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@ARTICLE{LaVitola:273935,
      author       = {La Vitola, Pietro and Szegoe, Eva and Pinto-Costa, Rita and
                      Rollar, Angela and Harbachova, Eugenia and Schapira, Anthony
                      Hv and Ulusoy, Ayse and Di Monte, Donato A},
      title        = {{M}itochondrial oxidant stress promotes α-synuclein
                      aggregation and spreading in mice with mutated
                      glucocerebrosidase.},
      journal      = {npj Parkinson's Disease},
      volume       = {10},
      number       = {1},
      issn         = {2373-8057},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {DZNE-2024-01409},
      pages        = {233},
      year         = {2024},
      abstract     = {In this study, heterozygous expression of a common
                      Parkinson-associated GBA1 variant, the L444P mutation, was
                      found to exacerbate α-synuclein aggregation and spreading
                      in a mouse model of Parkinson-like pathology targeting
                      neurons of the medullary vagal system. These neurons were
                      also shown to become more vulnerable to oxidative and
                      nitrative stress after L444P expression. The latter
                      paralleled neuronal formation of reactive oxygen species and
                      led to a pronounced accumulation of nitrated α-synuclein. A
                      causal relationship linked mutation-induced
                      oxidative/nitrative stress to enhanced α-synuclein
                      aggregation and spreading that could indeed be rescued by
                      neuronal overexpression of mitochondrial superoxide
                      dismutase 2. Further evidence supported a key involvement of
                      mitochondria as sources of reactive oxygen species as well
                      as targets of oxidative and nitrative damage within
                      L444P-expressing neurons. These findings support the
                      conclusion that enhanced vulnerability to mitochondrial
                      oxidative stress should be considered an important mechanism
                      predisposing to pathology conversion in carriers of GBA1
                      mutations.},
      cin          = {AG Di Monte},
      ddc          = {610},
      cid          = {I:(DE-2719)1013008},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39663354},
      pmc          = {pmc:PMC11634889},
      doi          = {10.1038/s41531-024-00842-8},
      url          = {https://pub.dzne.de/record/273935},
}