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72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene. [5] The MMP2 gene is located on chromosome 16 at position 12.2.
Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; [1] other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily. [2]
5-(spiropyrrolidin-5-yl)pyrimidinetrione is a compound named 848773-43-3 that is a potent MMP-2, MMP-9 and MMP-13 inhibitor that spares MMP-1 and TACE. By substituting 1,3,4-oxadiazol-2-yl heteroaryl at C-4’ of the diphenylether segment to accomplish MMP-13 selectivity over MT-1 MMP, made the
Metalloproteinase inhibitors are found in numerous marine organisms, including fish, cephalopods, mollusks, algae and bacteria. [5] Members of the M50 metallopeptidase family include: mammalian sterol-regulatory element binding protein (SREBP) site 2 protease and Escherichia coli protease EcfE, stage IV sporulation protein FB.
[2] 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 ( MMP-14 ), a membrane-anchored MMP.
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. The most notorious endogenous metalloproteinases are tissue inhibitors of metalloproteinases, followed by cartilage-derived angiogenesis ...