Evidence map›Paper›PMID 26986619›Full record

ArticlePloS one2016

Lactoferrin Is an Allosteric Enhancer of the Proteolytic Activity of Cathepsin G.

Steffen Eipper, Robin Steiner, Adam Lesner, Marcin Sienczyk, David Palesch, Marc-Eric Halatsch, Ewa Zaczynska, Christopher Heim, Marcus D Hartmann, Michal Zimecki and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

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  15. The Ontogeny of a Neutrophil: Mechanisms of Granulopoiesis and Homeostasis.Microbiology and molecular biology reviews : MMBR · 2018
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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

12 authors at 5 institutions in 2 countries.

Steffen EipperDepartment of Neurosurgery, Ulm University Medical Centre, Ulm, Germany.
Robin SteinerDepartment of Neurosurgery, Ulm University Medical Centre, Ulm, Germany.
Adam LesnerFaculty of Chemistry, University of Gdansk, Gdansk, Poland.
Marcin SienczykFaculty of Chemistry, Wroclaw University of Technology, Wroclaw, Poland.
David PaleschInstitute of Molecular Virology, Ulm University Medical Centre, Ulm, Germany.
Marc-Eric HalatschDepartment of Neurosurgery, Ulm University Medical Centre, Ulm, Germany.
Ewa ZaczynskaLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland.
Christopher HeimDepartment of Protein Evolution, Max-Planck-Institute for Developmental Biology, Tübingen, Germany.
Marcus D HartmannDepartment of Protein Evolution, Max-Planck-Institute for Developmental Biology, Tübingen, Germany.
Michal ZimeckiLudwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland.
Christian Rainer WirtzDepartment of Neurosurgery, Ulm University Medical Centre, Ulm, Germany.
Timo BursterDepartment of Neurosurgery, Ulm University Medical Centre, Ulm, Germany.
Ludwik Hirszfeld Institute of Immunology and Experimental Therapy · PLMax Planck Institute for Developmental Biology · DEUniversity Hospital Ulm · DEUniversity of Gdańsk · PLWrocław University of Science and Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protease-mediated degradation of proteins is critical in a plethora of physiological processes. Neutrophils secrete serine proteases including cathepsin G (CatG), neutrophile elastase (NE), and proteinase 3 (PR3) together with lactoferrin (LF) as a first cellular immune response against pathogens. Here, we demonstrate that LF increases the catalytic activity of CatG at physiological concentration, with its highest enhancing capacity under acidic (pH 5.0) conditions, and broadens the substrate selectivity of CatG. On a functional level, the enzymatic activity of CatG was increased in the presence of LF in granulocyte-derived supernatant. Furthermore, LF enhanced CatG-induced activation of platelets as determined by cell surface expression of CD62P. Consequently, LF-mediated enhancement of CatG activity might promote innate immunity during acute inflammation.

Indexed as

Allosteric RegulationBiocatalysisCathepsin GCulture Media, ConditionedElectrophoresis, Polyacrylamide GelEnzyme ActivationGranulocytesHumansHydrogen-Ion ConcentrationImmunity, InnateImmunoblottingInflammationLactoferrinLeukocyte ElastasePlatelet ActivationProteolysisCathepsin GCTSG protein, humanCulture Media, ConditionedLactoferrinLeukocyte ElastaseLTF protein, human

Identifiers

PMID26986619
PMCPMC4795699
OpenAlexW2299373862

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.