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. Author manuscript; available in PMC: 2014 Jul 1.
Published in final edited form as: Biochim Biophys Acta. 2012 Sep 26;1828(7):1522–1529. doi: 10.1016/j.bbamem.2012.09.018

Fig. 2.

Fig. 2

The potential impact of alternative splicing of CaV channels on the voltage range over which each channel subtype can operate. Boltzmann activation curves are plotted using V1/2 and k values from the literature from recordings using 1–2 mM calcium as charge carrier, except for data for CaV1.1 obtained from recordings using 10 mM calcium. A, CaV1.1 (V1/2 =6.2 mV, k=5.3 mV; [121]), CaV1.2 (V1/2 = −17 mV, k=8 mV; [122]), CaV1.3 (V1/2 = −36 mV, k=8 mV; [123,124]), CaV2.2 (V1/2 = −0.1 mV, k=7.5 mV; [125]), and CaV3.1 (CaV3.1, V1/2 = −46 mV, k=4.11; [126]). B, Alternative splicing of exons can modify voltage-dependence of activation and this will increase the operating voltage range for each CaV channel family. Approximate locations of regions encoded by alternatively spliced exons that influence the voltage-dependence of channel activation are shown. CaV2.2 data are from [125]; CaV1.1 data are from [64]; and CaV3.1 data are from [127]. CaV1.2 [128] and CaV1.3 [67,129] isoforms that have different activation properties were compared using 11 mM barium as charge carrier, this will shift the voltage-dependence of activation relative to recordings with 2 mM Ca. For comparison with other data, we illustrate an approximate operating range for CaV1.2 and CaV1.3 (dotted lines) based on the different V1/2 values from [67,128,129] but with reference to the activation curves shown in A obtained with 2 mM Ca.