Matrix metalloproteinase-15 (IPR028729)
Short name: MMP15
Overlapping homologous superfamilies
- Peptidase M10A (IPR021190)
- Matrix metalloproteinase-15 (IPR028729)
Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). They degrade most components of the extracellular matrix (such as growth factors, their binding proteins, and other bioactive molecules, as well as binding sites for cell-surface molecules) and some non-extracellular-matrix molecules [PMID: 12801404]. Two categories of MMPs can be recognised based on their cellular localisation: soluble vs. membrane-bound. The soluble MMPs are divided into the collagenases (MMP1, MMP8 and MMP13), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP12) and those yet to be classified. The membrane-bound MMPs include MT1, 2, 3, 4, 5 and their hallmark is the presence of plasma membrane anchoring domains [PMID: 12027585]. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages [PMID: 12801404].
Matrix metalloproteinase-15 (MMP15; MEROPS identifier M10.015) or membrane-type matrix metalloproteinase 2 degrades various components of the extracellular matrix [PMID: 7559440, PMID: 9461298]. The increase expression of MMP15 has been linked to cancer progression [PMID: 22998427].
- PTHR10201:SF25 (PTHR10201:SF25)