Literature DB >> 8842207

[K+] dependence of open-channel conductance in cloned inward rectifier potassium channels (IRK1, Kir2.1).

A N Lopatin1, C G Nichols.   

Abstract

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 alpha. When intracellular K+ concentration (KIN) was varied, at constant extracellular K+ concentration (KOUT) the conductance at the reversal potential (GREV) 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 KOUT was varied, at constant KIN, GREV saturated at concentrations of > 150 mM. A square-root dependence of conductance on KOUT 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.

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Year:  1996        PMID: 8842207      PMCID: PMC1233525          DOI: 10.1016/S0006-3495(96)79268-8

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  41 in total

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Authors:  H Matsuda; A Saigusa; H Irisawa
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4.  Cooperative effects in models of steady-state transport across membranes. IV. One-site, two-site, and multisite models.

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5.  Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel.

Authors:  Y Kubo; E Reuveny; P A Slesinger; Y N Jan; L Y Jan
Journal:  Nature       Date:  1993-08-26       Impact factor: 49.962

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9.  Spermine and spermidine as gating molecules for inward rectifier K+ channels.

Authors:  E Ficker; M Taglialatela; B A Wible; C M Henley; A M Brown
Journal:  Science       Date:  1994-11-11       Impact factor: 47.728

10.  Ionic selectivity, saturation, and block in a K+-selective channel from sarcoplasmic reticulum.

Authors:  R Coronado; R L Rosenberg; C Miller
Journal:  J Gen Physiol       Date:  1980-10       Impact factor: 4.086

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  23 in total

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4.  Low-affinity spermine block mediating outward currents through Kir2.1 and Kir2.2 inward rectifier potassium channels.

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7.  Regulation of ROMK by extracellular cations.

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9.  Multi-ion versus single-ion conduction mechanisms can yield current rectification in biological ion channels.

Authors:  Tamsyn A Hilder; Ben Corry; Shin-Ho Chung
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10.  Translocation of double-stranded DNA through membrane-adapted phi29 motor protein nanopores.

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