Matrix metalloproteinase-3 (MMP-3), also known as stromelysin-1, is a critical enzyme involved in tissue remodeling and repair through its role in degrading extracellular matrix proteins, facilitating cell migration. This enzyme has been implicated in various physiological processes including vascular remodeling associated with aneurysm formation, wound healing, the progression of atherosclerosis, and tumor initiation. MMP-3 inhibitor VIII, a cell-permeable sulfonamide-based hydroxamic acid, effectively inhibits MMP-3 by binding to its active site (Ki = 23 nM), thus blocking its enzymatic activity. Additionally, this inhibitor has been demonstrated to suppress the activity of mouse macrophage metalloelastase MME MMP-12, with an IC50 value of 13 nM, highlighting its potential utility in research on tissue remodeling and disease processes involving MMPs.
UK-370106 is a potent and highly selective inhibitor of MMP-3 with IC50 of 23 nM and MMP-12 with IC50 of 42 nM, and potently inhibits cleavage of [3H]-fibronectin by MMP-3 (IC50: 320 nM).
CMC2.24 (TRB-N0224) is an orally active tricarbonylmethane agent that demonstrates effectiveness in inhibiting Ras activation and the downstream effector ERK1 2 pathway, thus effectively combating pancreatic tumor formation in mice. Additionally, CMC2.24 exerts potent inhibitory effects on zinc-dependent MMPs, with IC50s ranging from 2.0-69 μM. Furthermore, CMC2.24 aids in alleviating the progression of osteoarthritis by restoring cartilage homeostasis and inhibiting chondrocyte apoptosis through the NF-κB HIF-2α axis[1][2][3].