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dc.contributor.author
Maïza, Auriane
dc.contributor.author
Chantepie, Sandrine
dc.contributor.author
Vera, Claudia Cecilia
dc.contributor.author
Fifre, Alexandre
dc.contributor.author
Huynh, Minh Bao
dc.contributor.author
Stettler, Olivier
dc.contributor.author
Ouidja, Mohand Ouidir
dc.contributor.author
Papy Garcia, Dulce
dc.date.available
2020-04-03T18:27:45Z
dc.date.issued
2018-06
dc.identifier.citation
Maïza, Auriane; Chantepie, Sandrine; Vera, Claudia Cecilia; Fifre, Alexandre; Huynh, Minh Bao; et al.; The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration; Wiley; FEBS Letters; 592; 23; 6-2018; 3806-3818
dc.identifier.issn
0014-5793
dc.identifier.uri
http://hdl.handle.net/11336/101926
dc.description.abstract
Neurodegenerative disorders, such as Alzheimer´s, Parkinson´s, and prion diseases, are directly linked to the formation and accumulation of protein aggregates in the brain. These aggregates, principally made of proteins or peptides that clamp together after acquisition of β-folded structures, also contain heparan sulfates. Several lines of evidence suggest that heparan sulfates centrally participate in the protein aggregation process. In vitro, they trigger misfolding, oligomerization, and fibrillation of amyloidogenic proteins, such as Aβ, tau, α-synuclein, prion protein, etc. They participate in the stabilization of protein aggregates, protect them from proteolysis, and act as cell-surface receptors for the cellular uptake of proteopathic seeds during their spreading. This review focuses attention on the importance of heparan sulfates in protein aggregation in brain disorders including Alzheimer´s, Parkinson´s, and prion diseases. The presence of these sulfated polysaccharides in protein inclusions in vivo and their capacity to trigger protein aggregation in vitro strongly suggest that they might play critical roles in the neurodegenerative process. Further advances in glyco-neurobiology will improve our understanding of the molecular and cellular mechanisms leading to protein aggregation and neurodegeneration.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ALZHEIMER'S DISEASE
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PARKINSON'S DISEASE
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HEPARAN SULFATES
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NEURODEGENERATION
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PRION DISEASES
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PROTEIN AGGREGATION
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-16T19:29:41Z
dc.identifier.eissn
1873-3468
dc.journal.volume
592
dc.journal.number
23
dc.journal.pagination
3806-3818
dc.journal.pais
Reino Unido
dc.journal.ciudad
West Sussex
dc.conicet.avisoEditorial
FEBS Letters 592 (2018) 3806–3818 ª 2018 Federation of European Biochemical Societies
[The copyright line for this article was changed on 25 March 2019 after original publication].
dc.description.fil
Fil: Maïza, Auriane. Universite de Paris; Francia
dc.description.fil
Fil: Chantepie, Sandrine. Universite de Paris; Francia
dc.description.fil
Fil: Vera, Claudia Cecilia. Universite de Paris; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Fifre, Alexandre. Universite de Paris; Francia
dc.description.fil
Fil: Huynh, Minh Bao. Universite de Paris; Francia
dc.description.fil
Fil: Stettler, Olivier. Universite de Paris; Francia
dc.description.fil
Fil: Ouidja, Mohand Ouidir. Universite de Paris; Francia
dc.description.fil
Fil: Papy Garcia, Dulce. Universite de Paris; Francia
dc.journal.title
FEBS Letters
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/1873-3468.13082
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13082
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