The accumulation kinetics of the abnormal form of prion protein (PrP(Sc)) in spleens and brains of scrapie (Obihiro-1)-infected mice at various times after intracerebral (i.c.), intraperitoneal (i.p.), or oral inoculation were studied. PrP(Sc) was first detected by Western blotting with anti-prion protein antibodies on days 70 and 116 after i.c. (3 microg) in spleens and brains, respectively. Although the amount of cerebral PrP(Sc) gradually increased to the maximum level on day 152 after i.c. inoculation, splenic PrP(Sc) established the maximum level on day 116 after i.c. inoculation then registered slight decreases up to day 152 with further incubation. The detectable levels of cerebral PrP(Sc) by Western blotting were established on day 231 or 259, whereas those of splenic PrP(Sc) were detected on day 94 or 93, after i.p. and oral infection, respectively. The splenic PrP(Sc) decreased slightly thereafter. These results indicate that splenic PrP(Sc) increased before cerebral PrP(Sc) established a detectable level in a manner independent of the inoculation route.
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PLoS Pathog
September 2024
Institute of Neuropathology, University Hospital Zurich, University of Zurich, Zurich, Switzerland.
In prion diseases (PrDs), aggregates of misfolded prion protein (PrPSc) accumulate not only in the brain but also in extraneural organs. This raises the question whether prion-specific pathologies arise also extraneurally. Here we sequenced mRNA transcripts in skeletal muscle, spleen and blood of prion-inoculated mice at eight timepoints during disease progression.
View Article and Find Full Text PDFPLoS Pathog
July 2024
Faculty of Veterinary Medicine, University of Calgary, Calgary, Canada.
Chronic wasting disease (CWD) is a prion disease affecting deer, elk and moose in North America and reindeer, moose and red deer in Northern Europe. Pathogenesis is driven by the accumulation of PrPSc, a pathological form of the host's cellular prion protein (PrPC), in the brain. CWD is contagious among North American cervids and Norwegian reindeer, with prions commonly found in lymphatic tissue.
View Article and Find Full Text PDFBMB Rep
December 2023
Department of Bioinformatics and Life Science, Soongsil University, Seoul 06978, Korea.
Numerous studies have investigated the cellular prion protein (PrP) since its discovery. These investigations have explained that its structure is predominantly composed of alpha helices and short beta sheet segments, and when its abnormal scrapie isoform (PrP) is infected, PrP transforms the PrP, leading to prion diseases, including Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in cattle. Given its ubiquitous distribution across a variety of cellular types, the PrP manifests a diverse range of biological functions, including cell-cell adhesion, neuroprotection, signalings, and oxidative stress response.
View Article and Find Full Text PDFInt J Mol Sci
December 2022
Department of Pharmacy, College of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University, 55 Hanyangdaehak-ro, Sangnok-gu, Ansan 15588, Gyeonggi-do, Republic of Korea.
Prion diseases are neurodegenerative disorders in humans and animals for which no therapies are currently available. Here, we report that Valeton (Zingiberaceae) () extract was partly effective in decreasing prion aggregation and propagation in both in vitro and in vivo models. extract inhibited self-aggregation of recombinant prion protein (PrP) in a test tube assay and decreased the accumulation of scrapie PrP (PrP) in ScN2a cells, a cultured neuroblastoma cell line with chronic prion infection, in a concentration-dependent manner.
View Article and Find Full Text PDFPLoS Pathog
July 2020
Université Paris-Saclay, INRAE, UVSQ, VIM Jouy-en-Josas, France.
Prions are pathogens formed from abnormal conformers (PrPSc) of the host-encoded cellular prion protein (PrPC). PrPSc conformation to disease phenotype relationships extensively vary among prion strains. In particular, prions exhibit a strain-dependent tropism for lymphoid tissues.
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