Toxicity of Alzheimer's disease-associated Aβ peptide is ameliorated in aDrosophilamodel by tight control of zinc and copper availability
Copyright policy )Toxicity of Alzheimer's disease-associated Aβ peptide is ameliorated in aDrosophilamodel by tight control of zinc and copper availability
AbstractAmyloid plaques consisting of aggregated Aβ peptide are a hallmark of Alzheimer's disease. Among the different forms of Aβ, the one of 42aa length (Aβ42) is most aggregation-prone and also the most neurotoxic. We find that eye-specific expression of human Aβ42 inDrosophilaresults in a degeneration of eye structures that progresses with age. Dietary supplements of zinc or copper ions exacerbate eye damage. Positive effects are seen with zinc/copper chelators, or with elevated expression of MTF-1, a transcription factor with a key role in metal homeostasis and detoxification, or with human or fly transgenes encoding metallothioneins, metal scavenger proteins. These results show that a tight control of zinc and copper availability can minimize cellular damage associated with Aβ42 expression.
- University of Zurich Switzerland
- McGill University Canada
- Freie Universität Berlin Germany
- RERO - Library Network of Western Switzerland Switzerland
570, Aging, 1303 Biochemistry, 610, Gene Expression, 1308 Clinical Biochemistry, Eye, Transcription Factor MTF-1, Alzheimer Disease, Amyloid-bprotein, 1312 Molecular Biology, Animals, Humans, Transgenes, Heavy metal stress, Chelating Agents, Amyloid beta-Peptides, MTF-1, 10124 Institute of Molecular Life Sciences, Peptide Fragments, Up-Regulation, DNA-Binding Proteins, Zinc, 570 Life sciences; biology, Drosophila, Metallothionein, Alzheimer’s disease, Copper, Transcription Factors
570, Aging, 1303 Biochemistry, 610, Gene Expression, 1308 Clinical Biochemistry, Eye, Transcription Factor MTF-1, Alzheimer Disease, Amyloid-bprotein, 1312 Molecular Biology, Animals, Humans, Transgenes, Heavy metal stress, Chelating Agents, Amyloid beta-Peptides, MTF-1, 10124 Institute of Molecular Life Sciences, Peptide Fragments, Up-Regulation, DNA-Binding Proteins, Zinc, 570 Life sciences; biology, Drosophila, Metallothionein, Alzheimer’s disease, Copper, Transcription Factors
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