Evidence map›Paper›PMID 21378385›Full record

ArticleCardiovascular research2011

Enhanced contractility and myosin phosphorylation induced by Ca(2+)-independent MLCK activity in hypertensive rats.

Young-Eun Cho, Duck-Sun Ahn, Kathleen G Morgan, Young-Ho Lee

Open access · bronzeAbstract read
In one paragraph

Article in Cardiovascular research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  5. Review
  6. 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
  7. Article
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  11. Highly sensitive myosin phosphorylation analysis in the renal afferent arteriole.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2016
    Review
  12. Article
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  14. Review
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  19. Role for PKCβ in enhanced endothelin-1-induced pulmonary vasoconstrictor reactivity following intermittent hypoxia.American journal of physiology. Lung cellular and molecular physiology · 2011
    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

4 authors at 3 institutions in 3 countries.

Young-Eun ChoDepartment of Physiology, College of Medicine, BK 21 Project for Medical Sciences, Yonsei University, CPO Box 8044, Seoul 120-752, Korea.
Duck-Sun Ahn
Kathleen G Morgan
Young-Ho Lee
Yonsei University · KRBoston University · USCzech Academy of Sciences, Institute of Physiology · CZ

Funding

Subcellular Organization of Signaling in Smooth MuscleR01HL080003 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2006 to 2009
$1.7M
NHLBI NIH HHS HL80003
6 · The paper itself

Abstract

aimsThe role of Ca(2+) sensitization induced by a Ca(2+)-independent myosin light chain kinase (MLCK) in hypertension has not been determined. The aim of this study was to clarify the role of possible Ca(2+)-independent MLCK activity in hypertension. METHODS AND

resultsWe compared increases in contractile force and phosphorylation of myosin light chain (MLC) evoked by calyculin A, a phosphatase inhibitor, in β-escin-permeabilized mesenteric arteries at pCa 9.0 between spontaneously hypertensive rat (SHR) and Wistar Kyoto rat (WKY). We found that there was no detectable phosphorylation of MLC at pCa 9.0, but that the administration of 1 μM calyculin A gradually increased force and mono- and di-phosphorylation of MLC. This contraction was inhibited by staurosporine but not by wortmannin, Y-27632, or calphostin-C. The calyculin A-induced contraction was significantly greater in the SHR than in the WKY and was associated with an increase in mono- and di-phosphorylation of MLC. SM-1, a zipper-interacting protein kinase (ZIPK)-inhibiting peptide, significantly inhibited the amplitude of the calyculin A-induced contraction and di-phosphorylation. Total ZIPK expression (54 + 32 kDa) was greater in the SHR than in the WKY. Phosphorylation of myosin phosphatase target subunit at Thr(697), but not at Thr(855), was consistently stronger in the SHR than in the WKY in calyculin A-treated tissues at pCa 9.0.

conclusionsOur results suggest that Ca(2+)-independent MLCK activity is enhanced in the SHR, and that ZIPK plays, at least in part, an important role as a candidate for this kinase in rat mesenteric arteries.

Indexed as

VasoconstrictionAnalysis of VarianceAnimalsApoptosis Regulatory ProteinsCalcium-Calmodulin-Dependent Protein KinasesDeath-Associated Protein KinasesDisease Models, AnimalDose-Response Relationship, DrugEnzyme InhibitorsHypertensionMaleMarine ToxinsMesenteric ArteriesMuscle ProteinsMuscle, Smooth, VascularMyosin-Light-Chain KinaseApoptosis Regulatory ProteinsCalcium-Calmodulin-Dependent Protein Kinasescalyculin ADeath-Associated Protein KinasesEnzyme InhibitorsMarine ToxinsMuscle ProteinsMyosin-Light-Chain KinaseMyosin Light ChainsOxazolesPhosphoprotein PhosphatasesPhosphoproteinsPpp1r12a protein, ratPpp1r14a protein, ratProtein Kinase CProtein Phosphatase 1Vasoconstrictor Agents

Identifiers

PMID21378385
PMCPMC3112018
OpenAlexW2163481427

What OpenQuestion holds

Textmetadata
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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.