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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 ...
A matrix metalloproteinase inhibitor (INN stem –mastat [1]) inhibits matrix metalloproteinases.Because they inhibit cell migration, they have antiangiogenic effects. They are endogenous or exogenous.
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.
MMP-11 shows more similarity to the MT-MMPs, is convertase-activatable and is secreted therefore usually associated to convertase-activatable MMPs. Substrates include Col IV, fibronectin, laminin, aggrecan MMP12: Macrophage metalloelastase: HME, ME, MME, MMP-12: secreted: Substrates include elastin, fibronectin, Col IV MMP13: Collagenase 3 ...
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7077 21858 Ensembl ENSG00000035862 ENSMUSG00000017466 UniProt P16035 P25785 RefSeq (mRNA) NM_003255 NM_011594 RefSeq (protein) NP_003246 n/a Location (UCSC) Chr 17: 78.85 – 78.93 Mb Chr 11: 118.19 – 118.25 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tissue inhibitor of metalloproteinases 2 (TIMP2) is a gene and a corresponding protein. The gene is a member of the TIMP gene ...
ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13)—also known as von Willebrand factor-cleaving protease (VWFCP)—is a zinc-containing metalloprotease enzyme that cleaves von Willebrand factor (vWf), a large protein involved in blood clotting.