Evidence map›Paper›PMID 26895626›Full record

ArticleMolecular neurodegeneration2016

Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site.

Caroline Schönherr, Jessica Bien, Simone Isbert, Rielana Wichert, Johannes Prox, Hermann Altmeppen, Sathish Kumar, Jochen Walter, Stefan F Lichtenthaler, Sascha Weggen and 3 more

Open access · goldAbstract read
In one paragraph

Article in Molecular neurodegeneration, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 71 citations in OpenAlex.

  1. 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
  2. Review
  3. 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
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  5. Review
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  12. Review
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  14. Article
  15. The Blood-Brain Barrier in Alzheimer's Disease.Handbook of experimental pharmacology · 2022
    Article
  16. Article
  17. The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Article
  20. Meprin β: A novel regulator of blood-brain barrier integrity.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2021
    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

13 authors at 8 institutions in 1 country.

Caroline SchönherrInstitute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University of Mainz, Duesbergweg 6, 55128, Mainz, Germany.
Jessica BienInstitute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University of Mainz, Duesbergweg 6, 55128, Mainz, Germany.
Simone IsbertInstitute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University of Mainz, Duesbergweg 6, 55128, Mainz, Germany.
Rielana WichertInstitute of Biochemistry, Unit for Degradomics of the Protease Web, Christian-Albrechts-University, Otto-Hahn-Platz 9, 24118, Kiel, Germany.
Johannes ProxInstitute of Biochemistry, Unit for Degradomics of the Protease Web, Christian-Albrechts-University, Otto-Hahn-Platz 9, 24118, Kiel, Germany.
Hermann AltmeppenInstitute of Neuropathology, University Medical Center Hamburg-Eppendorf, 20246, Hamburg, Germany.
Sathish KumarDepartment of Neurology, Molecular Cell Biology, University of Bonn, 53127, Bonn, Germany.
Jochen WalterDepartment of Neurology, Molecular Cell Biology, University of Bonn, 53127, Bonn, Germany.
Stefan F LichtenthalerGerman Center for Neurodegenerative Diseases (DZNE) and Neuroproteomics, Klinikum rechts der Isar, Technische Universität München, 81675, Munich, Germany.
Sascha WeggenDepartment of Neuropathology, Heinrich Heine University, 40225, Duesseldorf, Germany.
Markus GlatzelInstitute of Neuropathology, University Medical Center Hamburg-Eppendorf, 20246, Hamburg, Germany.
Christoph Becker-PaulyInstitute of Biochemistry, Unit for Degradomics of the Protease Web, Christian-Albrechts-University, Otto-Hahn-Platz 9, 24118, Kiel, Germany. cbeckerpauly@biochem.uni-kiel.de.
Claus U PietrzikInstitute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University of Mainz, Duesbergweg 6, 55128, Mainz, Germany. pietrzik@uni-mainz.de.
Johannes Gutenberg University Mainz · DEKiel University · DEUniversity of Bonn · DEHeinrich Heine University Düsseldorf · DEKlinikum rechts der Isar · DEUniversität Hamburg · DEUniversity Medical Center Hamburg-Eppendorf · DEUniversity Medical Center of the Johannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe metalloprotease meprin β cleaves the Alzheimer's Disease (AD) relevant amyloid precursor protein (APP) as a β-secretase reminiscent of BACE-1, however, predominantly generating N-terminally truncated Aβ2-x variants.

resultsHerein, we observed increased endogenous sAPPα levels in the brains of meprin β knock-out (ko) mice compared to wild-type controls. We further analyzed the cellular interaction of APP and meprin β and found that cleavage of APP by meprin β occurs prior to endocytosis. The N-terminally truncated Aβ2-40 variant shows increased aggregation propensity compared to Aβ1-40 and acts even as a seed for Aβ1-40 aggregation. Additionally, we observed that different APP mutants affect the catalytic properties of meprin β and that, interestingly, meprin β is unable to generate N-terminally truncated Aβ peptides from Swedish mutant APP (APPswe).

conclusionConcluding, we propose that meprin β may be involved in the generation of N-terminally truncated Aβ2-x peptides of APP, but acts independently from BACE-1.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsAspartic Acid EndopeptidasesBrainMetalloendopeptidasesMice, KnockoutNeuronsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBace1 protein, mousemeprin BMetalloendopeptidases

Identifiers

PMID26895626
PMCPMC4759862
OpenAlexW2275405720

What OpenQuestion holds

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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.