Exogenous calmodulin increases Ca2+ sensitivity of isometric tension activation and myosin phosphorylation in skinned smooth muscle.
We have investigated the effect of exogenous calmodulin on chicken gizzard or rabbit ileum smooth muscle functionally skinned by mechanical grinding or exposure to Triton X-100 detergent. We found that specific protein inhibitor, modulator binding protein, caused a loss of Ca2+-activated tension which was restored by subsequent treatment with calmodulin. Calmodulin at 5 microM increased 10-fold the speed of development of isometric tension while it had no significant effect on the rate of relaxation or on maximum tension at high Ca2+ concentrations. The Ca2+ sensitivity of steady state tension and LC20 phosphorylation were also increased by 5 microM calmodulin. These results are consistent with a calmodulin-regulated light chain kinase/phosphatase system being responsible for activation of tension in smooth muscle.
D000818:Animals; D001711:Biotransformation; D002118:Calcium / Q000502:physiology*; D002135:Calcium-Binding Proteins / Q000494:pharmacology*; D002147:Calmodulin / Q000494:pharmacology*; D002645:Chickens; D066298:In Vitro Techniques; D009119:Muscle Contraction; D009124:Muscle Proteins / Q000378:metabolism; D009130:Muscle, Smooth / Q000187:drug effects* / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D010766:Phosphorylation; D011817:Rabbits
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D009124:Muscle Proteins; D009218:Myosins; D002118:Calcium