Matrix metalloproteinase-25 (IPR028733)
Short name: MMP25
Overlapping homologous superfamilies
- Metallopeptidase, catalytic domain superfamily (IPR024079)
- Peptidase M10A (IPR021190)
- Matrix metalloproteinase-25 (IPR028733)
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-25 (MMP25; MEROPS identifier M10.024) or membrane-type matrix metalloproteinase 6 (MT6-MMP) is, as well as MT4-MMP, a glycosyl-phosphatidyl inositol (GPI)-anchored MMP [PMID: 11034316]. It may facilitate tumour progression through its ability to activate progelatinase A [PMID: 10706098] and may be part of the leukocytes proteolytic arsenal during inflammatory responses [PMID: 10628838].
- PTHR10201:SF142 (PTHR10201:SF142)