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• W2073218614 abstract "Interactions of Ba2+ with K+ and molecules contributing to inward rectification were studied in the cloned inward rectifier K+ channels, Kir2.1. Extracellular Ba2+ blocked Kir2.1 channels with first-order kinetics in a Vm-dependent manner. At Vm more negative than -120 mV, the Kd-Vm relationship became less steep and the dissociation rate constants were larger, suggesting Ba2+ dissociation into the extracellular space. Both depolarization and increasing [K+]i accelerated the recovery from extracellular Ba2+ blockade. Intracellular K+ appears to relieve Ba2+ blockade by competitively slowing the Ba2+ entrance rate, instead of increasing its exit rate by knocking off action. Intracellular spermine (100 microM) reduced, whereas 1 mM [Mg2+]i only slightly reduced, the ability of intracellular K+ to repulse Ba2+ from the channel pore. Intracellular Ba2+ also blocked outward IKir2.1 in a voltage-dependent fashion. At Vm >/= +40 mV, where intrinsic inactivation is prominent, intracellular Ba2+ accelerated the inactivation rate of the outward IKir2.1 in a Vm-independent manner, suggesting interaction of Ba2+ with the intrinsic gate of Kir2.1 channels." @default.
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• W2073218614 date "1998-11-01" @default.
• W2073218614 modified "2023-10-10" @default.
• W2073218614 title "Interaction of Ba2+ with the Pores of the Cloned Inward Rectifier K+ Channels Kir2.1 Expressed in Xenopus Oocytes" @default.
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• W2073218614 doi "https://doi.org/10.1016/s0006-3495(98)77675-1" @default.
• W2073218614 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1299905" @default.
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