Acta Neuropathologica

, Volume 103, Issue 5, pp 516–520

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

Authors

  •  S. Haïk
    • Raymond Escourolle Neuropathology Laboratory, Association Claude Bernard, INSERM U 360, Pitié-Salpêtrière Hospital, 47 Bd. de l'Hôpital, 75013 Paris, France
  •  N. Privat
    • Raymond Escourolle Neuropathology Laboratory, Association Claude Bernard, INSERM U 360, Pitié-Salpêtrière Hospital, 47 Bd. de l'Hôpital, 75013 Paris, France
  •  K. Adjou
    • Service de Neurovirologie, CEA, DSV/DRM, CRSSA, Fontenay aux Roses, France
  •  V. Sazdovitch
    • Raymond Escourolle Neuropathology Laboratory, Association Claude Bernard, INSERM U 360, Pitié-Salpêtrière Hospital, 47 Bd. de l'Hôpital, 75013 Paris, France
  •  D. Dormont
    • Service de Neurovirologie, CEA, DSV/DRM, CRSSA, Fontenay aux Roses, France
  •  C. Duyckaerts
    • Raymond Escourolle Neuropathology Laboratory, Association Claude Bernard, INSERM U 360, Pitié-Salpêtrière Hospital, 47 Bd. de l'Hôpital, 75013 Paris, France
  •  J. Hauw
    • Raymond Escourolle Neuropathology Laboratory, Association Claude Bernard, INSERM U 360, Pitié-Salpêtrière Hospital, 47 Bd. de l'Hôpital, 75013 Paris, France
Regular Paper

DOI: 10.1007/s00401-001-0499-z

Cite this article as:
Haïk, S., Privat, N., Adjou, K. et al. Acta Neuropathol (2002) 103: 516. doi:10.1007/s00401-001-0499-z

Abstract.

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 α-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). α-Synuclein accumulated close to PrPsc deposits but we did not observe strict colocalization of prion protein and α-synuclein immunoreactivities particularly in PrPsc plaques. α-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 α-synuclein in regulating PrPsc formation.

Creutzfeldt-Jakob disease Prion Aggregation Chaperone Neurodegeneration

Copyright information

© Springer-Verlag 2002