Journal
METALLOMICS
Volume 3, Issue 7, Pages 726-734Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1mt00015b
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Miyazaki Prefectural Industrial Support Foundation
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Prion diseases are progressive neurodegenerative diseases that are associated with the conversion of normal cellular prion protein (PrPC) to abnormal pathogenic prion protein (PrPSC) by conformational changes. Prion protein is a metal-binding protein that is suggested to be involved in metal homeostasis. We investigated here the effects of trace elements on the conformational changes and neurotoxicity of synthetic prion peptide (PrP106-126). PrP106-126 exhibited the formation of beta-sheet structures and enhanced neurotoxicity during the aging process. The co-existence of Zn2+ or Cu2+ during aging inhibited b-sheet formation by PrP106-126 and attenuated its neurotoxicity on primary cultured rat hippocampal neurons. Although PrP106-126 formed amyloid-like fibrils as observed by atomic force microscopy, the height of the fibers was decreased in the presence of Zn2+ or Cu2+. Carnosine (beta-alanyl histidine) significantly inhibited both the beta-sheet formation and the neurotoxicity of PrP106-126. Our results suggested that Zn2+ and Cu2+ might be involved in the pathogenesis of prion diseases. It is also possible that carnosine might become a candidate for therapeutic treatments for prion diseases.
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