Role of PrPC Expression in Tau Protein Levels and Phosphorylation in Alzheimer¿s Disease Evolution

Springer Science+Business Media New York 2014 Abstract Alzheimer’s disease (AD) is characterized by the presence of amyloid plaques mainly consisting of hydrophobic β-amyloid peptide (Aβ) aggregates and neurofibrillary tangles (NFTs) composed principally of hyperphosphorylated tau.Aβ oligomers have...

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Detalles Bibliográficos
Autores: Vergara, Cristina, Ordóñez-Gutiérrez, Lara, Wandosell, Francisco, Ferrer, I. M, Río, José Antonio del, Gavín, Rosalina
Tipo de recurso: otro
Estado:Versión publicada
Fecha de publicación:2014
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/140268
Acceso en línea:http://hdl.handle.net/10261/140268
Access Level:acceso abierto
Palabra clave:Aβ oligomers
Cellular prion protein
Alzheimer’s disease
Microtubule-associated protein tau
Descripción
Sumario:Springer Science+Business Media New York 2014 Abstract Alzheimer’s disease (AD) is characterized by the presence of amyloid plaques mainly consisting of hydrophobic β-amyloid peptide (Aβ) aggregates and neurofibrillary tangles (NFTs) composed principally of hyperphosphorylated tau.Aβ oligomers have been described as the earliest effectors to negatively affect synaptic structure and plasticity in the affected brains, and cellular prion protein (PrPC) has been proposed as receptor for these oligomers. The most widely accepted theory holds that the toxic effects ofAβ are upstream of change in tau, a neuronal microtubule-associated protein that promotes the polymerization and stabilization of microtubules. However, tau is considered decisive for the progression of neurodegeneration, and, indeed, tau pathology