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J. Biol. Chem., Vol. 283, Issue 32, 21837-21841, August 8, 2008

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Minireview

Oxidative Stress and Covalent Modification of Protein with Bioactive Aldehydes^*

From the Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455

The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of ,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes.

^* This work was supported, in whole or in part, by National Institutes of Health Grant AG25371 (to T. J. G.), Grant T32 HL07741 from NHLBI (to P. A. G.), and Grant DK053189 (to D. A. B.). This work was also supported by an award from Eli Lilly and Co. (to T. J. G.) and by the Minnesota Agricultural Experiment Station and the Minnesota Obesity Center (to D. A. B.). This minireview will be reprinted in the 2008 Minireview Compendium, which will be available in January, 2009.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ To whom correspondence should be addressed. E-mail: Bernl001{at}umn.edu.

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