Critical as it is, collagenase is just one member of a large class of enzymes called metalloproteinases—protein-digesting enzymes whose catalytic activity depends on the presence of metal ions. Metalloproteinases can be inhibited by chelators, such as EDTA, which coordinate metal ions.2 Several zinc (Zn2+)-dependent endopeptidases exist, and are known collectively as matrix metalloproteinases (MMPs), or matricins.2 Both secreted and membrane-bound MMPs catalyze the breakdown of proteins located either on the cell's plasma membrane, or within the extracellular matrix (ECM).2
Researchers have come to recognize the critical role these enzymes play in regulating processes that range from development and morphogenesis to angiogenesis and metastasis. Biotech companies have stepped in to offer a wide range of reagents to facilitate the study of these diverse proteins.
A major task of MMPs in vivo is thought to be disruption of the ECM's structural organization during development, tissue resorption, and disease progression.2,4 This is accomplished ...
