Metalloproteinases (MMPs)
Matrix metalloproteinases (MMPs) represent a family of 20+ members of secreted or transmembrane bound proteolytic endopeptidases that require zinc ions for their enzymatic activity and share particular structural similarities. (Dzwonek, FEBS Letters 2004; 567:129–135). Collectively, they are capable of processing and degrading various extracellular matrix proteins. MMPs play critical roles in many normal growth and developmental aspects of tissue remodeling, wound healing, and angiogenesis. In many pathological situations, they are associated with cell migration and invasion in arthritis and cancer tumor progression. Most MMPs are secreted from cells into their extracellular environment in their inactive, or proforms, thus making activation a key step in regulating the amount of degradative activity outside the cell.
For most MMPs, including MMP-1, -3, -7, and -9, serine proteases such as plasmin, urokinase-type plasminogen activators, and furin are known to initiate activation. In addition, some MMPs also activate other members of the family, for example, MT1-MMP activation of MMP-2 or MMP-13 and MMP-3 activation of MMP-9. Once activated, the MMPs are subject to inhibition by the tissue inhibitors of metalloproteinases (TIMPs) that bind MMPs non-covalently. To date, four TIMPs have been identified: TIMP-1, -2, -3, and -4. The regulation of MMP expression and activity appears to be a complex process, requiring the interplay of several different signaling and enzymatic systems. Millipore offers a full range of MMP antibodies, proteins, and activity assays for research into the function and regulation of metalloproteinases in both normal and disease states.
Eight domain motifs for the matrix metallopreteinases, or matrixins, are identified to date.
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