Background:

MMP Inhibitor II is a potent, reversible and broad-range inhibitor of matrix metalloproteinases (MMPs) with IC50 values of 24 nM, 18.4 nM, 30 nM and 2.7 nM for MMP-1, MMP-3, MMP-7 and MMP-9, respectively [1].

MMPs belong to a family of at least fifteen secreted and membrane-bound zinc-endopeptidases. MMPs have been engaged in several pathological processes, including tumor growth and metastasis, arthritis, multiple sclerosis, and periodontal disease. These enzymes play a vital role in tissue repair and remodeling via degrading all the extracellular matrix components, including fibrallar and non-fibrallar collagens, laminin, fibronectin, and basement membrane glycoproteins, which enables cell migration. In addition, MMPs exert function in metastasis by promoting tumor invasion and angiogenesis. It was shown that the expression of various members of the MMP family by tumors is closely associated with their proliferative and invasive behavior and metastatic potential. Furthermore, MMPs are broadly sub-divided into three classes: stromelysins, gelatinases, and collagenases, which are secreted in a proenzyme form and require activation to digest an extracellular matrix [1].

In vitro: Up to now, in vitro study of MMP Inhibitor II is still in the development stage.

In vivo: Up to now, in vivo study of MMP Inhibitor II is still in the development stage.

Reference:
[1].  Slawomir M. Wojtowicz-Praga, Robert B. Dickson and Michael J. Hawkins. Matrix metalloproteinase inhibitors. Investigational New Drugs. 1997; 15: 61–75.