Matrix metalloproteinase-1 (MMP-1) is a member of the matrix metalloproteinases (MMPs) family, which are zinc-containing endopeptidases involved in the degradation of extracellular matrix components. MMP-1, also known as human fibroblast collagenase, was the first vertebrate collagenase to be purified and cloned, making it the prototype for interstitial collagenases. It is synthesized as an inactive zymogen that becomes active through proteolytic removal of N-terminal residues. MMP-1 has a catalytic domain and a carboxy terminal domain similar to hemopexin, which allows it to cleave collagen fibrils in the extracellular space. Beyond its role in collagen turnover, MMP-1 also cleaves non-matrix substrates and…