MMP-2 (matrix metalloproteinase 2), also known as Gelatinase A, is upregulated at sites of tissue damage, inflammation, and in stromal cells surrounding the invading front of metastatic tumors. The latent proenzyme (proMMP-2) is activated by MT-MMPs, Thrombin, or activated Protein C. Mature MMP-2 activity is inhibited by alpha 2-Macroglobulin or TIMPs 1, 2, 3, and -4. TIMP-2 and -3 can also tether proMMP-2 into cell surface ternary complexes with MT-MMPs. MMP-2 degrades Gelatin (denatured Collagen) and type IV Collagen, the major component of basement membranes. It can also degrade the matrix proteins Collagens V, VII and X, Decorin, Elastin, and Fibronectin. MMP-2 processes and modulates the functions of many other vasoactive and proinflammatory molecules including Adrenomedullin, Big Endothelin-1, Calcitonin gene-related peptide, CCL7/MCP-3, CXCL12/SDF-1, Galectin-3, IGFBP-3, IL-1 beta, S100A8, and S100A9.