Calcium-dependent interactions of an ionophore A23187 with calmodulin |
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| Authors: | M Inagaki T Tanaka Y Sasaki H Hidaka |
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| Affiliation: | 1. Department of Chemistry, Georgia State University, Atlanta, GA 30302-3965, USA;2. Department of Biology, Georgia State University, Atlanta, GA 30302-3965, USA;3. Department of Center for Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30302-3965, USA;4. Department of Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30302-3965, USA;1. Department of Chemistry, Universidad de Burgos, Pza. Misael Bañuelos s/n, E-09001 Burgos, Spain;2. School of Chemistry, University of Bristol, Cantocks Close, Bristol BS8 1TS, UK |
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| Abstract: | We found that ionophore A23187 interacted reversibly with calmodulin (CaM), in a calcium-dependent fashion. It was found that A23187 interacts selectively with CaM, among calcium binding proteins (such as troponin C and S-100 protein) and other proteins. However, apparently differing from W-7, A23187 did not suppress CaM-dependent enzyme activity such as myosin light chain kinase and Ca2+-dependent cyclic nucleotide phosphodiesterase. Our observations suggest that there are novel calcium-dependent regions of CaM which can be monitored using ionophore A23187 and may not be related to enzyme activation. |
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