Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 7

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  PRION DISEASE
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1
Content available remote

The tubulovesicular structures - the ultrastructural hallmark for all prion diseases

100%
Liberski P. P.
Acta Neurobiologiae Experimentalis
|
2008
|
vol. 68
|
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.
2
Content available remote

Bovine spongiform encephalopathy Update

100%
Bradley R.
Acta Neurobiologiae Experimentalis
|
2002
|
vol. 62
|
issue 3
183-195
EN
Bovine spongiform encephalopathy (BSE) is a zoonosis being the origin of variant Creutzfeldt-Jakob disease and an important cattle disease in its own right. Countries have been slow to learn the importance of protecting, not only their cattle populations, but also their human populations. Since 2000, several additional European countries have reported BSE in native-born stock and this has led to a concern about the BSE status of countries that have imported cattle and cattle products from infected countries. Extensive feed and offal bans and application of newly-developed, ?Rapid? tests for prion protein in central nervous tissue of targeted, high-risk animals and slaughter cattle over 30 months old now provides the tools whereby the public are fully protected and BSE can be eradicated.
3
Content available remote

How do neurons degenerate in prion diseases or transmissible spongiform encephalopathies (TSEs): neuronal autophagy revisited

100%
Liberski P. P., Gajdusek D. C., Brown P.
Acta Neurobiologiae Experimentalis
|
2002
|
vol. 62
|
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.
4
Content available remote

Tubulovesicular structures are present in brains of hamsters infected with the Echigo-1 strain of Creutzfeldt-Jakob disease agent

100%
Liberski P. P.
Acta Neurobiologiae Experimentalis
|
2008
|
vol. 68
|
issue 1
39-42
EN
Tubulovesicular structures (particles; TVS) are virion-like particles 25?30 nm in diameter found by thin-section electron microscopy in brains of all prion diseases including scrapie, Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI) and Gerstmann-Str?ussler-Scheineker disease (GSS), as well as in cell cultures infected with TSE agents. TVS are regarded as a disease-specific ultrastructural marker for TSEs and, by those not completely satisfied with the prion hypothesis, they are even considered to be a possible candidate for the infectious TSE agent itself. A caveat regarding that interpretation stemmed from previous failures to find TVS by electron microscopic studies of tissues from animals infected with the Echigo-1 strain of CJD agent. We now report detecting TVS in brains of hamsters infected with that strain of CJD agent, albeit with a very low frequency.
5
Content available remote

Tubulofilamentous particles

100%
Liberski P. P.
|
|
issue 3
149-154
EN
Tubulofilamentous particles
6
Content available remote

Apoptosis in relation to neuronal loss in experimental Creutzfeldt-Jakob disease in mice

88%
Jesionek-Kupnicka D., Kordek R., Buczynski J., Liberski P. P.
|
EN
Apoptosis constitutes a genetically determined process to eliminate superfluous or damaged cells in tissues. Deficiencies in apoptosis regulation are involved in different pathologies including prion diseases. Some experimental studies show that neuronal loss - one of the hallmarks of prion diseases may be accomplished by apoptosis. We evaluated twenty five mice infected experimentally with the Fujisaki strains of CJD and sacrified sequentially in one week intervals. Apoptotic cells in various brain regions were detected by in situ end labelling (TUNEL) and electron microscopy in comparison with neuronal cell loss. The number of labelled cells per brain was very low - from a few labelled cells 6 weeks after inoculation to a maximum of 14 in the terminal stage. The number of neurones counted in 8 selected areas were considerably lower in terminally sick animals (20 and 21 week of incubation period) than in control mice. The mean value of loss of neuronal cells was 32%. The greatest loss (55%) of neurones was noted in the septal nuclei of the paraterminal body and the least lost (16%) in the hypothalamus. Compared to the extensive neuronal loss (30-50%), the number of apoptotic cells detected by in situ end labelling seems to be very low, and the process of neuronal death become more intensive during the progression of the disease.
7

Prions - the new infectious agent

88%
Gogiel T.
|
|
issue 3
35-51
EN
Prions are devoid of nucleic acids and they are composed mainly or exclusively of protein PrPSC, that is a conformational variant of the normal cellular prion protein PrPC, encoded by a chromosomal gene. Conversion of PrPC into PrPSC is a posttranslational process which is accompanied by the acquisition of high b-sheet content. Human prion diseases may be of sporadic, genetic or infectious origin. Human activity caused a 'mad cow disease' epidemic, iatrogenic Creutzfeldt-Jakob disease (CJD), and lately, a new variant of CJD, which is thought to be a result of transmission of bovine prions to humans. Prion diseases are always fatal, and there is a need to develop effective methods of prevention and therapy for these disorders.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.