PEDARZANI, P., D'HOEDT, D., DOORTY, K. B., WADSWORTH, J. D. F., JOSEPH, J. S., JEYASEELAN, K., KINI, R. M., GADRE, S. V., SAPATNEKAR, S. M., STOCKER, M. and STRONG, Peter (2002). Tamapin, a venom peptide from the Indian red scorpion (mesobuthus tamulus) that targets small conductance Ca2+-activated K+ channels and afterhyperpolarization currents in central neurons. Journal of Biological Chemistry, 277 (48), 46101-46109.Full text not available from this repository.
The biophysical properties of small conductance Ca2+-activated K+ (SK) channels are well suited to underlie afterhyperpolarizations (AHPs) shaping the firing patterns of a conspicuous number of central and peripheral neurons. We have identified a new scorpion toxin (tamapin) that binds to SK channels with high affinity and inhibits SK channel-mediated currents in pyramidal neurons of the hippocampus as well as in cell lines expressing distinct SK channel subunits. This toxin distinguished between the SK channels underlying the apamin-sensitive IAHP and the Ca2+-activated K+ channels mediating the slow IAHP (sIAHP) in hippocampal neurons. Compared with related scorpion toxins, tamapin displayed a unique, remarkable selectivity for SK2 versus SK1 (~1750-fold) and SK3 (~70-fold) channels and is the most potent SK2 channel blocker characterized so far (IC50 for SK2 channels = 24 pM). Tamapin will facilitate the characterization of the subunit composition of native SK channels and help determine their involvement in electrical and biochemical signaling.
|Research Institute, Centre or Group:||Biomolecular Sciences Research Centre|
|Depositing User:||Ann Betterton|
|Date Deposited:||11 Mar 2008|
|Last Modified:||10 Oct 2012 12:05|
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