Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological and pathological processes such as morphogenesis, differentiation, angiogenesis, tissue remodeling, and tumor invasion. A typical MMP consists of a pro-peptide of about 80 amino acids, a catalytic metalloproteinase domain of about 170 amino acids, a linker peptide of variable lengths and a hemopexin domain of about 200 amino acids. The zinc binding motif HEXXHXXGXXH in the catalytic domain, and the ‘‘cysteine switch’’ motif PRCGXPD in the pro-peptide are common structural signatures. MMP-7, Matrilysin, is one of the smallest members of the MMP family consisting of a pro-peptide domain and a catalytic domain. It can degrade casein, laminin, fibronectin, collagen type III/IV/V/IX/X/XI, gelatin type I/II/IV/ V, elastin, and proteoglycans. MMP-7 is secreted specifically by epithelial cells and its over-expression has been observed in many tumor types such as colorectal cancer, epidermolysisbullosa associated skin cancer, bladder cancer, gastric cancers, pancreatic cancer and esophageal cancer. This enzyme serves essential functions in both innate defense and wound healing, and appears to be one of the most important MMPs in human colon cancers. It has been reported that MMP-7 contributes to tumor malignancy probably by cleaving cell surface proteins such as Fas ligand (reducing its effectiveness in triggering Fas-mediated apoptosis) and E-cadherin (disruption to the E-cadherin/beta-catenin complex results in a switch to a more invasive phenotype in cancer cells). In addition, degradation of IgG by MMP-7 may protect tumor cells from the immune system, since cleavage of IgG will remove much of the immunoglobulins' functionality.