TY - JOUR
T1 - [K+] dependence of open-channel conductance in cloned inward rectifier potassium channels (IRK1, Kir2.1)
AU - Lopatin, A. N.
AU - Nichols, C. G.
N1 - Funding Information:
Kir2.1 (IRKI) was a gift from Dr. Lou Philipson and Dr. Dottie Hanck (University of Chicago). This research was supported by grant HL54171 from the National Institutes of Health (to CGN) and an Established Inves- tigatorship from the American Heart Association (to CGN).
PY - 1996/8
Y1 - 1996/8
N2 - Potassium conduction through unblocked inwardly rectifying (IRK1, Kir2.1) potassium channels was measured in inside-out patches from Xenopus oocytes, after removal of polyamine-induced strong inward rectification. Unblocked IRK1 channel current-voltage (I-V) relations show very mild inward rectification in symmetrical solutions, are linearized in nonsymmetrical solutions that bring the K+ reversal potential to extreme negative values, and follow Goldman-Hodgkin-Katz constant field equation at extreme positive E(K). When intracellular K+ concentration (K(IN)) was varied, at constant extracellular K+ concentration (K(OUT)) the conductance at the reversal potential (G(REV)) followed closely the predictions of the Goldman-Hodgkin- Katz constant field equation at low concentrations and saturated sharply at concentrations of >150 mM. Similarly, when K(OUT) was varied, at constant K(IN), G(REV) saturated at concentrations of >150 mM. A square-root dependence of conductance on K(OUT) is a well-known property of inward rectifier potassium channels and is a property of the open channel. A nonsymmetrical two-site three-barrier model can qualitatively explain both the I-V relations and the [K+] dependence of conductance of open IRK1 (Kir2.1) channels.
AB - Potassium conduction through unblocked inwardly rectifying (IRK1, Kir2.1) potassium channels was measured in inside-out patches from Xenopus oocytes, after removal of polyamine-induced strong inward rectification. Unblocked IRK1 channel current-voltage (I-V) relations show very mild inward rectification in symmetrical solutions, are linearized in nonsymmetrical solutions that bring the K+ reversal potential to extreme negative values, and follow Goldman-Hodgkin-Katz constant field equation at extreme positive E(K). When intracellular K+ concentration (K(IN)) was varied, at constant extracellular K+ concentration (K(OUT)) the conductance at the reversal potential (G(REV)) followed closely the predictions of the Goldman-Hodgkin- Katz constant field equation at low concentrations and saturated sharply at concentrations of >150 mM. Similarly, when K(OUT) was varied, at constant K(IN), G(REV) saturated at concentrations of >150 mM. A square-root dependence of conductance on K(OUT) is a well-known property of inward rectifier potassium channels and is a property of the open channel. A nonsymmetrical two-site three-barrier model can qualitatively explain both the I-V relations and the [K+] dependence of conductance of open IRK1 (Kir2.1) channels.
UR - http://www.scopus.com/inward/record.url?scp=0029738418&partnerID=8YFLogxK
U2 - 10.1016/S0006-3495(96)79268-8
DO - 10.1016/S0006-3495(96)79268-8
M3 - Article
C2 - 8842207
AN - SCOPUS:0029738418
SN - 0006-3495
VL - 71
SP - 682
EP - 694
JO - Biophysical Journal
JF - Biophysical Journal
IS - 2
ER -