Evidence map›Paper›PMID 21312222›Full record

ArticleJournal of neuroscience research2011

Classical 18.5-and 21.5-kDa isoforms of myelin basic protein inhibit calcium influx into oligodendroglial cells, in contrast to golli isoforms.

Graham S T Smith, Pablo M Paez, Vilma Spreuer, Celia W Campagnoni, Joan M Boggs, Anthony T Campagnoni, George Harauz

Abstract read
In one paragraph

Article in Journal of neuroscience research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Identification of Molecular Correlations of GSDMD with Pyroptosis inAlzheimer's Disease.Combinatorial chemistry & high throughput screening · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Oligodendroglial membrane dynamics in relation to myelin biogenesis.Cellular and molecular life sciences : CMLS · 2016
    Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Myelin architecture: zippering membranes tightly together.Cellular and molecular life sciences : CMLS · 2014
    Review
  18. Article
  19. Review
  20. 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

7 authors at 3 institutions in 2 countries.

Graham S T SmithDepartment of Molecular and Cellular Biology, and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada.
Pablo M Paez
Vilma Spreuer
Celia W Campagnoni
Joan M Boggs
Anthony T Campagnoni
George Harauz
University of California, Los Angeles · USUniversity of Guelph · CAHospital for Sick Children · CA

Funding

GENETIC ELEMENTS REGULATIONG MYELIN GENE EXPRESSIONR01NS033091 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CAMPAGNONI, ANTHONY T · 1994 to 2001
$522k
CIHR 86483CIHR MOP 86483NINDS NIH HHS NS33091
6 · The paper itself

Abstract

The myelin basic protein (MBP) family arises from different transcription start sites of the golli (gene of oligodendrocyte lineage) complex, with further variety generated by differential splicing. The "classical" MBP isoforms are peripheral membrane proteins that facilitate compaction of the mature myelin sheath but also have multiple protein interactions. The early developmental golli isoforms have previously been shown to promote process extension and enhance Ca(2+) influx into primary and immortalized oligodendrocyte cell lines. Here, we have performed similar studies with the classical 18.5- and 21.5-kDa isoforms of MBP. In contrast to golli proteins, overexpression of classical MBP isoforms significantly reduces Ca(2+) influx in the oligodendrocyte cell line N19 as well as in primary cultures of oligodendroglial progenitor cells. Pharmacological experiments demonstrate that this effect is mediated by voltage-operated Ca(2+) channels (VOCCs) and not by ligand-gated Ca(2+) channels or Ca(2+) release from intracellular stores. The pseudo-deiminated 18.5-kDa and the full-length 21.5-kDa isoforms do not reduce Ca(2+) influx as much as the unmodified 18.5-kDa isoform. However, more efficient membrane localization (of overexpressed, pseudo-deiminated 18.5-kDa and 21.5-kDa isoforms of classical MBP containing the 21-nt 3'-untranslated region transit signal) further reduces the Ca(2+) response after plasma membrane depolarization, suggesting that binding of classical MBP isoforms to the plasma membrane is important for modulation of Ca(2+) homeostasis. Furthermore, we have found that the mature 18.5-kDa isoform expressed in oligodendrocytes colocalizes with VOCCs, particularly at the leading edge of extending membrane processes. In summary, our findings suggest a key role for classical MBP proteins in regulating voltage-gated Ca(2+) channels at the plasma membrane of oligodendroglial cells and thus also in regulation of multiple developmental stages in this cell lineage.

Indexed as

3' Untranslated RegionsAnimalsBlotting, WesternCalciumCalcium ChannelsCalcium SignalingCell LineCell MembraneFluorescent Antibody TechniqueHumansImage Processing, Computer-AssistedMiceMicroscopy, ConfocalMolecular WeightMyelin Basic ProteinOligodendroglia3' Untranslated RegionsCalciumCalcium ChannelsMyelin Basic ProteinProtein Isoforms

Identifiers

PMID21312222
PMCPMC3605075
OpenAlexW2119970652

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.