BIBLIOS

Document type
Journal articles

Document subtype
Full paper

Title
Metallothioneins in Prion- and Amyloid-Related Diseases

Participants in the publication
Pavlína Adam (Author)
So?a K?ížková (Author)
Zbyn?k Heger (Author)
Petr Babula (Author)
Vladimír Peka?ík (Author)
Markéta Vaculovi?oá (Author)
Cláudio M. Gomes (Author)
Dep. Química e Bioquímica
BioISI
René Kizek (Author)
Vojt?ch Adam (Author)

Summary
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.


Where published
Journal of Alzheimer's Disease

Publication Identifiers
ISSN - 1387-2877

Publisher
IOS Press



Document Identifiers
DOI - https://doi.org/10.3233/jad-150984
URL - http://dx.doi.org/10.3233/jad-150984

Rankings
SCIMAGO Q1 (2016) - 1.584 - Medicine (miscellaneous)
SCIMAGO Q1 (2017) - 1.635 - Neuroscience (miscellaneous)

Keywords
Alzheimer’s disease brain copper metallothionein nneurodegenerative disorders prion protein