Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases. MMPs mainly target components of the extracellular matrix (ECM). Over 24 distinct MMPs have been identified in humans, and these MMPs have been classified into six groups: collagenases, gelatinases, stromelysins, matrilysin, and two membrane binding MMPs (MT-MMPs). MMPs are directly involved in several biological and physiological processes, such as in the release of signaling molecules, repair of wounds, and new formation of new blood vessels. Previous research revealed that MMPs are involved in cancer, including in metastasis and abnormal angiogenesis. Therefore, MMPs have been considered to be targets for anti-cancer drugs, and hundreds of MMP inhibitors (MMPi) have been reported over the last several decades. Unforunately, none of these MMPi's has demonstrated suitable specificity, selectivity, and/or efficacy to be considered as viable drugs. The goal of our MMP project is to develop MMPi's that are specific to MMPs and selective towards a specific MMP. To achieve this goal, we are characterizing a representative MMP from each of the distinct MMP subclasses. We are using mechanistic and spectroscopic studies to identify differences in the MMPs, and we will target these differences in future MMPi design efforts. The catalytic subunit of MMP16 has been cloned, over-expressed, and purified. The biochemical, kinetic, and spectroscopic properties of the recombinant enzyme will be reported, and initial inhibition studies will be presented.

Characterization of matrix metalloproteinase 16 (MMP-16)

246th National Meeting (2013)

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