Target Name: MMP11
NCBI ID: G4320
Review Report on MMP11 Target / Biomarker Content of Review Report on MMP11 Target / Biomarker
MMP11
Other Name(s): ST3 | STMY3 | matrix metallopeptidase 11 (stromelysin 3) | MMP-11 (Stromelysin 3) | matrix metallopeptidase 11 | MMP11 variant 1 | MMP-11 | stromelysin III | MMP11_HUMAN | Matrix metallopeptidase 11, transcript variant 1 | Stromelysin III | Stromelysin-3 | SL-3 | Stromelysin 3 | Matrix metalloproteinase-11

MMP11: A Potential Drug Target for Various Diseases

MMP11 (Mucinases and equine enolase 11) is a protein that is expressed in various cell types of the body, including epithelial, prostatic, and uterine surfaces. It is a member of the equine enolase family 11 (MMP) and is involved in the degradation of extracellular matrix (ECM) components, such as cadherins, laminins, andvimentin. MMP11 has been identified as a potential drug target and a biomarker for various diseases, including cancer, urolithiasis, and wound healing.

The MMP11 gene was first identified in the late 1990s by researchers at the University of California, San Diego (UCSD) as a gene that was expressed in various tissues and was involved in the regulation of cell adhesion. Subsequently, studies have shown that MMP11 is involved in the degradation of ECM components, including cadherins, laminins, and vimentin. These ECM components are critical for cell-cell and cell-tissue interactions and are often used as biomarkers for various diseases.

One of the key functions of MMP11 is its role in cell-cell adhesion. MMP11 is involved in the formation of tight junctions, which are a type of cell-cell adhesion that helps to maintain tissue structure and prevent the loss of cells. MMP11 has has been shown to be involved in the regulation of tight junction formation and has been linked to various diseases, including cancer.

In addition to its role in cell-cell adhesion, MMP11 is also involved in the degradation of extracellular matrix (ECM) components. ECM components are complex structures that are involved in the regulation of cell behavior and are composed of a variety of proteins, including cadherins, laminins, and vimentin. MMP11 is shown to be involved in the degradation of these ECM components, which is important for maintaining tissue structure and promoting wound healing.

MMP11 has also been identified as a potential drug target for various diseases, including cancer, urolithiasis, and wound healing. For example, studies have shown that MMP11 is overexpressed in various types of cancer, including breast, ovarian, and prostate cancer. This overexpression is thought to contribute to the development and progression of these diseases. In addition, MMP11 has also been shown to be involved in the regulation of wound healing and has been used as a biomarker for this process.

In conclusion, MMP11 is a protein that is involved in the degradation of ECM components and has been identified as a potential drug target for various diseases. Its role in cell-cell adhesion and its involvement in the regulation of ECM components make it an attractive target for small molecule inhibitors. Further research is needed to fully understand the role of MMP11 in these diseases and to develop effective treatments.

Protein Name: Matrix Metallopeptidase 11

Functions: May play an important role in the progression of epithelial malignancies

The "MMP11 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about MMP11 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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MMP12 | MMP13 | MMP14 | MMP15 | MMP16 | MMP17 | MMP19 | MMP2 | MMP2-AS1 | MMP20 | MMP20-AS1 | MMP21 | MMP23A | MMP23B | MMP24 | MMP24-AS1-EDEM2 | MMP24OS | MMP25 | MMP25-AS1 | MMP26 | MMP27 | MMP28 | MMP3 | MMP7 | MMP8 | MMP9 | MMRN1 | MMRN2 | MMS19 | MMS22L | MMS22L-TONSL complex | MMUT | MMXD complex | MN1 | MNAT1 | MND1 | MNDA | MNS1 | MNT | MNX1 | MNX1-AS1 | MOAP1 | MOB1A | MOB1B | MOB2 | MOB3A | MOB3B | MOB3C | MOB4 | MOBP | MOCOS | MOCS1 | MOCS2 | MOCS2-DT | MOCS3 | MOG | MOGAT1 | MOGAT2 | MOGAT3 | MOGS | MOK | MON1A | MON1B | MON2 | Monoamine oxidase (MAO) | Monoamine Transporter (MAT) | MORC1 | MORC2 | MORC2-AS1 | MORC3 | MORC4 | MORF4 | MORF4L1 | MORF4L1P1 | MORF4L1P3 | MORF4L1P7 | MORF4L2 | MORF4L2-AS1 | MORN1 | MORN2 | MORN3 | MORN4 | MORN5 | MOS | MOSMO | MOSPD1 | MOSPD2 | MOSPD3 | MOV10 | MOV10L1 | MOXD1 | MOXD2P | MPC1 | MPC2 | MPDU1 | MPDU1-AS1 | MPDZ | MPEG1 | MPG | MPHOSPH10