Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-14 (MT1-MMP), membrane-type MMP, plays an important role in tumor invasion. MMP-14 is expressed on the surface of invasive tumor cells, in stromal cells of human colon, breast, and head and neck carcinomas. MMP-14 is secreted as zymogen with a prodomain, a catalytic domain, a hinge region, a hemopexin-like domain, and a transmembrane domain. It can activate pro-MMP-23 and degrade a variety of substrates, including fibrillar collagens I, II, III, fibronectin, vitronectin and laminin-1.
A truncated human MMP-14 with His-tag was expressed in E. coli. The Mr on SDS-PAGE is 31-kDa. Incubation with 1 mM APMA at 37°C for 2 hr will activate MMP-14. Its activity can be measured by FRET peptides