title: Mitochondrial Abeta: a potential cause of metabolic dysfunction in Alzheimer's disease.
abstract: Deficits in mitochondrial function are a characteristic finding in Alzheimer's disease (AD), though the mechanism remains to be clarified. Recent studies revealed that amyloid beta peptide (Abeta) gains access into mitochondrial matrix, which was much more pronounced in both AD brain and transgenic mutant APP mice than in normal controls. Abeta progressively accumulates in mitochondria and mediates mitochondrial toxicity. Interaction of mitochondrial Abeta with mitochondrial enzymes such as amyloid beta binding alcohol dehydrogenase (ABAD) exaggerates mitochondrial stress by inhibiting the enzyme activity, releasing reactive oxygen species (ROS), and affecting glycolytic, Krebs cycle and/or the respiratory chain pathways through the accumulation of deleterious intermediate metabolites. The pathways proposed may play a key role in the pathogenesis of this devastating neurodegenerative disorder, Alzheimer's disease.
authors.affiliation: Department of Neurology and Veteran Administration Medical Center, School of Medicine, Saint Louis University, St. Louis, Missouri, USA.
authors.forename: Xi
authors.initials: X
authors.lastname: Chen
authors.forename: Shi Du
authors.initials: SD
authors.lastname: Yan
mesh_terms: D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism; D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D004579:Electron Transport / Q000502:physiology; D004734:Energy Metabolism / Q000502:physiology*; D004798:Enzymes / Q000378:metabolism; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*
chemical_list: D016229:Amyloid beta-Peptides; D004798:Enzymes; D015094:3-Hydroxyacyl CoA Dehydrogenases; C108634:HSD17B10 protein, human