Evidence map›Paper›PMID 29054928›Full record

ArticleThe Journal of biological chemistry2017

The type II transmembrane serine protease matriptase cleaves the amyloid precursor protein and reduces its processing to β-amyloid peptide.

Erwan Lanchec, Antoine Désilets, François Béliveau, Anthony Flamier, Shaimaa Mahmoud, Gilbert Bernier, Denis Gris, Richard Leduc, Christine Lavoie

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.

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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

9 authors at 3 institutions in 1 country.

Erwan LanchecFrom the Department of Pharmacology-Physiology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec J1H5N4, Canada.
Antoine DésiletsFrom the Department of Pharmacology-Physiology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec J1H5N4, Canada.
François BéliveauFrom the Department of Pharmacology-Physiology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec J1H5N4, Canada.
Anthony FlamierStem Cell and Developmental Biology Laboratory, Hôpital Maisonneuve-Rosemont, 5415 Boulevard de l'Assomption, Montréal, Quebec H1T 2M4, Canada.
Shaimaa MahmoudDepartment of Pediatrics, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec J1H5N4, Canada, and.
Gilbert BernierStem Cell and Developmental Biology Laboratory, Hôpital Maisonneuve-Rosemont, 5415 Boulevard de l'Assomption, Montréal, Quebec H1T 2M4, Canada.
Denis GrisDepartment of Pediatrics, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec J1H5N4, Canada, and.
Richard LeducFrom the Department of Pharmacology-Physiology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec J1H5N4, Canada, Richard.Leduc@USherbrooke.ca.
Christine LavoieFrom the Department of Pharmacology-Physiology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec J1H5N4, Canada, Christine.L.Lavoie@USherbrooke.ca.
Université de Sherbrooke · CAHôpital Maisonneuve-Rosemont · CAUniversité de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent studies have reported that many proteases, besides the canonical α-, β-, and γ-secretases, cleave the amyloid precursor protein (APP) and modulate β-amyloid (Aβ) peptide production. Moreover, specific APP isoforms contain Kunitz protease-inhibitory domains, which regulate the proteolytic activity of serine proteases. This prompted us to investigate the role of matriptase, a member of the type II transmembrane serine protease family, in APP processing. Using quantitative RT-PCR, we detected matriptase mRNA in several regions of the human brain with an enrichment in neurons. RNA sequencing data of human dorsolateral prefrontal cortex revealed relatively high levels of matriptase RNA in young individuals, whereas lower levels were detected in older individuals. We further demonstrate that matriptase and APP directly interact with each other and that matriptase cleaves APP at a specific arginine residue (Arg-102) both

Indexed as

AgedAge FactorsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorBrainCadaverCell LineComputational BiologyGene Expression Regulation, EnzymologicHumansMutagenesis, Site-DirectedMutationNerve Tissue ProteinsNeuronsOrgan SpecificityPeptide FragmentsAmyloid beta-Peptidesamyloid beta-protein (1-40)Amyloid beta-Protein PrecursorNerve Tissue ProteinsPeptide FragmentsRecombinant Fusion ProteinsRNA, MessengerSerine EndopeptidasesST14 protein, humanAlzheimer diseaseamyloid precursor protein (APP)amyloid-β (Aβ)brainenzyme processingextracellular matrix proteinmatriptaseserine proteaseST14

Identifiers

PMID29054928
PMCPMC5733603
OpenAlexW2765573024

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.