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Oxidative damage to collagen

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Part of the EXS book series (EXS,volume 62)

Summary

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.

Keywords

  • Oxygen Free Radical
  • Collagen Molecule
  • Collagen Degradation
  • Hypochlorous Acid
  • Sodium Formate

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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References

  • Bailey, A. J., Rhodes, D. N., and Cater, C. W. (1964) Irradiation-induced crosslinking of collagen. Radiation Res. 22: 606–621.

    PubMed  CrossRef  CAS  Google Scholar 

  • 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.

    CrossRef  CAS  Google Scholar 

  • Borel, J. P. (1991) Les collagènes. L,Eurobiologiste 15: 247–271.

    Google Scholar 

  • Davies, K. J. A. (1987) Protein damage and degradation by oxygen radicals. I-General aspects. J. Biol. Chem. 262: 9895–9901.

    CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    CrossRef  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Fujimori, E. (1988) Cross-linking of collagen CNBr peptides by ozone and UV light. FEBS Lett. 235: 98–102.

    PubMed  CrossRef  CAS  Google Scholar 

  • 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.

    CAS  Google Scholar 

  • 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.

    CrossRef  CAS  Google Scholar 

  • Greenwald, R. A., and Moy, W. W. (1979) Inhibition of collagen gelation by action of the superoxide radical. Arth. Rheum. 22: 251–259.

    CrossRef  CAS  Google Scholar 

  • Halliwell, B. (1987) Oxidants and human disease: some new concepts. FASEB J. 1: 358–364.

    PubMed  CAS  Google Scholar 

  • Monboisse, J. C. (1989) Contribution à l’étude des interactions entre collagène et radicaux libres oxygénés. Thesis Univ. Reims.

    Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    CAS  Google Scholar 

  • 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.

    PubMed  CrossRef  CAS  Google Scholar 

  • 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.

    PubMed  CrossRef  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CrossRef  CAS  Google Scholar 

  • 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.

    CrossRef  CAS  Google Scholar 

  • Van der Rest, M., and Garrone, R. (1990) Collagens as multidomain proteins. Biochimie 72: 473–484.

    PubMed  CrossRef  Google Scholar 

  • 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.

    CrossRef  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • Wolff, S. P., Garner, A., and Dean, R. T. (1986) Free radicals, lipids and protein degradation. TIBS 11: 27–31.

    CAS  Google Scholar 

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© 1992 Birkhäuser Verlag Basel/Switzerland

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Monboisse, J.C., Borel, J.P. (1992). Oxidative damage to collagen. In: Emerit, I., Chance, B. (eds) Free Radicals and Aging. EXS, vol 62. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7460-1_32

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  • DOI: https://doi.org/10.1007/978-3-0348-7460-1_32

  • Publisher Name: Birkhäuser Basel

  • Print ISBN: 978-3-0348-7462-5

  • Online ISBN: 978-3-0348-7460-1

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