Abstract
Incubation of isolated rat liver nuclei with ATP, NAD +, and micromolar Ca 2+ concentrations of various metal ions resulted in extensive DNA hydrolysis. Half-maximal activity occurred with 1.0 μM Ca 2+ added, and saturation of the process was observed with 10 μM Ca 2+, The Ca 2+ (10 μM)-activated DNA fragmentation was inhibited by the presence of Ca 2+-binding protein regucalcin isolated from rat liver cytosol. The inhibitory effect of regucalcin was complete at 0.5 μM. At 25μM Ca 2+ added, such an effect of regucalcin (1.0μM) was not seen, Regucalcin also inhibited Ca 2+-activated DNA fragmentation in the presence or calmodulin (10 and 20 μg). The results show that regucalcin can inhibit the Ca 2+-activated DNA fragmentation due to binding the metal, suggesting a role in regulation of liver nuclear functions.
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