Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
Open accessAbstract
We compared Lon protease expression in murine skeletal muscle of young and old, wild‐type and Sod2 −/+ heterozygous mice, and studied Lon involvement in the accumulation of damaged (oxidized) proteins. Lon protease protein levels were lower in old and oxidatively challenged animals, and this Lon deficiency was associated with increased levels of carbonylated proteins. We identified one of these proteins as aconitase, and another as an aconitase fragmentation product, which we can also generate in vitro by treating purified aconitase with H 2 O 2. These results imply that aging and oxidative stress down‐regulate Lon protease expression which, in turn, may be responsible for the accumulation of damaged proteins, such as aconitase, within mitochondria.
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Aging is associated with impaired activity of the proteasome and mitochondrial Lon proteases and reduced capacity for macromolecule repair.
“aging is associated with impaired activity of the proteasome and mitochondrial Lon proteases [203,204,205] and reduced capacity for macromolecule repair [201,202].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [203]
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References 24 · Cited by 233
- Authors
- Bota, D. A., Van Remmen, H., & Davies, K. J. A.
- Affiliations
- University of Southern California (US)
- Corresponding author
- Davies, Kelvin J.A
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2002-11-07
- Volume
- 532
- Issue
- 1-2
- Pages
- 103-106
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2043603162
- Cited by
- 233
- References
- 24
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 6 · 2023: 3 · 2022: 7 · 2021: 4 · 2020: 7 · 2019: 6 · 2018: 12 · 2017: 13 · 2016: 12 · 2015: 10 · 2014: 15 · 2013: 13 · 2012: 12
- FWCI
- 3.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- National Institutes of Health (ES-03598)
- University of California, San Francisco
- National Institute on Aging (R01AG016256, AG16256)
- National Institute of Environmental Health Sciences (ES03598)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- Lon protease, aconitase, aging, oxidative stress, protein oxidation, protein carbonyls, mitochondrial protein turnover, skeletal muscle, manganese superoxide dismutase, hydrogen peroxide, protein degradation
- MeSH terms
- Superoxide Dismutase 2, Aconitate Hydratase, Aging, Aldehydes, Animals, Heat-Shock Proteins, Mitochondria, Serine Endopeptidases, Superoxide Dismutase, Down-Regulation, Mice, Knockout, Oxidative Stress, Muscle, Skeletal, ATP-Dependent Proteases, Mice
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