Evidence map›Paper›PMID 18231807›Full record

ArticlePflugers Archiv : European journal of physiology2008

Dual regulation of the ATP-sensitive potassium channel by activation of cGMP-dependent protein kinase.

Yongping Chai, Yu-Fung Lin

Abstract read
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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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Functional modulation of sarcolemmal KAmerican journal of physiology. Cell physiology · 2020
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  9. Hypoxia. 4. Hypoxia and ion channel function.American journal of physiology. Cell physiology · 2011
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  17. Concepts of neural nitric oxide-mediated transmission.The European journal of neuroscience · 2008
    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

2 authors at 1 institution in 1 country.

Yongping ChaiDepartment of Physiology and Membrane Biology, University of California, Rm. 4144, Tupper Hall, One Shields Avenue, Davis, CA, 95616, USA.
Yu-Fung Lin
University of California, Davis · US

Funding

EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR012088 · NCRR · UNIVERSITY OF CALIFORNIA DAVIS · PI CURRY, FITZ-ROY E · 1996 to 1996
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NCRR NIH HHS C06 RR-12088-01
6 · The paper itself

Abstract

Adenosine triphosphate (ATP)-sensitive potassium (K(ATP)) channels couple cellular metabolic status to membrane electrical activity. In this study, we performed patch-clamp recordings to investigate how cyclic guanosine monophosphate (cGMP)-dependent protein kinase (PKG) regulates the function of K(ATP) channels, using both transfected human SH-SY5Y neuroblastoma cells and embryonic kidney (HEK) 293 cells. In intact SH-SY5Y cells, the single-channel currents of Kir6.2/sulfonylurea receptor (SUR) 1 channels, a neuronal-type K(ATP) isoform, were enhanced by zaprinast, a cGMP-specific phosphodiesterase inhibitor; this enhancement was abolished by inhibition of PKG, suggesting a stimulatory role of cGMP/PKG signaling in regulating the function of neuronal K(ATP) channels. Similar effects of cGMP accumulation were confirmed in intact HEK293 cells expressing Kir6.2/SUR1 channels. In contrast, direct application of purified PKG suppressed rather than activated Kir6.2/SUR1 channels in excised, inside-out patches, while tetrameric Kir6.2LRKR368/369/370/371AAAA channels expressed without the SUR subunit were not modulated by zaprinast or purified PKG. Lastly, reconstitution of the soluble guanylyl cyclase/cGMP/PKG signaling pathway by generation of nitric oxide led to Kir6.2/SUR1 channel activation in both cell types. Taken together, here, we report novel findings that PKG exerts dual functional regulation of neuronal K(ATP) channels in a SUR subunit-dependent manner, which may provide new means of therapeutic intervention for manipulating neuronal excitability and/or survival.

Indexed as

Adenosine TriphosphateAnimalsCarbazolesCell LineCyclic GMP-Dependent Protein KinasesEnzyme InhibitorsHumansKATP ChannelsKcnj11 ChannelNeuronsNitric OxideNitric Oxide DonorsNitroso CompoundsPatch-Clamp TechniquesPotassium Channels, Inwardly RectifyingPurinonesAdenosine TriphosphateCarbazolesCyclic GMP-Dependent Protein KinasesEnzyme InhibitorsKATP ChannelsKcnj11 ChannelKT 5823Nitric OxideNitric Oxide DonorsNitroso CompoundsNOC 18Potassium Channels, Inwardly RectifyingPurinonesRecombinant Fusion Proteinszaprinast

Identifiers

PMID18231807
OpenAlexW2006583445

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.