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Cell Chem Biol ; 25(5): 595-610.e5, 2018 05 17.
Article in English | MEDLINE | ID: mdl-29657084

ABSTRACT

The basis for selective vulnerability of certain cell types for misfolded proteins (MPs) in neurodegenerative diseases is largely unknown. This knowledge is crucial for understanding disease progression in relation to MPs spreading in the CNS. We assessed this issue in Drosophila by cell-specific expression of human Aß1-42 associated with Alzheimer's disease. Expression of Aß1-42 in various neurons resulted in concentration-dependent severe neurodegenerative phenotypes, and intraneuronal ring-tangle-like aggregates with immature fibril properties when analyzed by aggregate-specific ligands. Unexpectedly, expression of Aß1-42 from a pan-glial driver produced a mild phenotype despite massive brain load of Aß1-42 aggregates, even higher than in the strongest neuronal driver. Glial cells formed more mature fibrous aggregates, morphologically distinct from aggregates found in neurons, and was mainly extracellular. Our findings implicate that Aß1-42 cytotoxicity is both cell and aggregate morphotype dependent.


Subject(s)
Alzheimer Disease/pathology , Amyloid beta-Peptides/metabolism , Drosophila/metabolism , Neuroglia/pathology , Neurons/pathology , Peptide Fragments/metabolism , Protein Aggregation, Pathological/pathology , Alzheimer Disease/metabolism , Amyloid beta-Peptides/ultrastructure , Animals , Disease Models, Animal , Humans , Neuroglia/metabolism , Neurons/metabolism , Peptide Fragments/ultrastructure , Protein Aggregation, Pathological/metabolism
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