The matrix metalloproteinases (MMPs) are a family of structurally and functionally related proteinases, initially characterized by their ability to degrade the extracellular matrix (ECM) [1]. Nowadays, at least 20 enzymes that share considerable homology within their major domains (signal peptide, propeptide, catalytic, hinge and hemopexin-like domains) were included in MMPs family [2]. Most of MMPs are synthesised and secreted as partially activated latent forms, requiring, for full activation, removal of the entire propeptide domain by proteinases including other MMPs AbstractThe goal of our study was to analyse the prognostic values for some matrix metalloproteinases (MMPs) and tissue inhibitors of matrix metalloproteinases (TIMPs) in breast cancer. We evaluated the activity and the expression levels of MMP-9, MMP-2, TIMP-1 and TIMP-2 in malignant versus benign fresh breast tumor extracts. For this purpose, gelatinzymography, immunoblotting and ELISA were used to analyse the activity and expression of MMPs and TIMPs. We found that MMP-9 expression level and activity are increased in malignant tumors. In addition, MMP-9/TIMP-1 and MMP-2/TIMP-2 ratio values obtained by us were significantly different in malignant tumors compared to benign tumors. We suggest that the abnormal MMP-9/TIMP-1 balance plays a role in the configuration of breast invasive carcinoma of no special type and also in tumor growth, while altered MMP-2/TIMP-2 ratio value could be associated with lymph node invasion and used as a prognostic marker in correlation with Nottingham Prognostic Index. Finally, we showed that in malignant tumors high expression of estrogen receptors is associated with enhanced activity of MMP-2 and increased bcl-2 levels, while high expression of progesterone receptors is correlated with low TIMP-1 protein levels.

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