Fe(II) formation after interaction of the amyloid beta-peptide with iron-storage protein ferritin

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F18%3A00492375" target="_blank" >RIV/60077344:_____/18:00492375 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1007/s10867-018-9498-3" target="_blank" >http://dx.doi.org/10.1007/s10867-018-9498-3</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s10867-018-9498-3" target="_blank" >10.1007/s10867-018-9498-3</a>

Result language
angličtina
Original language name
Fe(II) formation after interaction of the amyloid beta-peptide with iron-storage protein ferritin
Original language description
The interaction of amyloid beta-peptide (A beta) with the iron-storage protein ferritin was studied in vitro. We have shown that A beta during fibril formation process is able to reduce Fe(III) from the ferritin core (ferrihydrite) to Fe(II). The A beta-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 A beta 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.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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