Evidence map›Paper›PMID 9315897›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1997

Neurons promote the translocation of peripheral myelin protein 22 into myelin.

S Pareek, L Notterpek, G J Snipes, R Naef, W Sossin, J Laliberté, S Iacampo, U Suter, E M Shooter, R A Murphy

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

63 citing papers in PubMed, 150 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Charcot-Marie-Tooth disease type 1E: Clinical Natural History and Molecular Impact ofmedRxiv : the preprint server for health sciences · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Mechanisms and Treatments in Demyelinating CMT.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    Review
  16. Ion mobility-mass spectrometry reveals the role of peripheral myelin protein dimers in peripheral neuropathy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Review
  19. Article
  20. Review

3 more citing papers are in PubMed but not listed here.

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

10 authors at 4 institutions in 3 countries.

S PareekMontreal Neurological Institute and the Faculty of Medicine, McGill University, Montreal, Quebec H3A 2B4, Canada.
L Notterpek
G J Snipes
R Naef
W Sossin
J Laliberté
S Iacampo
U Suter
E M Shooter
R A Murphy
McGill University · CAÉcole Polytechnique Fédérale de Lausanne · CHMontreal Neurological Institute and Hospital · CAStanford University · US

Funding

THE TRAFFICKING OF MYELIN PROTEINS AND NEUROTROPHINSR01NS004270 · NINDS · STANFORD UNIVERSITY · PI SHOOTER, ERIC M · 1985 to 2003
$2.0M
REGULATION OF NERVE INJURY AND REPAIRK08NS001559 · NINDS · STANFORD UNIVERSITY · PI SNIPES, GEORGE J · 1992 to 1995
–
NINDS NIH HHS NS01559NINDS NIH HHS NS04270NINDS NIH HHS NS09694
6 · The paper itself

Abstract

Schwann cells express low levels of myelin proteins in the absence of neurons. When Schwann cells and neurons are cultured together the production of myelin proteins is elevated, and myelin is formed. For peripheral myelin protein 22 (PMP22), the exact amount of protein produced is critical, because peripheral neuropathies result from its underexpression or overexpression. In this study we examined the effect of neurons on Schwann cell PMP22 production in culture and in peripheral nerve using metabolic labeling and pulse-chase studies as well as immunocytochemistry. Most of the newly synthesized PMP22 in Schwann cells is rapidly degraded in the endoplasmic reticulum. Only a small proportion of the total PMP22 acquires complex glycosylation and accumulates in the Golgi compartment. This material is translocated to the Schwann cell membrane in detectable amounts only when axonal contact and myelination occur. Myelination does not, however, alter the rapid turnover of PMP22 in Schwann cells. PMP22 may therefore be a unique myelin protein in that axonal contact promotes its insertion into the Schwann cell membrane and myelin without altering its rapid turnover rate within the cell.

Indexed as

AnimalsBiological TransportCells, CulturedCoculture TechniquesEndoplasmic ReticulumGlycosylationHomeostasisImmunohistochemistryMyelin ProteinsMyelin SheathNeuronsRatsRats, Sprague-DawleySchwann CellsSciatic NerveTime FactorsMyelin ProteinsPmp22 protein, rat

Identifiers

PMID9315897
PMCPMC6793898
OpenAlexW1480359191

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.