
IndraLab
Statements
sparser
"Although distinct mechanisms underlie Ca 2+ - and voltage-dependent activation of BK channels, it is apparent that the G–V relation shifts to more negative voltages with increasing [Ca 2+ ] i ( xref ), while the G-[Ca 2+ ] i dose response curve is altered by increasing voltage to decrease EC 50 and increase the Hill coefficient [ xref ]."
sparser
"The voltage-sensitive dye bis-(1, 3-dibutylbarbituric acid) trimethine oxonol [DiBAC4(3)] at submicromalor levels (Morimoto et al., xref ) produced a shift in the voltage-dependence of the BK channel only when β-1 and β-4 subunits were present, whereas saturating concentrations (30 μM), produced huge negative shifts by up to −300 mV in the voltage-dependent activation of BK channels, but this effect was neither dependent on calcium nor the presence of β-subunits (Scornik et al., xref )."
sparser
"The variables of voltage-dependent activation of BK channels calculated from the I-V relationships ( xref ) were fitted to a Boltzmann function ( xref ), and the V 1/2 of the channel activation was 6.6±1.4 mV in control, 10.2±1.7 mV in LDL, and 5.8±1.5 mV in LDL plus MβCD (n = 10 for each group, P = NS vs. control), suggesting that LDL, like MβCD-cholesterol, reduces BK current without significantly affecting the voltage-dependent activation."
sparser
"Although at least 10 µM Ca 2+ was required to bring the midpoint of voltage-dependent activation (V 1/2 ) of both BK 0 and BK SRKR channels into the physiological voltage range, the G-V relationships remained right-shifted when compared with mouse mbr5 channels, a benchmark clone of BK."