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- W4301179871 abstract "The progress of neurodegenerative disorders correlates with the spread of their associated amyloidogenic proteins. Here, we investigated whether amyloid entry into nonconstitutive neurons could drive cross-toxic outcomes. Amyloid β (Aβ) was stereotaxically introduced into the rodent midbrain tegmentum, where it is not endogenously expressed. Postinfusion, rodent motor and sensorimotor capacities were assessed by standard behavioral tests at 3, 6, 9, and 12 months. The longitudinal study revealed no behavioral abnormalities. However, Aβ insult provoked intraneuronal inclusions positive for phosphorylated α-synuclein in dopaminergic neurons and were seen throughout the midbrain, a pathognomonic biomarker suggesting Parkinson's pathogenesis. These findings not only underscore the cross-toxic potential of amyloid proteins but also provide a mechanism by which they disrupt homeostasis in nonconstitutive neurons and cause neuronal corruption, injury, and demise. This study may help reconcile the large incidence of neurodegenerative comorbidity observed clinically." @default.
- W4301179871 created "2022-10-04" @default.
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- W4301179871 date "2022-10-04" @default.
- W4301179871 modified "2023-10-16" @default.
- W4301179871 title "Preclinical Model to Evaluate Outcomes of Amyloid Cross-Toxicity in the Rodent Brain" @default.
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- W4301179871 doi "https://doi.org/10.1021/acschemneuro.2c00419" @default.
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