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Neurofilament Light Chain Levels in Serum and Cerebrospinal Fluid Do Not Correlate with Survival Times in Patients with Prion Disease.
Biomolecules
December 2024
Unit of Medical and Dental Sciences, Department of Health Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan.
Prion diseases, including Creutzfeldt-Jakob disease (CJD), are deadly neurodegenerative disorders characterized by the buildup of abnormal prion proteins in the brain. This accumulation disrupts neuronal functions, leading to the rapid onset of psychiatric symptoms, ataxia, and cognitive decline. The urgency of timely diagnosis for effective treatment necessitates the identification of strongly correlated biomarkers in bodily fluids, which makes our research crucial.
View Article and Find Full Text PDFIdentification of the Highly Polymorphic Prion Protein Gene () in Frogs ).
Animals (Basel)
January 2025
Department of Biological Sciences, Andong National University, Andong 36729, Republic of Korea.
Prion diseases are fatal neurodegenerative diseases that can be transmitted by infectious protein particles, PrPs, encoded by the endogenous prion protein gene (). The origin of prion seeds is unclear, especially in non-human hosts, and this identification is pivotal to preventing the spread of prion diseases from host animals. Recently, an abnormally high amyloid propensity in prion proteins (PrPs) was found in a frog, of which the genetic variations in the gene have not been investigated.
View Article and Find Full Text PDFEmerging targets of α-synuclein spreading in α-synucleinopathies: a review of mechanistic pathways and interventions.
Mol Neurodegener
January 2025
Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
α-Synucleinopathies constitute a spectrum of neurodegenerative disorders, including Parkinson's disease (PD), Lewy body dementia (LBD), Multiple System Atrophy (MSA), and Alzheimer's disease concurrent with LBD (AD-LBD). These disorders are unified by a pathological hallmark: aberrant misfolding and accumulation of α-synuclein (α-syn). This review delves into the pivotal role of α-syn, the key agent in α-synucleinopathy pathophysiology, and provides a survey of potential therapeutics that target cell-to-cell spread of pathologic α-syn.
View Article and Find Full Text PDFFunctional classification of tauopathy strains reveals the role of protofilament core residues.
Sci Adv
January 2025
Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Distinct tau amyloid assemblies underlie diverse tauopathies but defy rapid classification. Cell and animal experiments indicate tau functions as a prion, as different strains propagated in cells cause unique, transmissible neuropathology after inoculation. Strain amplification requires compatibility of the monomer and amyloid template.
View Article and Find Full Text PDFConnectome-based biophysical models of pathological protein spreading in neurodegenerative diseases.
PLoS Comput Biol
January 2025
Research Center for Social Computing and Information Retrieval, Harbin Institute of Technology, Harbin, China.
Neurodegenerative diseases are a group of disorders characterized by progressive degeneration or death of neurons. The complexity of clinical symptoms and irreversibility of disease progression significantly affects individual lives, leading to premature mortality. The prevalence of neurodegenerative diseases keeps increasing, yet the specific pathogenic mechanisms remain incompletely understood and effective treatment strategies are lacking.
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