The normal cellular prion protein, PrP(C) is a highly conserved and widely expressed cell surface glycoprotein in all mammals. The expression of PrP is pivotal in the pathogenesis of prion diseases; however, the normal physiological functions of PrP(C) remain incompletely understood. Based on the studies in cell models, a plethora of functions have been attributed to PrP(C). In this paper, we reviewed the potential roles that PrP(C) plays in cell physiology and focused on its contribution to tumorigenesis.
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http://dx.doi.org/10.1093/abbs/gmu019 | DOI Listing |
mSphere
January 2025
WOAH Reference Laboratory for CWD, Foreign Animal Disease Division, Animal and Plant Quarantine Agency, Gimcheon, South Korea.
Chronic wasting disease (CWD) is a highly contagious prion disease occurring in free-ranging and farmed cervids. CWD continues to spread uncontrolled across North America, and cases continue to be detected almost every year in the Republic of Korea. CWD-infected animals contaminate the soil by releasing infectious prions through their excreta, and shed prions accumulate and remain infectious in the soil for years.
View Article and Find Full Text PDFCureus
December 2024
Internal Medicine, Hospital Angeles Pedregal, Mexico City, MEX.
Prion disease is an uncommon entity characterized by exceptionally rapid neurodegenerative deterioration. There are three categories of prion disease: (1) sporadic: sporadic Creutzfeldt-Jakob disease (sCJD), sporadic fatal insomnia, and protease-sensitive prionopathy; (2) genetic: genetic Creutzfeldt-Jakob disease, familial fatal insomnia, and Gerstmann-Sträussler-Scheinker syndrome; and (3) acquired: Kuru, iatrogenic Creutzfeldt-Jakob disease, and variant Creutzfeldt-Jakob disease. Although it is an incurable disease, a specific pathophysiological mechanism exists involving neuronal loss, glial cell proliferation, absence of inflammatory response, development of vacuoles leading to a spongiform appearance, and the presence of prions.
View Article and Find Full Text PDFSci Rep
January 2025
Department of Immunology, Genetics and Pathology, Uppsala University, Rudbeck Laboratory, C11, 75185, Uppsala, Sweden.
The existence of transmissible amyloid fibril strains has long intrigued the scientific community. The strain theory originates from prion disorders, but here, we provide evidence of strains in systemic amyloidosis. Human AA amyloidosis manifests as two distinct clinical phenotypes called common AA and vascular AA.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
February 2025
Laboratory of Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892.
Hsp70, Hsp90, and ClpB/Hsp100 are molecular chaperones that help regulate proteostasis. Bacterial and yeast Hsp70s and their cochaperones function synergistically with Hsp90s to reactivate inactive and aggregated proteins by a mechanism that requires a direct interaction between Hsp90 and Hsp70 both in vitro and in vivo. and yeast Hsp70s also collaborate in bichaperone systems with ClpB and Hsp104, respectively, to disaggregate and reactivate aggregated proteins and amyloids such as prions.
View Article and Find Full Text PDFDecades after their initial observation in prion-infected brain tissues, the identities of virus-like dense particles, varicose tubules, and oval bodies containing parallel bands and fibrils have remained elusive. Our recent work revealed that a phenotype of dilation of the endoplasmic reticulum (ER), most notable for the perinuclear space (PNS), contributes to spongiform degeneration. To assess the significance of this phenotype for the etiology of prion diseases, we explored whether it can be functionally linked to other neuropathological hallmarks observed in these diseases, as this would indicate it to be a central event.
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