Evidence map›Paper›PMID 10878101›Full record

ArticleThe Journal of physiology2000

Potassium inhibition of sodium-activated potassium (K(Na)) channels in guinea-pig ventricular myocytes.

X W Niu, R W Meech

Abstract read
In one paragraph

Article in The Journal of physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Activation of Slo2.1 channels by niflumic acid.The Journal of general physiology · 2010
    Article
  4. Article
  5. The N-terminal domain of Slack determines the formation and trafficking of Slick/Slack heteromeric sodium-activated potassium channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  6. Article
  7. Article
  8. Review
  9. Sodium-dependent plateau potentials in electrocytes of the electric fish Gymnotus carapo.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2005
    Article
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

2 authors.

X W NiuDepartment of Physiology, University Walk, Bristol BS8 1TD, UK.
R W Meech

Funding

Molecular Regulation of Cardiac KATP Channels in IschemiaR01HL057414 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MAKIELSKI, JONATHAN C · 1997 to 2012
$3.8M
Molecular Regulation of Cardiac KATP Channels in IschemiaR56HL057414 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MAKIELSKI, JONATHAN C · 2013 to 2013
$376k
NHLBI NIH HHS HL-57414NHLBI NIH HHS R01 HL057414NHLBI NIH HHS R56 HL057414
6 · The paper itself

Abstract

N(a+)-activated potassium channels (K(Na) channels) were studied in inside-out patches from guinea-pig ventricular myocytes at potentials between -100 and +80 mV. External K(+) (K(+)(o)) was set to 140 mM. For inwardly directed currents with 105 mM internal K(+) (K(+)(1)), the unitary current-voltage relationship was fitted by the constant field equation with a potassium permeability coefficient, P(K), of 3.72 x 10(-13) cm(3) s(-1). The slope conductance (-100 to -10 mV) was 194 +/- 4.5 pS (mean +/- s.d., n = 4) with 105 mM K(+)(i) (35 mM Na(+)(i)) but it decreased to 181 +/- 5.6 pS (n = 5) in 70 mM K(+)(i) (70 mM Na(+)(i)). K(Na) channels were activated by internal Na(+) in a concentration-dependent fashion. With 4 mM K(+)(i), maximal activation was recorded with 100 mM Na(+)(i) (open probability, P(o), about 0.78); half-maximal activation required about 35 mM Na(+)(i). When K(+)(i) was increased to 70 mM, half-maximal activation shifted to about 70 mM Na(+)(i). With Na(+)(i) set to 105 mM, channel activity was markedly inhibited when K(+)(i) was increased from 35 to 105 mM. Channel openings were abolished with 210 mM K(+)(i). The inhibitory effect of internal K(+) was also observed at more physiological conditions of osmolarity, ionic strength and chloride concentration. With 35 mM Na(+)(i) and 4 mM K(+)(i), P(o) was 0.48 +/- 0.10 (n = 6); when K(+)(i)was increased to 35 mM, P(o) was reduced to 0.04 +/- 0.05 (n = 7, P < 0.001). The relationship between P(o) and Na(+)(i) concentration at different levels of K(+)(i) is well described by a modified Michaelis-Menten equation for competitive inhibition; the Hill coefficients were 4 for the P(o)-Na(+)(i) relationship and 1.2 for the P(o)-K(+)(i) relationship. It is suggested that Na(+) and K(+) compete for a superficial site on the channel's permeation pathway. K(Na) channels would be most likely to be activated in vivo when an increase in Na(+)(i) is accompanied by a decrease of K(+)(i).

Indexed as

Adenosine TriphosphateAnimalsCells, CulturedGuinea PigsHeart VentriclesIntracellular FluidLithiumMeglumineMembrane PotentialsMyocardiumOsmolar ConcentrationPatch-Clamp TechniquesPerfusionPotassiumPotassium ChannelsSodiumAdenosine TriphosphateLithiumMegluminePotassiumPotassium ChannelsSodium

Identifiers

PMID10878101
PMCPMC2270000

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.