Figure 7 | Scientific Reports

Figure 7

From: The molecular nature of the 17β-Estradiol binding site in the voltage- and Ca2+-activated K+ (BK) channel β1 subunit

Figure 7

E2 effect on BK channel macroscopic currents. (a) Representative macroscopic ion current recordings from α channels (black traces), α/β1 channels (red traces), α/β1W163I (blue traces) and α/β1F166A (green traces) without 10 μM E2 at time 0 min or with E2 at 30 min. (b,c) Conductance-voltage relationships for α (black), α/β1 (red), α/β1W163I (blue) and α/β1F166A (green) channel complexes before (circles) and after exposition to 10 μM E2 (squares). Lines represent the best Boltzmann fit. (d) Quantification of V0.5 obtained from the G-V curves from BK α channels (black bars), α/β1 channels (red bars), α/β1W163I channels (blue bars) and α/β1F166A channels (green bars)with or without E2 as indicated (mean ± SEM). Differences between channels and experimental conditions were analysed using t-test. Half activation voltages (V0.5) were: α: 164 ± 6 mV (black filled bar); α/β1: 173 ± 3 mV (red filled bar); α/β1W163I: 164 ± 4 mV (blue filled bar), α/β1F166A: 160 ± 4 mV (green filled bar); α + E2: 163 ± 3 mV (black empty bar); α/β1 + E2: 119 ± 2 mV (red empty bar); α/β1W163I + E2: 172 ± 4 mV (blue empty bar), α/β1F166A + E2: 164 ± 5 mV (green empty bar). ****P < 0.0001. n = 5–8.

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