NR AXWI
AU Sikorska,B.; Liberski,P.P.; Budka,H.; Ironside,J.W.
TI Ultrastructural Study of Florid Plaques in vCJD: A Comparison with Kuru Plaques in sCJD and Multicentric Plaques of GSS
QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Pathology and Pathogenesis P03.16
IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf
PT Konferenz-Poster
AB Amyloid plaques are a hallmark of transmissible and non-transmissible brain amyloidoses, and in human transmissible spongiform encephalopathies occur in sporadic CJD, kuru (both of which may contain kuru plaques), Gerstmann-Sträussler Scheinker disease (multicentric plaques) and variant CJD (florid plaques). The ultrastructure of kuru and multicentric plaques has been studied for decades, but florid plaques in variant CJD have been described at the ultrastructural level in only one case report. To rectify this situation, we studied vCJD plaques systematically and compared them to plaques in sCJD, GSS and Alzheimer disease. Florid plaques were either compact (resembling kuru plaques) or diffuse; even in more compact plaques the radiating fibrils were organized into thick "tongues", in contrast to classical kuru plaques. Florid plaques were also neuritic - i.e. they contained dystrophic neurites; the latter contained lysosomal electron-dense bodies or vesicles. Microglial cells were found within florid plaques and in certain specimens the amyloid fibrils were clearly present in membrane-bound pockets of microglial cells. Morphometric analysis showed significant differences in fibril diameter between vCJD nad GSS. Overall, the ultrastructure of florid plaques of vCJD is more reminiscent of neuritic plaques in AD than kuru or multicentric plaques. The reasons for these differences in prion protein plaque structures are poorly understood, but are likely to reflect differences in the strains of the transmissible agents responsible for these disorders and to host factors, particularly the codon 129 polymorphism in the prion protein gene.
AD B. Sikorska, P. Liberski, Medical University of Lodz, Deaprtment of Molecular Pathology and Neuropatholo, Poland; H. Budka, Medical University of Vienna, Institute of Neurology, Austria; J. Ironside, University of Edinburgh, National CJD Surveillance Unit, UK
SP englisch
PO Schottland