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Pyrimidine dicarboxamides are highly selective MMP-13 inhibitors. In the S1’ pocket of MMP-13 is an S1’ side pocket that is unique to the matrix metalloproteiase. Pyrimidine dicarboxamides bind to this side pocket, which increases the selectivity. The role of MMP-13 is cleaving fibrillar collagen at neutral pH and higher mRNA levels of MMP ...
[5] [6] It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. [7] MMP-13 has a predicted molecular weight around 54 kDa. [8] It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain . Although the actual ...
The most notorious endogenous metalloproteinases are tissue inhibitors of metalloproteinases, followed by cartilage-derived angiogenesis inhibitors. Exogenous matrix metalloproteinase inhibitors were developed as anticancer drugs. [2] Examples include: Batimastat; Cipemastat; Ilomastat; Marimastat; Prinomastat; Rebimastat; Tanomastat
The most commonly used groupings (by researchers in MMP biology) are based partly on historical assessment of the substrate specificity of the MMP and partly on the cellular localization of the MMP. These groups are the collagenases, the gelatinases, the stromelysins, and the membrane-type MMPs (MT-MMPs).
Overall, all MMPs are inhibited by TIMPs once they are activated, but the gelatinases (MMP-2 and MMP-9) can form complexes with TIMPs when the enzymes are in their latent form. The complex of latent MMP-2 (pro-MMP-2)with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP , a membrane-anchored MMP.
The collective MMP family is capable of degrading all known ECM macromolecules. MMP activity is regulated at the level of transcription, post-translationally by proteolytic cleavage, and by endogenous inhibitors known as tissue inhibitors of metalloproteinases (TIMPs). The role of matrix metalloproteinases and TIMPs in several pathological ...
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