Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 46, Issue 8, Pages 1042-1048Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2008.12.024
Keywords
Heat shock; Mitochondria; Oxidative stress; Proteolysis; Serum starvation; Free radicals
Funding
- NIH/NIEHS [ES 03598]
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The targeted removal of damaged proteins by proteolysis is crucial for cell survival. We have shown previously that the Lon protease selectively degrades oxidized mitochondrial proteins, thus preventing their aggregation and cross-linking. We now show that the Lon protease is a stress-responsive protein that is induced by multiple stressors, including heat shock, serum starvation, and oxidative stress. Lon induction, by pretreatment with low-level stress, protects against oxidative protein damage, diminished mitochondrial function, and loss of cell proliferation induced by toxic levels of hydrogen peroxide. Blocking Lon induction with Lon siRNA also blocks this induced protection. We propose that Lon is a generalized stress-protective enzyme whose decline may contribute to the increased levels of protein damage and mitochondrial dysfunction observed in aging and age-related diseases. (C) 2009 Elsevier Inc. All rights reserved.
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