TY - JOUR
T1 - Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases
AU - Loch, Rolf Antonie
AU - Wang, Hongzhi
AU - Perálvarez-Marín, Alex
AU - Berger, Philipp
AU - Nielsen, Henrietta
AU - Chroni, Angeliki
AU - Luo, Jinghui
N1 - Funding Information:
We acknowledge financial support from the Paul Scherrer Institute , the Swiss National Scientific Foundation ( 310030_197626 to J.L.), the BrightFocus Foundation ( A20201759S to J.L.), and the Spanish Ministry of Science and Innovation and Agencia Estatal de Investigación ( MCIN/AEI/ 10.13039/501100011033 project PID2020-120222GB-I00 to A.P.-M.).
Publisher Copyright:
© 2023 The Authors
PY - 2023/1
Y1 - 2023/1
N2 - 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.
AB - 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.
KW - Amyloid proteins
KW - ApoE
KW - Cytotoxicity
KW - Endogenous molecules
KW - Interaction
KW - Therapeutics
UR - http://www.scopus.com/inward/record.url?scp=85147545182&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/d5795f9c-f63a-3f6a-be99-93bf736f9708/
U2 - 10.1016/j.csbj.2023.01.022
DO - 10.1016/j.csbj.2023.01.022
M3 - Review article
C2 - 36817952
AN - SCOPUS:85147545182
SN - 2001-0370
VL - 21
SP - 1189
EP - 1204
JO - Computational and Structural Biotechnology Journal
JF - Computational and Structural Biotechnology Journal
ER -