Evidence map›Paper›PMID 9417141›Full record

ArticleThe Journal of general physiology1998

Properties of an inwardly rectifying ATP-sensitive K+ channel in the basolateral membrane of renal proximal tubule.

U R Mauerer, E L Boulpaep, A S Segal

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Epithelial transport inThe Journal of general physiology · 2017
    Review
  2. Review
  3. Basolateral membrane K+ channels in renal epithelial cells.American journal of physiology. Renal physiology · 2012
    Review
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  12. Volume regulatory responses of basolateral membrane vesicles from Necturus enterocytes: role of the cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 1999
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

U R MauererDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
E L Boulpaep
A S Segal
University of Vermont · USYale University · US

Funding

The Regulation of Renal Epithelial Cell Junction Assembly and PolarizationP01DK017433 · NIDDK · YALE UNIVERSITY · PI CAPLAN, MICHAEL J. · 1986 to 2018
$29.5M
REGULATION OF ION CHANNELS IN RENAL PROXIMAL TUBULEK11DK002103 · NIDDK · YALE UNIVERSITY · PI SEGAL, ALAN · 1992 to 1996
–
NIDDK NIH HHS DK-02103NIDDK NIH HHS DK-17433NIDDK NIH HHS P01 DK017433
6 · The paper itself

Abstract

The potassium conductance of the basolateral membrane (BLM) of proximal tubule cells is a critical regulator of transport since it is the major determinant of the negative cell membrane potential and is necessary for pump-leak coupling to the Na+,K+-ATPase pump. Despite this pivotal physiological role, the properties of this conductance have been incompletely characterized, in part due to difficulty gaining access to the BLM. We have investigated the properties of this BLM K+ conductance in dissociated, polarized Ambystoma proximal tubule cells. Nearly all seals made on Ambystoma cells contained inward rectifier K+ channels (gammaslope, in = 24.5 +/- 0.6 pS, gammachord, out = 3.7 +/- 0.4 pS). The rectification is mediated in part by internal Mg2+. The open probability of the channel increases modestly with hyperpolarization. The inward conducting properties are described by a saturating binding-unbinding model. The channel conducts Tl+ and K+, but there is no significant conductance for Na+, Rb+, Cs+, Li+, NH4+, or Cl-. The channel is inhibited by barium and the sulfonylurea agent glibenclamide, but not by tetraethylammonium. Channel rundown typically occurs in the absence of ATP, but cytosolic addition of 0. 2 mM ATP (or any hydrolyzable nucleoside triphosphate) sustains channel activity indefinitely. Phosphorylation processes alone fail to sustain channel activity. Higher doses of ATP (or other nucleoside triphosphates) reversibly inhibit the channel. The K+ channel opener diazoxide opens the channel in the presence of 0.2 mM ATP, but does not alleviate the inhibition of millimolar doses of ATP. We conclude that this K+ channel is the major ATP-sensitive basolateral K+ conductance in the proximal tubule.

Indexed as

Adenosine TriphosphateAmbystomaAnimalsBariumBiological TransportCationsCells, CulturedCytidine TriphosphateDiazoxideDiureticsElectric ConductivityGlyburideGuanosine TriphosphateHypoglycemic AgentsInosine TriphosphateIon Channel GatingAdenosine TriphosphateBariumCationsCytidine TriphosphateDiazoxideDiureticsGlyburideGuanosine TriphosphateHypoglycemic AgentsInosine TriphosphatePotassium ChannelsSodium Chloride Symporter InhibitorsSodium-Potassium-Exchanging ATPaseThalliumthymidine 5'-triphosphateThymine NucleotidesUridine Triphosphate

Identifiers

PMID9417141
PMCPMC1887768
OpenAlexW4252637378

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.