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Ultrastructural studies of experimental scrapie and Creutzfeldt-Jakob disease in hamsters. I. Alterations of myelinated axons

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Liberski P. P., Bratosiewicz-Wasik J., Gajdusek D. C., Brown P.
Acta Neurobiologiae Experimentalis
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2002
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vol. 62
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issue 3
121-129
EN
Classical and ultrastructural neuropathology of prion diseases are generally well described. Here we report that alterations of myelinated fibres in hamsters infected either with polioencephalopathic strains of scrapie or panencephalopathic strains of CJD (Echigo-1) are virtually identical and differ only quantitatively. In contrast, mice infected with the panencephalopathic Fujisaki strain of CJD exhibited much more elaborate changes of myelinated fibres.
2

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Piasecki E.
Postępy Higieny i Medycyny Doświadczalnej
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1993
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vol. 47
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issue 2
85-99
EN
are proteinaceous infection particles. They are probably devoid of nucleic acid. (PrP) is encoded by the normal cellular gene. of prion protein has different conformation than the normal PrP protein. The exact nature of the posttranslational modification of prion protein is unknown. This modification may be caused by infection with prions infectious disease or occures spontaneously sporadic disease. Some mutations in PrP gene results in the production of pathological protein familial disease.
3
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Ultrastructural studies of experimental scrapie and Creutzfeldt-Jakob disease in hamsters. II. Astrocytic and macrophage reaction toward the axonal destruction

100%
Liberski P. P., Bratosiewicz-Wasik J., Gajdusek D. C., Brown P.
Acta Neurobiologiae Experimentalis
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2002
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vol. 62
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issue 3
131-139
EN
We report here the microglial (macrophage) and astrocytic reaction in several models of transmissible spongiform encephalopathies (TSEs) or prion diseases. With the low power electron microscopy it was readily apparent that myelinated vacuoles were surrounded by cells and their processes. The latter belonged either to hyperplastic reactive astrocytes or to macrophages. Typically reactive astrocytes exhibited cytoplasm filled with innumerable glial filaments and, occasionally, other organelles (like cilia) and abundant tortuous intercellular junctions of adhesive plaque junction type. Desmosome-like junctions connecting astrocytic elements were also seen. As described earlier, astrocytic processes were occasionally interdigitated with oligodendroglial cells and their processes. Two types of macrophages were readily described. The majority of them exhibited electron-dense cytoplasm and numerous ?empty? vacuoles (digestive chambers) containing cellular debris. Occasional vacuoles were surrounded by a thin collar reminiscent of ?lyre-like inclusions? of the second type of macrophages. The latter were rare and characterized by numerous ?lyre-like? inclusions. Several mylinated fibres were clearly engulfed by the cytoplasm of a macrophage containing unusual annulate lamellae.
4
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How do neurons degenerate in prion diseases or transmissible spongiform encephalopathies (TSEs): neuronal autophagy revisited

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Liberski P. P., Gajdusek D. C., Brown P.
Acta Neurobiologiae Experimentalis
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2002
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vol. 62
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issue 3
141-147
EN
As in other neurodegenerative diseases such as Alzheimer?s disease, neurons in prion diseases or transmissible spongiform encephalopathies (TSEs) die via programmed cell death of which the apoptotic process is relatively well characterized. A subcellular alteration linked to apoptosis is the formation of autophagic vacuoles, which we and others demonstrated in CJD- and scrapie-affected rodent brains. Autophagy may co-exist with apoptosis or may precede it and the process may be induced by apoptotic stimuli. Here, we extend these observations using different model of scrapie and CJD. Both scrapie models (the 263K and 22C-H) demonstrated autophagic vacuoles with the same frequency; hence, they will be described together. While the following changes had been observed simultaneously in different areas of the same sample, this description is organised as if it followed a sequence of events. First, a part of the neuronal cytoplasm was sequestrated by concentric arrays of membrane; that part of the cytoplasm closed by membranes appeared relatively normal but its density often appeared increased. Next, electron density of the central dramatically increased. Then, membranes proliferated within the cytoplasm in a labyrinth-like manner and an area sequestrated by these membranes enlarged and became more complex structure consisting of vacuoles, electron-dense area and areas of normally-looking cytoplasm connected with convoluted membranes. Finally, a large area of the cytoplasm was transformed into a collection of autophagic vacuoles of different sizes. Virtually identical alterations, albeit with much lower frequency, were seen in terminally ill CJD-affected hamsters.
5
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The tubulovesicular structures - the ultrastructural hallmark for all prion diseases

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Liberski P. P.
Acta Neurobiologiae Experimentalis
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2008
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vol. 68
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issue 1
113-121
EN
Tubulovesicular structures (particles ? TVS) are the only ultrastructural marker for all prion diseases as seen by thin-section electron microscopy as opposed to ?negative-staining' techniques. TVS are spheres or short rods of approximately 27 nm in diameter. That size of TVS is also the size of filter cut-off of infectivity as judged from the ultrafiltration studies and the size of the smallest infectious unit as recently estimated. TVS have been found in all naturally occurring and experimentally induced prion diseases, including variant Creutzfeldt-Jakob disease and human familial TSEs ? fatal familial insomnia and Gerstmann-Str?ussler-Scheinker disease. In longitudinal studies, the number of neuronal processes containing TVS correlates roughly with the incubation period and with infectivity. Hence, they are readily found in hamsters infected with the 263K strain of scrapie but it is very difficult to find them in human TSEs where titer is lower. The composition of TVS is unknown but they are not composed of PrP. Their consistent presence in all TSEs suggests the unexplained role at least of TSE pathogenesis.
6
Content available remote

Tubulofilamentous particles

100%
Liberski P. P.
Acta Neurobiologiae Experimentalis
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1995
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vol. 55
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issue 3
149-154
EN
Tubulofilamentous particles
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