Caldesmon150 regulates the tropomyosin-enhanced actin-myosin interaction in gizzard smooth muscle |
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| Authors: | K Sobue K Takahashi I Wakabayashi |
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| Affiliation: | 1. Program in Petrochemistry and Polymer Science, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand;2. Department of Chemical Technology, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand;3. Center of Excellence in Green Materials for Industrial Application, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand;4. Center of Excellence on Petrochemical and Materials Technology, Chulalongkorn University, Bangkok 10330, Thailand;1. ISA, School of Physics A28, The University of Sydney, NSW 2006, Australia;2. Energy Planning Program, Graduate School of Engineering, Federal University of Rio de Janeiro, Centro de Tecnologia, Bloco C, Sala 211, Cidade Universitária, Ilha do Fundão, Rio de Janeiro, RJ 21941-972, Brazil;3. Faculty of Economics and Business, University of Groningen, P.O. Box 800, NL-9700 AV Groningen, The Netherlands |
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| Abstract: | Using a reconstituted system in which myosin was preferentially phosphorylated, we examined the regulatory action of caldesmon150 on the smooth muscle actin-myosin interaction. Caldesmon150 inhibited the tropomyosin-enhanced actomyosin ATPase activity in a Ca2+-independent manner. This inhibitory effect of caldesmon150 was observed to be overcome by the addition of calmodulin in a Ca2+-dependent manner. In accordance with the observations of ATPase activity, we demonstrated evidence that the regulatory action of caldesmon150 on the actin site was mainly through control of the tropomyosin-enhanced actin-myosin interaction and calmodulin confers the Ca2+-sensitivity upon the caldesmon150 action determined by the cosedimentation method. |
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