Evidence map›Paper›PMID 26068620›Full record

ArticlePloS one2015

Syndecan-4 Regulates Muscle Differentiation and Is Internalized from the Plasma Membrane during Myogenesis.

Sissel B Rønning, Cathrine R Carlson, Espen Stang, Svein O Kolset, Kristin Hollung, Mona E Pedersen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

27 citing papers in PubMed, 45 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Overexpression ofJournal of animal science and technology · 2025
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  15. Exerkines in health, resilience and disease.Nature reviews. Endocrinology · 2022
    Review
  16. Article
  17. An Atlas of Heparan Sulfate Proteoglycans in the Postnatal Rat Lens.Investigative ophthalmology & visual science · 2021
    Article
  18. Review
  19. Syndecan-4Frontiers in cell and developmental biology · 2020
    Article
  20. Genetic Deletion ofNutrients · 2019
    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

6 authors at 4 institutions in 1 country.

Sissel B RønningNofima AS, Pb 210, NO-1431 Ås, Norway.
Cathrine R CarlsonInstitute for Experimental Medical Research, Oslo University Hospital and University of Oslo, Oslo, Norway; KG Jebsen Cardiac Research Center and Center for Heart Failure Research, University of Oslo, Oslo, Norway.
Espen StangDepartment of Pathology, Oslo University Hospital, Rikshospitalet, P.O. Box 4950 Nydalen, 0424 Oslo, Norway.
Svein O KolsetDepartment of Nutrition, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Kristin HollungNofima AS, Pb 210, NO-1431 Ås, Norway.
Mona E PedersenNofima AS, Pb 210, NO-1431 Ås, Norway.
Nofima · NOOslo University Hospital · NOFafo Foundation · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cell surface proteoglycan syndecan-4 has been reported to be crucial for muscle differentiation, but the molecular mechanisms still remain to be fully understood. During in vitro differentiation of bovine muscle cells immunocytochemical analyses showed strong labelling of syndecan-4 intracellularly, in close proximity with Golgi structures, in membranes of intracellular vesicles and finally, in the nuclear area including the nuclear envelope. Chase experiments showed that syndecan-4 was internalized from the plasma membrane during this process. Furthermore, when syndecan-4 was knocked down by siRNA more myotubes were formed, and the expression of myogenic transcription factors, β1-integrin and actin was influenced. However, when bovine muscle cells were treated with a cell-penetrating peptide containing the cytoplasmic region of syndecan-4, myoblast fusion and thus myotube formation was blocked, both in normal cells and in syndecan-4 knock down cells. Altogether this suggests that the cytoplasmic domain of syndecan-4 is important in regulation of myogenesis. The internalization of syndecan-4 from the plasma membrane during muscle differentiation and the nuclear localization of syndecan-4 in differentiated muscle cells may be part of this regulation, and is a novel aspect of syndecan biology which merits further studies.

Indexed as

Cell DifferentiationMuscle DevelopmentAmino Acid SequenceAnimalsCattleCell MembraneCells, CulturedMolecular Sequence DataMuscle Fibers, SkeletalProtein Structure, TertiaryProtein TransportSyndecan-4Syndecan-4

Identifiers

PMID26068620
PMCPMC4467083
OpenAlexW1153240504

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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.