The consequences of mitochondrial amyloid beta-peptide in Alzheimer's disease

Kirsty E A Muirhead, Eva Borger, Laura Aitken, Stuart J Conway, Frank J Gunn-Moore

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The Abeta (amyloid-beta peptide) has long been associated with Alzheimer's disease, originally in the form of extracellular plaques. However, in the present paper we review the growing evidence for the role of soluble intracellular Abeta in the disease progression, with particular reference to Abeta found within the mitochondria. Once inside the cell, Abeta is able to interact with a number of targets, including the mitochondrial proteins ABAD (amyloid-binding alcohol dehydrogenase) and CypD (cyclophilin D), which is a component of the mitochondrial permeability transition pore. Interference with the normal functions of these proteins results in disruption of cell homoeostasis and ultimately cell death. The present review explores the possible mechanisms by which cell death occurs, considering the evidence presented on a molecular, cellular and in vivo level.

Original languageEnglish
Pages (from-to)255-70
Number of pages16
JournalBiochemical Journal
Volume426
Issue number3
DOIs
Publication statusPublished - 15 Mar 2010

Keywords / Materials (for Non-textual outputs)

  • 3-Hydroxyacyl CoA Dehydrogenases
  • Alzheimer Disease
  • Amyloid beta-Peptides
  • Apoptosis
  • Cyclophilins
  • Humans
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins
  • Models, Biological
  • Protein Binding

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