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Am J Physiol Regul Integr Comp Physiol 274: R453-R461, 1998;
0363-6119/98 $5.00
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Vol. 274, Issue 2, R453-R461, February 1998

Markers of protein oxidation by hydroxyl radical and reactive nitrogen species in tissues of aging rats

Christiaan Leeuwenburgh1, Polly Hansen1, Aviv Shaish1, John O. Holloszy1, and Jay W. Heinecke1,2

Departments of 1 Internal Medicine and 2 Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110

Many lines of evidence implicate oxidative damage in aging. Possible pathways include reactions that modify aromatic amino acid residues on proteins. o-Tyrosine is a stable marker for oxidation of protein-bound phenylalanine by hydroxyl radical, whereas 3-nitrotyrosine is a marker for oxidation of protein-bound tyrosine by reactive nitrogen species. To test the hypothesis that proteins damaged by hydroxyl radical and reactive nitrogen accumulate with aging, we used isotope dilution gas chromatography-mass spectrometry to measure levels of o-tyrosine and 3-nitrotyrosine in heart, skeletal muscle, and liver from young adult (9 mo) and old (24 mo) female Long-Evans/Wistar hybrid rats. We also measured these markers in young adult and old rats that received antioxidant supplements (alpha -tocopherol, beta -carotene, butylated hydroxytoluene, and ascorbic acid) from the age of 5 mo. We found that aging did not significantly increase levels of protein-bound o-tyrosine or 3-nitrotyrosine in any of the tissues. Antioxidant supplementation had no effect on the levels of protein-bound o-tyrosine and 3-nitrotyrosine in either young or old animals. These observations indicate that the o-tyrosine and 3-nitrotyrosine do not increase significantly in heart, skeletal muscle, and liver in old rats, suggesting that proteins damaged by hydroxyl radical and reactive nitrogen species do not accumulate in these tissues with advancing age.

nitric oxide; peroxynitrite; alpha -tocopherol; beta -carotene; ascorbic acid; oxidative stress


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