ArticleHuman molecular genetics2017
Comparison of the in vivo induction and transmission of α-synuclein pathology by mutant α-synuclein fibril seeds in transgenic mice.
Article in Human molecular genetics, 2017. 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, 32 citations in OpenAlex.
- Strategies for Optimizing Genetic Mouse Models to Enhance the Understanding of Parkinson's Disease.Biomedicines · 2026Review
- Features of Cross-Seeding of Wild-Type Alpha-Synuclein and Its Mutant Form A53T Potentially Useful for the Development of Test Systems.Life (Basel, Switzerland) · 2026Article
- A high-fidelity microfluidic platform reveals retrograde propagation as the main mechanism of α-Synuclein spread in human neurons.NPJ Parkinson's disease · 2025Article
- The G51D SNCA mutation generates a slowly progressive α-synuclein strain in early-onset Parkinson's disease.Acta neuropathologica communications · 2023Article
- Unique seeding profiles and prion-like propagation of synucleinopathies are highly dependent on the host in human α-synuclein transgenic mice.Acta neuropathologica · 2022Article
- Rapid Induction of Dopaminergic Neuron Loss Accompanied by Lewy Body-Like Inclusions in A53T BAC-SNCA Transgenic Mice.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2022Article
- Collusion of α-Synuclein and Aβ aggravating co-morbidities in a novel prion-type mouse model.Molecular neurodegeneration · 2021Article
- Differential seeding and propagating efficiency of α-synuclein strains generated in different conditions.Translational neurodegeneration · 2021Article
- Carboxy-terminal truncation and phosphorylation of α-synuclein elongates survival in a prion-like seeding mouse model of synucleinopathy.Neuroscience letters · 2020Article
- The emerging role of α-synuclein truncation in aggregation and disease.The Journal of biological chemistry · 2020Review
- Carboxy-terminal truncations of mouse α-synuclein alter aggregation and prion-like seeding.FEBS letters · 2020Article
- Structurally distinct α-synuclein fibrils induce robust parkinsonian pathology.Movement disorders : official journal of the Movement Disorder Society · 2020Article
- Pathogenic Mutations Differentially Regulate Cell-to-Cell Transmission of α-Synuclein.Frontiers in cellular neuroscience · 2020Article
- Nuclear Factor-κB Dysregulation and α-Synuclein Pathology: Critical Interplay in the Pathogenesis of Parkinson's Disease.Frontiers in aging neuroscience · 2020Review
- Seeded propagation of α-synuclein aggregation in mouse brain using protein misfolding cyclic amplification.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Oral and intravenous transmission of α-synuclein fibrils to mice.Acta neuropathologica · 2019Article
- Comparative analyses of the in vivo induction and transmission of α-synuclein pathology in transgenic mice by MSA brain lysate and recombinant α-synuclein fibrils.Acta neuropathologica communications · 2019Article
- Physiological C-terminal truncation of α-synuclein potentiates the prion-like formation of pathological inclusions.The Journal of biological chemistry · 2018Article
- Localized Induction of Wild-Type and Mutant Alpha-Synuclein Aggregation Reveals Propagation along Neuroanatomical Tracts.Journal of virology · 2018Article
- Locomotor differences in mice expressing wild-type human α-synuclein.Neurobiology of aging · 2018Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Parkinson's disease (PD) is one of many neurodegenerative diseases termed synucleinopathies, neuropathologically defined by inclusions containing aggregated α-synuclein (αS). αS gene (SNCA) mutations can directly cause autosomal dominant PD. In vitro studies demonstrated that SNCA missense mutations may either enhance or diminish αS aggregation but cross-seeding of mutant and wild-type αS proteins appear to reduce aggregation efficiency. Here, we extended these studies by assessing the effects of seeded αS aggregation in αS transgenic mice through intracerebral or peripheral injection of various mutant αS fibrils. We observed modestly decreased time to paralysis in mice transgenic for human A53T αS (line M83) intramuscularly injected with H50Q, G51D or A53E αS fibrils relative to wild-type αS fibrils. Conversely, E46K αS fibril seeding was significantly delayed and less efficient in the same experimental paradigm. However, the amount and distribution of αS inclusions in the central nervous system were similar for all αS fibril muscle injected mice that developed paralysis. Mice transgenic for human αS (line M20) injected in the hippocampus with wild-type, H50Q, G51D or A53E αS fibrils displayed induction of αS inclusion pathology that increased and spread over time. By comparison, induction of αS aggregation following the intrahippocampal injection of E46K αS fibrils in M20 mice was much less efficient. These findings show that H50Q, G51D or A53E can efficiently cross-seed and induce αS pathology in vivo. In contrast, E46K αS fibrils are intrinsically inefficient at seeding αS inclusion pathology. Consistent with previous in vitro studies, E46K αS polymers are likely distinct aggregated conformers that may represent a unique prion-like strain of αS.
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