Expression of activated gelatinase in human invasive breast carcinoma

P D Brown, R E Bloxidge, E Anderson, A Howell

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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.

Original languageEnglish
Pages (from-to)183-9
Number of pages7
JournalClinical and Experimental Metastasis
Issue number2
Publication statusPublished - Mar 1993


  • Biomarkers, Tumor
  • Breast Neoplasms
  • Collagenases
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Activation
  • Female
  • Humans
  • Isoenzymes
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9
  • Metalloendopeptidases
  • Molecular Weight
  • Neoplasm Invasiveness
  • Neoplasm Proteins
  • Protein Denaturation
  • Sensitivity and Specificity
  • Sodium Dodecyl Sulfate
  • Comparative Study
  • Journal Article


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