Evidence map›Paper›PMID 24614744›Full record

ArticleThe Journal of physiology2014

Modulation of ionotropic glutamate receptor function by vertebrate galectins.

Bryan A Copits, Claire G Vernon, Ryuichi Sakai, Geoffrey T Swanson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. The Neuronal Golgi Network and Its Acolytes.Sub-cellular biochemistry · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Architecture and Dynamics of the Neuronal Secretory Network.Annual review of cell and developmental biology · 2019
    Review
  8. Article
  9. Frontiers in molecular neuroscience · 2018
    Article
  10. Article
  11. Article
  12. Neto2 Assembles with Kainate Receptors in DRG Neurons during Development and Modulates Neurite Outgrowth in Adult Sensory Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  13. Review
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Bryan A CopitsDepartment of Molecular Pharmacology and Biological Chemistry, Northwestern University Feinberg School of Medicine, Chicago, IL, 60611, USA.
Claire G VernonDepartment of Molecular Pharmacology and Biological Chemistry, Northwestern University Feinberg School of Medicine, Chicago, IL, 60611, USA.
Ryuichi SakaiGraduate School of Fisheries Sciences, Hokkaido University, Hakodate, 041-8611, Japan.
Geoffrey T SwansonDepartment of Molecular Pharmacology and Biological Chemistry, Northwestern University Feinberg School of Medicine, Chicago, IL, 60611, USA gtswanson@northwestern.edu.
Northwestern University · USHakodate University · JP

Funding

Novel marine-derived ligands for probing GluR functionR01NS044322 · NINDS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI SWANSON, GEOFFREY T · 2002 to 2011
$2.6M
Galectin Modulation of Glutamate Receptors and Neuronal FunctionR01NS080598 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SWANSON, GEOFFREY T · 2013 to 2017
$1.9M
NINDS NIH HHS R01 NS044322NINDS NIH HHS R01 NS080598
6 · The paper itself

Abstract

AMPA and kainate receptors are glutamate-gated ion channels whose function is known to be altered by a variety of plant oligosaccharide-binding proteins, or lectins, but the physiological relevance of this activity has been uncertain because no lectins with analogous allosteric modulatory effects have been identified in animals. We report here that members of the prototype galectin family, which are β-galactoside-binding lectins, exhibit subunit-specific allosteric modulation of desensitization of recombinant homomeric and heteromeric AMPA and kainate receptors. Galectin modulation of GluK2 kainate receptors was dependent upon complex oligosaccharide processing of N-glycosylation sites in the amino-terminal domain and downstream linker region. The sensitivity of GluA4 AMPA receptors to human galectin-1 could be enhanced by supplementation of culture media with uridine and N-acetylglucosamine (GlcNAc), precursors for the hexosamine pathway that supplies UDP-GlcNAc for synthesis of complex oligosaccharides. Neuronal kainate receptors in dorsal root ganglia were sensitive to galectin modulation, whereas AMPA receptors in cultured hippocampal neurons were insensitive, which could be a reflection of differential N-glycan processing or receptor subunit selectivity. Because glycan content of integral proteins can be modified dynamically, we postulate that physiological or pathological conditions in the CNS could arise in which galectins alter excitatory neurotransmission or neuronal excitability through their actions on AMPA or kainate receptors.

Indexed as

AnimalsCaudataCells, CulturedDose-Response Relationship, DrugGalectin 1GalectinsGanglia, SpinalGlutamic AcidHippocampusHumansIon Channel GatingMice, Inbred C57BLNeuronsRatsRats, Sprague-DawleyReceptors, Ionotropic Glutamatecongerin protein, Conger myriasterGalectin 1GalectinsGlutamic AcidReceptors, Ionotropic Glutamate

Identifiers

PMID24614744
PMCPMC4227896
OpenAlexW1508936447

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.