Metallothioneins in Prion- and Amyloid-Related Diseases

Kód výsledku v 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>

Nalezeny alternativní kódy

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

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Metallothioneins in Prion- and Amyloid-Related Diseases

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Metallothioneins in Prion- and Amyloid-Related Diseases

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

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

Návaznosti

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

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Journal of Alzheimer's Disease

ISSN

1387-2877

e-ISSN

—

Svazek periodika

51

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

20

Strana od-do

637-656

Kód UT WoS článku

000374240200001

EID výsledku v databázi Scopus

2-s2.0-84963757777