Artículo
The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration
Maïza, Auriane; Chantepie, Sandrine; Vera, Claudia Cecilia
; Fifre, Alexandre; Huynh, Minh Bao; Stettler, Olivier; Ouidja, Mohand Ouidir; Papy Garcia, Dulce
Fecha de publicación:
06/2018
Editorial:
Wiley
Revista:
FEBS Letters
ISSN:
0014-5793
e-ISSN:
1873-3468
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
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Articulos(INSIBIO)
Articulos de INST.SUP.DE INVEST.BIOLOGICAS
Articulos de INST.SUP.DE INVEST.BIOLOGICAS
Citación
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
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