Evidence map›Paper›PMID 35122600›Full record

ArticleMolecular biology reports2022

Human Coxsackie- and adenovirus receptor is a putative target of neutrophil elastase-mediated shedding.

Leonie Herrmann, Louise Schelletter, Raimund Hoffrogge, Karsten Niehaus, Volker Rudolph, Martin Farr

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

6 authors at 2 institutions in 1 country.

Leonie HerrmannClinic for General and Interventional Cardiology/Angiology, Herz- und Diabeteszentrum NRW, Ruhr-Universität Bochum, Georgstr. 11, 32545, Bad Oeynhausen, Germany.ORCID http://orcid.org/0000-0003-1248-0374
Louise SchelletterCell Culture Technology, Technical Faculty, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.ORCID http://orcid.org/0000-0003-2817-7919
Raimund HoffroggeCell Culture Technology, Technical Faculty, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.ORCID http://orcid.org/0000-0003-0118-0990
Karsten NiehausProteome and Metabolome Research, Center for Biotechnology (CeBiTec), Faculty of Biology, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.ORCID http://orcid.org/0000-0003-4078-9870
Volker RudolphClinic for General and Interventional Cardiology/Angiology, Herz- und Diabeteszentrum NRW, Ruhr-Universität Bochum, Georgstr. 11, 32545, Bad Oeynhausen, Germany.ORCID http://orcid.org/0000-0001-5385-6839
Martin FarrClinic for General and Interventional Cardiology/Angiology, Herz- und Diabeteszentrum NRW, Ruhr-Universität Bochum, Georgstr. 11, 32545, Bad Oeynhausen, Germany. mfarr@hdz-nrw.de.ORCID http://orcid.org/0000-0002-3844-5991
Bielefeld University · DEHeart and Diabetes Center North Rhine-Westphalia · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundDuring viral-induced myocarditis, immune cells migrate towards the site of infection and secrete proteases, which in turn can act as sheddases by cleaving extracellular domains of transmembrane proteins. We were interested in the shedding of the Coxsackie- and adenovirus receptor (CAR) that acts as an entry receptor for both eponymous viruses, which cause myocarditis. CAR shedding by secreted immune proteases could result in a favourable outcome of myocarditis as CAR's extracellular domain would be removed from the cardiomyocytes' surface leading to decreased susceptibility to ongoing viral infections. METHODS AND

resultsIn this work, matrix metalloproteinases and serine proteinases were screened for their proteolytic activity towards human CAR. Whereas matrix metalloproteinases, proteinase 3, and cathepsin G did not cleave human recombinant CAR or only within long incubation times, neutrophil elastase showed a distinct cleavage pattern of CAR's extracellular domain that was time- and dose-dependent. Neutrophil elastase cleaves CAR at its membrane-proximal immunoglobulin domain as we determined by nanoLC-MS/MS. Furthermore, neutrophil elastase treatment of cells reduced CAR surface levels as seen by flow cytometry and immunofluorescence microscopy.

conclusionsWith this study, we show that CAR might be a target for shedding by neutrophil elastase.

Indexed as

Leukocyte ElastaseTandem Mass SpectrometryCoxsackie and Adenovirus Receptor-Like Membrane ProteinHumansReceptors, Virusadenovirus receptorCoxsackie and Adenovirus Receptor-Like Membrane ProteinLeukocyte ElastaseReceptors, VirusCoxsackie- and adenovirus receptorNeutrophil elastaseProteolysisShedding

Identifiers

PMID35122600
PMCPMC8924087
OpenAlexW4210504863

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.