Evidence map›Paper›PMID 15136749›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

NO stimulation of ATP-sensitive potassium channels: Involvement of Ras/mitogen-activated protein kinase pathway and contribution to neuroprotection.

Yu-Fung Lin, Kimberly Raab-Graham, Yuh Nung Jan, Lily Yeh Jan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
–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

27 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Regulation of Ras Signaling by S-Nitrosylation.Antioxidants (Basel, Switzerland) · 2023
    Review
  3. Review
  4. Functional modulation of sarcolemmal KAmerican journal of physiology. Cell physiology · 2020
    Article
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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

4 authors.

Yu-Fung LinHoward Hughes Medical Institute and Department of Physiology, University of California, San Francisco, CA 94143-0725, USA. yflin@ucdavis.edu
Kimberly Raab-Graham
Yuh Nung Jan
Lily Yeh Jan

Funding

Genetic Studies of the SynapseR01MH065334 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAN, LILY Y · 2001 to 2020
$3.8M
Genetic Studies of the SynapseR37MH065334 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAN, LILY Y · 2006 to 2015
$3.8M
NIMH NIH HHS MH65334NIMH NIH HHS R01 MH065334NIMH NIH HHS R37 MH065334
6 · The paper itself

Abstract

ATP-sensitive potassium (K(ATP)) channels regulate insulin release, vascular tone, and neuronal excitability. Whether these channels are modulated by NO, a membrane-permeant messenger in various physiological and pathological processes, is not known. The possibility of NO signaling via K(ATP) channel modulation is of interest because both NO and K(ATP) have been implicated in physiological functions such as vasodilation and neuroprotection. In this report, we demonstrate a mechanism that leads to K(ATP) activation via NO/Ras/mitogen-activated protein kinase pathway. By monitoring K(ATP) single-channel activities from human embryonic kidney 293 cell-attached patches expressing sulfonylurea receptor 2B and Kir6.2, we found K(ATP) stimulation by NO donor Noc-18, a specific NO effect abolished by NO scavenger 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) but not guanylyl cyclase inhibitor 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ). NO stimulation of K(ATP) is indirect and requires Ras and mitogen-activated protein kinase kinase activities. Blockade of Ras activation by pharmacological means or by coexpressing either a dominant-negative or an S-nitrosylation-site mutant Ras protein significantly abrogates the effects of NO. Inhibition of mitogen-activated protein kinase kinase abolishes the NO activation of K(ATP) but suppression of phosphatidylinositol 3-kinase does not. The NO precursor l-Arg also stimulates K(ATP) via endogenous NO synthase and the Ras signaling pathway. In addition, in rat hippocampal neurons, the protective effect of ischemic preconditioning induced by oxygen-glucose deprivation requires K(ATP) and NO synthase activity during preconditioning. Thus, neuroprotection caused by NO released during the short episode of sublethal ischemia may be mediated partly by K(ATP) stimulation.

Indexed as

Adenosine TriphosphateAnimalsArginineHumansMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesNeuronsNeuroprotective AgentsNitric OxideNitric Oxide Synthaseomega-N-MethylargininePotassium Channelsras ProteinsRatsAdenosine TriphosphateArginineMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesNeuroprotective AgentsNitric OxideNitric Oxide Synthaseomega-N-MethylargininePotassium Channelsras Proteins

Identifiers

PMID15136749
PMCPMC419686

What OpenQuestion holds

Textmetadata
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.