Mitochondrial Lon protease is a human stress protein.
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.
Division of Molecular and Computational Biology, Ethel Percy Andrus Gerontology Center, University of Southern California, Los Angeles, CA 90089-0191, USA.
Jenny K
JK
Ngo
Kelvin J A
KJ
Davies
D000375:Aging / Q000502:physiology; D045744:Cell Line, Tumor; D049109:Cell Proliferation; D002470:Cell Survival / Q000502:physiology; D016895:Culture Media, Serum-Free; D005609:Free Radicals / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature / Q000009:adverse effects; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D008928:Mitochondria / Q000502:physiology*; D018384:Oxidative Stress / Q000502:physiology*; D049070:Protease La / Q000235:genetics / Q000378:metabolism*; D050050:Protein Carbonylation; D034741:RNA, Small Interfering / Q000235:genetics
D016895:Culture Media, Serum-Free; D005609:Free Radicals; D006360:Heat-Shock Proteins; D034741:RNA, Small Interfering; D006861:Hydrogen Peroxide; D049070:Protease La