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Free Radical Mediated Oxidation of Proteins

  • Earl R. Stadtman
Chapter
Part of the NATO ASI Series book series (NSSA, volume 296)

Abstract

Living organisms are constantly bombarded with a battery of oxygen free radicals and other forms of reactive oxygen, leading to the modification of proteins. These modifications include: (a) fragmentation of the polypeptide chain, (b) formation of intra- and inter-molecular cross-linkages, direct oxidation of amino acid residue side chains, (c) derivatization of amino groups of lysine by reducing sugars or their oxidation products (glycation), (d) derivatization of lysine, histidine, or cysteine residues by lipid oxidation products (malondialdehyde, 2,3 unsaturated aldehydes), and (e) nitration of tyrosine residues. The generation of carbonyl derivatives (aldehydes, ketones) by some of these reactions may serve as markers of oxidative protein damage in aging and disease. The nitration of tyrosine residues can seriously compromise major mechanisms of enzyme regulation and signal transduction. And the formation of protein-protein cross linkages can lead to the accumulation of protease resistant protein polymers and inhibitors of proteases that degrade the oxidized forms of oxidatively modified proteins.

Keywords

Nitric Oxide Glutamine Synthetase Tyrosine Residue Methionine Residue Carbonyl Derivative 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Earl R. Stadtman
    • 1
  1. 1.Laboratory of Biochemistry National Heart, Lung, and Blood InstituteNational Institutes of HealthBethesdaUSA

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