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Publicly Available Published by De Gruyter July 30, 2011

Toxicity of Alzheimer's disease-associated Aβ peptide is ameliorated in a Drosophila model by tight control of zinc and copper availability

  • Haiqing Hua , Lisa Münter , Anja Harmeier , Oleg Georgiev , Gerd Multhaup and Walter Schaffner EMAIL logo
From the journal Biological Chemistry

Abstract

Amyloid 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 in Drosophila results 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.


Corresponding author

Received: 2011-6-7
Accepted: 2011-6-24
Published Online: 2011-7-30
Published in Print: 2011-10-1

©2011 by Walter de Gruyter Berlin Boston

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