Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress

FEBS Letters

Van Remmen, Holly²  Bota, Daniela A¹  Davies, Kelvin J.A¹ 

[1] Ethel Percy Andrus Gerontology Center, and Division of Molecular and Computational Biology, 3715 McClintock Avenue, University of Southern California, Los Angeles, CA 90089-0191, USA;Department of Physiology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA

关键词: Lon protease;    Aconitase;    Protein oxidation;    Mitochondria;    Aging;    Sod2;    MnSOD;    manganese superoxide dismutase;    Sod2;    mitochondrial superoxide dismutase gene;    Sod2 −/+;    heterozygous B6-Sod2;    Sod2 +/+;    wild-type littermate control mice;    SDS;    sodium dodecyl sulfate;    SDC;    sodium deoxycholate;   

DOI  :  10.1016/S0014-5793(02)03638-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 H₂O₂. 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.

【 授权许可】

Unknown