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Background
Matrix metalloproteinase-2 (MMP2) is a Type IV collagenase, 72-kD, which is also known as gelatinase1 and is a member of a group of secreted zinc metalloproteases2. The MMP2 gene is 17 kb long with 13 exons varying in size from 110 to 901 bp and 12 introns ranging from 175 to 4,350 bp 3, located within a region of human chromosome 16q13. In addition,The extra exons encode the amino acids of the fibronectin-like domain which has so far been found in only the 72- and 92-kDa type IV collagenase2. MMP2,which has a critical role in the binding of progelatinase A and TIMP4 via the C-terminal hemopexin-like domain (C domain)5, is functionally associated on the surface of angiogenic blood vessels6. NOT only is a likely effector of endometrial menstrual breakdown4, MMP2 is also effector and regulator of the inflammatory response7. Moreover, MMP2 could be helpful in diagnosing Takayasu arteritis8.