Fast activation of Ca2+-ATPases in plasma membranes from cardiac muscle and from ascites carcinoma cells: a possible function of endogenous calmodulin.
Content of endogenous calmodulin, binding of calmodulin to, and Ca2+-ATPase activity in plasma membranes of cardiac muscle. Ehrlich ascites carcinoma (EAC) cells and erythrocytes were examined. The content of endogenous calmodulin in cardiac and EAC cells was shown to be considerably higher than in erythrocyte membranes. Ca2+-independent binding of calmodulin to cardiac and EAC cell membranes was found to be realized by some low molecular weight proteins. Ca2+-ATPases in cardiac and EAC cell membranes differ from those in erythrocytes with respect to their activation by Ca2+ and calmodulin. The erythrocyte enzyme is strongly stimulated by exogenous calmodulin and reaches its maximum activity about 2 min after Ca2+-addition. In contrast, the Ca2+-ATPases in cardiac and EAC cell plasma membranes cannot be considerably stimulated by exogenous calmodulin and are instantaneously activated by Ca2+.
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004789:Enzyme Activation; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D009206:Myocardium / Q000378:metabolism*; D013552:Swine
D002147:Calmodulin; D000252:Calcium-Transporting ATPases