Matrix metalloproteinase-3 (MMP-3), also known as stromelysin-1, is a member of the matrix metalloproteinase family (MMPs). The function of this molecule depends on zinc ions in the internal environment. MMP-3 is composed of 475–478 amino acids in mammals, and its amino acid sequence is highly conserved among different species and genera, suggesting its potential for cross-species applications1. Like that of most MMPs, the structure of MMP-3 can be divided into four parts: a propeptide of approximately 80 amino acids, a metalloproteinase catalytic domain of approximately 170 amino acids, a ligating peptide of variable length (hinged region) and a heme protein domain of approximately 200 amino acids. MMP-3 can digest a variety of extracellular matrix (ECM) components, including matrix proteins, growth factors, proteases, surface receptors, and adhesion molecules. In particular, this enzyme can process a variety of pro-MMPs, and thus, the synthesis and activation of MMP-3 the first step in the MMP-mediated degradation process ; furthermore, this molecule is associated with cellular fibrinolytic activity. Tissue inhibitor of metalloproteinase (TIMP) is a natural MMP inhibitor.
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