Activation and inactivation of glycogen phosphorylase isoenzymes purified from diabetic rat heart.
1. Hearts of diabetic rats gradually accumulate glycogen, although the activities of glycogen synthase and glycogen phosphorylase are altered in favor of a depletion of glycogen. 2. Phosphorylase in diabetic hearts has been reported to be even more activated in response to adrenaline than controls. 3. The situation is further complicated by the fact that in rat heart two isoenzymes of phosphorylase are present. Therefore we have studied the properties of phosphorylases purified from diabetic rat heart in more detail. 4. This investigation revealed that compared to controls: (A) the amount of enzyme protein which could be isolated from diabetic animals is drastically lower; (B) the affinities towards glycogen and inorganic phosphate are decreased; (C) the activation by phosphorylase kinase is delayed; and (D) the inactivation by protein phosphatase-1 is accelerated. 5. We conclude that all of the reported changes in diabetes might contribute to a phosphorylase system less able to catalyze glycogen breakdown effectively.
Berndt
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N
Department of Clinical Biochemistry, Diabetes-Forschungsinstitut, Düsseldorf, F.R.G.
Rösen
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P
D000818:Animals; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D004789:Enzyme Activation; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D006005:Phosphorylases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D051381:Rats
D007527:Isoenzymes; D006005:Phosphorylases