Para acceder a los documentos con el texto completo, por favor, siga el siguiente enlace: http://hdl.handle.net/2445/141772

Título:	Reelin expression in Creutzfeldt-Jakob disease and experimental models of transmissible spongiform encephalopathies
Autor/a:	Mata, Agata; Urrea Zazurca, Laura; Vilches Saez, Silvia; Llorens Torres, Franc; Thüne, Katrin; Espinosa, Juan Carlos; Andréoletti, Olivier; Sevillano, Alejandro M.; Torres, Juan Maria; Rodríguez Requena, Jesús; Zerr, Inga; Ferrer, Isidro (Ferrer Abizanda); Gavín Marín, Rosalina; Río Fernández, José Antonio del
Abstract:	Reelin is an extracellular glycoprotein involved in key cellular processes in developing and adult nervous system, including regulation of neuronal migration, synapse formation, and plasticity. Most of these roles are mediated by the intracellular phosphorylation of disabled-1 (Dab1), an intracellular adaptor molecule, in turn mediated by binding Reelin to its receptors. Altered expression and glycosylation patterns of Reelin in cerebrospinal and cortical extracts have been reported in Alzheimer's disease. However, putative changes in Reelin are not described in natural prionopathies or experimental models of prion infection or toxicity. With this is mind, in the present study, we determined that Reelin protein and mRNA levels increased in CJD human samples and in mouse models of human prion disease in contrast to murine models of prion infection. However, changes in Reelin expression appeared only at late terminal stages of the disease, which prevent their use as an efficient diagnostic biomarker. In addition, increased Reelin in CJD and in in vitro models does not correlate with Dab1 phosphorylation, indicating failure in its intracellular signaling. Overall, these findings widen our understanding of the putative changes of Reelin in neurodegeneration.
Materia(s):	-Metabolisme -Malaltia de Creutzfeldt-Jakob -Matriu extracel·lular -Teixit nerviós -Malalties per prions -Metabolism -Creutzfeldt-Jakob disease -Extracellular matrix -Nerve tissue -Prion diseases
Derechos:	(c) Humana Press., 2017
Tipo de documento:	Artículo Artículo - Versión aceptada
Editor:	Humana Press.
Compartir:

Mostrar el registro completo del ítem