Abstract
K+ currents were recorded from ATP-sensitive channels in inside-out patches from isolated rat ventricular myocytes. In the absence of internal divalent cations the current voltage relationship could be described by constant-field assumptions with a permeability of 1.25×10−13 cm2/s; outward currents saturated under a high driving force for K+ movement. Internal 0.1–5.0 mM Mg2+, 0.1 μM Ca2+ and 10 mM Na+ each depressed the flux of K+ ions moving outwards through open channels. Internal 0.1–5.0 mM Mg2+, 0.1–1.0 μM Ca2+ and 1–10 μM Ba2+ and Sr2+ blocked K+ channel activity in a dose-and voltage-dependent manner. Run-down channels could be reactivated by Mg-ATP, but not by AMP-PNP, ATPγS or Mg-free ATP which suggested that phosphorylation of the channels was involved in their activity. Ca2+ (>=1 μM) and Sr2+ (1 mM) markedly inactivated K+ ATP channels, millimolar Ba2+ or Mg2+ were less effective. This suggested that the run down of the channels was a Ca2+-dependent dephosphorylation of the K+ channel protein.
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Findlay, I. ATP-sensitive K+ channels in rat ventricular myocytes are blocked and inactivated by internal divalent cations. Pflugers Arch. 410, 313–320 (1987). https://doi.org/10.1007/BF00580282
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DOI: https://doi.org/10.1007/BF00580282