Evidence map›Paper›PMID 29124212›Full record

ArticleBiochemistry and biophysics reports2015

Enhancing hypothiocyanite production by lactoperoxidase - mechanism and chemical properties of promotors.

Jana Gau, Paul-Georg Furtmüller, Christian Obinger, Jürgen Arnhold, Jörg Flemmig

Open access · goldAbstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 21 citations in OpenAlex.

  1. Trial
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  4. Phenolic Compounds ofAntioxidants (Basel, Switzerland) · 2021
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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

5 authors at 2 institutions in 2 countries.

Jana GauInstitute for Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Härtelstraße 16-18, 04107 Leipzig, Germany.
Paul-Georg FurtmüllerDepartment of Chemistry, Division of Biochemistry, University of Natural Resources and Life Sciences (BOKU) Vienna, Muthgasse 18, 1190 Vienna, Austria.
Christian ObingerDepartment of Chemistry, Division of Biochemistry, University of Natural Resources and Life Sciences (BOKU) Vienna, Muthgasse 18, 1190 Vienna, Austria.
Jürgen ArnholdInstitute for Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Härtelstraße 16-18, 04107 Leipzig, Germany.
Jörg FlemmigInstitute for Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Härtelstraße 16-18, 04107 Leipzig, Germany.
Leipzig University · DEBOKU University · AT

Funding

Austrian Science Fund FWF P 25538
6 · The paper itself

Abstract

backgroundThe heme enzyme lactoperoxidase is found in body secretions where it significantly contributes to the humoral immune response against pathogens. After activation the peroxidase oxidizes thiocyanate to hypothiocyanite which is known for its microbicidal properties. Yet several pathologies are accompanied by a disturbed hypothiocyanite production which results in a reduced immune defense.

methodsThe results were obtained by measuring enzyme-kinetic parameters using UV-vis spectroscopy and a standardized enzyme-kinetic test system as well as by the determination of second order rate constants using stopped-flow spectroscopy.

resultsIn this study we systematically tested thirty aromatic substrates for their efficiency to promote the lactoperoxidase-mediated hypothiocyanite production by restoring the native ferric enzyme state. Thereby hydrophobic compounds with a 3,4-dihydroxyphenyl partial structure such as hydroxytyrosol and selected flavonoids emerged as highly efficient promotors of the (pseudo-)halogenating lactoperoxidase activity.

conclusionsThis study discusses important structure-function relationships of efficient aromatic LPO substrates and may contribute to the development of new agents to promote lactoperoxidase activity in secretory fluids of patients. SIGNIFICANCE: This study may contribute to a better understanding of the (patho-)physiological importance of the (pseudo-)halogenating lactoperoxidase activity. The presented results may in future lead to the development of new therapeutic strategies which, by reactivating lactoperoxidase-derived hypothiocyanite production, promote the immunological activity of this enzyme.

Indexed as

3,4-dihydroxylated compoundsABTS, 2,2′-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)Aromatic compoundsDB, double bondDTNB, 5,5′-dithiobis-(2-nitrobenzoic acid)EPO, eosinophil peroxidaseHypothiocyaniteInflammationLactoperoxidaseLPO, lactoperoxidaseMPO, myeloperoxidasePeroxidasesSB, single bondssp., subspeciesTNB, 5-thio-2-nitrobenzoic acid.

Identifiers

PMID29124212
PMCPMC5669353
OpenAlexW2185830380

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Registered trials

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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.