Metallothioneins in Prion- and Amyloid-Related Diseases

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Publikace nespadá pod Fakultu sportovních studií, ale pod Lékařskou fakultu. Oficiální stránka publikace je na webu muni.cz.
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ADAM Pavlína KŘÍŽKOVÁ Soňa HEGER Zbyněk BABULA Petr PEKAŘÍK Vladimír VACULOVIČOVÁ Markéta GOMES Cláudio M. KIZEK René ADAM Vojtěch

Rok publikování 2016
Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Alzheimers Disease
Fakulta / Pracoviště MU

Lékařská fakulta

Citace
Doi http://dx.doi.org/10.3233/JAD-150984
Obor Neurologie, neurochirurgie, neurovědy
Klíčová slova Alzheimer's disease; brain; copper; metallothionein; neurodegenerative disorders; prion protein
Popis 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.

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