MMP-7 ELISA Kit, Human

Matrilysin/MMP-7 is distinguished from other MMP family members as being the smallest member containing only the common catalytic domain and Zn²⁺ binding region, but lacking the haemopexin-like domain common to other MMPs. Along with its prometastatic function, a fundamental role for MMP-7 has also been established in early tumour development. Ablation of MMP-7 in a mouse model for intestinal cancer reduced tumour formation by 67%. On the other hand, overexpression of MMP-7 in MMTV-neu mice, a mouse model for mammary tumorigenesis, significantly promoted tumour development in mammary glands. Tumorigenesis is a multistep process involving cell growth, invasion, metastasis, and angiogenesis. MMP-7 has been shown to play important roles not only in degradation of ECM proteins, but also in the regulation of several biochemical processes such as activation, degradation, and shedding of non-ECM proteins. Proteolysis of insulin-like growth factor binding protein by MMP-7 results in increased bioavailability of insulin-like growth factors and enhanced cellular proliferation.² MMP-7 has also been implicated in the ectodomain shedding of several cell surface molecules. Heparin-binding epidermal growth factor precursor (proHB-EGF) is cleaved by MMP-7 into mature HB-EGF, which promotes cellular proliferation. Membrane-bound Fas ligand (FasL) is cleaved into soluble FasL, which increases apoptosis of cells adjacent to tumor cells.³ E-cadherin is converted to soluble E-cadherin to promote invasion. Tumor necrosis factor (TNF)-alpha precursor is cleaved to release soluble TNF-alpha to increase apoptosis. It is suggested that these matrilysin-mediated pathways provide the necessary and logical mechanisms to promote cancer progression. In addition, it has been revealed that MMP-7 also plays an essential role in innate immunity, and, more particularly, in inflammatory disorders. Although MMP-7 may be expressed at low levels by noninjured, noninflamed mucosal epithelia in many adult human tissues, its expression is increased in injured epithelium of gastrointestinal tract and lung. For example, MMP-7 is prominently expressed by airway and alveolar epithelium in a variety of human lung diseases, such as cystic fibrosis and pulmonary fibrosis. However, the diminished expression of MMP-7may play a role in fibronectin accumulation in the diabetic kidney in response to AGEs and/or TGF-beta.⁴