The role of oxygen in chemical modification and cross-linking of rat tail collagen by glucose was studied at physiological pH and temperature in vitro. Cross-linking of collagen under air depended on glucose concentration, but was inhibited under antioxidative conditions (nitrogen atmosphere with transition metal chelators). The cross-linking reaction under air depended on phosphate buffer concentration, but this effect was eliminated by addition of chelators, identifying trace metal ions in the buffer as catalysts of oxidative cross-linking reaction. Antioxidative conditions had no effect on glycation, that is, formation of fructose lysine, but inhibited formation of the glycoxidation products Ne-(carboxymethyl)lysine and pentosidine as well as the development of fluorescence in glycated collagen. Glycation itself decreased during continued incubation of the collagen without glucose; however, cross-linking and concentrations of glycoxidation products and fluorescence in collagen were not reversible under either oxidative or antioxidative conditions. These observations are consistent with recent studies in vivo on the reversibility of collagen glycation, the irreversibility of formation of glycoxidation products and fluorescence, and the strong correlations between glycoxidation products and fluorescence in collagen (1). These results indicate that oxidation reactions play a critical role in the extended chemical modification and cross-linking of collagen by glucose and suggest that measurement of glycoxidation products should be useful for assessing cumulative chemical modification of collagen by glucose in vivo.
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October 01 1992
Role of Oxygen in Cross-Linking and Chemical Modification of Collagen by Glucose
Min-Xin Fu;
Min-Xin Fu
Department of Chemistry and Biochemistry, and School of Medicine, University of South Carolina
Columbia, South Carolina
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Kevin J Knecht;
Kevin J Knecht
Department of Chemistry and Biochemistry, and School of Medicine, University of South Carolina
Columbia, South Carolina
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Suzanne R Thorpe;
Suzanne R Thorpe
Department of Chemistry and Biochemistry, and School of Medicine, University of South Carolina
Columbia, South Carolina
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John W Baynes
John W Baynes
Department of Chemistry and Biochemistry, and School of Medicine, University of South Carolina
Columbia, South Carolina
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Address correspondence and reprint requests to John W. Baynes, Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208
Diabetes 1992;41(Supplement_2):42–48
Article history
Received:
April 03 1992
Accepted:
May 12 1992
PubMed:
1526335
Citation
Min-Xin Fu, Kevin J Knecht, Suzanne R Thorpe, John W Baynes; Role of Oxygen in Cross-Linking and Chemical Modification of Collagen by Glucose. Diabetes 1 October 1992; 41 (Supplement_2): 42–48. https://doi.org/10.2337/diab.41.2.S42
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