Calcium-stimulated, ATP-magnesium-dependent inactivation of pig liver glycogen synthase.
Ca2+-stimulated inactivation of liver glycogen synthase was observed when a partially purified liver phosphorylase kinase fraction containing glycogen synthase was incubated with ATP-Mg2+. The Ca2+-stimulated portion of this inactivation was partially counteracted by trifluoperazine and slightly stimulated by exogenously added calmodulin. These results suggest that Ca2+-calmodulin may be involved as one of the factors causing this glycogen synthase inactivation. Although the exact mechanism mediated by Ca2+ has not been clearly determined, the possibility of the participation of some Ca2+-dependent protein kinase is discussed.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002147:Calmodulin / Q000494:pharmacology; D006006:Glycogen Synthase / Q000037:antagonists & inhibitors*; D008099:Liver / Q000201:enzymology*; D010764:Phosphorylase Kinase / Q000378:metabolism; D010766:Phosphorylation; D011817:Rabbits; D013552:Swine; D014268:Trifluoperazine / Q000494:pharmacology
D002147:Calmodulin; D014268:Trifluoperazine; D000255:Adenosine Triphosphate; D006006:Glycogen Synthase; D010764:Phosphorylase Kinase; D002118:Calcium