Fe(II) formation after interaction of the amyloid β-peptide with iron-storage protein ferritin
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
29740739
PubMed Central
PMC6082800
DOI
10.1007/s10867-018-9498-3
PII: 10.1007/s10867-018-9498-3
Knihovny.cz E-resources
- Keywords
- Alzheimer’s disease, Aβ, Ferritin, Iron reduction, Magnetite, Metallochaperone,
- MeSH
- Amyloid chemistry MeSH
- Amyloid beta-Peptides chemistry metabolism MeSH
- Ferritins chemistry metabolism MeSH
- Humans MeSH
- Oxidation-Reduction MeSH
- Iron metabolism MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amyloid MeSH
- Amyloid beta-Peptides MeSH
- Ferritins MeSH
- Iron MeSH
The interaction of amyloid β-peptide (Aβ) with the iron-storage protein ferritin was studied in vitro. We have shown that Aβ during fibril formation process is able to reduce Fe(III) from the ferritin core (ferrihydrite) to Fe(II). The Aβ-mediated Fe(III) reduction yielded a two-times-higher concentration of free Fe(II) than the spontaneous formation of Fe(II) by the ferritin itself. We suggest that Aβ can also act as a ferritin-specific metallochaperone-like molecule capturing Fe(III) from the ferritin ferrihydrite core. Our observation may partially explain the formation of Fe(II)-containing minerals in human brains suffering by neurodegenerative diseases.
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Destruction of Lysozyme Amyloid Fibrils Induced by Magnetoferritin and Reconstructed Ferritin
