Evidence map›Paper›PMID 26512720›Full record

ArticlePloS one2015

New Isoform of Cardiac Myosin Light Chain Kinase and the Role of Cardiac Myosin Phosphorylation in α1-Adrenoceptor Mediated Inotropic Response.

Masaya Taniguchi, Ryuji Okamoto, Masaaki Ito, Itaru Goto, Satoshi Fujita, Katsuhisa Konishi, Hideo Mizutani, Kaoru Dohi, David J Hartshorne, Takeo Itoh

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 16% 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. Regulation of myosin light-chain phosphorylation and its roles in cardiovascular physiology and pathophysiology.Hypertension research : official journal of the Japanese Society of Hypertension · 2022
    Review
  4. Article
  5. α1-Adrenergic receptor regulates papillary muscle and aortic segment contractile function via modulation of store-operated CaJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2021
    Article
  6. Targeting Adrenergic Receptors in Metabolic Therapies for Heart Failure.International journal of molecular sciences · 2021
    Review
  7. Life science alliance · 2020
    Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Cardiac myosin light chain is phosphorylated by Ca2+/calmodulin-dependent and -independent kinase activities.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Masaya TaniguchiDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
Ryuji OkamotoDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
Masaaki ItoDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
Itaru GotoDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
Satoshi FujitaDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
Katsuhisa KonishiDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
Hideo MizutaniDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
Kaoru DohiDepartment of Cardiology and Nephrology, Mie University Graduate School of Medicine, Edobashi, Tsu 514-8507, Mie, Japan.
David J HartshorneMuscle Biology Group, University of Arizona, Tucson, Arizona, United States of America.
Takeo ItohDepartment of Pharmacology, Graduate School of Medical Sciences, Nagoya City University, Nagoya 467-8601, Japan.
Mie University · JPNagoya City University · JPUniversity of Arizona · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BACKGROUND &

aimsCardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. To test this hypothesis, the role played by ventricular MLC2 (MLC2v) phosphorylation was investigated in the phenylephrine-induced increase in twitch tension using the naturally-occurring mouse strain, C57BL/6N, in which cMLCK is down regulated. METHODS AND

resultsBy Western blot and nanoLC-MS/MS analysis, cMLCKs with molecular mass of 61-kDa (cMLCK-2) and/or 86-kDa were identified in mice heart. Among various mouse strains, C57BL/6N expressed cMLCK-2 alone and the closest relative strain C57BL/6J expressed both cMLCKs. The levels of MLC2v phosphorylation was significantly lower in C57BL/6N than in C57BL/6J. The papillary muscle twitch tension induced by electrical field stimulation was smaller in C57BL/6N than C57BL/6J. Phenylephrine had no effect on MLC2v phosphorylation in either strains but increased the twitch tension more potently in C57BL/6J than in C57BL/6N. Calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N. There was a significant positive correlation between the phenylephrine-induced inotropic response and the levels of MLC2v phosphorylation within ranges of 15-30%.

conclusionsWe identified a new isoform of cMLCK with a molecular mass of 61kDa(cMLCK-2) in mouse heart. In the C57BL/6N strain, only cMLCK-2 was expressed and the basal MLC2v phosphorylation levels and the phenylephrine-induced inotropic response were both smaller. We suggest that a lower phenylephrine-induced inotropic response may be caused by the lower basal MLC2v phosphorylation levels in this strain.

Indexed as

Myocardial ContractionAlternative SplicingAmino Acid SequenceAnimalsCardiac MyosinsGene ExpressionGene OrderIsoenzymesMaleMiceMolecular Sequence DataMyocardiumMyocytes, CardiacMyosin-Light-Chain KinasePhosphorylationRatsCardiac MyosinsIsoenzymesMyosin-Light-Chain KinaseReceptors, Adrenergic, alpha-1RNA, Messenger

Identifiers

PMID26512720
PMCPMC4626101
OpenAlexW2230936396

What OpenQuestion holds

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LicenceCC BY
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.