Skip to main content
SpringerLink
Log in

Collagen degradation in the pregnant human cervix at term and after prostaglandin-induced cervical ripening

  • Originals
  • Published:
Archives of gynecology Aims and scope Submit manuscript

Summary

The role of enzymatic collagen degradation in prostaglandin-induced and physiological cervical ripening was studied by determining collagenase and other proteolytic activity in extracts of cervical biopsies. Collagenase activity was assayed in a highly specific and sensitive system using native collagen type I as substrate. The intracervical application of sulprostone gel prior to termination of 1st trimester pregnancy led to a marked improvement in cervical dilatability. Collagenase and proteolytic activity were found to be significantly higher in postpartum samples than in specimens obtained from the nonpregnant or early pregnant cervix. After sulprostone treatment enzymatic activities were only marginally elevated. Analysis of extractable peptides showed that sub partu collagen was degraded in preference to noncollagenous proteins into very small fragments, whereas in the process of prostaglandin-induced cervical ripening collagen degradation appears to be of minor importance.

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

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Abe S, Nagai Y (1973) Evidence for the presence of a complex of collagenase with α2-macroglobulin in human rheumatoid synovial fluid: a possible regulatory mechanism of collagenase activity in vivo. J Biochem [Tokyo] 73:897–900

    CAS  PubMed  Google Scholar 

  2. Adelmann BC, Kirrane JA, Glynn LE (1972) The structural basis of cell-mediated immunological reactions of collagen. Immunology 23:723–738

    CAS  PubMed  Google Scholar 

  3. Adelmann-Grill BC (1982) Säugetierkollagenasen: physiologische und pathologische Aspekte. Arzneimittelforsch 32:1357–1362

    CAS  PubMed  Google Scholar 

  4. Anson ML (1938) The estimation of pepsin, trypsin, papain and kathepsin with hemoglobin. J Gen Physiol 22:79–89

    Article  CAS  Google Scholar 

  5. Cawston TE, Murphy G, Mercer E, Galloway WA, Hazleman GL, Reynolds JJ (1983) The interaction of purified rabbit bone collagenase with purified rabbit bone metallo proteinase inhibitor. Biochem J 211:313–318

    CAS  PubMed  Google Scholar 

  6. Harris E, Krane S (1974) Collagenase. New Engl J Med 291:557–563

    CAS  PubMed  Google Scholar 

  7. Huszar G, Naftolin F (1984) The myometrium and uterine cervix in normal and preterm labor. N Engl J Med 311:571–581

    CAS  PubMed  Google Scholar 

  8. Kitamura K, Ito A, Mori Y (1980) The existing forms of collagenase in the human uterine cervix. J Biochem [Tokyo] 87:753–760

    CAS  PubMed  Google Scholar 

  9. Kleissl HP, van der Rest M, Naftolin F, Glorieux FH, de Leon A (1978) Collagen changes in the human cervix at parturition. Am J Obstet Gynecol 130:748–753

    CAS  PubMed  Google Scholar 

  10. Krieg T, Hörlein D, Wiestner M, Müller PK (1978) Aminoterminal extension peptides from type I collagen normalize excessive collagen synthesis of scleroderm fibroblasts. Arch Dermatol Res 263:171–180

    CAS  PubMed  Google Scholar 

  11. Kühnle H, Grande P, Kuhn W (1977) Vermeidung dilatationsbedingter Komplikationen beim Schwangerschaftsabbruch durch intrazervikale Applikation eines prostaglandinhaltigen Gels. Geburtshilfe Frauenheilkd 37:675–680

    PubMed  Google Scholar 

  12. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature [Lond] 227:680–685

    PubMed  Google Scholar 

  13. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275

    CAS  PubMed  Google Scholar 

  14. Maillot v K, Zimmermann BK (1976) The solubility of collagen of the uterine cervix during pregnancy and labor. Arch Gynecol 220:275–280

    CAS  Google Scholar 

  15. Maillot v K, Stuhlsatz HW, Mohanaradha Krishnan V, Greiling H (1979) Changes in the glycosaminoglycans distribution pattern in the human cervix during pregnancy and labor. Am J Obstet Gynecol 135: 503–506

