Evidence map›Paper›PMID 25261584›Full record

ArticleJournal of biochemistry2015

CCN family protein 2 (CCN2) promotes the early differentiation, but inhibits the terminal differentiation of skeletal myoblasts.

Takashi Nishida, Satoshi Kubota, Eriko Aoyama, Danilo Janune, Karen M Lyons, Masaharu Takigawa

Open access · greenAbstract read
In one paragraph

Article in Journal of biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

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  13. Article
  14. Frontiers in cellular and infection microbiology · 2019
    Article
  15. Article
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  17. Article
  18. 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

6 authors at 2 institutions in 2 countries.

Takashi NishidaDepartment of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama 700-8525, Japan; Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School, Okayama 700-8525, Japan; and Department of Orthopaedic Surgery, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA tnishida@md.okayama-u.ac.jp.
Satoshi KubotaDepartment of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama 700-8525, Japan; Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School, Okayama 700-8525, Japan; and Department of Orthopaedic Surgery, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
Eriko AoyamaDepartment of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama 700-8525, Japan; Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School, Okayama 700-8525, Japan; and Department of Orthopaedic Surgery, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
Danilo JanuneDepartment of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama 700-8525, Japan; Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School, Okayama 700-8525, Japan; and Department of Orthopaedic Surgery, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
Karen M LyonsDepartment of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama 700-8525, Japan; Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School, Okayama 700-8525, Japan; and Department of Orthopaedic Surgery, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
Masaharu TakigawaDepartment of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama 700-8525, Japan; Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School, Okayama 700-8525, Japan; and Department of Orthopaedic Surgery, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA Department of Biochemistry and Molecular Dentistry, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama 700-8525, Japan; Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School, Okayama 700-8525, Japan; and Department of Orthopaedic Surgery, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA takigawa@md.okayama-u.ac.jp.
University of California, Los Angeles · USOkayama University · JP

Funding

BMPS IN SKELETAL GROWTH AND OSTEOGENIC DIFFERENTIATIONR01AR044528 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LYONS, KAREN M. · 1998 to 2017
$5.2M
NIAMS NIH HHS R01 AR044528
6 · The paper itself

Abstract

Many studies have reported that CCN family protein 2 (also known as connective tissue growth factor) induces fibrotic response in skeletal muscle, thus emphasizing the pathological role of CCN2 in muscle tissues. However, the physiological role of CCN2 in myogenesis is still unknown. This study clarified the CCN2 functions during myogenesis. Recombinant CCN2 (rCCN2) promoted proliferation and MyoD production in C2C12 cells and primary myoblasts, but inhibited myogenin production. In accordance with these findings, the gene expression levels of myosin heavy chain, which is a marker of terminally differentiated myoblasts and desmin, which is the main intermediate filament protein of muscle cells, were decreased by rCCN2 treatment. In vivo analyses with Ccn2-deficient skeletal muscle revealed decreased proliferating cell nuclear antigen (PCNA)/MyoD double positive cells and muscle hypoplasia. Consistent with this finding, myogenic marker genes and myotube formation were repressed in Ccn2-deficient myoblasts. The protein production of CCN2 was increased in C2C12 myoblasts treated with tumor necrosis factor-α, which is a pro-inflammatory cytokine, suggesting its role in muscle regeneration after inflammation. These findings indicate that CCN2 promotes proliferation and early differentiation but inhibits the terminal differentiation of myoblasts, thus suggesting that CCN2 plays a physiological role in myogenesis.

Indexed as

Cell DifferentiationConnective Tissue Growth FactorGene Expression Regulation, DevelopmentalHumansMuscle DevelopmentMuscle, SkeletalMyoblastsMyoD ProteinCCN2 protein, humanConnective Tissue Growth FactorMyoD ProteinC2C12 cellsCCN2CTGFmyoblastsskeletal myogenesisTNFα

Identifiers

PMID25261584
PMCPMC6281389
OpenAlexW2120026169

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.