Lack of quinone reductase activity suggests that amyloid-β peptide/ERAB induced lipid peroxidation is not directly related to production of reactive oxygen species by redoxcycling

Mitochondrial type II hydroxyacyl-CoA dehydrogenase (ERAB) has recently been shown to mediate amyloid-β peptide (Aβ) induced apoptosis and neurodegeneration. The precise mechanism of cell death induction is unknown, however, Aβ inhibits ERAB activities and as a result of ERAB-Aβ interactions, enhanc...

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Bibliographic Details
Published in:Toxicology (Amsterdam) 2000-04, Vol.144 (1), p.163-168
Main Authors: Salim, Samina, Filling, Charlotta, Mårtensson, Eva, Oppermann, Udo C.T
Format: Article
Language:English
Subjects:
3-Hydroxyacyl CoA Dehydrogenases
Acyl Coenzyme A - metabolism
Alzheimer's disease
Amyloid beta-Peptides - metabolism
amyloid-^b peptide
Amyloid-β peptide
Apoptosis
Biological and medical sciences
Carrier Proteins - metabolism
Cell metabolism, cell oxidation
Cell physiology
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
ERAB
Fundamental and applied biological sciences. Psychology
Humans
Kinetics
Lipid Peroxidation - physiology
Molecular and cellular biology
NAD(P)H Dehydrogenase (Quinone) - metabolism
Oxidation-Reduction
Oxidative Stress - physiology
quinone reductase
Reactive Oxygen Species - metabolism
Short-chain dehydrogenases/reductases (SDR)
Substrate Specificity
Xenobiotics - metabolism
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Summary:Mitochondrial type II hydroxyacyl-CoA dehydrogenase (ERAB) has recently been shown to mediate amyloid-β peptide (Aβ) induced apoptosis and neurodegeneration. The precise mechanism of cell death induction is unknown, however, Aβ inhibits ERAB activities and as a result of ERAB-Aβ 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 Aβ, suggesting that the observed in vivo lipid peroxidation is a result of other mechanisms than redoxcycling by quinones.
ISSN:0300-483X
1879-3185
DOI:10.1016/S0300-483X(99)00203-6