Journal
BIOCHEMICAL JOURNAL
Volume 426, Issue -, Pages 255-270Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20091941
Keywords
Alzheimer's disease; amyloid-binding alcohol dehydrogenase (ABAD); cyclophilin D (CypD); intracellular amyloid-beta peptide (A beta); mitochondrial dysfunction; mitochondrial permeability transition pore
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Funding
- Alzheimer's Research Trust
- German Academic Exchange Service
- Biotechnology and Biological Sciences Research Council, U.K.
- St Hugh's College, University of Oxford, Oxford. U.K.
- Alzheimers Research UK [ART-PG2009-3, ART-PhD2007-5] Funding Source: researchfish
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The A beta (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 A beta in the disease progression, with particular reference to A beta found within the mitochondria. Once inside the cell, A beta 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 Oil a molecular, cellular and in vivo level.
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