Regulatory Effect of Calcium-Binding protein Isolated from Rat Liver Cytosol on Activation of Fructose 1,6-Diphosphatase by Ca^<2+>-Calmodulin

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The role of a calcium-binding protein (CaBP) isolated from rat liver cytosol was investigated in relation to the activation of hepatic fructose 1,6-diphosphatase by Ca^<2+>-calmodulin. Fructose 1,6-diphosphatase activity in rat liver cytosol was markedly increased by addition of Ca^<2+> (1.0-5.0 μM) to the incubation mixture. This increase was completely inhibited in the presence of N-(6-aminohexyl)-5-chloro-1-napthalenesulfonamide (W-7 15 μM), an inhibitor of calmodulin. Added Ca^<2+> (5.0 μM)-increased cytosolic fructose 1,6-diphosphatase activity was markedly enhanced by the coexistence of calmodulin (2.5 μg/ml). Further, fructose 1,6-diphosphatase isolated from rabbit liver cytosol was activated by Ca^<2+>-calmodulin. This activation was completely inhibited by CaBP (20 μg/ml) isolated from rat liver cytosol, though CaBP in the absence of calmodulin had no effect on liver fructose 1,6-diphosphatase activity. The present data suggest that CaBP can modify the action of Ca^<2+>-calmodulin in liver cells. It is proposed that CaBP, which may regulate Ca^<2+> effects on liver function, should be named calregulin.
公益社団法人日本薬学会の論文
1985-10-25