Evidence map›Paper›PMID 27658374›Full record

ArticleGlia2016

Cadm3 (Necl-1) interferes with the activation of the PI3 kinase/Akt signaling cascade and inhibits Schwann cell myelination in vitro.

Ming-Shuo Chen, Hyosung Kim, Léonard Jagot-Lacoussiere, Patrice Maurel

Open access · greenAbstract read
In one paragraph

Article in Glia, 2016. 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
1.2field-weighted citation impact, top 24% 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, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Differential Contribution of Cadm1-Cadm3 Cell Adhesion Molecules to Peripheral Myelinated Axons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Molecular Mechanisms Involved in Schwann Cell Plasticity.Frontiers in molecular neuroscience · 2017
    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

4 authors at 1 institution in 1 country.

Ming-Shuo ChenDepartment of Biological Sciences, Rutgers, The State University of New Jersey, Newark, New Jersey.
Hyosung KimDepartment of Biological Sciences, Rutgers, The State University of New Jersey, Newark, New Jersey.
Léonard Jagot-LacoussiereDepartment of Biological Sciences, Rutgers, The State University of New Jersey, Newark, New Jersey.
Patrice MaurelDepartment of Biological Sciences, Rutgers, The State University of New Jersey, Newark, New Jersey. maurep01@andromeda.rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

Nectin-like cell adhesion molecules and the mechanisms of myelinationR01NS065218 · NINDS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI MAUREL, PATRICE · 2011 to 2015
$1.7M
NINDS NIH HHS R01 NS065218
6 · The paper itself

Abstract

Axo-glial interactions are critical for myelination and the domain organization of myelinated fibers. Cell adhesion molecules belonging to the Cadm family, and in particular Cadm3 (axonal) and its heterophilic binding partner Cadm4 (Schwann cell), mediate these interactions along the internode. Using targeted shRNA-mediated knockdown, we show that the removal of axonal Cadm3 promotes Schwann cell myelination in the in vitro DRG neuron/Schwann cell myelinating system. Conversely, over-expressing Cadm3 on the surface of DRG neuron axons results in an almost complete inability by Schwann cells to form myelin segments. Axons of superior cervical ganglion (SCG) neurons, which do not normally support the formation of myelin segments by Schwann cells, express higher levels of Cadm3 compared to DRG neurons. Knocking down Cadm3 in SCG neurons promotes myelination. Finally, the extracellular domain of Cadm3 interferes in a dose-dependent manner with the activation of ErbB3 and of the pro-myelinating PI3K/Akt pathway, but does not interfere with the activation of the Mek/Erk1/2 pathway. While not in direct contradiction, these in vitro results shed lights on the apparent lack of phenotype that was reported from in vivo studies of Cadm3

Indexed as

AnimalsAxonsCell Adhesion MoleculesCell ProliferationCells, CulturedCoculture TechniquesGanglia, SpinalGene Expression RegulationImmunoglobulinsImmunoprecipitationMyelin Basic ProteinNeuritesNeuronsOncogene Protein v-aktPhosphatidylinositol 3-KinasesRatsCell Adhesion MoleculesIgsf4b protein, mouseImmunoglobulinsMyelin Basic ProteinOncogene Protein v-aktPhosphatidylinositol 3-KinasesRNA, Small InterferingCadm3cell adhesionmyelinationneuregulinSchwann cell

Identifiers

PMID27658374
PMCPMC5073025
OpenAlexW2424555050

What OpenQuestion holds

Textmetadata
LicenceTDM
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.