ArticleCNS & neurological disorders drug targets2012
Effects of α-synuclein overexpression in transgenic Caenorhabditis elegans strains.
Article in CNS & neurological disorders drug targets, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 53 citations in OpenAlex.
- Review
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- Mono-UFMylation promotes misfolding-associated secretion of α-synuclein.Science advances · 2024Article
- Identification of proteotoxic and proteoprotective bacteria that non-specifically affect proteins associated with neurodegenerative diseases.bioRxiv : the preprint server for biology · 2023Article
- Small molecules disaggregate alpha-synuclein and prevent seeding from patient brain-derived fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Neuroprotective Capability of Narcissoside in 6-OHDA-Exposed Parkinson's Disease Models through Enhancing the MiR200a/Nrf-2/GSH Axis and Mediating MAPK/Akt Associated Signaling Pathway.Antioxidants (Basel, Switzerland) · 2022Article
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- Neuroprotective effects of a medium chain fatty acid, decanoic acid, isolated fromFrontiers in pharmacology · 2022Article
- Small molecule inhibitors of α-synuclein oligomers identified by targeting early dopamine-mediated motor impairment in C. elegans.Molecular neurodegeneration · 2021Article
- Diterpene glycosides from Holothuria scabra exert the α-synuclein degradation and neuroprotection against α-synuclein-Mediated neurodegeneration in C. elegans model.Journal of ethnopharmacology · 2021Article
- Emergence of Caenorhabditis elegans as a Model Organism for Dissecting the Gut-Brain Axis.mSystems · 2021Article
- Neurorescue Effects of Frondoside A and Ginsenoside Rg3 inMolecules (Basel, Switzerland) · 2021Article
- Hemiterpene compound, 3,3-dimethylallyl alcohol promotes longevity and neuroprotection in Caenorhabditis elegans.GeroScience · 2021Article
- Parallel-Channel Electrotaxis and Neuron Screening ofMicromachines · 2020Article
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neural protein α-synuclein aggregates both in vivo and in vitro to form insoluble fibrils that are involved in Parkinson's disease pathogenesis. We have generated α-synuclein/fluorescent-protein fusion constructs overexpressed in muscle cells of the nematode, Caenorhabdtis elegans. Green Fluorescent Protein (GFP) variants, Cerulean (C) or Venus (V), were fused to the C-terminus of human α-synuclein (S); the resultant fusion genes were designated SV and SC, plus a CV fusion as well as S, C and V singly. The aggregation behavior of the purified fusion proteins (expressed in E. coli) will be described elsewhere. These constructs were fused to a C. elegans unc-54 myosin promoter, and integrated transgenic lines generated by microinjection, λ-irradiation, and outcrossing of fluorescent progeny. All transgenic lines expressing α- synuclein showed significant reductions (p <0.05) in lifespan, motility and pharyngeal pumping, as compared to wildtype worms or lines expressing CFP and/or YFP only. We showed that CFP and YFP labels colocalised in granular inclusions throughout the body wall in transgenic lines expressing both SC and SV fusions (SC+SV), whereas SV+C worms displayed YFP-labelled inclusions on a diffuse CFP background. These findings implied that the α-synuclein moieties of these fusion proteins still aggregated together in vivo, whereas CFP or YFP moieties alone did not. This in turn suggested that Foerster Resonanace Energy Transfer (FRET) between CFP and YFP labels in α-synuclein aggregates could allow the extent of aggregation to be quantified. Accordingly, we also showed that net FRET signals increased 2- fold between L4 and adult SC+SV worms.
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