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Inflammation biomarkers and Alzheimer's disease: A pilot study using NULISAseq.
Alzheimers Dement (Amst)
January 2025
Introduction: Increasing evidence links amyloid beta (Aβ) aggregation with inflammation. This pilot study investigated the use of an immunoassay panel to map biomarker changes in patients with Alzheimer's disease (AD). Furthermore, we evaluated the stability of protein quantification after multiple freeze-thaw cycles (FTCs).
View Article and Find Full Text PDFPancreatic β cell-secreted factor FGF23 attenuates Alzheimer's disease-related amyloid β-induced neuronal death.
PNAS Nexus
January 2025
Department of Clinical Pharmacology, Faculty of Pharmaceutical Sciences, Sanyo-Onoda City University, 1-1-1 Daigaku-dori, Sanyo Onoda City, Yamaguchi 756-0884, Japan.
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by cognitive decline and memory impairment. The pathophysiology of AD may involve aggregated amyloid β (Aβ) accumulation, which may underlie the disease mechanism. Patients with diabetes exhibit an elevated risk of developing AD, indicating potential therapeutic implications upon elucidating the underlying mechanisms.
View Article and Find Full Text PDFMutations in hnRNP A1 drive neurodegeneration and alternative RNA splicing of neuronal gene targets.
Neurobiol Dis
January 2025
Office of the Saskatchewan Multiple Sclerosis Clinical Research Chair, University of Saskatchewan, Saskatoon, SK S7K 0M7, Canada; Neurology Division, Department of Medicine, University of Saskatchewan, Saskatoon, SK S7N 0X8, Canada. Electronic address:
RNA binding protein dysfunction is a pathogenic feature of multiple neurological diseases, including multiple sclerosis (MS). Neurodegeneration (the loss of, or damage to neurons and axons) is the primary driver of disease progression in MS. Herein, we utilized a novel, neuron-specific model of neurodegeneration by transducing primary mouse neurons with mutant forms of the RNA binding protein heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) identified from MS patients, including one within the M9-nuclear localization sequence of hnRNP A1 (A1(P275S)) and a second in the prion-like domain of hnRNP A1 (A1(F263S)) to test the hypothesis that neuronal hnRNP A1 dysfunction drives neurodegeneration in MS.
View Article and Find Full Text PDFRoles of C/EBPβ/AEP in Neurodegenerative Diseases.
Curr Top Med Chem
January 2025
Department of Histology and Embryology, School of Basic Medicine, Hengyang Medical School, University of South China, Hengyang, 421001, China.
In recent years, an increasing number of studies have shown that increased activation of aspartic endopeptidases (AEPs) is a common symptom in neurodegenerative diseases (NDDs). AEP cleaves amyloid precursor protein (APP), tau (microtubule-associated protein tau), α- synuclein (α-syn), SET (a 39-KDa phosphoprotein widely expressed in various tissues and localizes predominantly in the nucleus), and TAR DNA-binding protein 43 (TDP-43), and promotes their aggregation, contributing to Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease, multiple sclerosis (MS), amyotrophic lateral sclerosis (ALS), and frontotemporal dementia (FTD) pathogenesis. Abundant evidence supports the notion that CCAAT/enhancer-binding protein β (C/EBPβ)/AEP may play an important role in NDDs.
View Article and Find Full Text PDFLipidome disruption in Alzheimer's disease brain: detection, pathological mechanisms, and therapeutic implications.
Mol Neurodegener
January 2025
Sam and Ann Barshop Institute for Longevity and Aging Studies, University of Texas Health Science Center at San Antonio, San Antonio, TX, 78229, USA.
Alzheimer's disease (AD) is among the most devastating neurodegenerative disorders with limited treatment options. Emerging evidence points to the involvement of lipid dysregulation in the development of AD. Nevertheless, the precise lipidomic landscape and the mechanistic roles of lipids in disease pathology remain poorly understood.
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