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Research Article Free access | 10.1172/JCI119599

Age-dependent increase in ortho-tyrosine and methionine sulfoxide in human skin collagen is not accelerated in diabetes. Evidence against a generalized increase in oxidative stress in diabetes.

M C Wells-Knecht, T J Lyons, D R McCance, S R Thorpe, and J W Baynes

Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, USA.

Find articles by Wells-Knecht, M. in: JCI | PubMed | Google Scholar

Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, USA.

Find articles by Lyons, T. in: JCI | PubMed | Google Scholar

Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, USA.

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Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, USA.

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Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, USA.

Find articles by Baynes, J. in: JCI | PubMed | Google Scholar

Published August 15, 1997 - More info

Published in Volume 100, Issue 4 on August 15, 1997
J Clin Invest. 1997;100(4):839–846. https://doi.org/10.1172/JCI119599.
© 1997 The American Society for Clinical Investigation
Published August 15, 1997 - Version history
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Abstract

The glycoxidation products Nepsilon-(carboxymethyl)lysine and pentosidine increase in skin collagen with age and at an accelerated rate in diabetes. Their age-adjusted concentrations in skin collagen are correlated with the severity of diabetic complications. To determine the relative roles of increased glycation and/or oxidation in the accelerated formation of glycoxidation products in diabetes, we measured levels of amino acid oxidation products, distinct from glycoxidative modifications of amino acids, as independent indicators of oxidative stress and damage to collagen in aging and diabetes. We show that ortho-tyrosine and methionine sulfoxide are formed in concert with Nepsilon-(carboxymethyl)lysine and pentosidine during glycoxidation of collagen in vitro, and that they also increase with age in human skin collagen. The age-adjusted levels of these oxidized amino acids in collagen was the same in diabetic and nondiabetic subjects, arguing that diabetes per se does not cause an increase in oxidative stress or damage to extracellular matrix proteins. These results provide evidence for an age-dependent increase in oxidative damage to collagen and support previous conclusions that the increase in glycoxidation products in skin collagen in diabetes can be explained by the increase in glycemia alone, without invoking a generalized, diabetes-dependent increase in oxidative stress.

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