Objective: To describe a novel molecular and pathological phenotype of Creutzfeldt-Jakob disease. Patient A 69-year-old woman with behavioral and personality changes followed by rapidly evolving dementia.
Results: Postmortem examination of the brain showed intracellular prion protein deposition and axonal swellings filled with amyloid fibrils. Biochemical analysis of the pathological prion protein disclosed a previously unrecognized PrP(Sc) tertiary structure lacking diglycosylated species. Genetic analysis revealed a wild-type prion protein gene. The prion agent responsible for this atypical phenotype was successfully passaged to bank voles.
Conclusion: To our knowledge, our results define a new human prion disorder characterized by intracellular accumulation of a novel type of pathological prion protein.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1001/archneur.64.4.595 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Re-evaluation of the relationship between PrPc expression and patient prognosis in primary esophageal squamous cell carcinoma and primary hepatocellular carcinoma.
Sci Rep
December 2024
Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
PrPc is expressed in various tumors and is associated with cancer progression, but previous studies have shown conflicting results regarding its relationship with patient prognosis-potentially due to differences in the antibodies used. This study aimed to clarify the relationship between PrPc expression and primary esophageal squamous cell carcinoma (ESCC) and primary hepatocellular carcinoma (HCC) using a novel anti-PrPc antibody, 4AA-m, noted for its high specificity and sensitivity. We used flow cytometry to detect PrPc expression in ESCC and HCC cell lines.
View Article and Find Full Text PDFExcitatory neuron-prone prion propagation and excitatory neuronal loss in prion-infected mice.
Front Mol Neurosci
December 2024
Laboratory of Veterinary Hygiene, Faculty of Veterinary Medicine, Graduate School of Infectious Diseases, Hokkaido University, Sapporo, Japan.
The accumulation of a disease-specific isoform of prion protein (PrP) and histopathological lesions, such as neuronal loss, are unevenly distributed in the brains of humans and animals affected with prion diseases. This distribution varies depending on the diseases and/or the combinations of prion strain and experimental animal. The brain region-dependent distribution of PrP and neuropathological lesions suggests a neuronal cell-type-dependent prion propagation and vulnerability to prion infection.
View Article and Find Full Text PDFA Copper-Binding Peptide with Therapeutic Potential against Alzheimer's Disease: From the Blood-Brain Barrier to Metal Competition.
ACS Chem Neurosci
December 2024
Department of Chemistry, Center for Research and Advanced Studies (Cinvestav), Mexico City 07360, Mexico.
Alzheimer's disease (AD) is the most common form of dementia worldwide. AD brains are characterized by the accumulation of amyloid-β peptides (Aβ) that bind Cu and have been associated with several neurotoxic mechanisms. Although the use of copper chelators to prevent the formation of Cu-Aβ complexes has been proposed as a therapeutic strategy, recent studies show that copper is an important neuromodulator that is essential for a neuroprotective mechanism mediated by Cu binding to the cellular prion protein (PrP).
View Article and Find Full Text PDFChemokines in neurodegenerative diseases.
Immunol Cell Biol
December 2024
Cellular and Molecular Medicine Research Institute, Cellular and Molecular Research Center, Urmia University of Medical Sciences, Urmia, Iran.
Neurodegeneration and neuroinflammation disorders are mainly the result of the deposition of various proteins, such as α-synuclein, amyloid-β and prions, which lead to the initiation and activation of inflammatory responses. Different chemokines are involved in the infiltration and movement of inflammatory leukocytes into the central nervous system (CNS) that express chemokine receptors. Dysregulation of several members of chemokines has been shown in the CNS, cerebrospinal fluid and peripheral blood of patients who have neurodegenerative disorders.
View Article and Find Full Text PDFIn situ staining with antibodies cross-reactive in pigs, cattle, and white-tailed deer facilitates understanding of biological tissue status and immunopathology.
Vet Immunol Immunopathol
December 2024
Infectious Bacterial Diseases Research Unit, National Animal Disease Center, Agricultural Research Service, United States Department of Agriculture, Ames, IA, USA.
Identifying cellular markers within archived formalin-fixed, paraffin-embedded (FFPE) tissues is critical for understanding tissue landscapes impacting animal health, but in situ detection methods are limited in veterinary species by a restricted toolbox of species-compatible immunoreagents. We identify antibodies with conserved in situ reactivity to IBA-1 (macrophages/dendritic cells), CD3ε (T cells), Pax5 (B cells), Ki-67 (cycling cells), and cytokeratin type I/II (epithelial cells) in FFPE tissues of pigs, cattle, and white-tailed deer. Multiplexed brightfield detection (IBA-1/CD3ε/Pax5) in lymph nodes of all three species demonstrated species-specific and species-conserved features of cellular architecture.
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!