Role of cellular prion protein in interneuronal amyloid transmission

Publication date: Available online 9 March 2018
Source:Progress in Neurobiology
Author(s): José A. del Río, Isidre Ferrer, Rosalina Gavín
Several studies have indicated that certain misfolded amyloids composed of tau, β-amyloid or α-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 β-amyloid oligomers and cellular prion protein (PrP^C) binding has been a focus of interest in Alzheimer's disease (AD). At the molecular level, β-amyloid/PrP^C interaction takes place in two differently charged clusters of PrP^C. In addition to β-amyloid, participation of PrP^C in α-synuclein binding and brain spreading also appears to be relevant in α-synucleopathies. This review summarizes current knowledge about PrP^C as a putative receptor for amyloid proteins and the physiological consequences of these interactions.



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