Journal
PROGRESS IN NEUROBIOLOGY
Volume 165, Issue -, Pages 87-102Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pneurobio.2018.03.001
Keywords
Cellular prion protein; Amyloid; Proteinaceous species; 'Prion-like' spreading; Spreading; Neurodegeneration
Categories
Funding
- Spanish Ministry of Economy, Industry and Competitiveness (MEICO/FEDER) [BFU2015-67777-R]
- Spanish Prion Network (Prionet Spain) [AGL2015-71764-REDT]
- Generalitat de Catalunya [SGR2017-648]
- CIBERNED [PRY-2016-2]
- CERCA Programme/Generalitat de Catalunya
- La Marato de TV3
- MEICO/FEDER
- Instituto de Salud Carlos III - Fondos FEDER
- Way to Build Europe FIS [PI14/00757, PI17/00809]
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Several studies have indicated that certain misfolded amyloids composed of tau, beta-amyloid or alpha-synuclein can be transferred from cell to cell, suggesting the contribution of mechanisms reminiscent of those by which infective prions spread through the brain. This process of a 'prion-like' spreading between cells is also relevant as a novel putative therapeutic target that could block the spreading of proteinaceous aggregates throughout the brain which may underlie the progressive nature of neurodegenerative diseases. The relevance of beta-amyloid oligomers and cellular prion protein (PrPC) binding has been a focus of interest in Alzheimer's disease (AD). At the molecular level, beta-amyloid/PrPC interaction takes place in two differently charged clusters of PrPC. In addition to beta-amyloid, participation of PrPC in alpha-synuclein binding and brain spreading also appears to be relevant in alpha-synucleopathies. This review summarizes current knowledge about PrPC as a putative receptor for amyloid proteins and the physiological consequences of these interactions.
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