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Mitochondrial type II hydroxyacyl-CoA dehydrogenase (ERAB) has recently been shown to mediate amyloid-beta peptide (Abeta) induced apoptosis and neurodegeneration. The precise mechanism of cell death induction is unknown, however, Abeta inhibits ERAB activities and as a result of ERAB-Abeta interactions, enhanced formation of lipid peroxidation products occur. The possibility that ERAB mediates quinone reduction is therefore investigated, thus giving the potential of redoxcycling and production of reactive oxygen species, leading to lipid peroxidation. Recombinant human ERAB was produced in a bacterial expression system and enzymological properties were evaluated. Using several orthoquinones as substrates, no ERAB mediated quinone reductase activity was found either in the presence or absence of Abeta, suggesting that the observed in vivo lipid peroxidation is a result of other mechanisms than redoxcycling by quinones.

Original publication




Journal article



Publication Date





163 - 168


3-Hydroxyacyl CoA Dehydrogenases, Acyl Coenzyme A, Amyloid beta-Peptides, Carrier Proteins, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Humans, Kinetics, Lipid Peroxidation, NAD(P)H Dehydrogenase (Quinone), Oxidation-Reduction, Oxidative Stress, Reactive Oxygen Species, Substrate Specificity, Xenobiotics