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Role of cellular prion protein in interneuronal amyloid transmission
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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 (PrPC) binding has been a focus of interest in Alzheimer's disease (AD). At the molecular level, β-amyloid/PrPC interaction takes place in two differently charged clusters of PrPC. In addition to β-amyloid, participation of PrPC in α-synuclein binding and brain spreading also appears to be relevant in α-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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RÍO FERNÁNDEZ, José Antonio del, FERRER, Isidro (Ferrer Abizanda) i GAVÍN MARÍN, Rosalina. Role of cellular prion protein in interneuronal amyloid transmission. Progress in Neurobiology. 2018. Vol. 165-167, núm. 87-102. ISSN 0301-0082. [consulta: 10 de maig de 2026]. Disponible a: https://hdl.handle.net/2445/141852