This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
1 Citations 5 Q&As
11 Citations 9 Q&As
5 Citations 9 Q&As
Facts about Macrophage metalloelastase.
Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred in the P1 site, with small hydrophobic residues (preferably alanine) inhabiting P3.
Human | |
---|---|
Gene Name: | MMP12 |
Uniprot: | P39900 |
Entrez: | 4321 |
Belongs to: |
---|
peptidase M10A family |
EC 3.4.24; hME; HMEEC 3.4.24.65; Macrophage elastase; macrophage metalloelastase; matrix metallopeptidase 12 (macrophage elastase); matrix metalloproteinase 12 (macrophage elastase); Matrix metalloproteinase-12; ME; MGC138506; MME; MMP12; MMP-12
Mass (kDA):
54.002 kDA
Human | |
---|---|
Location: | 11q22.2 |
Sequence: | 11; NC_000011.10 (102862736..102874982, complement) |
Found in alveolar macrophages but not in peripheral blood monocytes.
Secreted, extracellular space, extracellular matrix.
This Boster Bio: Best Uses Of The Matrix product will assist you to identify the presence of MMP12 in samples. Its specific primers can help you conduct qPCR tests to aid in MMP12 detection. This product allows you to perform specific tests on the species you are interested in and earn credits. This product is accessible to all scientists around the world. The MMP12 marker can help you discover new diagnostics, treatments as well as drugs for animal and human use and other pertinent information.
It has been challenging to detect MMP12 in the sputum samples. Standard immunoassays do not have sensitivity enough to detect MMP-12. This is due to the fact that MMP-12 can be found in significant amounts of human sputum. To improve the sensitivity of this assay numerous studies have investigated novel inhibitors of MMP-12.
Matrix metalloproteinases (MMP) are a family of zinc-endocrine peptidases that play an essential role in the process of tissue breakdown and remodeling. MMP-12 is involved in the destruction of extracellular matrix (ECM) components of both ill and normal processes. These enzymes favor leucine and hydrophobic residues at the P1 and P3 sites. Some studies have shown that MMP-12 plays an important role in the regulation of other proteins within our bodies, such as pro-inflammatory chemicals and p-proteins.
One of the initial studies of MMP-12 in rodents has demonstrated its role in cigarette smoke-induced emphesyma. This mechanism is thought to be related to the release from macrophages of the TNF-alpha signaling molecule that triggers the activation of neutrophils as well as endothelial cell activation. MMP-12 also secretes matrix-degrading protases. MMP-12 also makes fragments of Elastin that can be chemotactically drawn by monocytes and contribute to the inflammation cascade.
An antibody against MMP-12 may be used to identify MMP-12 within the OLs. The antibody is derived from MMP-12 from human. The antibody is produced against human MMP-12. It inhibits the process of morphological differentiation and results in an increase in the percentage of low-med-low cells. MMP-12 is a vital regulator of the OL lineage. The study was funded by the Multiple Sclerosis Society of Canada and the Alberta Heritage Foundation for Medical Research and the Boster Bio Corporation.
MMP-12 is essential for renal function. It degrades the basement membrane within the glomerular sulcus and bowman's capsule, a process known as glomerular fibrogenesis. In a mouse model of chronic kidney disease, MMP-12 deactivation slowed the macrophage infiltration into the Bowman's capsule, thus protecting mice from glomerular fibrosis.
One of the benefits of using the MMP12 Marker is the ability to quantify MMP activities. MMP-12 activity is one mechanism that helps reduce inflammation, which is one reason for pain. The pain associated with inflammation could also be a sign that there is tissue damaged. MMP-12 activity has been demonstrated in mice to reduce PMN recruitment and LPS in Mmp12/ mice.
Researchers have examined the MMP12 Marker to find premalignant tumors, but it isn't yet established whether this marker is a reliable indicator of OSCC. Researchers discovered that saliva MMP-12 expression was significantly greater in oral squamous cells cancer patients than in healthy volunteers. This study suggests that it could be a helpful indicator of extracapsular cancers of the neck and head.
The MMP-12 marker has been proved to be extremely effective in diagnosing inflammatory conditions. The immune system has many roles for the MMPs which are produced by macrophages. They play a role in modulating the immune system by processing chemokines and increasing neutrophil migration. They also serve as a crucial biomarker to determine the presence of the existence of new drug targets.
