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- W1969905477 abstract "Cav1.3 voltage-gated L-type calcium channels can activate at more negative membrane potentials than other high-voltage activated calcium channels. This allows them to contribute to specific physiological functions, such as cardiac pacemaking and hearing. Cav1.3 α1-subunits are regulated by a C-terminal modulatory domain (CTM) serving an auto-inhibitory function. Alternative splicing removes the CTM in C-terminally short variants (e.g. Cav1.342A) thereby stabilizing an even more negative activation voltage-range than in the long variant (Cav1.3L). It is unknown if the CTM affects gating of the voltage-sensor, its coupling to pore opening or both. We therefore investigated CTM effects on Cav1.3 voltage-sensor function (ON-gating charge). We compared Cav1.3 gating properties with low voltage-gated Cav3.1 T-type channels and with somatic Cav1.3 mutants recently discovered in human adrenal aldosterone-producing adenomas (APA).We expressed Cav3.1, Cav1.3 and Cav1.2 α1 subunits (the latter with α2-δ1 and β3 subunits) in tsA-201 cells. ON-gating charge (QON) and inward calcium currents (ICa) were measured using whole cell patch-clamp.Cav3.1 ICa activated about 25mV more negative than Cav1.3L despite a much lower overall voltage-sensitivity of Cav3.1 voltage-sensor movements (QON-V). Half-maximal QON-V of Cav1.3L was also more negative than of Cav1.2. Although a proportionally higher fraction of QON had to be moved to activate Cav1.3L ICa, Cav1.3L channel activated at lower voltages than Cav1.2. Removal of the Cav1.3L CTM lowered Cav1.342A ICa half-maximal activation-voltage without affecting QON-V. The CTM therefore must enhance ICa at lower potentials by facilitating pore-opening upon voltage-sensor movements. APA mutations V259D (IS4-S5), I750M (IIS6) and P1336R (IVS4-S5) induced about 15 mV negative shifts in activation-voltage and/or slowed inactivation. Gain of Cav1.3 channel function can therefore explain enhanced calcium-dependent aldosterone synthesis in these tumors.(Support: Austrian Science Fund F44020)" @default.
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- W1969905477 date "2014-01-01" @default.
- W1969905477 modified "2023-09-27" @default.
- W1969905477 title "Gating Properties of Cav1.3 Calcium Channels: Insight from Alternative Splicing and Human Mutations" @default.
- W1969905477 doi "https://doi.org/10.1016/j.bpj.2013.11.788" @default.
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