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Acta Neuropathol. 2002 May;103(5):516-20. Epub 2002 Feb 5.

Alpha-synuclein-immunoreactive deposits in human and animal prion diseases.

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Raymond Escourolle Neuropathology Laboratory, Association Claude Bernard, INSERM U 360, Pitié-Salpêtrière Hospital, 47 Bd. de l'Hôpital, 75013 Paris, France.


Prion related disorders are associated with the accumulation of a misfolded isoform (PrPsc) of the host-encoded prion protein, PrP. There is strong evidence for the involvement of unidentified co-factors in the PrP to PrPsc conversion process. In this study, we show alpha-synuclein-immunoreactive deposits in the central nervous system of various prion diseases (sporadic, iatrogenic and new variant Creutzfeldt-Jakob diseases, and experimental scrapie of hamsters). alpha-Synuclein accumulated close to PrPsc deposits but we did not observe strict colocalization of prion protein and alpha-synuclein immunoreactivities particularly in PrPsc plaques. alpha-Synuclein is thought to be a key player in some neurodegenerative disorders, is able to interact with amyloid structures and has known chaperone-like activities. Our results, in various prion diseases, suggest a role for alpha-synuclein in regulating PrPsc formation.

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