Introduction: The presentation of subacute spongiform encephalopathies is varied and includes various movement disorders such as parkinsonism, myoclonus, or dystonia. These signs, especially when asymmetrical, can lead to the diagnostic of corticobasal degeneration.
Case Report: We report the case of a 75-Year-old woman who developed clinical signs suggestive of corticobasal degeneration: asymmetric rigidity and apraxia, limb dystonia, and postural instability. The final diagnosis of spongiform encephalopathy was suspected because of rapid decline and confirmed by post-mortem examination.
Conclusion: This case highlights the importance of considering subacute spongiform encephalopathy in patients with a clinical presentation compatible with corticobasal degeneration.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/s0035-3787(04)70995-9 | DOI Listing |
Commun Biol
January 2025
Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, TX, USA.
Aggregation of microtubule-associated tau protein is a distinct hallmark of several neurodegenerative disorders such as Alzheimer's disease (AD), dementia with Lewy bodies (DLB), and progressive supranuclear palsy (PSP). Tau oligomers are suggested to be the primary neurotoxic species that initiate aggregation and propagate prion-like structures. Furthermore, different diseases are shown to have distinct structural characteristics of aggregated tau, denoted as polymorphs.
View Article and Find Full Text PDFVet Res
January 2025
UVSQ, INRAE, BREED, Université Paris-Saclay, 78350, Jouy-en-Josas, France.
Misfolding of the cellular PrP (PrP) protein causes prion disease, leading to neurodegenerative disorders in numerous mammalian species, including goats. A lack of PrP induces complete resistance to prion disease. The aim of this work was to engineer Alpine goats carrying knockout (KO) alleles of PRNP, the PrP-encoding gene, using CRISPR/Cas9-ribonucleoproteins and single-stranded donor oligonucleotides.
View Article and Find Full Text PDFNeurobiol Dis
January 2025
Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. Electronic address:
Bank voles are susceptible to prion strains from many different species, yet the molecular mechanisms underlying the ability of bank vole prion protein (BVPrP) to function as a universal prion acceptor remain unclear. Potential differences in molecular environments and protein interaction networks on the cell surface of brain cells may contribute to BVPrP's unusual behavior. To test this hypothesis, we generated knock-in mice that express physiological levels of BVPrP (M109 isoform) and employed mass spectrometry to compare the interactomes of mouse (Mo) PrP and BVPrP following mild in vivo crosslinking of brain tissue.
View Article and Find Full Text PDFVet Microbiol
January 2025
Department of Agricultural and Environmental Sciences, College of Agriculture, Tennessee State University, Nashville, TN, United States. Electronic address:
Porcine reproductive and respiratory syndrome (PRRS), caused by the highly variable PRRS virus (PRRSV), presents a significant challenge to the swine industry due to its pathogenic and economic burden. The virus evades host immune responses, particularly interferon (IFN) signaling, through various viral mechanisms. Traditional vaccines have shown variable efficacy in the field, prompting the exploration of novel vaccination strategies.
View Article and Find Full Text PDFJ Neurogenet
January 2025
Institute of Prion Diseases, MRC Prion Unit at University College London, London, UK.
Inherited prion diseases (IPD) secondary to mutations of the prion protein gene, exhibit diverse clinical phenotypes, capable of mimicking numerous primary neurodegenerative conditions. We describe the clinical phenotype and neuropathological findings in a family from County Limerick in Ireland presenting with Alzheimer's disease-like cognitive decline and motor symptoms caused by a novel missense mutation of This mutation occurs in the central lysine cluster (CLC; codon 101-110), resulting in substitution of threonine with isoleucine at codon 107 (T107I). This case series highlights that IPD can be hard to distinguish from overlapping clinical syndromes seen in other neurodegenerative diseases.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!