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Protein modification by the lipid peroxidation product 4‐hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients
Abstract
We report increased modification of proteins by 4‐hydroxynoneal (HNE), a product of membrane lipid peroxidation, in the lumbar spinal cord of sporadic amyotrophic lateral sclerosis (ALS) patients versus that of neurologically normal controls. By immunohistochemistry, HNE‐protein modification was detected in ventral horn motor neurons, and immunoprecipitation analysis revealed that one of the proteins modified by HNE was the astrocytic glutamate transporter EAAT2. Given that the function of proteins modified by HNE can be severely compromised as previously demonstrated for glutamate transporters in cortical synaptosome preparatations, our findings suggest a scenario in which oxidative stress leads to the production of HNE, impairment of gluatmate transport, and excitotoxic motor neuron degeneration in ALS.
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Cites
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Neurodegenerative diseases and oxidative stress
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Self-citationProtein carbonylation in human diseases
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The SLC1 high-affinity glutamate and neutral amino acid transporter family
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Self-citationOxidative damage and the Nrf2-ARE pathway in neurodegenerative diseases
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Failure of protein quality control in amyotrophic lateral sclerosis
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“In vivo, the major conformational changes of SOD1 in affected tissues reported are oxidation, protein nitration and 4-hydroxy-2-nonenal (HNE) modifications of amino acids [48–51].”
BackgroundNitric Oxide Signaling Is Disrupted in the Yeast Model for Batten Disease
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Metadata
- Authors
- Pedersen, W. A., Fu, W., Keller, J. N., Markesbery, W. R., Appel, S., Smith, R. G., Kasarskis, E., & Mattson, M. P.
- Venue
- Annals of Neurology
- Publisher
- Wiley
- Published
- 1998-11
- Volume
- 44
- Issue
- 5
- Pages
- 819-824
- ISSN
- 0364-5134 (ISSN-L)
- 1531-8249
- OpenAlex
- W1978874104
- Cited by
- 391
- References
- 1
- FWCI
- 14.66
- Type
- journal article
- Language
- en
- Open access
- closed
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