Natural polyphenols effects on protein aggregates in Alzheimer's and Parkinson's prion-like diseases
Autor: | Bernard Fauconneau, Aline Freyssin, Guylène Page, Agnès Rioux Bilan |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Parkinson's disease Amyloid amyloid plaques Disease Protein aggregation Pharmacology Neuroprotection lcsh:RC346-429 03 medical and health sciences Developmental Neuroscience Medicine natural polyphenols protein aggregates Alzheimer′s disease amyloid peptide hyperphosphorylated tau Parkinson′s disease α-synuclein synphilin-1 lcsh:Neurology. Diseases of the nervous system Invited Review business.industry Alzheimer's disease medicine.disease In vitro a-synuclein 030104 developmental biology Polyphenol Synuclein business |
Zdroj: | Neural Regeneration Research, Vol 13, Iss 6, Pp 955-961 (2018) Neural Regeneration Research |
ISSN: | 1673-5374 |
DOI: | 10.4103/1673-5374.233432 |
Popis: | Alzheimer's and Parkinson's diseases are the most common neurodegenerative diseases. They are characterized by protein aggregates and so can be considered as prion-like disease. The major components of these deposits are amyloid peptide and tau for Alzheimer's disease, α-synuclein and synphilin-1 for Parkinson's disease. Drugs currently proposed to treat these pathologies do not prevent neurodegenerative processes and are mainly symptomatic therapies. Molecules inducing inhibition of aggregation or disaggregation of these proteins could have beneficial effects, especially if they have other beneficial effects for these diseases. Thus, several natural polyphenols, which have antioxidative, anti-inflammatory and neuroprotective properties, have been largely studied, for their effects on protein aggregates found in these diseases, notably in vitro. In this article, we propose to review the significant papers concerning the role of polyphenols on aggregation and disaggregation of amyloid peptide, tau, α-synuclein, synphilin-1, suggesting that these compounds could be useful in the treatments in Alzheimer's and Parkinson's diseases. |
Databáze: | OpenAIRE |
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