Matrix Metalloproteinase-14 (MMP-14), also known as MT1-MMP (Membrane-Type 1 Matrix Metalloproteinase), is a member of the matrix metalloproteinase (MMP) family. These enzymes are involved in the breakdown of extracellular matrix (ECM) components, playing crucial roles in various physiological and pathological processes, including tissue remodeling, embryonic development, and disease progression such as cancer metastasis .
MMP-14 is a membrane-anchored zinc-binding endopeptidase. Unlike most MMPs, which are secreted as inactive proenzymes and activated extracellularly, MMP-14 is tethered to the cell surface via a transmembrane domain . This localization is essential for its function in pericellular proteolysis, where it degrades ECM components such as collagen .
One of the key roles of MMP-14 is the activation of progelatinase A (MMP-2), which further contributes to ECM degradation. This activity is particularly important in processes like tumor invasion, where MMP-14 facilitates the breakdown of ECM barriers, allowing cancer cells to invade surrounding tissues .
Recombinant MMP-14 (Human, His Tag) is a form of the enzyme produced through recombinant DNA technology. This involves inserting the gene encoding MMP-14 into a host organism, such as bacteria or yeast, which then expresses the protein. The “His Tag” refers to a sequence of histidine residues added to the protein to facilitate purification using affinity chromatography .
MMP-14 has been implicated in several pathological conditions. Overexpression of MMP-14 is often observed in various cancers and is associated with increased tumor invasiveness and poor prognosis. Additionally, deficits in MMP-14 activity have been linked to conditions such as Winchester syndrome and multicentric osteolysis-nodulosis-arthropathy spectrum .