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  • Iron promotes the toxicity of amyloid beta peptide by impeding its ordered aggregation.

Iron promotes the toxicity of amyloid beta peptide by impeding its ordered aggregation.

The Journal of biological chemistry (2010-12-15)
Beinan Liu, Aileen Moloney, Sarah Meehan, Kyle Morris, Sally E Thomas, Louise C Serpell, Robert Hider, Stefan J Marciniak, David A Lomas, Damian C Crowther
摘要

We have previously shown that overexpressing subunits of the iron-binding protein ferritin can rescue the toxicity of the amyloid β (Aβ) peptide in our Drosophila model system. These data point to an important pathogenic role for iron in Alzheimer disease. In this study, we have used an iron-selective chelating compound and RNAi-mediated knockdown of endogenous ferritin to further manipulate iron in the brain. We confirm that chelation of iron protects the fly from the harmful effects of Aβ. To understand the pathogenic mechanisms, we have used biophysical techniques to see how iron affects Aβ aggregation. We find that iron slows the progression of the Aβ peptide from an unstructured conformation to the ordered cross-β fibrils that are characteristic of amyloid. Finally, using mammalian cell culture systems, we have shown that iron specifically enhances Aβ toxicity but only if the metal is present throughout the aggregation process. These data support the hypothesis that iron delays the formation of well ordered aggregates of Aβ and so promotes its toxicity in Alzheimer disease.

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青链霉素, Solution stabilized, with 10,000 units penicillin and 10 mg streptomycin/mL, 0.1 μm filtered, BioReagent, suitable for cell culture
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SH-SY5Y Cell Line human, NOTE: Both the cell line and DNA from the cell line may be available for this product. Please choose -1VL or VIAL for cells, or -DNA-5UG for DNA, 94030304, human nerve, Neuroblast
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