Authors: Tudor PETREUŞ1*, Carmen Elena COTRUTZ1, Monica NEAMŢU1, Constantin COTRUTZ1, Andrei NEAMŢU2
Affiliation: 1 Department of Cell and Molecular Biology, ”Gr.T.Popa” University of Medicine and Pharmacy, Iaşi; 2 Excellence Centre for Pain study and Therapy, ”Gr.T.Popa” University of Medicine and Pharmacy, Iaşi
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ABSTRACT. Matrix metalloproteinases (MMP) and the factors that are regulating their activity (tissue inhibitors of MMP – TIMP) plays a complementary role in stimulating or inhibiting the advance of ureteric bud in the mesenchime together with various growth factors. The inhibitors of matrix metalloproteinases can play also various roles in these processes. Even if there is a correspondence of the pairs MMP2-TIMP2 and MMP9-TIMP1, the relation between these enzymes and their specific inhibitors is especially complex. In order to complete the observations referring to co-localization of MMP2, MMP9 and TIMP2 we have used a molecular modeling technique in order to investigate the coupling possibilities between MMP2, 9 and the natural inhibitor TIMP2. The present study analyzes the possible conformations and interactions between MMP2, MMP9 with TIMP2.
Keywords: MMP2, MMP9, TIMP1, TIMP2, docking, molecular modeling