Evidence map›Paper›PMID 22234579›Full record

ArticleNeurochemical research2012

Ganglioside GM1/galectin-dependent growth regulation in human neuroblastoma cells: special properties of bivalent galectin-4 and significance of linker length for ligand selection.

Jürgen Kopitz, Seda Ballikaya, Sabine André, Hans-Joachim Gabius

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Neurochemical research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. How galectins have become multifunctional proteins.Histology and histopathology · 2020
    Review
  6. Review
  7. Exploring functional pairing between surface glycoconjugates and human galectins using programmable glycodendrimersomes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. The sugar code in neuronal physiology.Histochemistry and cell biology · 2017
    Review
  10. Review
  11. Sweet complementarity: the functional pairing of glycans with lectins.Cellular and molecular life sciences : CMLS · 2016
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Evolving mechanistic insights into galectin functions.Methods in molecular biology (Clifton, N.J.) · 2015
    Review
  17. Review
  18. Article
  19. 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 2 institutions in 1 country.

Jürgen KopitzPathologisches Institut, Abteilung Angewandte Tumorbiologie, Ruprecht-Karls-Universität, Im Neuenheimer Feld 220, 69120 Heidelberg, Germany. juergen.kopitz@med.uni-heidelberg.de
Seda Ballikaya
Sabine André
Hans-Joachim Gabius
Heidelberg University · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Orchestrated upregulation of cell surface presentation of ganglioside GM1 and homodimeric galectin-1 is the molecular basis for growth regulation of human neuroblastoma (SK-N-MC) cells. Further study led to the discovery of competitive inhibition by galectin-3, prompting us to test tandem-repeat-type galectin-4 (two different lectin domains connected by a 42-amino-acid linker). This lectin bound to cells at comparably high affinity without involvement of the ganglioside, as disclosed by assays in the presence of cholera toxin B-subunit or galectin-1 and blocking glucosylceramide synthesis. Notably, when tested separately, binding of both lectin domains showed partial sensitivity to the bacterial agglutinin. Despite its ability for cross-linking surface association of galectin-4 did not affect proliferation, in contrast to homodimeric galectins. The truncation of linker length from 42 to 16 amino acids altered binding properties to let partial sensitivity to the bacterial lectin emerge. Cross-competition between parental and engineered proteins did not exceed 40%. No effect on cell growth was detected. This study reveals complete functional divergence between galectins differing in the spatial mode of lectin-site presentation and dependence of reactivity to distinct counter-receptor(s) on linker length. Due to the documented presence of galectin-4 in the nervous system and its affinity for sulfatide these in vitro results indicate the potential for a distinct functionality profile of this lectin in vivo, giving further research direction.

Indexed as

Cell Line, TumorCell ProliferationCholera ToxinGalectin 1Galectin 4GalectinsG(M1) GangliosideHumansLigandsNeuroblastomaStructure-Activity RelationshipCholera ToxinGalectin 1Galectin 4GalectinsG(M1) GangliosideLigands

Identifiers

PMID22234579
OpenAlexW2041733357

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.