MMP2 is a member of the Matrix Metalloproteinase (MMP) family, which are involved in extracellular matrix degradation under both normal physiological and disease processes. Specifically, MMP-2 is responsible for degrading collagens type IV, V, VII, and X and gelatin type I. Other reported functions of MMP 2 include angiogenesis, tumor invasion, tissue repair, remodeling of the vasculature, inflammation, and atherosclerotic plaque rupture. MMP-2 secretion is activated by the Ras signaling pathway.
MMP2 triggers cells to begin migration by cleaving laminin-5 and exposing an integrin-binding site on the epithelial basement membrane. The cleaved of laminin has been detected in tumors and in tissues being altered, howver the activated form of MMP2 is not found in benign tumors. Thus, detection of MMP2 is a possible early indicator of tumor activity.
MMP2 is most strongly expressed in normal skin fibroblasts, but may also be found in gliomas, breast and prostate tumors. Mutations in the MMP-2 gene have been linked to Torg-Winchester syndrome, Nodulosis-Arthropathy-Osteolysis (NAO) syndrome, and arthritis. Additionally, abnormal expression of matrix matalloproteinases have been associated with neoplastic traits such as loss of negative growth regulation and high invasive potential.
72 kDa gelatinase , CLG4 , CLG4A72 kDa type IV collagenase , collagenase type IV-A , EC 3.4.24 , EC 126.96.36.199 , Gelatinase A , matrix metallopeptidase 2 (gelatinase A, 72kDa gel, matrix metalloproteinase 2 (gelatinase A, 72kD gel, Matrix metalloproteinase-2 , matrix metalloproteinase-II , MMP-2 , MMP-II , MONA , neutrophil gelatinase , TBE-1matrix metalloproteinase 2 (gelatinase A, 72k