Skip to main content
Log in

Expression of activated gelatinase in human invasive breast carcinoma

  • Published:
Clinical & Experimental Metastasis Aims and scope Submit manuscript

The expression of both 92- and 72-kDa gelatinases has been studied in 20 samples of human breast carcinoma by the technique of gelatin zymography. This technique allowed the relative amount of each gelatinase to be determined in small samples of tissue (<10 mg). More importantly, active and latent forms of the two gelatinases were resolved. Two samples (10–20 mg) were cut from each piece of tumour in order to monitor the variability of gelatinase distribution within that section of tumour. The 72-kDa latent progelatinase was present in 15 of the 20 tumours, with trace amounts in two others. The 62-kDa activated form of this gelatinase was detected in all 15 of the tumours in which the latent form was present. The 92-kDa latent progelatinase was present in 11 of the 20 tumours, with trace amounts in four others. However, the 82-kDa activated form of this gelatinase was only clearly detected in two tumours, although three others showed the presence of trace amounts. The ratio of active to latent forms of the 72-kDa gelatinase ranged from 0.9 to 3.6. There were no marked correlations between gelatinase expression and established staging and prognostic markers. Analysis of three samples of fibroadenoma revealed only very low levels of gelatinase expression. On the basis of these results, activation of the 72-kDa progelatinase appears to be a more common event in invasive breast carcinoma than activation of the 92-kDa progelatinase. However, neither proteinase showed a correlation with metastatic progression, as measured by lymph node involvement.

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

Access this article

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. Liotta LA, Steeg PS and Stetler-Stevenson WG, 1991, Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell, 64, 327–336.

    Google Scholar 

  2. Matrisian LM and Bowden GT, 1990, Stromelysin/ transin and tumour progression. Seminars in Cancer Biology, 1, 107–116.

    Google Scholar 

  3. Matrisian LM, 1990, Metalloproteinases and their inhibitors in matrix remodeling. Trends in Genetics, 6, 121–125.

    Google Scholar 

  4. Monteagudo C, Merino MJ, San-Juan J, Liotta LA and Stetler-Stevenson WG, 1990, Immunohistochemical distribution of type IV collagenase in normal, benign, and malignant breast tissue. American Journal of Pathology, 136, 585–592.

    Google Scholar 

  5. Basset P, Bellocq JP, Wolf C, Stoll I, Hutin P, Limacher JM, Podhajcer OL, Chenard MP, Rio MC and Chambon P, 1990, A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. Nature, 348, 699–704.

    Google Scholar 

  6. Muller D, Breathnach R, Engelmann A, Millon R, Bronner G, Flesch H, Dumont P, Eber M and Abecassis J, 1991, Expression of collage nase-related metalloproteinase genes in human lung or head and neck tumours. International Journal of Cancer, 48, 550–556.

    Google Scholar 

  7. Birkedal-Hansen H and Taylor RE, 1982, Detergent-activation of latent collagenase and resolution of its component molecules. Biochemical and Biophysical Research Communications, 107, 1173–1178.

    Google Scholar 

  8. Brown PD, Levy AT, Margulies IMK, Liotta LA and Stetler-Stevenson WG, 1990, Independent expression and cellular processing of Mr 72,000 type IV collagenase and interstitial collagenase in human tumorigenic cell lines. Cancer Research, 50, 6184–6191.

    Google Scholar 

  9. Brown PD, Kleiner DE, Unsworth EJ and Stetler-Stevenson WG, 1993, Cellular activation of 72 kDa type IV procollagenase/TIMP-2 complex. Kidney International, in press.

  10. Heussen C and Dowdle EB, 1980, Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulphate and copoly merised substrates. Analytical Biochemistry, 102, 196–202.

    Google Scholar 

  11. Ballin M, Gomez DE, Sinha CC and Thorgeirsson UP, 1988, ras Oncogene mediated induction of a 92-kDa metalloproteinase; strong correlation with the malignant phenotype. Biochemical and Biophysical Research Communications, 154, 832–838.

    Google Scholar 

  12. Bernard EJ, Muschel RJ and Hughes EN, 1990, Mr 92,000 gelatinase release correlates with the metastatic phenotype in transformed rat embryo cells. Cancer Research, 50, 3872–3877.

    Google Scholar 

  13. Albini A, Melchiori A, Santi L, Liotta LA, Brown PD and Stetler-Stevenson WG, 1991, Tumour cell invasion inhibited by TIMP-2. Journal of the National Cancer Institute, 83, 775–779.

    Google Scholar 

  14. Hoyhtya M, Hujanen E, Turpeenniemi-Hujanen T, Thorgeirsson U, Liotta LA and Tryggvason K, 1990, Modulation of type-IV collagenase activity and in vasive behaviour of metastatic human melanoma (A2058) cells in vitro by monoclonal antibodies to type-IV collagenase. International Journal of Cancer, 46, 282–286.

    Google Scholar 

  15. D'Errico A, Garbisa S, Liotta LA, Castronovo V, Stetler-Stevenson WG and Grigioni WF, 1991, Augmentation of type IV collagenase, laminin receptor, and Ki67 proliferation antigen associated with human colon, gastric, and breast carcinoma progression. Modern Pathology, 4, 239–246.

    Google Scholar 

  16. Daidone MG, Silvestrini R, D'Errico AD, Di Fronzo G, Benini E, Mancini AM, Garbisa S, Liotta LA and Grigioni WF, 1991, Laminin receptors, collagenase IV and prognosis in node-negative breast cancers. International Journal of Cancer, 48, 529–532.

    Google Scholar 

  17. Okada Y, Morodomi T, Enghild JJ, Suzuki K, Yasui A, Nakanishi I, Salvesen G and Nagase H, 1990, Matrix metalloproteinase-2 from human rheu matoid synovial fibroblasts—purification and activation of the precursor and enzymic properties. European Journal of Biochemistry, 194, 721–730.

    Google Scholar 

  18. Ward RV, Atkinson SJ, Slocombe PM, Docherty AJP, Reynolds JJ and Murphy G, 1991, Tissue inhibitor of metalloproteinase-2 inhibits the activa tion of 72-kDa progelatinase by fibroblast membranes. Biochimica et Biophysica Acta, 1079, 242–246.

    Google Scholar 

  19. Clavel C, Polette M, Doco M, Binninger I and Birembaut P, 1992, Immunolocalisation of matrix metallo-proteinases and their tissue inhibitor in hu man mammary pathology. Bulletin du Cancer, 79, 261–270.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Brown, P.D., Bloxidge, R.E., Anderson, E. et al. Expression of activated gelatinase in human invasive breast carcinoma. Clin Exp Metast 11, 183–189 (1993). https://doi.org/10.1007/BF00114976

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00114976

Keywords

Navigation