MMP7
MMP7 (matrix metallopeptidase 7), also called matrilysin, PUMP-1 or MPSL1, is a secreted zinc-dependent protease of the matrix metalloproteinase family. It degrades extracellular matrix components and activates procollagenase. Browse Assay Genie's current range of MMP7 research reagents below, or read on for the biology behind the target.
MMP7 is a secreted protease that breaks down components of the extracellular matrix. Reported substrates include casein, gelatins of types I, III, IV and V, fibronectin, proteoglycans and elastin. It also activates procollagenase, placing it upstream of other matrix-degrading activity. The enzyme is made as a preproprotein that is proteolytically processed to give the mature protease. It differs from most MMP family members because it lacks the conserved C-terminal hemopexin domain.
The MMP7 gene encodes a member of the peptidase M10 family, in the M10A subfamily of matrix metalloproteinases, and sits within a cluster of MMP genes on chromosome 11. The protein is found in the extracellular space and extracellular matrix. Mouse and rat both carry an Mmp7 ortholog, and studies in mice suggest the enzyme regulates the activity of defensins in intestinal mucosa. It has also been implicated in wound healing.
Matrix metalloproteinases take part in normal processes such as embryonic development, reproduction and tissue remodelling, and in disease processes such as arthritis and metastasis. The MMP7 gene shows elevated expression in multiple human cancers. Its previous HGNC name was matrix metalloproteinase 7 (matrilysin, uterine), and HGNC also places it in the elastase gene group. Researchers studying MMP7 protein levels or MMP7 gene expression often do so in the context of matrix remodelling and tumour biology.
MMP7 expression is elevated in multiple human cancers, making it a focus for studies of tumour progression and metastasis.
MMP7 degrades fibronectin, gelatins, proteoglycans and elastin, so it is used to study matrix breakdown in tissue remodelling.
The enzyme is involved in wound healing, and its activity is relevant to repair processes.
Mouse studies suggest MMP7 regulates defensin activity in intestinal mucosa, supporting work on mucosal defence.
MMP7 is a secreted matrix metalloproteinase that degrades casein, fibronectin, gelatins of types I, III, IV and V, proteoglycans and elastin. It also activates procollagenase. It contributes to extracellular matrix breakdown in development, reproduction, tissue remodelling and wound healing.
MMP7 is also known as matrilysin, PUMP-1 and MPSL1. Its earlier HGNC name was matrix metalloproteinase 7 (matrilysin, uterine). The encoded preproprotein is proteolytically processed to give the mature protease, and the enzyme carries the EC number 3.4.24.23.
Mouse and rat both have an Mmp7 ortholog, and mouse studies point to a role in regulating defensins in intestinal mucosa. MMP7 expression is elevated in multiple human cancers, and the MMP family is linked to arthritis and metastasis. Check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases, including collagenases, gelatinases, stromelysins and membrane-type MMPs, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P09237; product specifications from Assay Genie datasheets.