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. 2020 Nov 20;23(1):70. doi: 10.3892/mmr.2020.11708

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Copyright: © Li et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 1. — Expression and activation of MMP2. After being secreted, proMMP2 is activated by the collaboration between TIMP-2 and MMP14. Extracellular proMMP2 binding with the C-terminal tail of TIMP-2 is indirectly linked to the cell membrane-anchored MMP14 through the interaction between the N-terminal domain of TIMP-2 and the catalytic domain of MMP14. This proMMP2/TIMP-2/MMP14 complex is recruited to another adjacent MMP14 that converts proMMP2 to the active enzyme form. On the other hand, MMP2 activity can also be inhibited by TIMP-2 when its active site binds to the N-terminal inhibitory domain of TIMP-2. While several TIMPs inhibit the activity of MMP2 and lead to LRP-mediated endocytosis and degradation, Naa10p can stabilize MMP2 protein. LRP, lipoprotein receptor-related proteins; MMP, matrix metalloproteinase; Naa10p, N-α-acetyltransferase 10 protein; TIMP, tissue inhibitors of metalloproteinase.