Abstract
Amyloid formation is a pathological process associated with a wide range of degenerative disorders, including Alzheimer’s disease, Parkinson’s disease, and diabetes mellitus type 2. During disease progression, abnormal accumulation and deposition of proteinaceous material are accompanied by tissue degradation, inflammation, and dysfunction. Agents that can interfere with the process of amyloid formation or target already formed amyloid assemblies are consequently of therapeutic interest. In this context, a few endogenous proteins have been associated with an anti-amyloidogenic activity. Here, we review the properties of transthyretin, apolipoprotein E, clusterin, and BRICHOS protein domain which all effectively interfere with amyloid in vitro, as well as displaying a clinical impact in humans or animal models. Their involvement in the amyloid formation process is discussed, which may aid and inspire new strategies for therapeutic interventions.
Highlights
Amyloidosis refers to a variety of increasingly common human diseases, includingAlzheimer’s disease (AD), Parkinson’s disease (PD), and diabetes mellitus type 2 (T2D).Amyloids are composed of insoluble proteinaceous material with a β-sheet rich fibrillar morphology that can reach several microns in length and are typically between 5–10 nm in diameter
We summarize the information accumulated in the literature regarding some of these proteins, which have been intensively studied in recent years, namely, TTR [33–37], Apolipoprotein E (ApoE) [31,38–42], clusterin
ApoE has been found co-localized with amyloid-β peptide (Aβ)-amyloid plaques with relative prevalence of ApoE4 > ApoE3 > ApoE2 [109,110]. These results suggested that ApoE might play a specific role in Aβ amyloid formation and related AD pathology, which has been explored in numerous studies [39–42,110–117]
Summary
Amyloidosis refers to a variety of increasingly common human diseases, including. Alzheimer’s disease (AD), Parkinson’s disease (PD), and diabetes mellitus type 2 (T2D). The rapid serve as sites that catalyze the formation of new nuclei and further enhance the rate process of elongation is followed by a saturation phase where the reaction reaches a steady of the reaction This mechanism is called surface-catalyzed secondary nucleation (SCSN). In the case of the some tissue damages different forms, associated pathological amyloids, such vary as Aβbetween [7],amyloid and IAPP [8] thethe surface of mature fibrils can effects are often linked to cytotoxic properties of amyloid structures. This has been observed serve as sites that catalyze the formation of new nuclei and further enhance the rate of both reaction. We will give an overview of their physiological function, their role in pathology with a special focus on the amyloid formation process, and possible mechanisms of intervention
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