Product Sheet CL0463
Description
BACKGROUND MMPs (matrix metalloproteinases) are zinc-dependent endopeptidases that are mainly involved in turnover and proteolytic degradation of the extracellular matrix and are believed to play a role in tissue remodeling in a number of normal and pathological conditions. MMPs may play a key role in physiologic and pathologic remodeling of tissues, including embryogenesis and tissue morphogenesis, wound repair, inflammatory diseases, cancerogenesis, etc. These multiple actions of MMPs are due to their ability to degrade extracellular matrices, basement membranes, and other proteins. So far, more than 25 members of the MMP family have been identified, and they can be divided into four groups on the basis of their domain structure, substrate specificity and cellular localization. These four groups are collagenases (MMP-1, -8 and -13), stromelysins (MMP-3, -7, -10, -11 and -12), gelatinases (MMP-2 and -9) and membrane-type MMPs.1
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
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
REFERENCES
1. Chakraborti, S. et al: Mol Cell Biochem. 253:269-85, 2003
2. Ii, M. et al: Exp. Biol. Med. 231:20-7, 2006
3. Strand, S. et al: Oncogene 23:3732-6, 2004
4. McLennan, S.V. et al: Kidney Int. 72:481-488, 2007
2. Ii, M. et al: Exp. Biol. Med. 231:20-7, 2006
3. Strand, S. et al: Oncogene 23:3732-6, 2004
4. McLennan, S.V. et al: Kidney Int. 72:481-488, 2007
Products are for research use only. They are not intended for human, animal, or diagnostic applications.
(Click to Enlarge) Matrix Metalloproteinase 7 (MMP-7, Matrilysin, PUMP-1 Protease) Standard Curve: Using the human MMP-7 ELISA Kit, O.D. data was graphed against MMP-7 protein concentration. The TMB reaction was incubated at 37°C for 25 min.
Details
Cat.No.: | CL0463 |
Target Protein Species: | Human |
Range: | 156pg/ml – 10000pg/ml |
Specificity: | no detectable cross-reactivity with any other cytokine. |
Storage: | Store at 4°C. Use within 6 months. |
ELISA Kits are based on standard sandwich enzyme-linked immunosorbent assay technology. Freshly prepared standards, samples, and solutions are recommended for best results.
Products
| Product | Size | CAT.# | Price | Quantity |
|---|---|---|---|---|
| Human MMP-7 ELISA Kit: Human Matrix Metalloproteinase-7 ELISA Kit | Size: 96 Wells | CAT.#: CL0463 | Price: $500.00 |