Oligomeropathies, inflammation and prion protein binding

Bibliographic Details
Title: Oligomeropathies, inflammation and prion protein binding
Authors: Gianluigi Forloni, Pietro La Vitola, Claudia Balducci
Source: Frontiers in Neuroscience, Vol 16 (2022)
Publisher Information: Frontiers Media S.A., 2022.
Publication Year: 2022
Collection: LCC:Neurosciences. Biological psychiatry. Neuropsychiatry
Subject Terms: Alzheimer, Parkinson, amyloid, neurotoxicity, gliosis, oligomers, Neurosciences. Biological psychiatry. Neuropsychiatry, RC321-571
More Details: The central role of oligomers, small soluble aggregates of misfolded proteins, in the pathogenesis of neurodegenerative disorders is recognized in numerous experimental conditions and is compatible with clinical evidence. To underline this concept, some years ago we coined the term oligomeropathies to define the common mechanism of action of protein misfolding diseases like Alzheimer, Parkinson or prion diseases. Using simple experimental conditions, with direct application of synthetic β amyloid or α-synuclein oligomers intraventricularly at micromolar concentrations, we could detect differences and similarities in the biological consequences. The two oligomer species affected cognitive behavior, neuronal dysfunction and cerebral inflammatory reactions with distinct mechanisms. In these experimental conditions the proposed mediatory role of cellular prion protein in oligomer activities was not confirmed. Together with oligomers, inflammation at different levels can be important early in neurodegenerative disorders; both β amyloid and α-synuclein oligomers induce inflammation and its control strongly affects neuronal dysfunction. This review summarizes our studies with β-amyloid or α-synuclein oligomers, also considering the potential curative role of doxycycline, a well-known antibiotic with anti-amyloidogenic and anti-inflammatory activities. These actions are analyzed in terms of the therapeutic prospects.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1662-453X
Relation: https://www.frontiersin.org/articles/10.3389/fnins.2022.822420/full; https://doaj.org/toc/1662-453X
DOI: 10.3389/fnins.2022.822420
Access URL: https://doaj.org/article/21789499a9f348e1b5fdcd0c0215957a
Accession Number: edsdoj.21789499a9f348e1b5fdcd0c0215957a
Database: Directory of Open Access Journals
More Details
ISSN:1662453X
DOI:10.3389/fnins.2022.822420
Published in:Frontiers in Neuroscience
Language:English