Evidence map›Paper›PMID 23817200›Full record

ArticleCirculation research2013

Inhibitor κB kinase 2 is a myosin light chain kinase in vascular smooth muscle.

Zhekang Ying, Jussara M do Carmo, Lusha Xiang, Alexandre A da Silva, Minjie Chen, Michael J Ryan, Michael Ostrowski, Sanjay Rajagopalan, John E Hall

Open access · bronzeAbstract read
In one paragraph

Article in Circulation research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Multiscale imaging of basal cell dynamics in the functionally mature mammary gland.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. The pathophysiological basis of vascular disease.Laboratory investigation; a journal of technical methods and pathology · 2019
    Article
  6. Article
  7. Involvement of inhibitor kappa B kinase 2 (IKK2) in the regulation of vascular tone.Laboratory investigation; a journal of technical methods and pathology · 2018
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Dual regulation of tumor necrosis factor-α on myosin light chain phosphorylation in vascular smooth muscle.American journal of physiology. Heart and circulatory physiology · 2015
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Zhekang YingDepartment of Physiology and Biophysics, University of Mississippi Medical Center, Jackson, MS, USA. yingzhekang@hotmail.com
Jussara M do Carmo
Lusha Xiang
Alexandre A da Silva
Minjie Chen
Michael J Ryan
Michael Ostrowski
Sanjay Rajagopalan
John E Hall
Shanghai East Hospital · CN

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Jennifer A. Woyach · 1985 to 2026
$132.3M
STRUCTURAL VASCULAR ADAPTATION OF THE MICROCIRCULATIONP01HL051971 · NHLBI · UNIVERSITY OF MISSISSIPPI MEDICAL CENTER · PI HALL, JOHN E · 1993 to 2018
$39.4M
NCI NIH HHS P30 CA016058NHLBI NIH HHS P01 HL051971NHLBI NIH HHS P01 HL-51971
6 · The paper itself

Abstract

rationaleMyosin light chain (MLC) phosphorylation determines vascular contractile status. In addition to the classic Ca²⁺-dependent MLC kinase (MLCK), another unidentified kinase(s) also contributes to MLC phosphorylation in living cells. Inhibitor κB kinase 2 (IKK2)-deficient mouse embryonic fibroblasts demonstrate abnormal morphology and migration, suggesting that IKK2 may be involved in MLC phosphorylation.

objectiveTherefore, we tested whether IKK2 is an MLCK in living cells and the role of IKK2 in mediating vasoconstriction and blood pressure regulation. METHODS AND

resultsIn the present study, we showed that recombinant IKK2-phosphorylated MLC and intact myosin in vitro, and the kinetic parameters were comparable with those of the classic MLCK. Overexpression of IKK2 increased cellular MLC phosphorylation level, and pharmacological inhibition of IKK2 markedly decreased vascular smooth muscle cell MLC phosphorylation, suggesting that IKK2 is an MLCK in living cells. IKK2 inhibitors dose- and time-dependently attenuated vasoconstriction elicited by diverse agonists, suggesting the physiological importance of IKK2 as an MLCK. Vascular smooth muscle cell-specific IKK2-deficient mice had decreased aortic contractile responses, and reduced hypertensive responses to several vasoconstrictors, compared with wild-type mice, confirming the physiological importance of IKK2 as an MLCK.

conclusionsOur data provide a novel mechanism whereby IKK2 regulates MLC phosphorylation as an MLCK and, thus, vascular function and blood pressure.

Indexed as

AnimalsBlood PressureCell LineCrosses, GeneticDermatitisHumansI-kappa B KinaseMiceMice, KnockoutMuscle, Smooth, VascularMyocytes, Smooth MuscleMyosin-Light-Chain KinaseMyosin Light ChainsMyosinsPeptide FragmentsPhosphorylationI-kappa B KinaseIkbkb protein, mouseMyosin-Light-Chain KinaseMyosin Light ChainsMyosinsPeptide FragmentsReceptors, Tumor Necrosis Factor, Type IRecombinant Fusion ProteinsSC 514ThiophenesTnfrsf1a protein, mouseVasoconstrictor AgentsVasodilator Agentsblood pressureblood vesselshypertensionIKK2MLCmuscle, smooth, vascularmyosinsphosphorylation

Identifiers

PMID23817200
PMCPMC3970202
OpenAlexW2106380162

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.