MMP14 monoclonal antibody

The matrix metalloproteinase (MMP) family of proteases are a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, and other proteases . Matrix metalloproteinases can be broadly categorized based on function and cellular localization, and include six distinct membrane-type (MT) metalloproteinases that share a transmembrane domain and short cytoplasmic tail . Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP14) is involved in regulating development, angiogenesis, tissue remodeling, and tumor progression . MT1-MMP and other metalloproteinases promote tumor cell invasion by accumulating in specialized structures known as invadopodia, which remodel the ECM and allow tumor cells to breach the basement membrane . The abundance and presence of MT1-MMP at the cell surface is controlled by targeted endocytosis, which may be regulated by the MT1-MMP cytoplasmic domain . MT1-MMP protease activity can be further regulated through homodimer formation, autocatalytic processing, domain shedding and the interaction with inhibitory proteins. Activation of the MT1-MMP proenzyme results from cleavage of full-length MT1-MMP by furin in the trans-Golgi network, which removes the inhibitory propeptide domain . At the cell surface, MT1-MMP can be found in a protein complex with the soluble metalloproteinase MMP2 and the MMP inhibitor TIMP2. MT1-MMP mediated cleavage and activation of MMP2 generates the active MMP2 collagenase, which plays important roles in ECM remodeling and tumor invasion. MT1-MMP interacts with a large number of substrates in addition to MMP2, including interstitial collagens, adhesive glycoproteins (i.e. laminin), and cell surface receptors .

Matrix metalloproteinase-14; MMP-14; MMP-X1; Membrane-type matrix metalloproteinase 1; MT-MMP 1; MTMMP1; Membrane-type-1 matrix metalloproteinase; MT1-MMP; MT1MMP