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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]
Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [5] MMP-3 has an estimated molecular weight of 54 kDa. [6]
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis .
[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.
Matrix metalloproteinase-16 is an enzyme that in humans is encoded by the MMP16 gene. [5] [6]Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.
The human MMP-20 gene contains 10 exons and is part of a cluster of matrix metalloproteinase genes that localize to human chromosome 11q22.3. [6] A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. Enamel in the absence of ...
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