MMP-2 Inhibitor I, a hydroxamate-based, long-chain fatty acid, is a reversible inhibitor of matrix metalloproteinase (MMP)-2.
Matrix metalloproteinases (MMPs) have been involved in the degradation of extracellular matrix. MMPs contribute to long-term remodeling processes such as embryogenesis, tumor invasion, inflammation, angiogenesis, and wound healing. MMP-2, also known as gelatinase A or type IV collagenase, has been involved in regulating diverse cellular functions independent of its action on the extracellular matrix, including vascular tone, platelet aggregation, and mediation of the acute mechanical dysfunction of the heart immediately after ischemia and reperfusion [2]. Up-regulation of MMP-2 has been associated with tumor invasion and metastasis [3].
MMP-2 Inhibitor I inhibited the activity of matrix metalloproteinase (MMP)-2 with the Ki value of 1.6 μM [1]. MMP-2 Inhibitor I attenuated cancer cell migration [3]. MMP-2 Inhibitor I had also been used to preserve blood-brain barrier function in a Wistar rat model of pneumococcal meningitis [4].
References:
[1] Berton A, Rigot V, Huet E, et al. Involvement of fibronectin type II repeats in the efficient inhibition of gelatinases A and B by long-chain unsaturated fatty acids[J]. Journal of Biological Chemistry, 2001, 276(23): 20458-20465.
[2] Wang W, Schulze C J, Suarez-Pinzon W L, et al. Intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury[J]. Circulation, 2002, 106(12): 1543-1549.
[3] Emmert-Buck M R, Roth M J, Zhuang Z, et al. Increased gelatinase A (MMP-2) and cathepsin B activity in invasive tumor regions of human colon cancer samples[J]. The American journal of pathology, 1994, 145(6): 1285.
[4] Barichello T, Generoso J S, Michelon C M, et al. Inhibition of matrix metalloproteinases-2 and-9 prevents cognitive impairment induced by pneumococcal meningitis in Wistar rats[J]. Experimental Biology and Medicine, 2014, 239(2): 225-231.