synucleinopathies.Journal of neural transmission (Vienna, Austria : 1996) · 2022Review
- Modeling the cellular fate of alpha-synuclein aggregates: A pathway to pathology.Current opinion in neurobiology · 2022Review
- Similar neuronal imprint and no cross-seeded fibrils in α-synuclein aggregates from MSA and Parkinson's disease.NPJ Parkinson's disease · 2022Article
- Contribution of Autophagy-Lysosomal Pathway in the Exosomal Secretion of Alpha-Synuclein and Its Impact in the Progression of Parkinson's Disease.Frontiers in molecular neuroscience · 2022Review
- Inhibition of Ceramide Synthesis Reduces α-Synuclein Proteinopathy in a Cellular Model of Parkinson's Disease.International journal of molecular sciences · 2021Article
- The Depolarization-Evoked, CaFrontiers in pharmacology · 2021Article
- Parkinson's disease and translational research.Translational neurodegeneration · 2020Review
- Autofluorescence-based analyses of intranuclear inclusions of Fragile X-associated tremor/ataxia syndrome.BioTechniques · 2020Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteinaceous α-synuclein-containing inclusions are found in affected brain regions in patients with Parkinson's disease (PD), Dementia with Lewy bodies (DLB) and multiple system atrophy (MSA). These appear in neurons as Lewy bodies in both PD and DLB and as glial cytoplasmic inclusions (GCIs) in oligodendrocytes in MSA. The role they play in the pathology of the diseases is unknown, and relatively little is still known about their composition. By purifying the inclusions from the surrounding tissue and comprehensively analysing their protein composition, vital clues to the formation mechanism and role in the disease process may be found. In this study, Lewy bodies were purified from postmortem brain tissue from DLB cases (n = 2) and GCIs were purified from MSA cases (n = 5) using a recently improved purification method, and the purified inclusions were analysed by mass spectrometry. Twenty-one percent of the proteins found consistently in the GCIs and LBs were synaptic-vesicle related. Identified proteins included those associated with exosomes (CD9), clathrin-mediated endocytosis (clathrin, AP-2 complex, dynamin), retrograde transport (dynein, dynactin, spectrin) and synaptic vesicle fusion (synaptosomal-associated protein 25, vesicle-associated membrane protein 2, syntaxin-1). This suggests that the misfolded or excess α-synuclein may be targeted to inclusions via vesicle-mediated transport, which also explains the presence of the neuronal protein α-synuclein within GCIs.
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