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December 1, 1996AJP Cell Physiology

Mutations in the pore region of ROMK enhance Ba2+ block

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Population

Xenopus laevis oocytes expressing ROMK2 potassium channels

Comparison

Mutation of the pore region of ROMK2 or… vs Wild-type ROMK2 channel

Design

Preclinical

Authors

HZHong ZhouUniversity of Wisconsin–MadisonSCS. ChepilkoCornell UniversityWSWolfgang SchüttIMC University of Applied Sciences Krems

Discussion

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Implication

Identifies distinct Ba2+ binding in ROMK2 pore; leaves open Kir channel pharmacology in humans.

Structured PICO

P
Population
Xenopus laevis oocytes expressing ROMK2 potassium channels
I
Intervention
Mutation of the pore region of ROMK2 (L117I and V121T) or substitution of asparagine with aspartic acid in the second membrane-spanning domain
C
Comparator
Wild-type ROMK2 channel
O
Outcome
Apparent inhibition constant at zero voltage [Ki(0)] in the presence of Ba2+surrogate

Mutations in the pore region of the ROMK2 channel, specifically V121T, significantly increase its sensitivity to Ba2+ block, indicating the Ba2+ binding site is distinct from internal Mg2+ block loci.

Cite This Study

Zhou et al. (1996) studied this question.

synapsesocial.com/papers/6a763848666dd073ee008f6chttps://doi.org/10.1152/ajpcell.1996.271.6.c1949
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Discrete Ba2+ block as a probe of ion occupancy and pore structure in the high-conductance Ca2+ -activated K+ channel.1988 · 284 citations
  2. 2Mutations Affecting Internal TEA Blockade Identify the Probable Pore-Forming Region of a K + Channel1991 · 630 citations
  3. 3Inward rectification of a potassium channel in cardiac ventricular cells depends on internal magnesium ions.1987 · 490 citations
  4. 4Spermine and Spermidine as Gating Molecules for Inward Rectifier K + Channels1994 · 525 citations
  5. 5Exchange of Conduction Pathways Between Two Related K + Channels1991 · 386 citations