Evidence map›Paper›PMID 14556648›Full record

ArticleThe Biochemical journal2004

N-Formyl peptide receptor subtypes in human neutrophils activate L-plastin phosphorylation through different signal transduction intermediates.

Marie-Hélène Paclet, Clare Davis, Peter Kotsonis, Jasminka Godovac-Zimmermann, Anthony W Segal, Lodewijk V Dekker

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 35 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

6 authors at 1 institution in 1 country.

Marie-Hélène PacletDepartment of Medicine, Centre for Molecular Medicine, The Rayne Institute, University College London, UK. MHPaclet@chu-grenoble.fr
Clare Davis
Peter Kotsonis
Jasminka Godovac-Zimmermann
Anthony W Segal
Lodewijk V Dekker
University College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We investigated the coupling of the fMLP (N -formyl-L-methionyl-L-leucyl-L-phenylalanine; 'chemotactic peptide') receptor with phosphorylation of the actin-binding protein L-plastin in neutrophils. Using two-dimensional IEF (isoelectric focusing)/PAGE and MALDI-TOF (matrix-assisted laser desorption ionization-time-of-flight)-MS, L-plastin was identified as a major phosphoprotein in fMLP-stimulated neutrophils whose phosphorylation was dependent on phosphoinositide 3-kinase, PLD (phospholipase D) and PKC (protein kinase C) activity. Two fMLP receptor subtypes were identified in neutrophils, characterized by a distinct sensitivity to fMLP and antagonistic peptides. Both receptor subtypes induced the phosphorylation of L-plastin. L-plastin phosphorylation induced by low-affinity fMLP receptors involves an action of phosphoinositide 3-kinase, PLD and PKC isotypes. In contrast, none of these intermediates are utilized by high-affinity fMLP receptors in the phosphorylation of L-plastin. However, the PKC inhibitor Ro-31-8220 inhibits L-plastin phosphorylation induced by the high-affinity fMLP receptor. Thus, an as yet unknown Ro-31-8220-sensitive kinase regulates L-plastin phosphorylation in response to the high-affinity fMLP receptor. The results suggest a model in which receptor subtypes induce a similar endpoint event through different signal-transduction intermediates. This may be relevant in the context of cell migration in which one receptor subpopulation may become desensitized in a concentration gradient of chemoattractant.

Indexed as

Signal TransductionElectrophoresis, Gel, Two-DimensionalHumansMembrane GlycoproteinsMicrofilament ProteinsNeutrophilsN-Formylmethionine Leucyl-PhenylalaninePhosphoproteinsPhosphorylationProtein Kinase CReceptors, Formyl PeptideSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationMembrane GlycoproteinsMicrofilament ProteinsN-Formylmethionine Leucyl-PhenylalaninePhosphoproteinsplastinProtein Kinase CReceptors, Formyl Peptide

Identifiers

PMID14556648
PMCPMC1223878
OpenAlexW2008235088

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.