Familial prion diseases are linked to point and insertional mutations in the prion protein (PrP) gene that are presumed to favor conversion of the cellular isoform of PrP to the infectious isoform. In this report, we have investigated the subcellular localization of PrP molecules carrying pathogenic mutations using immunofluorescence staining, immunogold labeling, and PrP-green fluorescent prot...

BACKGROUND There has been a dramatic decrease in the risk of transmission of bovine spongiform encephalopathy to humans. In contrast, the risk of human-to-human transmission of variant Creutzfeldt-Jakob disease (vCJD) via medical treatments became potentially high since 4 vCJD cases were reported to be possibly transmitted through blood transfusion in the UK. However, no treatments are yet avai...

Interleukin (IL)-1β-induced chondrocyte apoptosis is associated with the pathogenesis of arthritis. Platelet‑rich plasma (PRP), which is derived from the patient's own blood and contains numerous growth factors, has the potential for arthritis treatment. Therefore, the present study aimed to determine the effects of PRP on chondrocyte apoptosis, under IL‑1β‑induced pathological conditions. Chon...

Lansbury and Caughey state in their Primer on prion proteins [1] “Mice lacking the PrP gene, first produced by Charles Weissmann and colleagues, are viable, but have altered neuronal function and develop neurological abnormalities later in life.” This statement is misleading. The PrP-knockout mice produced in our laboratory [2] do not show neurological abnormalities at any time and we have neve...

Genetic ablation of cellular prion protein (PrP(C)) has been linked to increased neuronal excitability and synaptic activity in the hippocampus. We have previously shown that synaptic activity in hippocampi of PrP-null mice is increased due to enhanced N-methyl-D-aspartate receptor (NMDAR) function. Here, we focused on the effect of PRNP gene knock-out (KO) on intrinsic neuronal excitability, a...

Prion protein (PrP) is critically involved in the transmission and pathogenesis of the transmissible spongiform encephalopathies (TSEs), which include scrapie in sheep, variant and sporadic Creutzfeldt–Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) in cattle. The normal, cellular PrPc protein encoded by the Prnp gene is required for susceptibility to TSE. The interconv...

The physiological role of the cellular prion protein (PrP(C)) is incompletely understood. The expression of PrP(C) in hematopoietic stem cells and immune cells suggests a role in the development of these cells, and in PrP(C) knockout animals altered immune cell proliferation and phagocytic function have been observed. Recently, a spontaneous nonsense mutation at codon 32 in the PRNP gene in goa...

Deposition of PrP amyloid in cerebral vessels in conjunction with neurofibrillary lesions is the neuropathologic hallmark of the dementia associated with a stop mutation at codon 145 of PRNP, the gene encoding the prion protein (PrP). In this disorder, the vascular amyloid in tissue sections and the approximately 7.5-kDa fragment extracted from amyloid are labeled by antibodies to epitopes loca...

In sheep, susceptibility to scrapie is associated with the prion protein (PrP) gene polymorphism. In this study the association between selected growth traits (daily weight gain from birth to weaning and in farm fattening performance test, as well as body weight at one and two years) and PrP genotypes ARR/ARR, ARR/XXX and XXX/XXX (XXX representing AHQ, ARQ, ARH or VRQ) has been investigated in ...

Prion diseases are fatal neurodegenerative conditions in humans and animals. In this review, we summarize the molecular background of phenotypic variability, relation of prion protein (PrP) to other proteins associated with neurodegenerative diseases, and pathogenesis of neuronal vulnerability. PrP exists in different forms that may be present in both diseased and non-diseased brain, however, a...