Calcium-dependent binding of calmodulin to phospholipase A2 subunits induces enzymatic activation.
Calmodulin interacted with phospholipase A2 from two different sources, as established by affinity chromatography, dimethylsuberimidate protein crosslinking, and phospholipase A2 assays. Calmodulin was covalently crosslinked to pancreatic and bee venom phospholipases A2 in a calcium-dependent manner, and enhanced the enzymatic activities of these phospholipases. Pancreatic phospholipase A2 was separated into two species of identical molecular weight by calmodulin affinity chromatography; the species that bound to immobilized calmodulin in a calcium-dependent manner was stimulated by calmodulin. This presents further evidence that phospholipase A2 is directly activated by calmodulin.
D000818:Animals; D002118:Calcium / Q000502:physiology*; D002147:Calmodulin / Q000378:metabolism* / Q000494:pharmacology; D002846:Chromatography, Affinity; D004533:Egtazic Acid / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000032:analysis / Q000378:metabolism*; D054467:Phospholipases A2; D013552:Swine
D002147:Calmodulin; D004533:Egtazic Acid; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium