Abstract
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 a specific protein inhibitor, modulator binding protein, caused a loss of Ca2+-activated tension which was restored by subsequent treatment with calmodulin. Calmodulin at 5 μM 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 μM calmodulin. These results are consistent with a calmodulin-regulated light chain kinase/phosphatase system being responsible for activation of tension in smooth muscle.
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A preliminary report of this work was given at the joint American Society of Biological Chemistry and the Biophysical Society Meetings, June 1980, Cassidy P., Hoar, P.E., and Kerrick, W.G. L. Exogenous calmodulin increases contraction kinetics, Ca2+ sensitivity and myosin phosphorylation in smooth muscle. Fed Proc, 39:2042, abstract No. 2300
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Cassidy, P.S., Kerrick, W.G.L., Hoar, P.E. et al. Exogenous calmodulin increases Ca2+ sensitivity of isometric tension activation and myosin phosphorylation in skinned smooth muscle. Pflugers Arch. 392, 115–120 (1981). https://doi.org/10.1007/BF00581258
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DOI: https://doi.org/10.1007/BF00581258