Abstract
The amyloid-ß peptide (Aß) has been associated with Alzheimer's disease (AD) for some time. The original amyloid cascade hypothesis declared that the insoluble extracellular plaques were responsible for main Aß toxicity.
Nowadays, this hypothesis is outdated and soluble intracellular Aß forms and their effects within the cell have come into the centre of attention. There are many intracellular proteins interacting with Aß including the mitochondrial enzyme amyloid-binding alcohol dehydrogenase (ABAD).
The interaction between ABAD and Aß impairs mitochondrial functions and ultimately results in cell death. In this review, current findings concerning the enzyme ABAD are summarized.
Its role in AD development and its interaction with Aß as a potential therapeutic target are discussed.