A study on mice revealed that MMP12 was an atherosclerosis-related candidate gene. In these mice, the expression of MMP12 correlates with elastin breakdown. While further research is needed to determine the role MMP12 is involved in human diseases however, the MMP12 marker could prove to be an effective tool for the identification of patients who might benefit from MMP12 inhibitors. In the near future, more studies on the MMP12 Marker will be able to assist healthcare professionals better understand the mechanisms of atherosclerosis.
Another study showed that MMP-12 levels in smokers were higher in smokers than those who had healthy oral habits. Smokeless tobacco and betelnut consumers had significantly higher MMP-12 levels in their saliva than smokers. Both groups had significantly different MMP-12 levels. The MMP-12 Marker can be used to determine oral health.
The MMP12 gene is a crucial mediator in the process of regulating the homeostasis of vascular blood. It is responsible for the remodeling of endothelial cells. MMP-12 has been the subject of very few studies. The enzyme is found in many tissues, and its presence could indicate an unidentified mediator. For tests using qPCR, it is crucial to use specific primers that target the MMP-12 gene.
To conduct quantitative PCR, we employed the QuantiTect SYBR Green PCR kit which we purchased from Qiagen, Ltd., and the Roche LightCycler 480. The primers were developed using denaturation curve analysis using the National Center for Biotechnology Information's web-based tool, and then purchased from Sigma. The PCR test was repeated to ensure the quality of the data.
TRIzol was used to extract total RNA from the liver tissues. Then we synthesized cDNA using 2 ug of pure total RNA. Then, we conducted an RT-qPCR using a particular primer set that contained MMP12 and GAPDH as an internal control. Our results showed that MMP-12 is expressed by cancerous cells in a variety of tissues and has antitumor capabilities in gastric, esophageal and skin tumors.
The RXP470.1 probe binds with the catalytic domain of the human MMP-12. They also have different colors of fluorescent that indicate their specificity for MMP-12. The probes were found be stable in PBS or mouse blood for as long as four hours at 37°C. The RXP470-derived probe 1 is able to maintain its interactions established by the parent molecule.
HCC tumor tissue contains significantly higher levels of MMP12 than normal tissues. HCC patients with high levels of MMP12 have had lower survival rates. This link isn't recognized. However, MMP12 protein is found in the nucleus of cancer cells. Further research is required to determine the molecular mechanism which are the basis for HCC progression.
We verified the MMP-12 human expression results using specific primers for qPCR using the MMP12 gene. MMP-12 expression was significantly more in the proinflammatory GM–MPh, compared to in M–MPh. MMP-14 and MMP-12 had the same expression levels. You should be cautious when selecting the primers used to qPCR MMP12 markers. The two primers could have very distinct effects.
MMP12 is a crucial player in the endothelial cell's life cycle and has many therapeutic applications. It is a major player in the regulation of vascular homeostasis and could be a novel mediator. Additionally, MMP-12 exerts an inhibitory effect on PIK3R1.
In addition to its role in cancer, MMP12 is implicated in non-small-cell lung cancer, skin cancer ovarian cancer, esophageal Squamous Cell Carcinoma and pancreatic cancer. While more research is needed to determine if MMP12 is connected to these diseases but it is a major player in a variety of clinical contexts. It is a determinant marker for many cancers, including HCC and ovarian cancer.
Hepatocellular carcinoma is a very common type of cancer. It is extremely deadly and can cause metastasis or it can recur. More research is needed on the molecular mechanisms involved in understanding how this disease develops. The use of immunohistochemical staining to determine if MMP12 was involved in the progression HCC. MMP12 mRNA expression was detected in 42 pairs of human liver tissue collected from patients suffering from HCC following surgery. In addition, the expression of the forkhead-box P3 (Forkhead box) was also identified in these samples.
Recent research has revealed that the plasma level of MMP-12 was linked to stiffness of the vascular wall. Researchers have linked MMP-12 to impaired renal function and ageing. These findings suggest that MMP-12 may be a novel biomarker to monitor the development of cardiovascular disease. These findings have implications for health care. There are currently several other clinical applications for MMP-12, including cardiovascular disease. MMP-12 is also linked to many diseases including stroke.
The higher levels of MMPs have been associated with an increased risk of CVD. MMP-12 levels were also linked to an increased risk of ischemic and cardiovascular events in Malmo Diet subjects and Cancer subjects. These findings suggest that MMP-12 could be a potential cardiovascular risk indicator for patients with CKD. More clinical studies must examine the role of MMP-12 in determining the risk of major adverse cardiovascular events.
PMID: 8226919 by Shapiro S.D., et al. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages.
PMID: 9115292 by Gronski T.J. Jr., et al. Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase.
*More publications can be found for each product on its corresponding product page