NR AFAH
AU Haik,S.; Privat,N.; Adjou,K.T.; Sazdovitch,V.; Dormont,D.; Duyckaerts,C.; Hauw,J.J.
TI Alpha-synuclein-immunoreactive deposits in human and animal prion diseases
QU Acta Neuropathologica 2002 May; 103(5): 516-20
PT journal article
AB 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.
MH Animal; Central Nervous System/*metabolism/pathology/physiopathology; Creutzfeldt-Jakob Syndrome/*metabolism/pathology/physiopathology; Hamsters; Human; Immunohistochemistry; Inclusion Bodies/metabolism; Nerve Tissue Proteins/*metabolism; Neurons/*metabolism/pathology; Neuropil/*metabolism/pathology; PrPsc Proteins/metabolism; Prions/metabolism; Scrapie/*metabolism/pathology/physiopathology; Support, Non-U.S. Gov't
AD Raymond Escourolle Neuropathology Laboratory, Association Claude Bernard, INSERM U 360, Pitie-Salpetriere Hospital, 47 Bd. de l'Hopital, 75013 Paris, France. haik@mailhost.chups.jussieu.fr
SP englisch
PO Deutschland