Evidence map›Paper›PMID 37000885›Full record

ArticleScience advances2023

Proteolytic processing of galectin-3 by meprin metalloproteases is crucial for host-microbiome homeostasis.

Cynthia Bülck, Elisabeth E L Nyström, Tomas Koudelka, Michael Mannbar-Frahm, Gerrit Andresen, Mariem Radhouani, Florian Tran, Franka Scharfenberg, Friederike Schrell, Fred Armbrust and 11 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. 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
2.6field-weighted citation impact, top 10% 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, 16 citations in OpenAlex.

  1. Trial
  2. Article
  3. The Role of Meprins on the Brain Extracellular Matrix and Perineuronal Nets.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Age-Related Transcriptomic Changes in the Vermiform Appendix.International journal of molecular sciences · 2025
    Article
  8. Article
  9. Meprin β Modulates Brevican Proteolysis Impairing Neural Plasticity and Memory Formation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
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

21 authors at 5 institutions in 3 countries.

Cynthia BülckInstitute of Biochemistry, University of Kiel, 24118 Kiel, Germany.ORCID 0000-0002-8354-6177
Elisabeth E L NyströmInstitute of Biochemistry, University of Kiel, 24118 Kiel, Germany.ORCID 0000-0002-6970-7894
Tomas KoudelkaInstitute of Experimental Medicine, University of Kiel, 24188 Kiel, Germany.
Michael Mannbar-FrahmInstitute of Infection Medicine, University of Kiel and University Medical Center Schleswig-Holstein, 24015 Kiel, Germany.
Gerrit AndresenInstitute of Infection Medicine, University of Kiel and University Medical Center Schleswig-Holstein, 24015 Kiel, Germany.
Mariem RadhouaniDivision of Infection Biology, Department of Medicine I, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0002-5739-9038
Florian TranInstitute of Clinical Molecular Biology, Kiel University and University Medical Center Schleswig-Holstein, 24105 Kiel, Germany.ORCID 0000-0002-3735-9872
Franka ScharfenbergInstitute of Biochemistry, University of Kiel, 24118 Kiel, Germany.
Friederike SchrellInstitute of Biochemistry, University of Kiel, 24118 Kiel, Germany.ORCID 0000-0001-5841-6007
Fred ArmbrustInstitute of Biochemistry, University of Kiel, 24118 Kiel, Germany.ORCID 0000-0002-3331-5522
Eileen DahlkeInstitute of Anatomy, University of Kiel, 24118 Kiel, Germany.
Bei ZhaoDepartment of Microbiome Research, Friedrich-Alexander-University Erlangen-Nürnberg, 91054 Erlangen, Germany.ORCID 0000-0002-2888-4472
Alex VervaekeDivision of Infection Biology, Department of Medicine I, Medical University of Vienna, 1090 Vienna, Austria.
Franziska TheiligInstitute of Anatomy, University of Kiel, 24118 Kiel, Germany.ORCID 0000-0001-8810-4717
Philip RosenstielInstitute of Clinical Molecular Biology, Kiel University and University Medical Center Schleswig-Holstein, 24105 Kiel, Germany.ORCID 0000-0002-9692-8828
Philipp StarklDivision of Infection Biology, Department of Medicine I, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0001-7521-129X
Stephan P RosshartDepartment of Microbiome Research, Friedrich-Alexander-University Erlangen-Nürnberg, 91054 Erlangen, Germany.ORCID 0000-0002-6989-8686
Helmut FickenscherInstitute of Infection Medicine, University of Kiel and University Medical Center Schleswig-Holstein, 24015 Kiel, Germany.
Andreas TholeyInstitute of Experimental Medicine, University of Kiel, 24188 Kiel, Germany.
Gunnar C HanssonDepartment of Medical Biochemistry and Cell Biology, University of Gothenburg, 405 30 Gothenburg, Sweden.ORCID 0000-0002-1900-1869
Christoph Becker-PaulyInstitute of Biochemistry, University of Kiel, 24118 Kiel, Germany.ORCID 0000-0002-5100-9916
Christian-Albrechts-Universität zu Kiel · DEHochschule für Angewandte Wissenschaften Kiel · DEMedical University of Vienna · ATFriedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The metalloproteases meprin α and meprin β are highly expressed in the healthy gut but significantly decreased in inflammatory bowel disease, implicating a protective role in mucosal homeostasis. In the colon, meprin α and meprin β form covalently linked heterodimers tethering meprin α to the plasma membrane, therefore presenting dual proteolytic activity in a unique enzyme complex. To unravel its function, we applied N-terminomics and identified galectin-3 as the major intestinal substrate for meprin α/β heterodimers. Galectin-3-deficient and meprin α/β double knockout mice show similar alterations in their microbiome in comparison to wild-type mice. We further demonstrate that meprin α/β heterodimers differentially process galectin-3 upon bacterial infection, in germ-free, conventionally housed (specific pathogen-free), or wildling mice, which in turn regulates the bacterial agglutination properties of galectin-3. Thus, the constitutive cleavage of galectin-3 by meprin α/β heterodimers may play a key role in colon host-microbiome homeostasis.

Indexed as

Galectin 3MetalloendopeptidasesAnimalsHomeostasisMetalloproteasesMiceMice, KnockoutProteolysisGalectin 3MetalloendopeptidasesMetalloproteases

Identifiers

PMID37000885
PMCPMC10065446
OpenAlexW4362465922

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.