Role of cellular prion protein in interneuronal amyloid transmission

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' s...

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Authors: Río Fernández, José Antonio del, Ferrer, Isidro (Ferrer Abizanda), Gavín Marín, Rosalina
Format: article
Status:Versión aceptada para publicación
Publication Date:2018
Country:España
Institution:Universidad de Barcelona
Repository:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/141852
Online Access:https://hdl.handle.net/2445/141852
Access Level:Open access
Keyword:Amiloïdosi
Pèptids
Metabolisme
Alfa-sinucleïna
Proteïnes
Amyloidosis
Peptides
Metabolism
Alpha-synuclein
Proteins
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spelling Role of cellular prion protein in interneuronal amyloid transmissionRío Fernández, José Antonio delFerrer, Isidro (Ferrer Abizanda)Gavín Marín, RosalinaAmiloïdosiPèptidsMetabolismeAlfa-sinucleïnaProteïnesAmyloidosisPeptidesMetabolismAlpha-synucleinProteinsSeveral 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.Elsevier Ltd2018info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://hdl.handle.net/2445/141852Articles publicats en revistes (Patologia i Terapèutica Experimental)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésVersió postprint del document publicat a: https://doi.org/10.1016/j.pneurobio.2018.03.001Progress in Neurobiology, 2018, vol. 165-167, p. 87-102https://doi.org/10.1016/j.pneurobio.2018.03.001cc-by-nc-nd (c) Elsevier Ltd, 2018http://creativecommons.org/licenses/by-nc-nd/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1418522026-05-27T06:46:51Z
dc.title.none.fl_str_mv Role of cellular prion protein in interneuronal amyloid transmission
title Role of cellular prion protein in interneuronal amyloid transmission
spellingShingle Role of cellular prion protein in interneuronal amyloid transmission
Río Fernández, José Antonio del
Amiloïdosi
Pèptids
Metabolisme
Alfa-sinucleïna
Proteïnes
Amyloidosis
Peptides
Metabolism
Alpha-synuclein
Proteins
title_short Role of cellular prion protein in interneuronal amyloid transmission
title_full Role of cellular prion protein in interneuronal amyloid transmission
title_fullStr Role of cellular prion protein in interneuronal amyloid transmission
title_full_unstemmed Role of cellular prion protein in interneuronal amyloid transmission
title_sort Role of cellular prion protein in interneuronal amyloid transmission
dc.creator.none.fl_str_mv Río Fernández, José Antonio del
Ferrer, Isidro (Ferrer Abizanda)
Gavín Marín, Rosalina
author Río Fernández, José Antonio del
author_facet Río Fernández, José Antonio del
Ferrer, Isidro (Ferrer Abizanda)
Gavín Marín, Rosalina
author_role author
author2 Ferrer, Isidro (Ferrer Abizanda)
Gavín Marín, Rosalina
author2_role author
author
dc.subject.none.fl_str_mv Amiloïdosi
Pèptids
Metabolisme
Alfa-sinucleïna
Proteïnes
Amyloidosis
Peptides
Metabolism
Alpha-synuclein
Proteins
topic Amiloïdosi
Pèptids
Metabolisme
Alfa-sinucleïna
Proteïnes
Amyloidosis
Peptides
Metabolism
Alpha-synuclein
Proteins
description 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.
publishDate 2018
dc.date.none.fl_str_mv 2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/141852
url https://hdl.handle.net/2445/141852
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.1016/j.pneurobio.2018.03.001
Progress in Neurobiology, 2018, vol. 165-167, p. 87-102
https://doi.org/10.1016/j.pneurobio.2018.03.001
dc.rights.none.fl_str_mv cc-by-nc-nd (c) Elsevier Ltd, 2018
http://creativecommons.org/licenses/by-nc-nd/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-nd (c) Elsevier Ltd, 2018
http://creativecommons.org/licenses/by-nc-nd/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier Ltd
publisher.none.fl_str_mv Elsevier Ltd
dc.source.none.fl_str_mv Articles publicats en revistes (Patologia i Terapèutica Experimental)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300724

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