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- W2766707944 abstract "The aggregation of the amyloid β-peptide (Aβ) is hypothesized to initiate the pathogenesis of Alzheimer's disease (AD). In order to prevent or treat AD, strategies to inhibit Aβ accumulation and toxicity in the brain are extensively explored. BRICHOS, a molecular chaperone protein, is possibly one of the physiological protection mechanisms against amyloid formation. Three recombinant adeno-associated viruses (rAAVs) encoding Bri-BRICHOS domain, proSP-C-BRICHOS domain or GFP, were injected to cerebral ventricles of newborn mice using somatic brain transgenesis method. 4 μl of each rAAV8 particles (1*1012genome particles/ml) were injected into newborn APP/PS1 mice (male, n=8 for each group). Eight months after rAAV8 injection, cognitive function and AD-related neuropathological phenotypes were analyzed in cortex. We demonstrate that molecular chaperone BRICHOS domains significantly decreased Aβ levels, inhibited amyloid accumulation, greatly reduced astroglial activation, and prevented cognitive decline in APP/PS1 mice. Together, our results show that the molecular chaperone BRICHOS domain promotes protein homeostasis and decreases the severity of Aβ aggregation and its associated pathology in the brain. These data suggest that the BRICHOS domain can be further investigated as a promising preventive and therapeutic strategy against AD." @default.
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- W2766707944 date "2017-07-01" @default.
- W2766707944 modified "2023-10-01" @default.
- W2766707944 title "[P4-125]: THE MOLECULAR CHAPERONE BRICHOS INHIBITS Aβ AGGREGATION AND OTHER NEUROPATHOLOGICAL PHENOTYPES IN A MOUSE MODEL OF Aβ AMYLOIDOSIS" @default.
- W2766707944 doi "https://doi.org/10.1016/j.jalz.2017.06.1991" @default.
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