Journal
REDOX BIOLOGY
Volume 1, Issue 1, Pages 258-264Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.redox.2013.01.015
Keywords
Adaptation; Hormesis; Lon Protease; Protein degradation and oxidation; Mitochondria; Oxidative stress
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Funding
- NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [R01ES003598] Funding Source: NIH RePORTER
- NIEHS NIH HHS [R01 ES003598] Funding Source: Medline
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The elimination of oxidatively modified proteins is a crucial process in maintaining cellular homeostasis, especially during stress. Mitochondria are protein-dense, high traffic compartments, whose polypeptides are constantly exposed to superoxide, hydrogen peroxide, and other reactive species, generated by 'electron leakage' from the respiratory chain. The level of oxidative stress to mitochondrial proteins is not constant, but instead varies greatly with numerous metabolic and environmental factors. Oxidized mitochonclrial proteins must be removed rapidly (by proteolytic degradation) or they will aggregate, cross-link, and cause toxicity. The Lon Protease is a key enzyme in the degradation of oxidized proteins within the mitochondrial matrix. Under conditions of acute stress Lon is highly inducible, possibly with the oxidant acting as the signal inducer, thereby providing increased protection. It seems that under chronic stress conditions, however, Lon levels actually decline. Lon levels also decline with age and with senescence, and senescent cells even lose the ability to induce Lon during acute stress. We propose that the regulation of Lon is biphasic, in that it is upregulated during transient stress and down-regulated during chronic stress and aging, and we suggest that the loss of Lon responsiveness may be a significant factor in aging, and in age related diseases. (C) 2013 The Authors. Published by Elsevier B.V. Open access under CC BY-NC-ND license.
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