Abnormal prion protein deposits with high seeding activities in the skeletal muscle, femoral nerve, and scalp of an autopsied case of sporadic Creutzfeldt–Jakob disease

2021 ◽  
Author(s):  
Hiroyuki Honda ◽  
Shinichiro Mori ◽  
Akihiro Watanabe ◽  
Naokazu Sasagasako ◽  
Shoko Sadashima ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Prion Protein ◽  
Femoral Nerve ◽  
Protein Deposits ◽  
Jakob Disease

The spatial patterns of prion protein deposits in cases of variant Creutzfeldt-Jakob disease

2002 ◽  
Vol 104 (6) ◽  
pp. 665-669 ◽  
Author(s):  
R. Armstrong ◽  
N. Cairns ◽  
J. Ironside ◽  
P. Lantos
Keyword(s):  
Prion Protein ◽  
Spatial Patterns ◽  
Protein Deposits ◽  
Jakob Disease

Spatial pattern of prion protein deposits in patients with sporadic Creutzfeldt–Jakob disease

2001 ◽  
Vol 21 (1) ◽  
pp. 19-24
Author(s):  
Richard A Armstrong ◽  
Nigel J Cairns ◽  
Peter L Lantos
Keyword(s):  
Spatial Pattern ◽  
Prion Protein ◽  
Protein Deposits ◽  
Jakob Disease

Prion protein deposits match magnetic resonance imaging signal abnormalities in Creutzfeldt-Jakob disease

2002 ◽  
Vol 51 (6) ◽  
pp. 797-799 ◽  
Author(s):  
Stéphane Haïk ◽  
Didier Dormont ◽  
Baptiste A. Faucheux ◽  
Claude Marsault ◽  
Jean-Jacques Hauw
Keyword(s):  
Magnetic Resonance Imaging ◽  
Magnetic Resonance ◽  
Prion Protein ◽  
Resonance Imaging ◽  
Protein Deposits ◽  
Magnetic Resonance Imaging Signal ◽  
Jakob Disease

Spatial pattern of prion protein deposits in patients with sporadic Creutzfeldt-Jakob disease

2001 ◽  
Vol 21 (1) ◽  
pp. 19-24 ◽  
Author(s):  
Richard A Armstrong ◽  
Nigel J Cairns ◽  
Peter L Lantos
Keyword(s):  
Spatial Pattern ◽  
Prion Protein ◽  
Protein Deposits ◽  
Jakob Disease

scholarly journals Extracellular Protein Aggregates Colocalization and Neuronal Dystrophy in Comorbid Alzheimer’s and Creutzfeldt–Jakob Disease: A Micromorphological Pilot Study on 20 Brains

2021 ◽  
Vol 22 (4) ◽  
pp. 2099
Author(s):  
Nikol Jankovska ◽  
Tomas Olejar ◽  
Radoslav Matej
Keyword(s):  
Prion Protein ◽  
Fluorescent Microscopy ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Key Characteristics ◽  
Jakob Disease ◽  
Immunohistochemical Methods ◽  
Confocal Fluorescent Microscopy ◽  
Codon 129

Alzheimer’s disease (AD) and sporadic Creutzfeldt–Jakob disease (sCJD) are both characterized by extracellular pathologically conformed aggregates of amyloid proteins—amyloid β-protein (Aβ) and prion protein (PrPSc), respectively. To investigate the potential morphological colocalization of Aβ and PrPSc aggregates, we examined the hippocampal regions (archicortex and neocortex) of 20 subjects with confirmed comorbid AD and sCJD using neurohistopathological analyses, immunohistochemical methods, and confocal fluorescent microscopy. Our data showed that extracellular Aβ and PrPSc aggregates tended to be, in most cases, located separately, and “compound” plaques were relatively rare. We observed PrPSc plaque-like structures in the periphery of the non-compact parts of Aβ plaques, as well as in tau protein-positive dystrophic structures. The AD ABC score according to the NIA-Alzheimer’s association guidelines, and prion protein subtype with codon 129 methionine–valine (M/V) polymorphisms in sCJD, while representing key characteristics of these diseases, did not correlate with the morphology of the Aβ/PrPSc co-aggregates. However, our data showed that PrPSc aggregation could dominate during co-aggregation with non-compact Aβ in the periphery of Aβ plaques.

scholarly journals Sensitive protein misfolding cyclic amplification of sporadic Creutzfeldt–Jakob disease prions is strongly seed and substrate dependent

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Maxime Bélondrade ◽  
Simon Nicot ◽  
Charly Mayran ◽  
Lilian Bruyere-Ostells ◽  
Florian Almela ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Misfolding ◽  
Protein Misfolding Cyclic Amplification ◽  
Bank Voles ◽  
Substrate Dependence ◽  
Brain Extracts ◽  
Jakob Disease ◽  
Human Prion Protein

AbstractUnlike variant Creutzfeldt–Jakob disease prions, sporadic Creutzfeldt–Jakob disease prions have been shown to be difficult to amplify in vitro by protein misfolding cyclic amplification (PMCA). We assessed PMCA of pathological prion protein (PrPTSE) from 14 human sCJD brain samples in 3 substrates: 2 from transgenic mice expressing human prion protein (PrP) with either methionine (M) or valine (V) at position 129, and 1 from bank voles. Brain extracts representing the 5 major clinicopathological sCJD subtypes (MM1/MV1, MM2, MV2, VV1, and VV2) all triggered seeded PrPTSE amplification during serial PMCA with strong seed- and substrate-dependence. Remarkably, bank vole PrP substrate allowed the propagation of all sCJD subtypes with preservation of the initial molecular PrPTSE type. In contrast, PMCA in human PrP substrates was accompanied by a PrPTSE molecular shift during heterologous (M/V129) PMCA reactions, with increased permissiveness of V129 PrP substrate to in vitro sCJD prion amplification compared to M129 PrP substrate. Combining PMCA amplification sensitivities with PrPTSE electrophoretic profiles obtained in the different substrates confirmed the classification of 4 distinct major sCJD prion strains (M1, M2, V1, and V2). Finally, the level of sensitivity required to detect VV2 sCJD prions in cerebrospinal fluid was achieved.

scholarly journals Gerstmann-Sträussler-Scheinker Disease and “Anchorless Prion Protein” Mice Share Prion Conformational Properties Diverging from Sporadic Creutzfeldt-Jakob Disease

2014 ◽  
Vol 289 (8) ◽  
pp. 4870-4881 ◽  
Author(s):  
Gianluigi Zanusso ◽  
Michele Fiorini ◽  
Sergio Ferrari ◽  
Kimberly Meade-White ◽  
Ilaria Barbieri ◽  
...  
Keyword(s):  
Prion Protein ◽  
Conformational Properties ◽  
Jakob Disease
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