MMP-7

Official Full Name

matrix metallopeptidase 7

Organism

Homo sapiens

GeneID

4316

Background

This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature protease. This secreted protease breaks down proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal hemopexin domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes on chromosome 11. This gene exhibits elevated expression levels in multiple human cancers. [provided by RefSeq, Jan 2016]

Synonyms

MMP-7; MPSL1; PUMP-1;

Bio Chemical Class

Peptidase

Protein Sequence

MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK

Open

Disease

Brain cancer, Kaposi sarcoma, Lung cancer, Pancreatic cancer, Prostate cancer, Solid tumour/cancer

Approved Drug

1 +

Clinical Trial Drug

1 +

Discontinued Drug

3 +

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Detailed Information

MMP-7, also known as matrix lysin, is a secreted protein. The human MMP-7 gene is located at 11q21~q22, and its cDNA is 1 094 bp long and encodes 267 amino acids. MMP-7 has the smallest molecular mass in the MMPs family, and the zymogen form has a molecular mass of 28 ku. When activated, it produces an active enzyme with a molecular mass of 19 ku, which is mainly expressed in epithelial-derived cells and secreted as a zymogen. MMP7 retains four MMPs characteristic regions, lacking the C-terminal heme-binding protein homologous region, which is less negatively regulated by MMP inhibitors. After activation, it participates in the degradation of most components of extracellular matrix and basement membrane, so MMP- 7 has strong matrix degradation activity and broad substrate specificity. Studies have shown that membrane proteins blocked by MMP-7 include integrin β4, tumor necrosis factor alpha, multi-ligand proteoglycan-1 and E-cadherin. MMP-7 can be expressed in the pathological and physiological processes of a variety of tissues, but is mainly expressed in the stroma of certain tumor cells or tumor infiltrating margins.

Figure 1. MMP-7, which is expressed upon β-catenin activation, mediates EMT through the following 3 pathways. (Ben, K., et al. 2017)

MMP-7 and Tumor

MMP-7 is highly expressed in esophageal cancer, and the expression of MMP-7 in advanced esophageal cancer is significantly higher than that in early esophageal cancer. The positive expression rate of MMP-7 in gastric cancer tissues was 68.8%. The expression site was mainly in deep cancer nests, especially in front of infiltration. The expression of MMP-7 at the infiltrating front was more accurately represented by tumor infiltration activity and expression level. It increases with the increase of infiltration depth, and its increased expression can promote the progression of gastric cancer. Therefore, analysis of the expression of MMP-7 in gastric cancer provides a new target for the treatment of gastric cancer. Synthetic MMP inhibitors are potential treatment options, laying the foundation for the use of broad-spectrum or selective MMP inhibitors.

The positive expression rate of MMP-7 in pancreatic cancer tissues was 63.8%, but it was negative in normal pancreatic tissues. Studies have shown that the effects of mesothelin (MSLN), cancer antigen125/mucin16 (CA125/MUC16) and over-regenerative gene family member 4 (REG4) on pancreatic cancer cell invasion and metastasis are produced by the activation mechanism of MMP-7. In the invasion of pancreatic cancer cells, MMP-7 and epidermal growth factor receptor-mediated activation of the MEK-ERK signal transduction pathway form a positive feedback loop. The positive rate of MMP-7 expression in renal cell carcinoma was 55.1%, but there was almost no expression in normal renal tissues. It is believed that the high expression of MMP-7 in renal cell carcinoma is closely related to the occurrence and development of tumor.

MMP-7 Promotes Tumor Cell Invasion and Metastasis

MMP-7 has broad substrate specificity and promotes cancer cell invasion and metastasis by proteolytic cleavage of extracellular matrix and basement membrane proteins. MMPs are expressed in vascular endothelial cells adjacent to tumor cells, suggesting that they may be involved in the process of tumor angiogenesis. MMP-7 has been shown to accelerate proliferation in human umbilical vein endothelium in a dose-dependent manner in vitro. Other studies have shown that MMP-7 and vascular endothelial growth factor (VEGF) are synergistically expressed in vascular endothelial cells of tumor cells. VEGF alters the activated form of endothelial cells, enhances the release of MMP-7, and accelerates degradation of the substrate and migration of endothelial cells. These findings suggest that MMPs directly promote angiogenesis, at least in part through the proliferation of vascular endothelium.

References:

Ben, K. , Chuqiao, F. , Liping, Y. , & Xiangdong, F. . (2017). Matrix metalloproteinases-7 and kidney fibrosis. Frontiers in Physiology, 8.
Bauer, Y. , White, E. S. , De Bernard, S. , Cornelisse, P. , Leconte, I. , & Morganti, A. , et al. (2017). Mmp-7 is a predictive biomarker of disease progression in patients with idiopathic pulmonary fibrosis. ERJ Open Research, 3(1), 00074-2016.
Taniguchi, M. , Matsuura, K. , Nakamura, R. , Kojima, A. , Konishi, M. , & Akizawa, T. . (2017). Mmp-7 cleaves amyloid β fragment peptides and copper ion inhibits the degradation. BioMetals.

Quick Inquiry

Interested in learning more?

Contact us today for a free consultation with the scientific team and discover how Creative Biogene can be a valuable resource and partner for your organization.

Request a quote today!

Inquiry