Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein

The physiological functions of PrP(C) remain enigmatic, but the central domain, comprising highly conserved regions of the protein may play an important role. Indeed, a large number of studies indicate that synthetic peptides containing residues 106-126 (CR) located in the central domain (CD, 95-133...

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Autores: Vilches Saez, Silvia, Vergara Paños, Cristina, Nicolás i Pallejà, Josep Oriol, Sanclimens Pérez de Rozas, Glòria, Varón, S., Acosta, Gerardo A., Albericio Palomera, Fernando, Royo Expósito, Miriam, Río Fernández, José Antonio del, Gavín Marín, Rosalina
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/46331
Acceso en línea:https://hdl.handle.net/2445/46331
Access Level:acceso abierto
Palabra clave:Prions
Pèptids
Proteïnes
Síntesi de pèptids
Mort cel·lular
Peptides
Proteins
Peptide synthesis
Cell death
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spelling Neurotoxicity of prion peptides mimicking the central domain of the cellular prion proteinVilches Saez, SilviaVergara Paños, CristinaNicolás i Pallejà, Josep OriolSanclimens Pérez de Rozas, GlòriaVarón, S.Acosta, Gerardo A.Albericio Palomera, FernandoRoyo Expósito, MiriamRío Fernández, José Antonio delGavín Marín, RosalinaPrionsPèptidsProteïnesSíntesi de pèptidsMort cel·lularPrionsPeptidesProteinsPeptide synthesisCell deathThe physiological functions of PrP(C) remain enigmatic, but the central domain, comprising highly conserved regions of the protein may play an important role. Indeed, a large number of studies indicate that synthetic peptides containing residues 106-126 (CR) located in the central domain (CD, 95-133) of PrP(C) are neurotoxic. The central domain comprises two chemically distinct subdomains, the charge cluster (CC, 95-110) and a hydrophobic region (HR, 112-133). The aim of the present study was to establish the individual cytotoxicity of CC, HR and CD. Our results show that only the CD peptide is neurotoxic. Biochemical, Transmission Electron Microscopy and Atomic Force Microscopy experiments demonstrated that the CD peptide is able to activate caspase-3 and disrupt the cell membrane, leading to cell death.Public Library of Science (PLoS)2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/46331Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0070881PLoS One, 2013, vol. 8, num. 8, p. e70881http://dx.doi.org/10.1371/journal.pone.0070881info:eu-repo/grantAgreement/EC/FP7/222887cc-by (c) Vilches Saez, Silvia et al., 2013http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/463312026-05-27T06:46:51Z
dc.title.none.fl_str_mv Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
title Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
spellingShingle Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
Vilches Saez, Silvia
Prions
Pèptids
Proteïnes
Síntesi de pèptids
Mort cel·lular
Prions
Peptides
Proteins
Peptide synthesis
Cell death
title_short Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
title_full Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
title_fullStr Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
title_full_unstemmed Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
title_sort Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein
dc.creator.none.fl_str_mv Vilches Saez, Silvia
Vergara Paños, Cristina
Nicolás i Pallejà, Josep Oriol
Sanclimens Pérez de Rozas, Glòria
Varón, S.
Acosta, Gerardo A.
Albericio Palomera, Fernando
Royo Expósito, Miriam
Río Fernández, José Antonio del
Gavín Marín, Rosalina
author Vilches Saez, Silvia
author_facet Vilches Saez, Silvia
Vergara Paños, Cristina
Nicolás i Pallejà, Josep Oriol
Sanclimens Pérez de Rozas, Glòria
Varón, S.
Acosta, Gerardo A.
Albericio Palomera, Fernando
Royo Expósito, Miriam
Río Fernández, José Antonio del
Gavín Marín, Rosalina
author_role author
author2 Vergara Paños, Cristina
Nicolás i Pallejà, Josep Oriol
Sanclimens Pérez de Rozas, Glòria
Varón, S.
Acosta, Gerardo A.
Albericio Palomera, Fernando
Royo Expósito, Miriam
Río Fernández, José Antonio del
Gavín Marín, Rosalina
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Prions
Pèptids
Proteïnes
Síntesi de pèptids
Mort cel·lular
Prions
Peptides
Proteins
Peptide synthesis
Cell death
topic Prions
Pèptids
Proteïnes
Síntesi de pèptids
Mort cel·lular
Prions
Peptides
Proteins
Peptide synthesis
Cell death
description The physiological functions of PrP(C) remain enigmatic, but the central domain, comprising highly conserved regions of the protein may play an important role. Indeed, a large number of studies indicate that synthetic peptides containing residues 106-126 (CR) located in the central domain (CD, 95-133) of PrP(C) are neurotoxic. The central domain comprises two chemically distinct subdomains, the charge cluster (CC, 95-110) and a hydrophobic region (HR, 112-133). The aim of the present study was to establish the individual cytotoxicity of CC, HR and CD. Our results show that only the CD peptide is neurotoxic. Biochemical, Transmission Electron Microscopy and Atomic Force Microscopy experiments demonstrated that the CD peptide is able to activate caspase-3 and disrupt the cell membrane, leading to cell death.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/46331
url https://hdl.handle.net/2445/46331
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0070881
PLoS One, 2013, vol. 8, num. 8, p. e70881
http://dx.doi.org/10.1371/journal.pone.0070881
info:eu-repo/grantAgreement/EC/FP7/222887
dc.rights.none.fl_str_mv cc-by (c) Vilches Saez, Silvia et al., 2013
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Vilches Saez, Silvia et al., 2013
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Public Library of Science (PLoS)
publisher.none.fl_str_mv Public Library of Science (PLoS)
dc.source.none.fl_str_mv Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)
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
_version_ 1869404133840125952
score 15,300719

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