Calmodulin dependency of calcitonin action on glucose-6-phosphatase and phosphorylase a activites in the liver of rats
Abstract. The calmodulin dependency of calcitonin (CT) action on glucose-6-phosphatase and phosphyrylase a activities in the liver of rats was investigated. A single sc administration of CT (synthetic [A1,7] eel CT; 80 MRC mU/100 g body weight) produced significant increases in calcium content and glucose-6-phosphatase activity in the hepatic microsomes of intact and thyroparathyroidectomized rats. These increases in enzyme activity were significantly inhibited by W-7 (100 μm), with a concentration which showed maximal effect. However, this inhibition was less than 50% of the enzyme activity increased by CT administration. Meanwhile, CT produced significant increases in calcium content and phosphorylase a activity in the hepatic glycogen particles from intact rats. However, this increase in enzyme activity was not influenced significantly by W-7 (100 μm), suggesting that the calcium ion may directly activate the enzyme. These results suggest that the increase in microsomal glucose-6-phosphatase activity of rat liver mediated by cellular calcium following CT administration may partly depend on calmodulin.