Evidence map›Paper›PMID 19830444›Full record

ArticleHistochemistry and cell biology2009

Switching of actin isoforms in skeletal muscle differentiation using mouse ES cells.

Yota Mizuno, Mayu Suzuki, Hiroki Nakagawa, Nana Ninagawa, Shigeko Torihashi

Abstract read
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In one paragraph

Article in Histochemistry and cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 46% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. CAP2 deficiency delays myofibril actin cytoskeleton differentiation and disturbs skeletal muscle architecture and function.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  3. Article
  4. 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

5 authors at 1 institution in 1 country.

Yota MizunoDepartment of Physical Therapy, Nagoya University School of Health Sciences, Nagoya, Japan.
Mayu Suzuki
Hiroki Nakagawa
Nana Ninagawa
Shigeko Torihashi
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among six actin isoforms, alpha-skeletal and alpha-cardiac actins have similar amino acid components and are highly conserved. Although skeletal muscles essentially express alpha-skeletal actins in the adult tissue, alpha-cardiac isoform actin is prominent in the embryonic muscle tissue. Switching of actin isoforms from alpha-cardiac to alpha-skeletal actin occurs during skeletal muscle differentiation. The cardiac type alpha-actin is expressed in the regeneration and patho-physiological states of the skeletal muscles as well. In the present study, we demonstrate the morphological switching of alpha-type actin isoforms from alpha-cardiac to alpha-skeletal actin in vitro using mouse ES cells for the first time. Immunofluorescent double staining with two specific antibodies revealed that alpha-cardiac actin appeared first in myoblasts. After cell fusion to form myotubes, the cardiac type actin decreased and alpha-skeletal actin conversely increased. Finally, the alpha-skeletal isoform remained as a main actin component in the fully mature skeletal muscle fibers. The exchange of isoforms is not directly linked to the sarcomere formation. As a result, ES cells provide a useful in vitro system for exploring skeletal muscle differentiation.

Indexed as

Cell DifferentiationActinsAnimalsEmbryonic Stem CellsMiceMuscle Fibers, SkeletalMuscle, SkeletalMyoblastsProtein IsoformsSarcomeresActinsProtein Isoforms

Identifiers

PMID19830444
OpenAlexW2043519276

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.