| Primary Identifier | IPR028708 | Type | Family |
| Short Name | 72kDa_collagenase |
| description | 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 []. 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 []. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages []. 72kDa type IV collagenase, also known as 72kDa gelatinase or matrix metalloproteinase-2 (MMP2; MEROPS identifier M10.003), is a ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumour invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction [, ]. PEX, a naturally occurring fragment of human MMP2, acts as an inhibitor of cell proliferation, migration, and angiogenesis [, ]. |
