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Matrix Metalloproteinase-1 (MMP-1)is interstitial collagenase and fibroblast collagenase. The enzyme in humans is encoded by the MMP1 gene. Human Fibroblast Collagenase (MMP-1) was actually the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA [1].

MMP-1 belongs to a family of enzymes known as Matrix metalloproteinases (MMPs). These enzymes are known as zinc-dependent endopeptidases because of the zinc ions involved in the catalytic site. The MMPs belong to a larger family of proteases known as the metzincin superfamily. MMPs are capable of degrading all kinds of extracellular matrix proteins as well as process a number of other bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand), and chemokine/cytokine in/activation. MMPs are also thought to play a major role on cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis,host defense, embryonic development, reproduction, and tissue remodeling. MMPs are also involved in disease processes, such as arthritis and metastasis [5].  

MMP's were first described in vertebrates in 1962 but have also been found in invertebrates and plants. They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade extracellular matrix, and their specific evolutionary DNA sequence. MMPs are secreted as inactive proproteins which is later activated when cleaved by extracellular proteases [2][3].