Matrix metalloproteinases are less essential for the in-situ gelatinolytic activity in heart muscle than in skeletal muscle.

In order to determine whether the contribution of matrix metalloproteinases (MMPs) to the tissue gelatinolytic activity is similar between myocardium and skeletal muscle tissue, in-situ zymography was applied to myoblasts originated from myocardium or skeletal muscle of rodents as well as tissue sections of heart and soleus muscles of rats. Gelatinolyic activity was observed in cytoplasm and nucleus of both heart and skeletal myoblasts. The chelating agent EDTA blocked much of the gelatinolytic activity and the organomercurial activator of MMPs increased the activity in cells of both muscle origins. However, the inhibition of gelatinolytic activity by a broad spectrum MMP inhibitor was less profound in heart myoblasts than that in skeletal myoblasts. Gelatinolytic activity was also expressed in the endomysium and perimysium of tissue sections of heart and soleus muscles. Similar with findings in the cell studies, the gelatinase activity was increased by the MMP activator, mostly blocked by EDTA and partially inhibited by the MMP inhibitor. In the presence of the MMP inhibitor, the remaining gelatinolytic activity in the tissue sections was again higher in myocardium than that in soleus muscle. This observation was further supported by the gelatinolytic activity examined in tissue homogenates. Our findings suggest that other proteinases, in addition to MMPs, are more responsive for the tissue gelatinolytic activity in heart muscle as compared with that in skeletal muscle.