Evidence map›Paper›PMID 27435226›Full record

ArticleBMC cancer2016

Galectin-3 interacts with components of the nuclear ribonucleoprotein complex.

Katharina Fritsch, Marco Mernberger, Andrea Nist, Thorsten Stiewe, Alexander Brehm, Ralf Jacob

Open access · goldAbstract read
In one paragraph

Article in BMC cancer, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. The Role of Galectin-3 in Liver Inflammation and Fibrosis.Journal of inflammation research · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Emergence ofCancers · 2022
    Review
  15. SREBP1 regulatesMolecular therapy. Nucleic acids · 2022
    Article
  16. The Involvement of Alarmins in the Pathogenesis of Sjögren's Syndrome.International journal of molecular sciences · 2022
    Review
  17. Gal3 Plays a Deleterious Role in a Mouse Model of Endotoxemia.International journal of molecular sciences · 2022
    Article
  18. Review
  19. Article
  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

6 authors at 1 institution in 1 country.

Katharina FritschDepartment of Cell Biology and Cell Pathology, Philipps-Universität Marburg, Robert-Koch-Str. 6, D-35037, Marburg, Germany.
Marco MernbergerInstitute of Molecular Oncology, Philipps-Universität Marburg, Marburg, Germany.
Andrea NistGenomics Core Facility, Philipps-Universität Marburg, Marburg, Germany.
Thorsten StieweInstitute of Molecular Oncology, Philipps-Universität Marburg, Marburg, Germany.
Alexander BrehmInstitute for Molecular Biology and Tumor Research, Philipps-Universität Marburg, Marburg, Germany.
Ralf JacobDepartment of Cell Biology and Cell Pathology, Philipps-Universität Marburg, Robert-Koch-Str. 6, D-35037, Marburg, Germany. jacob@staff.uni-marburg.de.
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe multifunctional β-galactoside-binding protein galectin-3 is found in many distinct subcellular compartments including the cell nucleus. Expression and distribution of galectin-3 between the cell nucleus and the cytosol changes during cell differentiation and cancer development. Nuclear functions of galectin-3 and how they contribute to tumorigenesis are not understood.

methodsIn order to identify nuclear galectin-3 interaction partners, we used affinity chromatography and co-immunoprecipitation. Spatial proximity in the nucleus was assessed by immunofluorescence and proximity ligation assay. We also investigated the function of galectin-3 on mRNA-export by fluorescence in situ hybridization and on mRNA-processing by RNA-sequencing.

resultsThe heterogeneous ribonucleoprotein particle component hnRNPA2B1 was identified as a novel galectin-3 binding protein that associates with the lectin in a lactose-dependent manner in the cell nucleus. Specific individual depletion of galectin-3 does not affect the mRNA distribution between cytoplasm and nucleus. A significant alteration of this distribution was observed after combined depletion of galectin-1 and -3. However, silencing of galectin-3 was sufficient to alter the splicing patterns of several genes.

conclusionsGalectin-3 and hnRNPA2B1 interact as members of the early splicing machinery. Galectin-3 and -1 have redundant functions in mRNA transport and at least in part in mRNA splicing. RNA-sequencing data points to a specific function of the hnRNPA2B1/galectin-3 interaction in the processing of transcripts coding for the nuclear oncoprotein SET.

Indexed as

Cell NucleusGalectin 3HeLa CellsHeterogeneous-Nuclear Ribonucleoprotein Group A-BHumansImmunoblottingImmunoprecipitationIn Situ Hybridization, FluorescenceMicroscopy, FluorescenceProtein BindingRNA InterferenceRNA, MessengerRNA SplicingRNA TransportSequence Analysis, RNAGalectin 3Heterogeneous-Nuclear Ribonucleoprotein Group A-BhnRNP A2RNA, MessengerGalectin-1Galectin-3hnRNPA2B1RNA-processingSpliceosome

Identifiers

PMID27435226
PMCPMC4952364
OpenAlexW2485159589

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.