Oxidative damage to collagen

  • J. C. Monboisse
  • J. P. Borel
Part of the EXS book series (EXS, volume 62)


Extracellular matrix molecules, such as collagens, are good targets for oxygen free radicals. Collagen is the only protein susceptible to fragmentation by superoxide anion as demonstrated by the liberation of small 4-hydroxyproline-containing-peptides. It seems likely that hydroxyl radicals in the presence of oxygen cleave collagen into small peptides, and the cleavage seems to be specific to proline or 4-hydroxyproline residues. Hydroxyl radicals in the absence of oxygen or hypochlorous acid do not induce fragmentation of collagen molecules, but they trigger a polymerization of collagen through the formation of new cross-links such as dityrosine or disulfure bridges. Morever, these cross-links can not explain the totality of high molecular weight components generated under these experimental conditions, and the nature of new cross-links induced by hydroxyl radicals or hypochlorous acid remains unclear.


Oxygen Free Radical Collagen Molecule Collagen Degradation Hypochlorous Acid Sodium Formate 
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  1. Bailey, A. J., Rhodes, D. N., and Cater, C. W. (1964) Irradiation-induced crosslinking of collagen. Radiation Res. 22: 606–621.PubMedCrossRefGoogle Scholar
  2. Boguta, G., and Dancewicz, A. M. (1983) Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen. Int. J. Radiat. Biol. 43: 249–265.CrossRefGoogle Scholar
  3. Borel, J. P. (1991) Les collagènes. L,Eurobiologiste 15: 247–271.Google Scholar
  4. Davies, K. J. A. (1987) Protein damage and degradation by oxygen radicals. I-General aspects. J. Biol. Chem. 262: 9895–9901.Google Scholar
  5. Davies, K. J. A., Lin, S. W., and Pacifici, R. E. (1987) Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. J. Biol. Chem. 262: 9914–9920.PubMedGoogle Scholar
  6. Dean, R. T., Wolff, S. P., and McElligott, M. A. (1989) Histidine and proline are important sites for free radical damage to proteins. Free Rad. Res. Commun. 7: 97–103.CrossRefGoogle Scholar
  7. Fligiel, S. E. G., Lee, E. C., McCoy, J. P., Johnson, K. J., and Varani, J. (1984) Protein degradation following treatment with hydrogen peroxide. Am. J. Pathol. 115: 418–425.PubMedGoogle Scholar
  8. Fujimori, E. (1988) Cross-linking of collagen CNBr peptides by ozone and UV light. FEBS Lett. 235: 98–102.PubMedCrossRefGoogle Scholar
  9. Gillery, P., Monboisse, J. C., Maquart, F. X., and Borel, J. P. (1988) Glycation of proteins as a source of superoxide. Diab. Metab. 14: 25–30.Google Scholar
  10. Girotti, A. W., Thomas, J. P., and Jordan, J. E. (1986) Xanthine-oxidase-catalyzed crosslinking of cell membranes proteins. Archs. Biochem. Biophys. 251: 639–653.CrossRefGoogle Scholar
  11. Greenwald, R. A., and Moy, W. W. (1979) Inhibition of collagen gelation by action of the superoxide radical. Arth. Rheum. 22: 251–259.CrossRefGoogle Scholar
  12. Halliwell, B. (1987) Oxidants and human disease: some new concepts. FASEB J. 1: 358–364.PubMedGoogle Scholar
  13. Monboisse, J. C. (1989) Contribution à l’étude des interactions entre collagène et radicaux libres oxygénés. Thesis Univ. Reims.Google Scholar
  14. Monboisse, J. C., Bellon, G., Dufer, J., Randoux, A., and Borel, J. P. (1987) Collagen activates superoxide anion production by human polymorphonuclear neutrophils. Biochem. J. 246: 599–603.PubMedGoogle Scholar
  15. Monboisse, J. C., Bellon, G., Randoux, A., Dufer, J., and Borel, J. P. (1990) Activation of human neutrophils by type I collagen. Requirement of two different sequences. Biochem. J. 270: 459–462.Google Scholar
  16. Monboisse, J. C., Braquet, P., Randoux, A., and Borel, J. P. (1983) Non enzymatic degradation of acid soluble collagen by superoxide anion: protective effect of fiavonoids. Biochem. Pharmacol. 32: 53–58.PubMedCrossRefGoogle Scholar
  17. Monboisse, J. C., Gardés-Albert, M., Randoux, A., Borel, J. P., and Ferrandini, C. (1988) Collagen degradation by superoxide anion in pulse and gamma radiolysis. Biochim. Biophys. Acta, 965: 29–35.PubMedCrossRefGoogle Scholar
  18. Monboisse, J. C., Garnotel, R., Randoux, A., Dufer, J., and Borel, J. P. (1991) Adhesion of human neutrophils to and activation by type I collagen involving a integrin. J. Leukoc. Biol. 50: 373–380.PubMedGoogle Scholar
  19. Monboisse, J. C., Poulin, G., Braquet, P., Randoux, A., Ferradini, C., and Borel, J. P. (1984) Effects of oxy radicals on several types of collagen. Int. J. Tissue React. 6: 385–390.PubMedGoogle Scholar
  20. Morel, F., Doussiére, J., and Vignais, P. (1991) The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects. Eur. J. Biochem. 201: 523–546.PubMedCrossRefGoogle Scholar
  21. Schuessler, H., and Schilling, K. (1984) Oxygen effect in the radiolysis of proteins - Part 2 - Bovine serum albumin. Int. J. Radiat. Biol. 45: 267–281.CrossRefGoogle Scholar
  22. Van der Rest, M., and Garrone, R. (1990) Collagens as multidomain proteins. Biochimie 72: 473–484.PubMedCrossRefGoogle Scholar
  23. Vissers, M. C. M., and Winterbourn, C. C. (1991) Oxidative damage to fibronectin — I — The effects of the neutrophil myeloperoxidase system and HOCl. Archs. Biochem. Biophys. 285: 53–59.CrossRefGoogle Scholar
  24. Wolff, S. P., and Dean, R. T. (1986) Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis. Biochem. J. 234: 399–403.PubMedGoogle Scholar
  25. Wolff, S. P., and Dean, R. T. (1987) Glucose autoxidation and protein modification. The potenteial role of “autoxidative glycosylation” in diabetes. Biochem. J. 245: 243–250.PubMedGoogle Scholar
  26. Wolff, S. P., Garner, A., and Dean, R. T. (1986) Free radicals, lipids and protein degradation. TIBS 11: 27–31.Google Scholar

Copyright information

© Birkhäuser Verlag Basel/Switzerland 1992

Authors and Affiliations

  • J. C. Monboisse
    • 1
  • J. P. Borel
    • 1
  1. 1.Lab. Biochemistry, CNRS URA 610, UFR MedicineUniv. Reims Champagne-ArdenneReims CedexFrance

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