Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Connective tissue metabolism in culture fibroblasts of a patient with Ehlers-Danlos syndrome type I

  • 33 Accesses

  • 17 Citations


Study on connective tissue metabolism was conducted with a patient with Ehlers-Danlos syndrome (E-D) of Type J who visited our institute.

The conversion of procollagen into tropocollagen in the medium of cultured fibroblasts was assayed by the chase technique using3H-proline. The conversion was inhibited in the cultured fibroblasts of the patient.

The components of glycosaminoglycans in cultured medium and fibroblasts from E-D were within normal ranges, however, the ratio of glycoprotein to glycosaminoglycans of intra-and extra-cellular fractions of E-D fibroblasts was higher than the normal one.

These findings suggest that the insufficient maturation of collagen fiber may be considered fundamental disorders of E-D.


Der Bindegewebsstoffwechsel wird bei einem Patienten mit einem Ehlers-Danlos-Syndrom des Typs I untersucht.

Die Umwandlung von Prokollagen in Tropokollagen in die Fibroblastenkultur wurde mittels3H-Prolin durchgeführt. Der Prozeß der Umwandlung wird in der Fibroblastenkultur des Patienten gehemmt.

Die Glykosaminoglykane im Kulturmedium und die Fibroblasten des Patienten zeigten keine Abweichung von der Norm, jedoch war das Verhältnis von Glykoproteinen zu Glykosaminoglykanen der intra- und extracellulären Fraktion der Fibroblasten des Patienten höher als bei normalen Patienten.

Diese Ergebnisse lassen den Hinweis zu, daß eine ungenügende Reife der Kollagenfaser eine der wesentlichsten Ursachen des Ehlers-Danlos-Syndroms ist.

This is a preview of subscription content, log in to check access.


  1. 1.

    Ferrante. N. D., Leacheman, R. D., Angelini, P., Donelly, P. V., Francis, G., Almazan, A., Segni, G.: Lysyl oxydase deficiency in Ehlers-Danlos syndrome type V. Conn. Tiss. Res.3. 49–53 (1975)

  2. 2.

    Hanset, R.: Dermatosparaxis of the calf, a genetic defect of the connective tissue. Hoppe-Seylers Z. Physiol. Chem.352, 13 (1971)

  3. 3.

    Juva, K., Prockop, D. J.: Modified procedure for the assay of3H- or14C-labelled hydroxyproline. Anal. Biochem.15, 79–83 (1966)

  4. 4.

    Krane, S. M., Pinnell, S. R., Erbe, R. W.: Lysyl-protocollagen hydroxylase deficiency in fibroblast from siblings with hydroxylysine-deficient collagen. Proc. Nat. Acad. Sci.69, 2899–2903 (1972)

  5. 5.

    Lapier, C. M., Lenaers. S., Kohn, L. D.: Procollagen peptidase: An enzyme excising the coordination peptidase of procollagen. Proc. Nat. Acad. Sci.68. 3054–3058 (1971)

  6. 6.

    Laymann, D. L., McGoodwin, E. B., Martin, G. R.: The nature of the collagen synthesized by culture human fibroblast. Proc. Nat. Acad. Sci.68, 1138–1142 (1971)

  7. 7.

    Lichtenstein, J. R., Martin, G. R.: Defect in conversion of procollagen to collagen in a form of Ehlers-Danlos syndrome. Science182. 298–300 (1973)

  8. 8.

    McKusick, V. A.: The Ehlers-Danlos syndrome. Heritable disorders of connective tissue. pp. 292–371. St. Louis: C. V. Mosby Co. 1972

  9. 9.

    Pinnell, S. R., Krane, S. M., Kenzora, J. E., Glimcher, M. J.: A heritable disorder of connective tissue hydroxylysine-deficient collagen disease. New Engl. J. Med.286, 1013–1020 (1972)

  10. 10.

    Podrazky, V., Steven, F. S., Jackson, D. S., Weiss, J. B., Leibovich, S. J.: Interaction of tropocollagen with protein-polysaccharide complexes. An analysis of the ionic groups responsible for interaction. Biochem. Biophys. Acta229, 690–697 (1971)

  11. 11.

    Pope, F. M., Martin, G. R., Lichtenstein, J. R., Penettinen, R., Gerson, B., Rowe, D. W., McKusick, V. A.: Patient with Ehlers-Danlos syndrome type IV lack type III collagen. Proc. Nat. Acad. Sci.72, 1314–1316 (1975)

  12. 12.

    Shinkai, H., Fujiwara, N., Matsubayashi, S., Sano, S.: Effect of thiocyanate on human skin collagenase activity. J. Derm.1, 145–151 (1974)

  13. 13.

    Sussman, M., Lichtenstein, J. R., Nigra, T. P., Martin, G. R., McKusick, V. A.: Hydroxyly-sine-deficient skin collagen in patient with from of the Ehlers-Danlos syndrome. J. Bone Jt. Surg.56A, 1228–1234 (1974)

  14. 14.

    Tajima, S., Nagai, Y.: Fractionation and partial characterization of collagen fibers from insoluble calf dermis. J. Conn. Tiss.7, 215 (1975)

  15. 15.

    Taubman, M. B., Goldgerg, B.: Deficiency of conversion of procollagen to tropocollagen by cultured normal, Ehlers-Danlos and Marfan fibroblasts. Fed. Proc.33, 617 (1974)

  16. 16.

    Timpl, R., Wolff, I., Weiser, M.: Acidic structural proteins of connective tissue. I. Solubilization and preliminary chemical characterization. Biochem. Biophys. Acta194, 112–120 (1969)

  17. 17.

    Weber, R., Osborn, M.: The reliability of molecular weight determinations by dodecyl sulfatepolyacrylamide gel electrophoresis. J. Biol. Chem.244, 4406–4412 (1969)

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Shinkai, H., Hirabayashi, O., Tamaki, A. et al. Connective tissue metabolism in culture fibroblasts of a patient with Ehlers-Danlos syndrome type I. Arch. Derm. Res. 257, 113–123 (1976). https://doi.org/10.1007/BF00558084

Download citation


  • Public Health
  • Collagen
  • Connective Tissue
  • Collagen Fiber
  • Glycosaminoglycan