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Impairment of Glucose and Glutamate Transport and Induction of Mitochondrial Oxidative Stress and Dysfunction in Synaptosomes by Amyloid β‐Peptide: Role of the Lipid Peroxidation Product 4‐Hydroxynonenal
Abstract
Deposits of amyloid beta-peptide (A beta), reduced glucose uptake into brain cells, oxidative damage to cellular proteins and lipids, and excitotoxic mechanisms have all been suggested to play roles in the neurodegenerative process in Alzheimer's disease. Synapse loss is closely correlated with cognitive impairments in Alzheimer's disease, suggesting that the synapse may be the site at which degenerative mechanisms are initiated and propagated. We report that A beta causes oxyradical-mediated impairment of glucose transport, glutamate transport, and mitochondrial function in rat neocortical synaptosomes. A beta induced membrane lipid peroxidation in synaptosomes that occurred within 1 h of exposure; significant decreases in glucose transport occurred within 1 h of exposure to A beta and decreased further with time. The lipid peroxidation product 4-hydroxynonenal conjugated to synaptosomal proteins and impaired glucose transport; several antioxidants prevented A beta-induced impairment of glucose transport, indicating that lipid peroxidation was causally linked to this adverse action of A beta. FeSO4 (an initiator of lipid peroxidation), A beta, and 4-hydroxynonenal each induced accumulation of mitochondrial reactive oxygen species, caused concentration-dependent decreases in 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide reduction, and reduced cellular ATP levels significantly. A beta also impaired glutamate transport, an effect blocked by antioxidants. These data suggest that A beta induces membrane lipid peroxidation, which results in impairment of the function of membrane glucose and glutamate transporters, altered mitochondrial function, and a deficit in ATP levels; 4-hydroxynonenal appears to be a mediator of these actions of A beta. These data suggest that oxidative stress occurring at synapses may contribute to the reduced glucose uptake and synaptic degeneration that occurs in Alzheimer's disease patients. They further suggest a sequence of events whereby oxidative stress promotes excitotoxic synaptic degeneration and neuronal cell death in a variety of different neurodegenerative disorders.
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“A variety of in vitro investigations have revealed that mitochondria have reduced membrane potential, increased permeability, increased ROS production, altered trafficking, and aberrant fission/fusion regulation when exposed to A (Keller et al., 1997;Mattson et al., 1998; Abramov et al., 2004;Lustbader et al., 2004;Manczak et al., 2006;Wang et al., 2008;Reddy, 2009;Calkins et al., 2011;Manczak et”
From Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model (2013) · cites this paper as Keller et al., 1997
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“Of interest is the fact that glucose consumption is inhibited at later time points, which could be explained by different mechanisms: it could be caused (a) by the loss of glucose transport systems, such as an inactivation of glucose transporters (Keller et al., 1997), (b) by an inactivation of pyruvate dehydrogenase…”
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“Some of these actions of Aβ are likely to be at least partly mediated by promoting oxidative stress and pro-inflammatory mechanisms (Keller et al. 1997; Bezzi et al. 2001; Vezzani and Viviani 2015).”
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“Additionally, synaptic terminals exposed to Aβ aggregates displayed mitochondrial dysfunction, higher levels of oxidative stress, and impaired glutamate and glucose transport [159].”
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Metadata
- Authors
- Keller, J. N., Pang, Z., Geddes, J. W., Begley, J. G., Germeyer, A., Waeg, G., & Mattson, M. P.
- Affiliations
- University of Kentucky (US)
- University of Graz (AT)
- Corresponding author
- Mattson, Mark P.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1997-07
- Volume
- 69
- Issue
- 1
- Pages
- 273-284
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2069303994
- Cited by
- 439
- References
- 0
- Citations by year
- 2025: 3 · 2024: 8 · 2023: 11 · 2022: 8 · 2021: 8 · 2020: 9 · 2019: 10 · 2018: 14 · 2017: 4 · 2016: 20 · 2015: 10 · 2014: 8 · 2013: 12 · 2012: 15
- FWCI
- 19.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns030583-04)
- National Institute on Aging (P50AG005144, AG-05144, P01AG010836, AG 10836)
- National Institute of Neurological Disorders and Stroke (NS30583)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- amyloid-beta, Alzheimer's disease, 4-hydroxynonenal, lipid peroxidation, glucose transport, glutamate uptake, mitochondrial dysfunction, oxidative stress, synaptosomes, reactive oxygen species, ATP depletion, synaptic degeneration, excitotoxicity, antioxidants, neurodegeneration
- MeSH terms
- Aldehydes, Animals, Biological Transport, Cell Membrane, Cross-Linking Reagents, Energy Metabolism, Female, Glucose, Mitochondria, Synapses, Synaptosomes, Lipid Peroxidation, Amyloid beta-Peptides, Rats, Sprague-Dawley, Reactive Oxygen Species, Oxidative Stress, Glutamic Acid, Rats
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