Cellular expression of host prion protein (PrP) is essential to infection with prion disease. Understanding the mechanisms that regulate prion protein expression at both the transcriptional and translational levels is therefore an important goal. The cellular prion protein has been associated with resistance to oxidative, and its expression is also increased by oxidative stress. The transcripti...

Prion proteins are considered as the main agents for the Transmissible Spongiform Encephalopathies (TSE). The misfolded form, PrP Sc , which is also indicated as the etiological agent for TSE, exhibits high resistance to degradation in environmental processes. Soil contamination by prion proteins is a real environmental issue since contaminated soils can become potential reservoir and diffuser ...

Prions are protein conformations that "self-seed" the misfolding of their non-prion iso-forms into prion, often amyloid, conformations. The most famous prion is the mammalian PrP protein that in its prion form causes transmissible spongiform encephalopathy. Curiously there can be distinct conformational differences even between prions of the same protein propagated in the same host species. The...

Inherited prion diseases are neurodegenerative disorders caused by autosomal dominant mutations in the human prion protein gene (PRNP). Kindred with inherited prion disease can show remarkable phenotypic variability that has yet to be explained. Here we report analysis of protease resistant disease-related prion protein (PrP(Sc)) isoforms from a range of inherited prion disease cases (point mut...

Prion diseases (e.g. Creutzfeldt-Jakob disease (CJD), variant CJD (vCJD), Gerstmann-Straussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI) and Kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE or 'mad-cow' disease) and chronic wasting disease (CWD) in cattles) are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. Ho...

Prions are unconventional self-propagating proteinaceous particles, devoid of any coding nucleic acid. These proteinaceous seeds serve as templates for the conversion and replication of their benign cellular isoform. Accumulating evidence suggests that many protein aggregates can act as self-propagating templates and corrupt the folding of cognate proteins. Although aggregates can be functional...

Prion diseases are infectious neurodegenerative disorders characterized by the conversion of the cellular prion protein (PrPc) to the misfolded isoform (PrPsc). Prion peptide PrP 106-126 [PrP (106-126)] shares many physiological properties with PrPsc; it is neurotoxic in vitro and in vivo. PrP (106-126) induces neurotoxicity by the overexpression of PrPc and activation of the mitogen-activated ...

About BSE BSE (bovine spongiform encephalopathy) is a progressive neurological disorder of cattle that results from infection by an unusual transmissible agent called a prion. The nature of the transmissible agent is not well understood. Currently, the most accepted theory is that the agent is a modified form of a normal protein known as prion protein. For reasons that are not yet understood, t...

Protein misfolding is common across many neurodegenerative diseases, with misfolded proteins acting as seeds for "prion-like" conversion of normally folded protein to abnormal conformations. A central hypothesis is that misfolded protein accumulation, spread, and distribution are restricted to specific neuronal populations of the central nervous system and thus predict regions of neurodegenerat...

2266 Emerging Infectious Diseases • www.cdc.gov/eid • Vol. 10, No. 12, December 2004 or inherited disease, or as a result of iatrogenic transmission. Prion diseases generated great public concern after an outbreak of bovine spongiform encephalopathy occurred in many European countries and scientific evidence indicated its transmission to humans. Research in prion diseases is hampered by certain...