    PubMed  Google Scholar 

  16. Maillot v K, Stuhlsatz HW, Gentsch HH (1981) Connective tissue changes in the human cervix in pregnancy and labour. In: Ellwood DA, Anderson ABM (eds) The cervix in pregnancy and labor. Livingstone, Edinburgh London Melbourne New York, p 123

    Google Scholar 

  17. Mori Y, Ito A, Hirikawa S, Kitamura K (1981) Proteinases in the human and rabbit cervix. In: Ellwood DA, Anderson ABM (eds) The cervix in pregnancy and labour. Livingstone, Edinburgh London Melbourne New York, p 136

    Google Scholar 

  18. Rath W, Meyer D, Hildebrandt J, Hilgers R, Kuhn W (1983) Comparative study of various intracervically administered PG gel preparations for termination of first trimester pregnancies. Contraception 28:209–222

    Article  CAS  PubMed  Google Scholar 

  19. Rath W, Meyer D, Harder D, Hilgers R, Kuhn W (1985) Cervical ripening in first trimester abortion by intracervical application of sulprostone gel. Geburtshilfe Frauenheilkd 45:51–56

    CAS  PubMed  Google Scholar 

  20. Stricklin GP, Bauer EA, Jeffrey JJ, Eisen AZ (1977) Human skin collagenase: isolation of precursor and active forms from both fibroblast and organ culture. Biochem J 16:1607–1615

    CAS  Google Scholar 

  21. Stricklin GP, Welgus HG) Human skin fibroblast collagenase inhibitor. Purification and biochemical characterization. J Biol Chem 258:12252–12258

  22. Szalay S, Husslein P, Grünberger W (1981) Die kollagenolytische Aktivität von menschlichem Zervixgewebe nach lokaler Applikation von Prostaglandin E2 (PGE2) mit einem Portioadapter. Zentralb Gynäkol 103:1107–1112

    CAS  Google Scholar 

  23. Uldbjerg N, Ekman G, Malmström A, Sporrong B, Ulmsten U et al. (1981) Biochemical and morphological changes of human cervix after local application of prostaglandin E2 in pregnancy. Lancet I:267–268

    Article  Google Scholar 

  24. Uldbjerg N, Ekman G, Malmström A, Olsson K, Ulmsten U (1983) Ripening of the human uterine cervix related to changes in collagen, glycosaminoglycans, and collagenolytic activity. Am J Obstet Gynecol 147:662–666

    CAS  PubMed  Google Scholar 

  25. Uldbjerg N, Ulmsten U, Ekman G (1983) The ripening of the human uterine cervix in terms of connective tissue biochemistry. Clin Obstet Gynecol 26:14–26

    CAS  PubMed  Google Scholar 

  26. Uldbjerg N, Ekman G, Malmström A, Ulmsten U, Wingerup L (1983) Biochemical changes in human cervical connective tissue after local application of prostaglandin E2. Gynecol Obstet Invest 15:291–299

    CAS  PubMed  Google Scholar 

  27. Welgus HG, Jeffrey JJ, Eisen AC, Roswit WT, Stricklin GP (1985) Human skin fibroblast collagenase. Interaction with substrate and inhibitor. Collagen Rel Res 5:167–179

    CAS  Google Scholar 

  28. Wooley DE, Roberts DR, Evanson JM (1975) Inhibition of human collagenase activity by a small molecular weight serum protein. Biochem Biophys Res Comm 66:747–754

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Universitäts-Frauenklinik, Humboldtallee 19, D-3400, Göttingen, Federal Republic of Germany

    W. Rath, U. Pieper & W. Kuhn

  2. Abteilung für Bindegewebsforschung, Max-Planck-Institut für Biochemie, D-8033, Martinsried, Federal Republic of Germany

    B. C. Adelmann-Grill

Authors
  1. W. Rath
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. B. C. Adelmann-Grill
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. U. Pieper
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. W. Kuhn
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Investigations presented here are part of a not yet submitted dissertation of U. Pieper

Rights and permissions

Reprints and permissions

About this article

Cite this article

Rath, W., Adelmann-Grill, B.C., Pieper, U. et al. Collagen degradation in the pregnant human cervix at term and after prostaglandin-induced cervical ripening. Arch Gynecol 240, 177–184 (1987). https://doi.org/10.1007/BF00207713

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00207713

Key words

Search

Navigation