Evidence map›Paper›PMID 18180950›Full record

ArticlePflugers Archiv : European journal of physiology2008

A structural motif in the C-terminal tail of slo1 confers carbon monoxide sensitivity to human BK Ca channels.

Sandile E Williams, Stephen P Brazier, Nian Baban, Vsevolod Telezhkin, Carsten T Müller, Daniela Riccardi, Paul J Kemp

Abstract read
PubMed Publisher
In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Gas Signaling Molecules and Mitochondrial Potassium Channels.International journal of molecular sciences · 2018
    Review
  6. Review
  7. Carbon monoxide in lung cell physiology and disease.American journal of physiology. Cell physiology · 2018
    Review
  8. Is Carotid Body Physiological OFrontiers in physiology · 2018
    Review
  9. CO-independent modification of KEuropean journal of pharmacology · 2017
    Article
  10. Review
  11. Functional Interactions between BKOxidative medicine and cellular longevity · 2016
    Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Carbon monoxide--physiology, detection and controlled release.Chemical communications (Cambridge, England) · 2014
    Review
  17. Heme sensor proteins.The Journal of biological chemistry · 2013
    Review
  18. The haptoglobin-CD163-heme oxygenase-1 pathway for hemoglobin scavenging.Oxidative medicine and cellular longevity · 2013
    Review
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Sandile E WilliamsSchool of Biosciences, Cardiff University, Cardiff, UK.
Stephen P Brazier
Nian Baban
Vsevolod Telezhkin
Carsten T Müller
Daniela Riccardi
Paul J Kemp
Cardiff University · GB

Funding

British Heart Foundation rg/03/001Medical Research Council G0600821
6 · The paper itself

Abstract

Carbon monoxide (CO) is a potent activator of large conductance, calcium-dependent potassium (BK Ca) channels of vascular myocytes and carotid body glomus cells or when heterologously expressed. Using the human BK Ca channel alpha1-subunit (hSlo1; KCNMA1) stably and transiently expressed in human embryonic kidney 293 cells, the mechanism and structural basis of channel activation by CO was investigated in inside-out, excised membrane patches. Activation by CO was concentration dependent (EC50 approximately 20 microM), rapid, reversible, and evoked a shift in the V 0.5 of -20 mV. CO evoked no changes in either single channel conductance or in deactivation rate but augmented channel activation rate. Activation was independent of the redox state of the channel, or associated compounds/protein partners, and was partially dependent on [Ca2+]i in the physiological range (100-1,000 nM). Importantly, CO "super-stimulated" BK Ca activity even in saturating [Ca2+]i. Single or double mutation of two histidine residues previously implicated in CO sensing did not suppress CO activation but replacing the S9-S10 module of the C-terminal of Slo1 with that of Slo3 completely prevented the action of CO. These findings show that a motif in the S9-S10 part of the C-terminal is essential for CO activation and suggest that this gas transmitter activates the BK Ca channel by redox-independent changes in gating.

Indexed as

Ion Channel GatingAmino Acid MotifsBinding SitesCalciumCarbon MonoxideCell LineHumansKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMembrane PotentialsMutagenesis, Site-DirectedOxidation-ReductionPatch-Clamp TechniquesProtein BindingProtein ConformationProtein Structure, TertiaryCalciumCarbon MonoxideKCNMA1 protein, humanLarge-Conductance Calcium-Activated Potassium Channel alpha Subunits

Identifiers

PMID18180950
OpenAlexW1999675865

What OpenQuestion holds

Textmetadata
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.