test_moissonnage_selune
type: Agent

Alpha-synuclein molecular pathology : potential relationship with prion diseases
type: Distribution
access URL: https://theses.hal.science/tel-00864013
format: HTML
issued: 2026-05-09T16:24:37.131090
modified: 2026-05-09T16:24:37.107665

Alpha-synuclein molecular pathology : potential relationship with prion diseases
type: Dataset
contact point: Organization
  fn: CCSD
keyword: encephalopathie-spongiforme-transmissible-est
keyword: parkinson
keyword: synucleinopathie
keyword: sdvsalife-sciences-q-bioagricultural-sciences
keyword: synucleinopathy
keyword: lpha-synuclein
keyword: theses
keyword: lpha-synucleine
keyword: maladie-neurodegenerative
keyword: prion
keyword: infoeu-reposemanticsdoctoralthesis
keyword: transmissible-spongiform-encephalopathies-est
keyword: neurodegenerative-disease
landing page: https://theses.hal.science/tel-00864013
description: The overlap of neurotoxic mecanisms involved in prion diseases and synucleinopathies, and the concomitant detection of pathological forms of prion and α-synuclein in a same neurodegenerative disease, raise questions about the existence of potential relationship between α‐synuclein molecular alteration and prion diseases. First, we developed monoclonal antibodies by immunizing mice presenting a spontaneous deletion of the α-synuclein gene with human recombinant α‐synuclein. Then, we characterized the molecular alterations appearing jointly to clinical signs during the aging of a transgenic mouse model of synucleinopathies (TgM83), overexpressing human A53T α‐synuclein. Then, an approach routinely done in the field of prion was used to trigger a synucleinopathy alongside a prion disease. For this purpose, TgM83 mice were inoculated intracerebrally by three different prion strains : transmission of H-type bovine spongiform encephalopathy allows the onset of a prion disease concomitantly to the α‐synuclein pathology developed by the TgM83 mouse model. Finally, intracerebral inoculation of TgM83 mice with brain homogenates from symptomatic mice affected by a synucleinopathy triggers an important acceleration of the α‐synuclein pathology, resulting in the early onset of motor clinical signs associated with molecular alterations of α-synuclein. These data suggest that α-synuclein alterations can be experimentally transmitted from one mouse to another, supporting the idea that, far from being confined to the transmissible spongiform encephalopathies, the « prion-like » propagation of misfolded neuronal proteins might occur in synucleinopathies
identifier: NNT: 2011LYO10057
issued: 2026-05-09T16:24:37.120977
language: fr
modified: 2026-05-09T16:24:37.120982