Aliases:This biomarker is also known as:
- Uterine metalloproteinase,
- Pump-1 protease,
- matrix metalloproteinase 7 (matrilysin, uterine),
Proteins of the matrix metalloproteinase (MMP) 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein 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 which localize to chromosome 11q22.3.
There are no datasets associated with this biomarker.
The following organs have data associated with this biomarker…
Matrix metalloproteinases (MMPs) play key roles in tumorigenesis. A recent study has shown that epithelial expression of MMP7 is higher in serous ovarian tumors than mucinous ovarian tumors, stromal expression of MMP7 is higher in serous ovarian tumors, and that alterations in MMP7 have been found in malignant serous ovarian tumors, while benign and borderline ovarian tumors share similar expression profiles.
Of the 28 ovarian cancer biomarkers tested in prediagnostic specimens, from the PLCO, CA125 remains the single best biomarker for ovarian cancer and has its strongest signal within six months of diagnosis. MMP7 alone was not a strong predictor.
|UniProt Accession #:||P09237|
|Mutated Sites Count:||40|
|Associated Pubmed ID Count||10|
|Affected Protein Function Sites Count:||4|