Evidence map›Paper›PMID 8557743›Full record

ArticleThe Journal of cell biology1995

Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function.

P von Arx, S Bantle, T Soldati, J C Perriard

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 92 citations in OpenAlex.

  1. Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023
    Review
  2. Review
  3. A solution to the long-standing problem of actin expression and purification.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Review
  5. Extracellular Matrix in Regulation of Contractile System in Cardiomyocytes.International journal of molecular sciences · 2019
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Context-dependent functional substitution of alpha-skeletal actin by gamma-cytoplasmic actin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    Article
  15. Diverse roles of the actin cytoskeleton in striated muscle.Journal of muscle research and cell motility · 2009
    Review
  16. Cytoplasmic gamma-actin contributes to a compensatory remodeling response in dystrophin-deficient muscle.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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 1 institution in 1 country.

P von ArxInstitute for Cell Biology, Swiss Federal Institute of Technology, Zürich, Switzerland.
S Bantle
T Soldati
J C Perriard
École Polytechnique Fédérale de Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intracompartmental sorting and functional consequences of ectopic expression of the six vertebrate actin isoforms was investigated in different types of cultured cells. In transfected fibroblasts all isoactin species associated with the endogenous microfilament cytoskeleton, even though cytoplasmic actins also showed partial localization to peripheral submembranous sites. Functional and structural studies were performed in neonatal and adult rat cardiomyocytes. All the muscle isoactin constructs sorted preferentially to sarcomeric sites and, to a lesser extent, also to stress-fiber-like structures. The expression of muscle actins did not interfere with cell contractility, and did not disturb the localization of endogenous sarcomeric proteins. In sharp contrast, ectopic expression of the two cytoplasmic actin isoforms resulted in rapid cessation of cellular contractions and induced severe morphological alterations characterized by an exceptional outgrowth of filopodia and cell flattening. Quantitative analysis in neonatal cardiomyocytes indicated that the levels of accumulation of the different isoactins are very similar and cannot be responsible for the observed isoproteins-specific effects. Structural analysis revealed a remodeling of the cytoarchitecture including a specific alteration of sarcomeric organization; proteins constituting the sarcomeric thin filaments relocated to nonmyofibrillar sites while thick filaments and titin remained unaffected. Experiments with chimeric proteins strongly suggest that isoform specific residues in the carboxy-terminal portion of the cytoplasmic actins are responsible for the dominant negative effects on function and morphology.

Indexed as

ActinsAnimalsAnimals, NewbornChickensCytoplasmEpitopesHeart VentriclesIsomerismMuscle ContractionMuscle Fibers, SkeletalMyosinsRatsRats, Sprague-DawleyRecombinant Fusion ProteinsSarcomeresTransfectionActinsEpitopesMyosinsRecombinant Fusion Proteins

Identifiers

PMID8557743
PMCPMC2120671
OpenAlexW2164428122

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.