Evidence map›Paper›PMID 32803826›Full record

ArticleJournal of leukocyte biology2021

Allosteric targeting of the FFA2 receptor (GPR43) restores responsiveness of desensitized human neutrophils.

Robert Frei, Johannes Nordlohne, Ulrike Hüser, Seda Hild, Johannes Schmidt, Frank Eitner, Manuel Grundmann

Open access · hybridAbstract read
In one paragraph

Article in Journal of leukocyte biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. GPR43 stimulation on TCRαβJournal of neuroinflammation · 2023
    Article
  3. Article
  4. Article
  5. Pharmacology of Free Fatty Acid Receptors and Their Allosteric Modulators.International journal of molecular sciences · 2021
    Review
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

7 authors at 3 institutions in 2 countries.

Robert FreiInstitute of Experimental and Clinical Pharmacology, Medical University of Graz, Graz, Austria.
Johannes NordlohneBayer AG, Pharmaceuticals R&D, Preclinical Research, Pharma Research Center, Wuppertal, Germany.
Ulrike HüserBayer AG, Pharmaceuticals R&D, Preclinical Research, Pharma Research Center, Wuppertal, Germany.
Seda HildMolecular, Cellular and Pharmacobiology Section, Institute of Pharmaceutical Biology, University of Bonn, Bonn, Germany.
Johannes SchmidtMolecular, Cellular and Pharmacobiology Section, Institute of Pharmaceutical Biology, University of Bonn, Bonn, Germany.
Frank EitnerBayer AG, Pharmaceuticals R&D, Preclinical Research, Pharma Research Center, Wuppertal, Germany.
Manuel GrundmannMolecular, Cellular and Pharmacobiology Section, Institute of Pharmaceutical Biology, University of Bonn, Bonn, Germany.ORCID 0000-0002-4473-7851
Bayer (Germany) · DEUniversity of Bonn · DEMedical University of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The G protein-coupled free fatty acid receptor 2 (FFA2R) is highly expressed on neutrophils and was previously described to regulate neutrophil activation. Allosteric targeting of G protein-coupled receptors (GPCRs) is increasingly explored to create distinct pharmacology compared to endogenous, orthosteric ligands. The consequence of allosteric versus orthosteric FFA2R activation for neutrophil response, however, is currently largely elusive. Here, different FFA2R desensitization profiles in human neutrophils following allosteric or orthosteric activation are reported. Using a set of neutrophil functional assays to measure calcium flux, pERK1/2, chemotaxis, cellular degranulation, and oxidative burst together with holistic and pathway-unbiased whole cell sensing based on dynamic mass redistribution, it is found that the synthetic positive allosteric modulator agonist 4-CMTB potently activates neutrophils and simultaneously alters FFA2R responsiveness toward the endogenous, orthosteric agonist propionic acid (C3) after homologous and heterologous receptor desensitization. Stimulation with C3 or the hierarchically superior chemokine receptor activator IL-8 led to strong FFA2R desensitization and rendered neutrophils unresponsive toward repeated stimulation with C3. In contrast, stimulation with allosteric 4-CMTB engaged a distinct composition of signaling pathways as compared to orthosteric receptor activation and was able to activate neutrophils that underwent homologous and heterologous desensitization with C3 and IL-8, respectively. Moreover, allosteric FFA2R activation could re-sensitize FFA2 toward the endogenous agonist C3 after homologous and heterologous desensitization. Given the fact that receptor desensitization is critical in neutrophils to sense and adapt to their current environment, these findings are expected to be useful for the discovery of novel pharmacological mechanisms to modulate neutrophil responsiveness therapeutically.

Indexed as

Allosteric RegulationCalciumChemotaxisGTP-Binding ProteinsHEK293 CellsHumansNeutrophil ActivationNeutrophilsPropionatesReactive Oxygen SpeciesReceptors, Cell SurfaceReceptors, G-Protein-CoupledSignal TransductionCalciumFFAR2 protein, humanGTP-Binding ProteinsPropionatespropionic acidReactive Oxygen SpeciesReceptors, Cell SurfaceReceptors, G-Protein-CoupledDMRGPCRGPR43neutrophilsPAMrescue

Identifiers

PMID32803826
PMCPMC8048482
OpenAlexW3067885102

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.