Matrix Metalloproteinase (MMP) Inhibitors
A metalloproteinase is any protease enzyme whose catalytic mechanism depends on the presence of a metal ion coordinated between different ligands. There are two sub categories of metalloproteinases: Exo-metalloproteinase (cleaves the peptide bond of a terminal amino acid) and Endo-metalloproteinase (cleaves a non-terminal/internal peptide bond within a protein). Matrix metalloproteinases (MMPs) fall in the latter category and are Zinc-dependent enzymes. They are part of the Metzincin superfamily of enzymes. The most common classification used by researchers in MMP biology is based on the putative substrate specificity of the MMP and their cellular localization. These groups are the collagenases, the gelatinases, the stromelysins, and the membrane-type MMPs (MT-MMPs).
MMPs are capable of degrading a large ensemble of extracellular matrix proteins and many bioactive molecules. They can cleave peptide bonds within cell surface receptors resulting in the release of apoptotic ligands (like FAS), and chemokine/cytokine in/activation. MMPs are also thought to play a major role in regulating cellular events such as proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense mechanisms. They are vital to tissue remodeling associated with various processes in normal physiology and in pathological conditions: morphogenesis, angiogenesis, tissue repair, cirrhosis, arthritis, and metastasis.
The MMPs can be inhibited by specific endogenous tissue inhibitor of MMPs (TIMPs): TIMP-1, 2, 3, and 4. Synthetic inhibitors are based on metal chelation and typically bind the catalytic zinc atom at the MMP active site tightly preventing enzyme activity. Doxycycline is an MMP inhibitor used for treatment of periodontal disease. BioVision offers a wide selection of MMP inhibitors in its product portfolio.
