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Iron stored in ferritin is chemically reduced in the presence of aggregating Aβ(1-42)
- Source :
- Scientific Reports, Vol 10, Iss 1, Pp 1-16 (2020), Scientific Reports
- Publication Year :
- 2020
- Publisher :
- Nature Publishing Group, 2020.
-
Abstract
- Atypical low-oxidation-state iron phases in Alzheimer’s disease (AD) pathology are implicated in disease pathogenesis, as they may promote elevated redox activity and convey toxicity. However, the origin of low-oxidation-state iron and the pathways responsible for its formation and evolution remain unresolved. Here we investigate the interaction of the AD peptide β-amyloid (Aβ) with the iron storage protein ferritin, to establish whether interactions between these two species are a potential source of low-oxidation-state iron in AD. Using X-ray spectromicroscopy and electron microscopy we found that the co-aggregation of Aβ and ferritin resulted in the conversion of ferritin’s inert ferric core into more reactive low-oxidation-states. Such findings strongly implicate Aβ in the altered iron handling and increased oxidative stress observed in AD pathogenesis. These amyloid-associated iron phases have biomarker potential to assist with disease diagnosis and staging, and may act as targets for therapies designed to lower oxidative stress in AD tissue.
- Subjects :
- 0301 basic medicine
Microscopy, Electron, Scanning Transmission
Iron
lcsh:Medicine
Peptide
medicine.disease_cause
Q1
Article
Pathogenesis
03 medical and health sciences
Protein Aggregates
0302 clinical medicine
Alzheimer Disease
medicine
Humans
Potential source
lcsh:Science
chemistry.chemical_classification
Multidisciplinary
Amyloid beta-Peptides
biology
Neurodegenerative diseases
lcsh:R
Spectrometry, X-Ray Emission
Alzheimer's disease
R1
Peptide Fragments
Ferritin
Oxidative Stress
030104 developmental biology
Biochemistry
chemistry
Metals
Toxicity
Ferritins
biology.protein
Ferric
Biomarker (medicine)
Dementia
lcsh:Q
Peptides
Oxidation-Reduction
030217 neurology & neurosurgery
Oxidative stress
Biomarkers
medicine.drug
Subjects
Details
- Language :
- English
- ISSN :
- 20452322
- Volume :
- 10
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....016282e88fe429d0b0fa27410977104b