In this study we report the formation of giant autophagic vacuoles (AV) in neurons in experimental scrapie in hamsters. Autophagy is an important step in the cellular turnover of proteins and organelles. It is known to occur in neurons under physiological as under pathological conditions. Giant AV, however, are seen very rarely only in pathological states. In our model AV are much more numerous after intracerebral (i.c.) transmission of the scrapie agent than after the transmission via the intraperitoneal route which points to a correlation between the intensity of the process and the period of incubation. As the appearance of the AV in our model is correlated chronologically with that of scrapie-associated fibrils, at least after i.c. transmission, the process may be related to a disturbance of cellular protein metabolism and, thus, to the processing of prion protein.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/BF00294449 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
assessment of neuroinflammatory cytokines in different stages of ovine natural prion disease.
Front Vet Sci
October 2024
Research Centre for Encephalopathies and Transmissible Emerging Diseases. Institute for Health Research Aragón (IIS) - WOAH Reference Laboratory for BSE and Scrapie, University of Zaragoza, Zaragoza, Spain.
Introduction: According to the neuroinflammatory hypothesis, a cytokine-mediated host innate immune response may be involved in the mechanisms that contribute to the process of neurodegeneration. Specifically, regarding prion diseases, some experimental murine models have evidenced an altered profile of inflammatory intermediaries. However, the local inflammatory response has rarely been assessed, and never in tissues from different natural models throughout the progression of neurodegeneration.
View Article and Find Full Text PDFPMCA to demonstrate the efficacy of prion inactivation methods on reusable medical devices: a relevant alternative to animal bioassays.
J Hosp Infect
December 2024
Molecular Virology Immunology Unit, Université Paris-Saclay, INRAE, UVSQ, Jouy-en-Josas, France. Electronic address:
Validation of prion inactivation processes for medical devices relies on in-vivo experimental protocols. However, bioassays are costly, long (1-2 years) and ethically disputable. Additionally, results obtained with one prion strain - for example, 263K (hamster-adapted strain originating from sheep scrapie) - cannot be easily extrapolated to relevant human prion strains, further questioning the utility of bioassays.
View Article and Find Full Text PDFUnfolding Mechanism and Fibril Formation Propensity of Human Prion Protein in the Presence of Molecular Crowding Agents.
Int J Mol Sci
September 2024
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DISTABiF), Università degli Studi della Campania Luigi Vanvitelli, 81100 Caserta, Italy.
The pathological process of prion diseases implicates that the normal physiological cellular prion protein (PrP) converts into misfolded abnormal scrapie prion (PrP) through post-translational modifications that increase β-sheet conformation. We recently demonstrated that HuPrP(90-231) thermal unfolding is partially irreversible and characterized by an intermediate state (β-PrPI), which has been revealed to be involved in the initial stages of PrP fibrillation, with a seeding activity comparable to that of human infectious prions. In this study, we report the thermal unfolding characterization, in cell-mimicking conditions, of the truncated (HuPrP(90-231)) and full-length (HuPrP(23-231)) human prion protein by means of CD and NMR spectroscopy, revealing that HuPrP(90-231) thermal unfolding is characterized by two successive transitions, as in buffer solution.
View Article and Find Full Text PDFRetention of prions in the polychaete and black soldier fly, , larvae after short-term experimental immersion and feeding with brain homogenate from scrapie infected sheep.
Heliyon
August 2024
SINTEF Ocean, Department of Fisheries and New Biomarine Industry, Brattørkaia 17C, 7010, Trondheim, Norway.
Finding alternative protein and lipid sources for aquafeeds is crucial for the sustainable growth of fed aquaculture. Upcycling industrial side streams and byproducts using extractive species can reduce waste and help reduce the sector's dependence on fish meal and fish oils. Polychaete worms () and black soldier fly () larvae (BSFL) are promising candidates for converting waste materials into valuable protein and lipid sources.
View Article and Find Full Text PDFTransmission of Norwegian reindeer CWD to sheep by intracerebral inoculation results in an unusual phenotype and prion distribution.
Vet Res
July 2024
Department of Production Animal Clinical Sciences, Norwegian University of Life Sciences, Sandnes, Norway.
Chronic wasting disease (CWD), a prion disease affecting cervids, has been known in North America (NA) since the 1960s and emerged in Norway in 2016. Surveillance and studies have revealed that there are different forms of CWD in Fennoscandia: contagious CWD in Norwegian reindeer and sporadic CWD in moose and red deer. Experimental studies have demonstrated that NA CWD prions can infect various species, but thus far, there have been no reports of natural transmission to non-cervid species.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!