Evidence map›Paper›PMID 24895400›Full record

ArticleJournal of cell science2014

Extracellular deposition of matrilin-2 controls the timing of the myogenic program during muscle regeneration.

Ferenc Deák, Lajos Mátés, Eva Korpos, Agnes Zvara, Tibor Szénási, Mónika Kiricsi, Luca Mendler, Anikó Keller-Pintér, Béla Ozsvári, Hajnalka Juhász and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Reorganization of chromatin architecture during prenatal development of porcine skeletal muscle.DNA research : an international journal for rapid publication of reports on genes and genomes · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

15 authors at 6 institutions in 2 countries.

Ferenc DeákInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary.
Lajos MátésInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary Institute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary mates@brc.hu kiss@brc.hu.
Eva KorposInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary Institute of Physiological Chemistry and Pathobiochemistry, Muenster University, D-48149 Muenster, Germany.
Agnes ZvaraInstitute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary.
Tibor SzénásiInstitute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary.
Mónika KiricsiInstitute of Biochemistry, Faculty of General Medicine, University of Szeged, H-6720 Szeged, Hungary Department of Biochemistry and Molecular Biology, Faculty of Natural Sciences and Informatics, University of Szeged, H-6720 Szeged, Hungary.
Luca MendlerInstitute of Biochemistry, Faculty of General Medicine, University of Szeged, H-6720 Szeged, Hungary.
Anikó Keller-PintérInstitute of Biochemistry, Faculty of General Medicine, University of Szeged, H-6720 Szeged, Hungary.
Béla OzsváriAvidin Ltd., H-6726 Szeged, Hungary.
Hajnalka JuhászInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary.
Lydia SorokinInstitute of Physiological Chemistry and Pathobiochemistry, Muenster University, D-48149 Muenster, Germany.
László DuxInstitute of Biochemistry, Faculty of General Medicine, University of Szeged, H-6720 Szeged, Hungary.
Nicolas MermodInstitute of Biotechnology, University of Lausanne, and Center for Biotechnology of the University of Lausanne and École Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
László G PuskásInstitute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary Avidin Ltd., H-6726 Szeged, Hungary.
Ibolya KissInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6701 Szeged, Hungary Avidin Ltd., H-6726 Szeged, Hungary mates@brc.hu kiss@brc.hu.
Institute of Biochemistry · HUUniversity of Szeged · HUHUN-REN Szegedi Biológiai Kutatóközpont · HUInstitute of Genetics · HUÉcole Polytechnique Fédérale de Lausanne · CHHungarian Academy of Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we identify a role for the matrilin-2 (Matn2) extracellular matrix protein in controlling the early stages of myogenic differentiation. We observed Matn2 deposition around proliferating, differentiating and fusing myoblasts in culture and during muscle regeneration in vivo. Silencing of Matn2 delayed the expression of the Cdk inhibitor p21 and of the myogenic genes Nfix, MyoD and Myog, explaining the retarded cell cycle exit and myoblast differentiation. Rescue of Matn2 expression restored differentiation and the expression of p21 and of the myogenic genes. TGF-β1 inhibited myogenic differentiation at least in part by repressing Matn2 expression, which inhibited the onset of a positive-feedback loop whereby Matn2 and Nfix activate the expression of one another and activate myoblast differentiation. In vivo, myoblast cell cycle arrest and muscle regeneration was delayed in Matn2(-/-) relative to wild-type mice. The expression levels of Trf3 and myogenic genes were robustly reduced in Matn2(-/-) fetal limbs and in differentiating primary myoblast cultures, establishing Matn2 as a key modulator of the regulatory cascade that initiates terminal myogenic differentiation. Our data thus identify Matn2 as a crucial component of a genetic switch that modulates the onset of tissue repair.

Indexed as

AnimalsApoptosisCell LineCell ProliferationElapid VenomsExtracellular MatrixHumansMatrilin ProteinsMiceMice, KnockoutMuscle DevelopmentMusclesMyoblastsNecrosisRatsRats, WistarElapid VenomsMatrilin ProteinsnotexinBMP signalingMatn2 shRNAMuscle regenerationMyogenesisNFITGF-β signalingTrf3

Identifiers

PMID24895400
PMCPMC4117230
OpenAlexW2008900589

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.