Evidence map›Paper›PMID 7543902›Full record

ArticleThe Journal of cell biology1995

The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo.

C Chaponnier, M Goethals, P A Janmey, F Gabbiani, G Gabbiani, J Vandekerckhove

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Regulation of actin isoforms in cellular and developmental processes.Seminars in cell & developmental biology · 2020
    Review
  5. Extracellular Matrix in Regulation of Contractile System in Cardiomyocytes.International journal of molecular sciences · 2019
    Review
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  7. Article
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  10. Review
  11. Review
  12. Article
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  15. Review
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  17. Article
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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

6 authors at 1 institution in 1 country.

C ChaponnierDepartment of Pathology, University of Geneva, Switzerland.
M Goethals
P A Janmey
F Gabbiani
G Gabbiani
J Vandekerckhove
University of Geneva · CH

Funding

REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR01AR038910 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI JANMEY, PAUL A · 1991 to 2006
$2.2M
REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR29AR038910 · NIAMS · MASSACHUSETTS GENERAL HOSPITAL · PI JANMEY, PAUL A · 1987 to 1989
–
NIAMS NIH HHS AR38910
6 · The paper itself

Abstract

The blocking effect of the NH2-terminal decapeptide of alpha-smooth muscle (SM) actin AcEEED-STALVC on the binding of the specific monoclonal antibody anti-alpha SM-1 (Skalli, O., P. Ropraz, A. Trzeviak, G. Benzonana, D. Gillessen, and G. Gabbiani. 1986. J. Cell Biol. 103:2787-2796) was compared with that of synthetic peptides modified by changing the acetyl group or by substituting an amino acid in positions 1 to 5. Using immunofluorescence and immunoblotting techniques, anti-alpha SM-1 binding was abolished by the native peptide and by peptides with a substitution in position 5, indicating that AcEEED is the epitope for anti-alpha SM-1. Incubation of anti-alpha SM-1 (or of its Fab fragment) with arterial SM actin increased polymerization in physiological salt conditions; the antibody binding did not hinder the incorporation of the actin antibody complex into the filaments. This action was not exerted on skeletal muscle actin. After microinjection of the alpha-SM actin NH2-terminal decapeptide or of the epitopic peptide into cultured aortic smooth muscle cells, double immunofluorescence for alpha-SM actin and total actin showed a selective disappearance of alpha-SM actin staining, detectable at approximately 30 min. When a control peptide (e.g. alpha-skeletal [SK] actin NH2-terminal peptide) was microinjected, this was not seen. This effect is compatible with the possibility that the epitopic peptide traps a protein involved in alpha-SM actin polymerization during the dynamic filament turnover in stress fibers. Whatever the mechanism, this is the first evidence that the NH2 terminus of an actin isoform plays a role in the regulation of polymerization in vitro and in vivo.

Indexed as

ActinsAmino Acid SequenceAnimalsAntibody SpecificityAortaBinding, CompetitiveCentrifugationEpitopesImmunoblottingMicroinjectionsMicroscopy, ElectronMicroscopy, FluorescenceMolecular Sequence DataMuscle, Smooth, VascularOligopeptidesPeptide FragmentsActinsEpitopesOligopeptidesPeptide FragmentsPolymers

Identifiers

PMID7543902
PMCPMC2199961
OpenAlexW2132858870

What OpenQuestion holds

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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.