Prion Protein Immunohistochemistry in Creutzfeldt-Jakob Disease

Gábor G KOVÁCS1, Katalin MAJTÉNYI2, Lajos LÁSZLÓ3

1Department of Neurology, Semmelweis University of Medicine, Budapest, Hungary
2Department of Neuropathology, National Institute of Psychiatry and Neurology, Budapest, Hungary
3Department of General Zoology, Eötvös University, Budapest, Hungary


Creutzfeldt-Jakob disease is a transmissible spongiform encephalopathy characterized clinically by dementia, myoclonus and, in some cases, periodic triphasic EEG-patterns. Neuropathologically the main features are spongiform change, astrocytosis, neuronal cell loss and, in a small percent of cases, amyloid plaques. Prion protein immunohistochemistry is used for definitive diagnosis of these diseases. In our study we present different immunostaining patterns in light microscopy using anti prion protein, and with immunogold labelling for ultrastructural localization of prion protein. Our results demonstrate the clinicopathological heterogeneity of Creutzfeldt-Jakob disease and reveal the role of the endosomal-lysosomal system in the pathogenesis. Pathology & Oncology Research, Vol 3, Nr 3, 193-197, 1997

Key words: Creutzfeldt-Jakob disease; prion protein; immunohistochemistry

Received: Jul 2, 1997; accepted: Aug 25, 1997
Correspondence: Lajos LÁSZLÓ, Department of General Zoology, Eötvös University, Budapest H-1445, Hungary; Tel: (36)(2)2669833, Fax: (36)(2)266788

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