Evidence map›Paper›PMID 21982947›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2012

Synemin isoforms differentially organize cell junctions and desmin filaments in neonatal cardiomyocytes.

Linda M Lund, Jaclyn P Kerr, Jenna Lupinetti, Yinghua Zhang, Mary A Russell, Robert J Bloch, Meredith Bond

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. TheToxins · 2022
    Article
  8. Review
  9. Synemin Redefined: Multiple Binding Partners Results in Multifunctionality.Frontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Myopathic changes in murine skeletal muscle lacking synemin.American journal of physiology. Cell physiology · 2015
    Article
  15. Article
  16. Article
  17. 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

7 authors at 2 institutions in 1 country.

Linda M LundDepartment of Physiology, University of Maryland, Baltimore, MD 21201, USA. llund001@umaryland.edu
Jaclyn P Kerr
Jenna Lupinetti
Yinghua Zhang
Mary A Russell
Robert J Bloch
Meredith Bond
University of Maryland, Baltimore · USKent State University · US

Funding

Intermediate Filaments & Costamere Structure & FunctionR01AR055928 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI BLOCH, ROBERT J · 2009 to 2010
$758k
NIAMS NIH HHS R01 AR055928NIAMS NIH HHS R01 AR055928RO1PHS HHS R01-02520711
6 · The paper itself

Abstract

Intermediate filaments (IFs) in cardiomyocytes consist primarily of desmin, surround myofibrils at Z disks, and transmit forces from the contracting myofilaments to the cell surface through costameres at the sarcolemma and desmosomes at intercalated disks. Synemin is a type IV IF protein that forms filaments with desmin and also binds α-actinin and vinculin. Here we examine the roles and expression of the α and β forms of synemin in developing rat cardiomyocytes. Quantitative PCR showed low levels of expression for both synemin mRNAs, which peaked at postnatal day 7. Synemin was concentrated at sites of cell-cell adhesion and at Z disks in neonatal cardiomyocytes. Overexpression of the individual isoforms showed that α-synemin preferentially localized to cell-cell junctions, whereas β-synemin was primarily at the level of Z disks. An siRNA targeted to both synemin isoforms reduced protein expression in cardiomyocytes by 70% and resulted in a failure of desmin to align with Z disks and disrupted cell-cell junctions, with no effect on sarcomeric organization. Solubility assays showed that β-synemin was soluble and interacted with sarcomeric α-actinin by coimmunoprecipitation, while α-synemin and desmin were insoluble. We conclude that β-synemin mediates the association of desmin IFs with Z disks, whereas α-synemin stabilizes junctional complexes between cardiomyocytes.

Indexed as

ActininAnimalsAnimals, NewbornCell AdhesionDesminIntercellular JunctionsIntermediate Filament ProteinsIntermediate FilamentsIsomerismMyocytes, CardiacPrimary Cell CultureRatsRNA, MessengerRNA, Small InterferingSarcomeresSolubilityActininDesminIntermediate Filament ProteinsRNA, MessengerRNA, Small InterferingSynm protein, ratVcl protein, ratVinculin

Identifiers

PMID21982947
PMCPMC3250239
OpenAlexW1989502888

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.