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. 2011 Jan;137(1):93–110. doi: 10.1085/jgp.201010519

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© 2010 Bukiya et al.

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Figure 2. — Substitution of cholesterol hydrophobic side chain with a chain including a highly polar (carboxyl) group abolishes sterol inhibition of BK channels. Representative single-channel recordings obtained after incorporation of cbv1 into control (A), cholesterol-containing (B), or cholesterol trisnorcholenic acid–containing (C) POPE/POPS (3:1 wt/wt) bilayers. Steroid levels corresponded to 33 mol% in the lipid mix. For A–C, channel openings are shown as upward deflections; arrows on the top trace of each panel indicate the baseline level. Po values were obtained from all-point amplitude histograms (Dopico et al., 1996; Liu et al., 2008) constructed from 3 min of continuous recording in each bilayer type. The membrane potential was set to 0 mV and free [Ca²⁺]_i ≈ 10 µM. (D) Scatter graph showing individual cbv1 Po values in control (sterol-free) and in the presence of cholesterol or cholesterol trisnorcholenic acid in the lipid mix. Each data point corresponds to one independent bilayer preparation. (E) Average Po values show that cholesterol but not cholesterol trisnorcholenic acid significantly reduced activity from controls. **, significantly different from control (P < 0.01); n, number of bilayers. In this and all studies shown in Figs. 3, 4, 6–8, S1, S3, and S4, control refers to sterol-free POPE/POPS (3:1 wt/wt). All lipid mixtures, whether sterol-containing or not, were dissolved in decane as described in Materials and methods.