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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

DOI

10.1016/s0300-483x(99)00203-6

Type

Journal article

Journal

Toxicology

Publication Date

04/2000

Volume

144

Pages

163 - 168

Addresses

Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77, Stockholm, Sweden.

Keywords

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