Collagen Cross-Linking: The Substrate Specificity of Lysyl Oxidase

  • Robert C. Siegel
  • Joseph C. C. Fu
  • Yu-Hua Chang
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

Lysyl oxidase is a specific amine oxidase that contains copper and is irreversibly inhibited by compounds called lathyrogens (1,2,3). 3-Aminopropionitrile (BAPN) is the most widely studied and best known of these compounds. When growing animals are either fed lathyrogens or made copper deficient they develop a wide variety of connective tissue and skeletal abnormalities such as dissecting aneurysms of the thoracic aorta, kyphoscoliosis and abdominal hernias. The pathogenesis of these abnormalities is related to decreased collagen cross-linking secondary to decreased lysyl oxidase activity which results from either lack of the copper cofactor(4) or irreversible inhibition by BAPN. Since clinical abnormalities in these disorders have been noted as a result of deranged biosynthesis in both elastin and collagen with lysyl oxidase deficiency, it seemed appropriate to define the substrate specificity of highly purified lysyl oxidase in more detail and to determine whether the same enzyme is active on collagen and elastin substrates(5,6,7,8).

Keywords

Urea Aldehyde Lysine Arginine Fibril 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Pinnel, S.R. and Martin, G.R. (1968) Froc. Nat. Acad. Sci. U.S. 61, 708.CrossRefGoogle Scholar
  2. 2.
    Narayanan, A.S., Siegel, R.C., and Martin, G.R. (1974) Arch. Biochem. Biophys. 162, 231.PubMedCrossRefGoogle Scholar
  3. 3.
    Chvapil, M., McCarthy, D.W., Misiorowski, R.L., Madden, J.W., and Peacock, E.E. (1974) Proc. Soc. Exp. Biol. Med. 146, 688.PubMedGoogle Scholar
  4. 4.
    Harris, E.D., Gonnerman, W.A., Savage, J.E., and O’Dell, B.L. (1974) Biochim. Biophys. Acta 341, 332.PubMedCrossRefGoogle Scholar
  5. 5.
    Shieh, J.J., Tamaye, R., and Yasunobu, K.T. (1975) Biochim. Biophys. Acta 377, 229.PubMedCrossRefGoogle Scholar
  6. 6.
    Siegel, R.C. (1974) Proc. Nat. Acad. Sci. U.S. 71, 4826.CrossRefGoogle Scholar
  7. 7.
    Martin, G.R., Pinnell, S.R., Siegel, R.C. and Goldstein, E.R. (1970) Chemistry and Molecular Biology of the Intercellular Matrix, Balazs, E.A., Ed., Academic Press, New York.Google Scholar
  8. 8.
    Vidal, G., Shieh, J.J., and Yasunobu, K.T. (1975) Biochim. Biophys. Res. Commun., 64, 989.CrossRefGoogle Scholar
  9. 9.
    Fowler, L.J., Peach, C.M., and Bailey, A.J. (1970) Biochem. Biophys. Res. Commun. 41, 251.PubMedCrossRefGoogle Scholar
  10. 10.
    Siegel, R. C. and Martin, G. R. (1970) J. Biol. Chem. 245, 1653.PubMedGoogle Scholar
  11. 11.
    Tanzer, M.L. (1973) Science 180, 561.PubMedCrossRefGoogle Scholar
  12. 12.
    Davis, N.R., Risen, O.M., and Pringle, G.A. (1975) Biochemistry 14, 2031.PubMedCrossRefGoogle Scholar
  13. 13.
    Gallop, P.M. and Paz, M. (1975) Phys. Rev. 55, 418.Google Scholar
  14. 14.
    Robins, S.P., Shimokomaki, M., and Bailey, A.J. (1973) Biochem, J. 131, 771.Google Scholar
  15. 15.
    Traub, W. and Piez, K.A. (1971) Adv. Prot. Chem. 25, 243.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Robert C. Siegel
    • 1
  • Joseph C. C. Fu
    • 1
  • Yu-Hua Chang
    • 1
  1. 1.University of CaliforniaSan FranciscoUSA

Personalised recommendations