Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases

Rolf Antonie Loch, Hongzhi Wang, Alex Perálvarez-Marín, Philipp Berger, Henrietta Nielsen, Angeliki Chroni, Jinghui Luo*

*Corresponding author for this work

Research output: Contribution to journalReview articleResearchpeer-review

7 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1189-1204
Number of pages16
JournalComputational and Structural Biotechnology Journal
Volume21
DOIs
Publication statusPublished - Jan 2023

Keywords

  • Amyloid proteins
  • ApoE
  • Cytotoxicity
  • Endogenous molecules
  • Interaction
  • Therapeutics

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