Experiments in mice suggest that matrilysin influences early-stage mammary tumorigenesis (Rudolph-Owen L.A. et al., 1998).
Cell lines:
- In breast cancer cells (BCC), MT1-MMP//MMP-14 and a recombinant catalytic domain of MT1-MMP were unable to activate pro-matrilysin, indicating that MT1-MMP is not a universal activator of all MMPs (Li H. et al., 1998).
Tumors:
- MMP7 mRNA has been detected in the neooplastic epithelial tumor cells of 70-91% of breast adenocarcinomas. MMP7 was expressed by morphologically normal epithelial ducts within tumors and in tissue from reduction mammoplasties, and by epithelial-derived tumor cells (Heppner K.J. et al., 1996).
- The association among matrix metalloprroteinases (gelatinases A/MMP-2 and B/MMP-9, stromelysin-3/MMP-11 and matrilysin/MMP-7) mRNAs expressed in primary breast carcinomas was investigated and standard prognostic parameters and clinical outcome. mRNA levels were determined by Northern analysis in samples of 81 breast cancer patients (median follow-up, 40 months) and 27 samples of uninvolved adjacent breast tissue. Proteases were expressed by the majority of the tumors and normal breast tissues examined. MMP-11, MMP-2 and MMP-7 mRNAs were more often expressed at high levels in carcinomatous than in normal breast tissues. Differences in the distribution of MMP-9 mRNA were not found. However, paired normal tissues generally produced weaker signals when compared to matched tumor samples. Univariate analysis showed no significant association of MMP-2 and MMP-7 mRNAs with the classical prognostic markers (age, menopausal status, stage, size, nodal status, vascular infiltrate, necrosis, steroid receptors, metastasis and survival). Overexpression of MMP-11 was more frequently found in tumors of post-menopausal women (P < 0.022). Elevated expression of MMP-9 mRNA was associated with the presence of vascular infiltrate (P < 0.026), necrosis (P < 0.039), PR negative tumors (P < 0.014) and inversely correlated to the number of survivors (P < 0.021). Multivariate analysis including 68 patients for whom all information was available indicated that neither stromelysin correlated significantly with pathological, clinical or biochemical features. High levels of MMP-2 and -9 mRNAs were inversely associated with the number of survivors (Pacheco M.M. et al., 1998).
Gaire M. et al. (1994) Structure and expression of the human gene for the matrix metalloproteinase matrilysin. J. Biol. Chem. 269, 2032-2040.
(PubMed)
Heppner K.J. et al. (1996) Expression of most matrix metalloproteinase family members in breast cancer represent a tumor-induced host response. Am. J. Pathol. 149, 273-282.
(PubMed)
Li H. et al. (1998) Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. Mol. Carcinog. 22, 84-94.
(PubMed)
Pacheco M.M. et al. (1998) Expression of gelatinases A and B, stromelysin-3 and matrilysin genes in breast carcinomas: clinico-pathological correlations. Clin. Exp. Metastasis 16, 577-585.
(PubMed)
Rudolph-Owen L.A. et al. (1998) The matrix metalloproteinase matrilysin influences early-stage mammary tumorigenesis. Cancer Res. 58, 5500-5506.
(PubMed)
Wilson C.L. and Matrisian L.M. (1996) Matrilysin: an epithelial matrix metalloproteinase with potentially novel functions. Int. J. Biochem. Cell Biol. 28, 123-136 (
Review).
(PubMed)
