Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels
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概要
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Although calmodulin binding to various sites of the Cav1.2 Ca2+ channel has been reported, the mechanism of the interaction is not fully understood. In this study we examined calmodulin binding to fragment channel peptides using a semi-quantitative pull-down assay. Calmodulin bound to the peptides with decreasing affinity order: IQ > preIQ > I-II loop > N-terminal peptide. A peptide containing both preIQ and IQ regions (Leu1599 – Leu1668) bound with approximately 2 mol of calmodulin per peptide. These results support the hypothesis that two molecules of calmodulin can simultaneously bind to the C-terminus of the Cav1.2 channel and modulate its facilitatory and inhibitory activities.
- 社団法人 日本薬理学会の論文
著者
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MINOBE Etsuko
Department of Physiology, Graduate School of Medicine and Dental Sciences, Kagoshima University
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KAMEYAMA Masaki
Department of Physiology, Graduate School of Medicine and Dental Sciences, Kagoshima University
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Kameyama Masaki
Department Of Aeronautics And Space Engineering Tohoku University
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SAUD Zahangir
Department of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University
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Saud Zahangir
Department Of Physiology Graduate School Of Medical And Dental Sciences Kagoshima University
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Asmara Hadhimulya
Department of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Japa
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Minobe Etsuko
Department Of Physiology Graduate School Of Medical And Dental Sciences Kagoshima University
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Asmara Hadhimulya
Department Of Physiology Graduate School Of Medical And Dental Sciences Kagoshima University
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Asmara Hadhimulya
Department of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Japan
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Saud Zahangir
Department of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Japan
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