Diagnosing Alzheimer's disease (AD) through pathological markers is typically costly and invasive. This study aims to find a noninvasive, cost-effective method using portable electroencephalography (EEG) to detect changes in AD-related biomarkers in cerebrospinal fluid (CSF). A total of 102 patients, both with and without AD-related biomarker changes (amyloid beta and phosphorylated tau), were recorded using a 2-minute resting-state portable EEG. A machine-learning algorithm then analyzed the EEG data to identify these biomarker changes. The results showed that the machine learning model could distinguish patients with AD-related biomarker changes, achieving 68.1% accuracy (AUROC 0.75) for amyloid beta and 71.2% accuracy (AUROC 0.77) for phosphorylated tau, with gamma activities being key features. When excluding cases with idiopathic normal pressure hydrocephalus, accuracy improved to 74.1% (AUROC 0.80) for amyloid beta and 73.1% (AUROC 0.80) for phosphorylated tau. This study suggests that portable EEG combined with machine learning is a promising noninvasive and cost-effective tool for early AD-related pathological marker screening, which could enhance neurophysiological understanding and diagnostic accessibility.
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http://dx.doi.org/10.1038/s41598-025-86449-2 | DOI Listing |
Alzheimers Dement
January 2025
Unitat de Trastorns Cognitius, Cognition and Behavior Study Group, Hospital Universitari Santa Maria Universitat de Lleida, Lleida, Spain.
Introduction: Changes in sleep physiology can predate cognitive symptoms by decades in persons with Alzheimer's disease (AD), but it remains unclear which sleep characteristics predict cognitive and neurodegenerative changes after AD onset.
Methods: Using data from a prospective cohort of mild to moderate AD (n = 60), we analyzed non-rapid eye movement sleep spindles and slow oscillations (SOs) at baseline and their associations with baseline amyloid beta (Aβ) and tau and with cognition from baseline to 3-year follow-up.
Results: Higher spindle and SO activity predicted significant changes in Aβ and tau at baseline, lower Alzheimer's Disease Assessment Scale Cognitive Subscale (better cognitive performance) score, and higher Mini-Mental State Examination score from baseline to 36 months.
Alzheimers Dement
January 2025
Department of Neurology, Neurological Institute, Taipei Veterans General Hospital, Taipei, Taiwan.
Introduction: Plasma phosphorylated tau (p-tau) biomarkers have improved Alzheimer's disease (AD) diagnosis, but data from diverse Asian populations are limited. This study evaluated plasma p-tau217 and p-tau181 levels in Korean and Taiwanese populations.
Methods: All participants (n = 270) underwent amyloid positron emission tomography (PET) and blood tests.
Brain Res
January 2025
Department of Psychiatry, Massachusetts General Hospital and Harvard Medical School, Charlestown, MA 02129, USA. Electronic address:
Background: Osteoarthritis is associated with a higher risk of developing dementia, though the underlying biological mechanisms have remained unclear. Recent studies suggest that blood phosphorylated tau proteins, particularly Tau-PT217, are sensitive biomarkers capable of detecting cognitive decline in its early stages, making it useful for early diagnosis of Alzheimer's disease and other forms of cognitive impairment.
Methods: In this study, we investigated the plasma phosphorylated tau protein levels (Tau-PT217 and Tau-PT181), hippocampus functional connectivity, and cognitive function in people with knee osteoarthritis compared to age and gender matched pain-free controls.
Eur J Pharmacol
January 2025
Department of Pharmacology and Toxicology, Faculty of Pharmacy, Cairo University, 11562 Cairo, Egypt.
Tau hyper-phosphorylation has been recognized as an essential contributor to neurodegeneration in Alzheimer's disease (AD) and related tauopathies. In the last decade, tau hyper-phosphorylation has gained considerable concern in AD therapeutic development. Tauopathies are manifested with a broad spectrum of symptoms, from dementia to cognitive decline and motor impairments.
View Article and Find Full Text PDFJ Chem Inf Model
January 2025
Department of Chemistry, Faculty of Science, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada.
Tau is a microtubule (MT)-associated protein that binds to and stabilizes the MTs of neurons. Due to its intrinsically disordered nature, it undergoes several post-translational modifications (PTMs) that are intricately linked to both the physiological and pathophysiological roles of Tau. Prior research has shown phosphorylation and O-GlcNAcylation to have contrasting effects on Tau aggregation; however, the precise molecular mechanisms and potential synergistic effects of these modifications remain elusive.
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