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Metallothioneins in Prion- and Amyloid-Related Diseases

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F16%3A43909567" target="_blank" >RIV/62156489:43210/16:43909567 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14110/16:00090727 RIV/00216305:26620/16:PU120145

  • Result on the web

    <a href="http://dx.doi.org/10.3233/JAD-150984" target="_blank" >http://dx.doi.org/10.3233/JAD-150984</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3233/JAD-150984" target="_blank" >10.3233/JAD-150984</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Metallothioneins in Prion- and Amyloid-Related Diseases

  • Original language description

    Prion and other amyloid-forming diseases represent a group of neurodegenerative disorders that affect both animals and humans. The role of metal ions, especially copper and zinc is studied intensively in connection with these diseases. Their involvement in protein misfolding and aggregation and their role in creation of reactive oxygen species have been shown. Recent data also show that metal ions not only bind the proteins with high affinity, but also modify their biochemical properties, making them important players in prion-related diseases. In particular, the level of zinc ions is tightly regulated by several mechanisms, including transporter proteins and the low molecular mass thiol-rich metallothioneins. From four metallothionein isoforms, metallothionein-3, a unique brain-specific metalloprotein, plays a crucial role only in this regulation. This review critically evaluates the involvement of metallothioneins in prion- and amyloid-related diseases in connection with the relationship between metallothionein isoforms and metal ion regulation of their homeostasis.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/ED1.1.00%2F02.0068" target="_blank" >ED1.1.00/02.0068: Central european institute of technology</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2016

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Alzheimer's Disease

  • ISSN

    1387-2877

  • e-ISSN

  • Volume of the periodical

    51

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    20

  • Pages from-to

    637-656

  • UT code for WoS article

    000374240200001

  • EID of the result in the Scopus database

    2-s2.0-84963757777