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A novel model of Amyloid-beta pathology in C. elegans reveals critically vulnerable neurons as seeds of pathogenicity

ABSTRACT: A novel model of amyloid-beta pathology in C. elegans has been generated which allows for substoichiometric fluorescent labeling of amyloid-beta species in living nematodes. By microscopy, FLIM, physiological and biochemical studies, the progress of neurodegeneration and general pathogenicity of amyloidogenic peptides is confirmed. Notably, a single set of neurons was shown to be most vulnerable to Amyloid-beta overexpression and putatively act as a seed for systemic pathogeny. A muscular version of the amyloid-beta reporter strain was used to perform proteomics analysis from worm lysates after enrichment by immunoprecipitation, using anti-amyloid-beta antibodies.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human) Caenorhabditis Elegans

TISSUE(S): Whole Body

SUBMITTER: Manuel Iburg

LAB HEAD: Janine Kirstein

PROVIDER: PXD017590 | Pride | 2020-09-18

REPOSITORIES: Pride

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A novel model of Amyloid-beta pathology in C. elegans reveals critically vulnerable neurons as seeds of pathogenicity

Project description:A novel model of amyloid-beta pathology in C. elegans has been generated which allows for substoichiometric fluorescent labeling of amyloid-beta species in living nematodes. By microscopy, FLIM, physiological and biochemical studies, the progress of neurodegeneration and general pathogenicity of amyloidogenic peptides is confirmed. Notably, a single set of neurons was shown to be most vulnerable to Amyloid-beta overexpression and putatively act as a seed for systemic pathogeny. A neuronal version of the amyloid-beta reporter strain was used to perform proteomics analysis from worm lysates after enrichment by immunoprecipitation, using anti-amyloid-beta antibodies.

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Chlorpyrifos oxon crosslinking of amyloid beta 42 peptides is a new route for generation of self-aggregating amyloidogenic oligomers that promote Alzheimer’s disease

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