Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases
Three common Apolipoprotein E isoforms, ApoE2, ApoE3, and ApoE4, are key regulators of lipid homeostasis, among other functions. Apolipoprotein E can interact with amyloid proteins. The isoforms differ by one or two residues at positions 112 and 158, and possess distinct structural conformations and...
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Format: | Article |
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Elsevier
2023-01-01
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Series: | Computational and Structural Biotechnology Journal |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037023000223 |
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author | Rolf Antonie Loch Hongzhi Wang Alex Perálvarez-Marín Philipp Berger Henrietta Nielsen Angeliki Chroni Jinghui Luo |
author_facet | Rolf Antonie Loch Hongzhi Wang Alex Perálvarez-Marín Philipp Berger Henrietta Nielsen Angeliki Chroni Jinghui Luo |
author_sort | Rolf Antonie Loch |
collection | DOAJ |
description | Three common Apolipoprotein E isoforms, ApoE2, ApoE3, and ApoE4, are key regulators of lipid homeostasis, among other functions. Apolipoprotein E can interact with amyloid proteins. The isoforms differ by one or two residues at positions 112 and 158, and possess distinct structural conformations and functions, leading to isoform-specific roles in amyloid-based neurodegenerative diseases. Over 30 different amyloid proteins have been found to share similar characteristics of structure and toxicity, suggesting a common interactome. The molecular and genetic interactions of ApoE with amyloid proteins have been extensively studied in neurodegenerative diseases, but have not yet been well connected and clarified. Here we summarize essential features of the interactions between ApoE and different amyloid proteins, identify gaps in the understanding of the interactome and propose the general interaction mechanism between ApoE isoforms and amyloid proteins. Perhaps more importantly, this review outlines what we can learn from the interactome of ApoE and amyloid proteins; that is the need to see both ApoE and amyloid proteins as a basis to understand neurodegenerative diseases. |
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format | Article |
id | doaj.art-b5df8e5a0b18462d977ed1bb7964472b |
institution | Directory Open Access Journal |
issn | 2001-0370 |
language | English |
last_indexed | 2024-03-08T21:31:32Z |
publishDate | 2023-01-01 |
publisher | Elsevier |
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series | Computational and Structural Biotechnology Journal |
spelling | doaj.art-b5df8e5a0b18462d977ed1bb7964472b2023-12-21T07:30:48ZengElsevierComputational and Structural Biotechnology Journal2001-03702023-01-012111891204Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseasesRolf Antonie Loch0Hongzhi Wang1Alex Perálvarez-Marín2Philipp Berger3Henrietta Nielsen4Angeliki Chroni5Jinghui Luo6Department of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, SwitzerlandDepartment of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, SwitzerlandBiophysics Unit, Department of Biochemistry and Molecular Biology, School of Medicine, Institut de Neurociències, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallés, Catalonia, SpainDepartment of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, SwitzerlandDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius Väg 16B, 10691 Stockholm, SwedenInstitute of Biosciences and Applications, National Center for Scientific Research 'Demokritos', 15341 Athens, GreeceDepartment of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, Switzerland; Corresponding author.Three common Apolipoprotein E isoforms, ApoE2, ApoE3, and ApoE4, are key regulators of lipid homeostasis, among other functions. Apolipoprotein E can interact with amyloid proteins. The isoforms differ by one or two residues at positions 112 and 158, and possess distinct structural conformations and functions, leading to isoform-specific roles in amyloid-based neurodegenerative diseases. Over 30 different amyloid proteins have been found to share similar characteristics of structure and toxicity, suggesting a common interactome. The molecular and genetic interactions of ApoE with amyloid proteins have been extensively studied in neurodegenerative diseases, but have not yet been well connected and clarified. Here we summarize essential features of the interactions between ApoE and different amyloid proteins, identify gaps in the understanding of the interactome and propose the general interaction mechanism between ApoE isoforms and amyloid proteins. Perhaps more importantly, this review outlines what we can learn from the interactome of ApoE and amyloid proteins; that is the need to see both ApoE and amyloid proteins as a basis to understand neurodegenerative diseases.http://www.sciencedirect.com/science/article/pii/S2001037023000223ApoEAmyloid proteinsInteractionEndogenous moleculesCytotoxicityTherapeutics |
spellingShingle | Rolf Antonie Loch Hongzhi Wang Alex Perálvarez-Marín Philipp Berger Henrietta Nielsen Angeliki Chroni Jinghui Luo Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases Computational and Structural Biotechnology Journal ApoE Amyloid proteins Interaction Endogenous molecules Cytotoxicity Therapeutics |
title | Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases |
title_full | Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases |
title_fullStr | Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases |
title_full_unstemmed | Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases |
title_short | Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases |
title_sort | cross interactions between apolipoprotein e and amyloid proteins in neurodegenerative diseases |
topic | ApoE Amyloid proteins Interaction Endogenous molecules Cytotoxicity Therapeutics |
url | http://www.sciencedirect.com/science/article/pii/S2001037023000223 |
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