Clinical & Experimental Metastasis

, Volume 18, Issue 2, pp 171–178 | Cite as

Specific expression of matrix metalloproteinases 1, 3, 9 and 13 associated with invasiveness of breast cancer cells in vitro

  • Malika Balduyck
  • Farid Zerimech
  • Valérie Gouyer
  • Raphael Lemaire
  • Brigitte Hemon
  • Georges Grard
  • Carole Thiebaut
  • Véronique Lemaire
  • Evelyne Dacquembronne
  • Thérèse Duhem
  • Anne Lebrun
  • Marie-José Dejonghe
  • Guillemette Huet


Several matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs) were studied in highly invasive (MDA-MB-231) and slightly invasive (MCF-7, T47D, BT-20) breast cancer cell lines. Investigations were carried out at the protein level and/or at the mRNA level, either in cells cultured as monolayers on plastic, or in cells seeded on a thin layer of Matrigel basement membrane matrix. Analysis of MMP expression by RT-PCR showed expression of MMP-1, MMP-3, and MMP-13 in highly invasive MDA-MB-231 cells, but not in slightly invasive cell lines. The extracellular secretion of MMP-1 and MMP-3 by MDA-MB 231 cells could be also shown by ELISA. TIMP-1 and TIMP-2 mRNAs were found in all cell lines, however, the extracellular secretion of both TIMPs was much higher in MDA-MB-231 cells than in the other cell lines. When the cells were cultured on Matrigel matrix, MMP-9 expression was induced in MDA-MB-231 cells only, as assessed by RT-PCR and zymography experiments. The invasive potential of MDA-MB-231 cells evaluated in vitro through Matrigel was significantly inhibited by the MMP inhibitor BB-2516, by 25% and 50% at the concentrations of 2 × 10−6M and 10−5M, respectively. In conclusion, our data show that highly invasive MDA-MB-231 cells but not slightly invasive T47D, MCF-7 and BT-20 cells express MMP-1, MMP-3, MMP-9 and MMP-13. MMP-9 which is specifically up-regulated by cell contact to Matrigel, may play a key role in the invasiveness of MDA-MB-231 cells through basement membranes.

metalloproteinases breast cancer cells invasiveness tissue inhibitors of metalloproteinases synthetic inhibitors of metalloproteinases 


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Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • Malika Balduyck
    • 1
  • Farid Zerimech
    • 1
  • Valérie Gouyer
    • 1
  • Raphael Lemaire
    • 2
  • Brigitte Hemon
    • 3
  • Georges Grard
    • 1
  • Carole Thiebaut
    • 1
  • Véronique Lemaire
    • 1
  • Evelyne Dacquembronne
    • 1
  • Thérèse Duhem
    • 1
  • Anne Lebrun
    • 1
  • Marie-José Dejonghe
    • 3
  • Guillemette Huet
    • 1
  1. 1.Laboratoire de BiochimieHôpital Claude HuriezLille CedexFrance
  2. 2.The Arthritis Center – Bldg. K-5Boston University School of MedicineBostonUSA
  3. 3.Unité INSERM 377Lille CedexFrance

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