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Endogenous Human Proteins Interfering with Amyloid Formation

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 d...

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Autores principales: Gharibyan, Anna L., Wasana Jayaweera, Sanduni, Lehmann, Manuela, Anan, Intissar, Olofsson, Anders
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8946693/
https://www.ncbi.nlm.nih.gov/pubmed/35327638
http://dx.doi.org/10.3390/biom12030446
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author Gharibyan, Anna L.
Wasana Jayaweera, Sanduni
Lehmann, Manuela
Anan, Intissar
Olofsson, Anders
author_facet Gharibyan, Anna L.
Wasana Jayaweera, Sanduni
Lehmann, Manuela
Anan, Intissar
Olofsson, Anders
author_sort Gharibyan, Anna L.
collection PubMed
description 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.
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spelling pubmed-89466932022-03-25 Endogenous Human Proteins Interfering with Amyloid Formation Gharibyan, Anna L. Wasana Jayaweera, Sanduni Lehmann, Manuela Anan, Intissar Olofsson, Anders Biomolecules Review 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. MDPI 2022-03-14 /pmc/articles/PMC8946693/ /pubmed/35327638 http://dx.doi.org/10.3390/biom12030446 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Gharibyan, Anna L.
Wasana Jayaweera, Sanduni
Lehmann, Manuela
Anan, Intissar
Olofsson, Anders
Endogenous Human Proteins Interfering with Amyloid Formation
title Endogenous Human Proteins Interfering with Amyloid Formation
title_full Endogenous Human Proteins Interfering with Amyloid Formation
title_fullStr Endogenous Human Proteins Interfering with Amyloid Formation
title_full_unstemmed Endogenous Human Proteins Interfering with Amyloid Formation
title_short Endogenous Human Proteins Interfering with Amyloid Formation
title_sort endogenous human proteins interfering with amyloid formation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8946693/
https://www.ncbi.nlm.nih.gov/pubmed/35327638
http://dx.doi.org/10.3390/biom12030446
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