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The Role of Mg2+ in the Inactivation of Inwardly Rectifying K+ Channels in Aortic Endothelial Cells

Overview
Journal J Gen Physiol
Specialty Physiology
Date 1995 Apr 1
PMID 7608654
Citations 10
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Abstract

We have studied the role of Mg2+ in the inactivation of inwardly rectifying K+ channels in vascular endothelial cells. Inactivation was largely eliminated in Mg(2+)-free external solutions and the extent of inactivation was increased by raising Mg2+o. The dose-response relation for the reduction of channel open probability showed that Mg2+o binds to a site (KD = approximately 25 microM at -160 mV) that senses approximately 38% of the potential drop from the external membrane surface. Analysis of the single-channel kinetics showed that Mg2+ produced a class of long-lived closures that separated bursts of openings. Raising Mg2+o reduced the burst duration, but less than expected for an open-channel blocking mechanism. The effects of Mg2+o are antagonized by K+o in manner which suggests that K+ competes with Mg2+ for the inactivation site. Mg2+o also reduced the amplitude of the single-channel current at millimolar concentrations by a rapid block of the open channel. A mechanism is proposed in which Mg2+ binds to the closed channel during hyperpolarization and prevents it from opening until it is occupied by K+.

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References
1.
ARMSTRONG C . Inactivation of the potassium conductance and related phenomena caused by quaternary ammonium ion injection in squid axons. J Gen Physiol. 1969; 54(5):553-75. PMC: 2225944. DOI: 10.1085/jgp.54.5.553. View

2.
Sakmann B, Trube G . Voltage-dependent inactivation of inward-rectifying single-channel currents in the guinea-pig heart cell membrane. J Physiol. 1984; 347:659-83. PMC: 1199470. DOI: 10.1113/jphysiol.1984.sp015089. View

3.
Kurachi Y . Voltage-dependent activation of the inward-rectifier potassium channel in the ventricular cell membrane of guinea-pig heart. J Physiol. 1985; 366:365-85. PMC: 1193038. DOI: 10.1113/jphysiol.1985.sp015803. View

4.
Ogden D, Colquhoun D . Ion channel block by acetylcholine, carbachol and suberyldicholine at the frog neuromuscular junction. Proc R Soc Lond B Biol Sci. 1985; 225(1240):329-55. DOI: 10.1098/rspb.1985.0065. View

5.
Blatz A, Magleby K . Correcting single channel data for missed events. Biophys J. 1986; 49(5):967-80. PMC: 1329677. DOI: 10.1016/S0006-3495(86)83725-0. View