1. Dynamic Changes in Matrix Metalloprotienase Activity Within the Human Myocardial Interstitium During Myocardial Arrest and Reperfusion by Francis G. Spinale, Christine N. Koval, Anne M. Deschamps, Robert E. Stroud, and John S. Ikonomidis Circulation Volume 118(14 suppl 1):S16-S23 September 30, 2008 Copyright © American Heart Association, Inc. All rights reserved.

2. Figure 1. A, Validation of the MMP fluorogenic substrate (0.03 mmol/L, Anaspec, #27074) was performed by using increasing concentrations of an MMP 2/9 recombinant catalytic domain (BIOMOL, SE-237, SE-244). Francis G. Spinale et al. Circulation. 2008;118:S16-S23 Copyright © American Heart Association, Inc. All rights reserved.

3. Figure 2. In order to further examine the specificity of the MMP substrate (0.03 mmol/L) was incubated in the presence of (A) a disintegrin and metalloprotease, ADAM-17 (1.25 μg/mL, R&D Systems, #930-ADB), or (B) with the serine protease plasmin (1.25 μg/mL, Sigma, #P1867) and fluorescence emission continuously monitored at 37°C. Francis G. Spinale et al. Circulation. 2008;118:S16-S23 Copyright © American Heart Association, Inc. All rights reserved.

4. Figure 3. A, Representative continuous fluorescence recording of myocardial interstitial fluid from a patient undergoing coronary bypass surgery requiring CPB and myocardial arrest. Francis G. Spinale et al. Circulation. 2008;118:S16-S23 Copyright © American Heart Association, Inc. All rights reserved.

5. Figure 4. Using the in vitro calibration curve generated from known MMP catalytic activity as shown in Figure 1, interstitial MMP activity was computed at the midpoint of the myocardial arrest period and at the myocardial reperfusion period, before microdialysis probe removal. Francis G. Spinale et al. Circulation. 2008;118:S16-S23 Copyright © American Heart Association, Inc. All rights reserved.