Calcium dyshomeostasis is involved in neuropathological conditions such as traumatic brain injury (TBI), stroke, and neurodegenerative diseases. Under such conditions in the brain, calmodulin (CaM), a Ca 2+ sensor, mediates critical signaling functions through binding and regulating a diverse population of downstream targets referred to as calmodulin-binding proteins (CaMBPs). We developed a CaM-affinity capture method followed by reversed-phase liquid chromatography tandem mass spectrometry (RPLC-MSMS) to study the calcium-dependent CaM-binding proteome in rat brain. A total of 69 potential CaMBPs were identified by this proteomic technique, of which 26 were known CaMBPs and 43 were putative novel CaMBPs. This study shows that the CaM-affinity capture when coupled with tandem mass spectrometry may serve as an effective tool toward constructing a brain CaM-binding proteomic network. The general methods described here can be applied to study possible alternations of calmodulin-binding proteome in neurological, neurodegenerative, and psychiatric disorders. © 2009 Humana Press, a part of Springer Science+Business Media, LLC.
CITATION STYLE
Zhang, Z., Kobeissy, F. H., Ottens, A. K., Martínez, J. A., & Wang, K. K. W. (2009). Calmodulin-binding proteome in the bra. Methods in Molecular Biology, 566, 181–190. https://doi.org/10.1007/978-1-59745-562-6_12
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