Resumen: The cellular prion protein, encoded by the gene Prnp, has been reported to be a receptor of ß-amyloid. Their interaction is mandatory for neurotoxic effects of ß-amyloid oligomers. In this study, we aimed to explore whether the cellular prion protein participates in the spreading of a-synuclein. Results demonstrate that Prnp expression is not mandatory for a-synuclein spreading. However, although the pathological spreading of a-synuclein can take place in the absence of Prnp, a-synuclein expanded faster in PrPC-overexpressing mice. In addition, a-synuclein binds strongly on PrPC-expressing cells, suggesting a role in modulating the effect of a-synuclein fibrils. Idioma: Inglés DOI: 10.1007/s12035-017-0451-4 Año: 2017 Publicado en: MOLECULAR NEUROBIOLOGY (2017), 1-14 ISSN: 0893-7648 Factor impacto JCR: 5.076 (2017) Categ. JCR: NEUROSCIENCES rank: 44 / 261 = 0.169 (2017) - Q1 - T1 Factor impacto SCIMAGO: 1.614 - Neurology (Q1) - Neuroscience (miscellaneous) (Q1) - Cellular and Molecular Neuroscience (Q2)