Prefibrillar oligomers of the beta-amyloid peptide (A beta) are recognized as potential mediators of Alzheimer's disease (AD) pathophysiology. Deficits in synaptic function, neurotoxicity, and the progression of AD have all been linked to the oligomeric A beta assemblies rather than to A beta monomers or to amyloid plaques. However, the molecular sites of A beta oligomer action have remained largely unknown. Recently, the cellular prion protein (PrP(C)) has been shown to act as a functional receptor for A beta oligomers in brain slices. Because PrP(C) serves as the substrate for Creutzfeldt-Jakob Disease (CJD), these data suggest mechanistic similarities between the two neurodegenerative diseases. Here, we review the importance of A beta oligomers in AD, commonalities between AD and CJD, and the newly emergent role of PrP(C) as a receptor for A beta oligomers.
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http://dx.doi.org/10.1007/s00109-009-0568-7 | DOI Listing |
Acta Neuropathol Commun
January 2025
Department of Neuroscience, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Via Mario Negri 2, 20156, Milan, Italy.
Deposition of abnormally phosphorylated tau aggregates is a central event leading to neuronal dysfunction and death in Alzheimer's disease (AD) and other tauopathies. Among tau aggregates, oligomers (TauOs) are considered the most toxic. AD brains show significant increase in TauOs compared to healthy controls, their concentration correlating with the severity of cognitive deficits and disease progression.
View Article and Find Full Text PDFFood Chem
January 2025
College of Food and Bioengineering, Xihua University, Chengdu 610039, China; Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Chengdu 610039, China; School of Future Food Modern Industry, Xihua University, Chengdu 610039, China. Electronic address:
The effects of high-intensity ultrasound (HIU) on the dispersibility of myofibrillar proteins (MPs) in low-salt medium were investigated. HIU-assisted STPP or TSPP could sharply improve the solubility and dispersibility of MPs (from 38.12 % to 94.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
Unidad de Investigación en Enfermedades Metabólicas, Centro Médico Nacional Siglo XXI, Instituto Mexicano del Seguro Social, Mexico City 06720, Mexico.
Diabetes Mellitus Type 1 (DM1) is an autoimmune disease characterized by the destruction of beta cells in the pancreas. Although amyloid formation has been well-studied in Diabetes Mellitus Type 2 (DM2), its role in DM1 remains unclear. Understanding how islet amyloid polypeptide (IAPP) contributes to beta cell dysfunction and death in DM1 could provide critical insights into disease mechanisms and pave the way for novel diagnostic and therapeutic strategies.
View Article and Find Full Text PDFBiomolecules
December 2024
Section of Cell Biology and Biophysics, Department of Biology, School of Sciences, National and Kapodistrian University of Athens, Panepistimiopolis, 157 01 Athens, Greece.
Alzheimer's disease (AD) is a complex neurodegenerative disorder characterized by extracellular amyloid plaques, predominantly consisting of amyloid- (A) peptides. The oligomeric form of A is acknowledged as the most neurotoxic, propelling the pathological progression of AD. Interestingly, besides A, other proteins are co-localized within amyloid plaques.
View Article and Find Full Text PDFDiseases
January 2025
Departamento de Medicina, Facultad de Ciencias de la Salud, Universidad de Oviedo, ES-33006 Oviedo, Spain.
Background/objective: Neurotoxic soluble amyloid-β (Aβ) oligomers are key drivers of Alzheimer's pathology, with evidence suggesting that early targeting of these soluble forms may slow disease progression. Traditional intravenous (IV) monoclonal antibodies (mAbs) face challenges, including limited brain penetration and risks such as amyloid-related imaging abnormalities (ARIA). This hypothetical study aimed to model amyloid dynamics in early-to-moderate Alzheimer's disease (AD) and compare the efficacy of IV mAn with intrathecal pseudodelivery, a novel method that confines mAbs in a subcutaneous reservoir for selective amyloid clearance in cerebrospinal fluid (CSF) without systemic exposure.
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