Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/141852
Title: Role of cellular prion protein in interneuronal amyloid transmission
Author: Río Fernández, José Antonio del
Ferrer, Isidro (Ferrer Abizanda)
Gavín Marín, Rosalina
Keywords: Amiloïdosi
Pèptids
Metabolisme
Alfa-sinucleïna
Proteïnes
Amyloidosis
Peptides
Metabolism
Alpha-synuclein
Proteins
Issue Date: 1-Jun-2018
Publisher: Elsevier Ltd
Abstract: 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.
Note: Versió postprint del document publicat a: https://doi.org/10.1016/j.pneurobio.2018.03.001
It is part of: Progress in Neurobiology, 2018, vol. 165-167, p. 87-102
URI: http://hdl.handle.net/2445/141852
Related resource: https://doi.org/10.1016/j.pneurobio.2018.03.001
ISSN: 0301-0082
Appears in Collections:Articles publicats en revistes (Institut de Bioenginyeria de Catalunya (IBEC))
Articles publicats en revistes (Patologia i Terapèutica Experimental)

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