Evidence map›Paper›PMID 26869200›Full record

ArticleArchives of biochemistry and biophysics2016

Functionally conservative substitutions at cardiac troponin I S43/45.

Sarah E Lang, Tamara K Stevenson, Dongyang Xu, Ryan O'Connell, Margaret V Westfall

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–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

2 citing papers in PubMed.

  1. Review
  2. Myofilament modulation of contraction.Archives of biochemistry and biophysics · 2016
    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

5 authors.

Sarah E LangProgram in Cellular and Molecular Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Tamara K StevensonDepartment of Cardiac Surgery, University of Michigan, Ann Arbor, MI 48109, USA; Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI 48109, USA.
Dongyang XuDepartment of Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109, USA.
Ryan O'ConnellDepartment of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI 48109, USA.
Margaret V WestfallProgram in Cellular and Molecular Biology, University of Michigan, Ann Arbor, MI 48109, USA; Department of Cardiac Surgery, University of Michigan, Ann Arbor, MI 48109, USA; Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: wfall@med.umich.edu.

Funding

PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
SYTEMS AND INTEGRATIVE BIOLOGYT32GM008322 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LOW, MALCOLM JAMES · 1990 to 2020
$5.7M
PKC Troponin I phosphorylation &contractile functionR01HL067254 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WESTFALL, MARGARET V · 2002 to 2010
$2.3M
NHLBI NIH HHS R01 HL067254NIDDK NIH HHS P30 DK020572NIDDK NIH HHS P60 DK020572NIGMS NIH HHS T32 GM007315NIGMS NIH HHS T32 GM008322
6 · The paper itself

Abstract

A phospho-null Ala substitution at protein kinase C (PKC)-targeted cardiac troponin I (cTnI) S43/45 reduces myocyte and cardiac contractile function. The goal of the current study was to test whether cTnIS43/45N is an alternative, functionally conservative substitution in cardiac myocytes. Partial and more extensive endogenous cTnI replacement was similar at 2 and 4 days after gene transfer, respectively, for epitope-tagged cTnI and cTnIS43/45N. This replacement did not significantly change thin filament stoichiometry. In functional studies, there were no significant changes in the amplitude and/or rates of contractile shortening and re-lengthening after this partial (2 days) and extensive (4 days) replacement with cTnIS43/45N. The cTnIS43/45N substitution also was not associated with adaptive changes in the myocyte Ca(2+) transient or in phosphorylation of the protein kinase A and C-targeted cTnIS23/24 site. These results provide evidence that cTnIS43/45N is a functionally conservative substitution, and may be appropriate for use as a phospho-null in rodent models designed for studies on PKC modulation of cardiac performance.

Indexed as

Amino Acid SubstitutionAnimalsCalciumEpitopesGene Transfer TechniquesMutagenesis, Site-DirectedMyocardial ContractionMyocardiumMyocytes, CardiacPhosphorylationProtein Kinase CRatsRats, Sprague-DawleySarcomeresSignal TransductionTroponin ICalciumEpitopesProtein Kinase CTroponin IHeartMyofilamentPhosphorylationTroponin

Identifiers

PMID26869200
PMCPMC4899172

What OpenQuestion holds

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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.