Detail publikačního výsledku

Metallothioneins in Prion- and Amyloid-Related Diseases

ADAM, P.; KŘÍŽKOVÁ, S.; HEGER, Z.; BABULA, P.; PEKAŘÍK, V.; VACULOVIČOVÁ, M.; GOMES, C.

Originální název

Metallothioneins in Prion- and Amyloid-Related Diseases

Anglický název

Metallothioneins in Prion- and Amyloid-Related Diseases

Druh

Článek WoS

Originální abstrakt

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.

Anglický abstrakt

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.

Klíčová slova

Alzheimer’s disease, brain, copper, metallothionein, neurodegenerative disorders, prion protein

Klíčová slova v angličtině

Alzheimer’s disease, brain, copper, metallothionein, neurodegenerative disorders, prion protein

Autoři

ADAM, P.; KŘÍŽKOVÁ, S.; HEGER, Z.; BABULA, P.; PEKAŘÍK, V.; VACULOVIČOVÁ, M.; GOMES, C.

Rok RIV

2017

Vydáno

01.01.2016

ISSN

1387-2877

Periodikum

JOURNAL OF ALZHEIMERS DISEASE

Svazek

51

Číslo

3

Stát

Nizozemsko

Strany od

637

Strany do

656

Strany počet

20

BibTex

@article{BUT127854,
  author="Pavlína {Adam} and Soňa {Křížková} and Zbyněk {Heger} and Petr {Babula} and Vladimír {Pekařík} and Markéta {Vaculovičová} and Cl´audio M. {Gomes} and René {Kizek} and Vojtěch {Adam}",
  title="Metallothioneins in Prion- and Amyloid-Related Diseases",
  journal="JOURNAL OF ALZHEIMERS DISEASE",
  year="2016",
  volume="51",
  number="3",
  pages="637--656",
  doi="10.3233/JAD-150984",
  issn="1387-2877"
}