Aliases:This biomarker is also known as:
- matrix metallopeptidase 3 (stromelysin 1, progelatinase),
- Matrix metalloproteinase-3,
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. MMP3 degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. 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…
No additional data available.
Ninety biomarkers were measured using a series of multiplexed immunoassays and results analyzed by the EDRN data management center splitting the cases and controls into training and validation sets, excluding subjects with DCIS or atypical hyperplasia from the training phase. We found little evidence that any of these markers can discriminate women with invasive cancer from those with benign breast conditions.
MMP3 has been shown to be overexpressed in cisplatin-resistant and sensitive ovarian carcinoma cells.
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. MMP3 alone was not a strong predictor.
No associated publications found.
External Resources for MMP3
|UniProt Accession #:||P08254|
|Mutated Sites Count:||99|
|Associated Pubmed ID Count||15|
|Affected Protein Function Sites Count:||5|