Evidence map›Paper›PMID 30428777›Full record

ArticleReproductive sciences (Thousand Oaks, Calif.)2019

Differential Regulation of Myosin Regulatory Light Chain Phosphorylation by Protein Kinase C Isozymes in Human Uterine Myocytes.

Bryan F Mitchell, Mei Chi, Elle Surgent, Bailey M Sorochan, Curtis N Tracey, Hector N Aguilar, Maily Mongin, Barbara Zielnik

Abstract read
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In one paragraph

Article in Reproductive sciences (Thousand Oaks, Calif.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 34% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

8 authors at 2 institutions in 1 country.

Bryan F MitchellDepartment of Obstetrics and Gynecology, The Women and Children's Health Research Institute, University of Alberta, Edmonton, Alberta, Canada. brymitch@ualberta.ca.
Mei ChiDepartment of Obstetrics and Gynecology, The Women and Children's Health Research Institute, University of Alberta, Edmonton, Alberta, Canada.
Elle SurgentDepartment of Obstetrics and Gynecology, The Women and Children's Health Research Institute, University of Alberta, Edmonton, Alberta, Canada.
Bailey M SorochanDepartment of Obstetrics and Gynecology, The Women and Children's Health Research Institute, University of Alberta, Edmonton, Alberta, Canada.
Curtis N TraceyDepartment of Physiology, The Women and Children's Health Research Institute, University of Albert, Edmonton, Alberta, Canada.
Hector N AguilarDepartment of Physiology, The Women and Children's Health Research Institute, University of Albert, Edmonton, Alberta, Canada.
Maily MonginDepartment of Obstetrics and Gynecology, The Women and Children's Health Research Institute, University of Alberta, Edmonton, Alberta, Canada.
Barbara ZielnikDepartment of Obstetrics and Gynecology, The Women and Children's Health Research Institute, University of Alberta, Edmonton, Alberta, Canada.
University of Alberta · CAWomen and Children’s Health Research Institute · CA

Funding

CIHR
6 · The paper itself

Abstract

backgroundPreterm birth is the most common cause of neonatal morbidity and mortality and a common precedent to lifelong disability. Current treatment has minimal efficacy.

objectiveWe assessed the role of isozymes of the protein kinase C (PKC) family in regulating the phosphorylation of myosin regulatory light chains (RLCs), which regulate uterine contractility. We also explored the mechanisms through which these isozymes function. STUDY

designWe used a previously characterized and validated quantitative in-cell Western (ICW) assay to measure site-specific phosphorylations on myosin RLC and CPI-17. Cultures of human uterine myocytes (hUM) were treated with the potent contractile stimulant oxytocin to induce uterine contractility or a pharmacological mimic of diacyl-glycerol to stimulate the conventional and novel isozymes of the PKC family. Combinations of isozyme-selective inhibitors were used to determine the effects of the conventional and novel classes of isozymes.

resultsStimulation of PKC using phospho-dibutyrate caused immediate, concentration-dependent inhibition of uterine activity

conclusionsSpecific agonists for the conventional isozymes or inhibitors of the novel isozymes of the PKC family could be useful pharmacological agents for regulation of uterine activity.

Indexed as

Uterine ContractionAnimalsCells, CulturedEnzyme ActivationEnzyme ActivatorsFemaleHumansIntracellular Signaling Peptides and ProteinsIsoenzymesMuscle ProteinsMyocytes, Smooth MuscleMyosin-Light-Chain KinaseMyosin Light ChainsOxytocicsPhosphorylationProtein Kinase CEnzyme ActivatorsIntracellular Signaling Peptides and ProteinsIsoenzymesMuscle ProteinsMyosin-Light-Chain KinaseMyosin Light ChainsOxytocicsPPP1R14A protein, humanProtein Kinase CProtein Kinase InhibitorsCPI-17myosin regulatory light chainsparturitionpreterm laborprotein kinase Cuterine contractility

Identifiers

PMID30428777
OpenAlexW2901758319

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.