Evidence map›Paper›PMID 20799926›Full record

ArticleThe Biochemical journal2010

Lysophosphatidylcholines activate G2A inducing G(αi)₋₁-/G(αq/)₁₁- Ca²(+) flux, G(βγ)-Hck activation and clathrin/β-arrestin-1/GRK6 recruitment in PMNs.

Samina Y Khan, Nathan J D McLaughlin, Marguerite R Kelher, Phillip Eckels, Fabia Gamboni-Robertson, Anirban Banerjee, Christopher C Silliman

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
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  5. Lysophosphatidylcholine induces azurophil granule translocationThe Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2022
    Article
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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

7 authors at 2 institutions in 1 country.

Samina Y KhanBonfils Blood Center, Denver, CO 80230, USA.
Nathan J D McLaughlin
Marguerite R Kelher
Phillip Eckels
Fabia Gamboni-Robertson
Anirban Banerjee
Christopher C Silliman
Roosevelt Institute · USUniversity of Colorado Denver · US

Funding

Trauma Reprograms CellsP50GM049222 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI BANERJEE, ANIRBAN · 1993 to 2017
$26.1M
Lyso-PCs activate PMNs and endothelium via PKCR01HL059355 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI SILLIMAN, CHRISTOPHER C. · 1999 to 2006
$1.7M
NHLBI NIH HHS HL59355NHLBI NIH HHS R01 HL059355NIGMS NIH HHS GM49222NIGMS NIH HHS P50 GM049222
6 · The paper itself

Abstract

Lyso-PCs (lysophosphatidylcholines) are a mixture of lipids that accumulate during storage of cellular blood components, have been implicated in TRALI (transfusion-related acute lung injury) and directly affect the physiology of neutrophils [PMNs (polymorphonuclear leucocytes)]. Because the G2A receptor, expressed on PMNs, has been reported to recognize lyso-PCs, we hypothesize that lyso-PC activation of G2A causes the increases in cytosolic Ca²(+) via release of G(α) and G(βγ) subunits, kinase activation, and the recruitment of clathrin, β-arrestin-1 and GRK6 (G-protein receptor kinase 6) to G2A for signal transduction. PMNs were isolated by standard techniques, primed with lyso-PCs for 5-180 s, and lysed for Western blot analysis, immunoprecipitation or subcellular fractionation, or fixed and smeared on to slides for digital microscopy. The results demonstrated that lyso-PCs cause rapid activation of the G2A receptor through S-phosphorylation and internalization resulting in G(αi)₋₁ and G(αq/)₁₁ release leading to increases in cytosolic Ca²(+), which was inhibited by an antibody to G2A or intracellular neutralization of these subunits. Lyso-PCs also caused the release of the G(βγ) subunit which demonstrated a physical interaction (FRET+) with activated Hck (haemopoietic cell kinase; Tyr⁴¹¹). Moreover, G2A recruited clathrin, β-arrestin-1 and GRK6: clathrin is important for signal transduction, GRK6 for receptor de-sensitization, and β-arrestin-1 both propagates and terminates signals. We conclude that lyso-PC activation of G2A caused release of G(αi)₋₁, G(αq/)₁₁ and G(βγ), resulting in cytosolic Ca²(+) flux, Hck activation, and recruitment of clathrin, β-arrestin-1 and GRK6.

Indexed as

Arrestinsbeta-Arrestin 1beta-ArrestinsBlotting, WesternCalciumCell Cycle ProteinsCells, CulturedClathrinCytosolEnzyme ActivationFluorescence Resonance Energy TransferG-Protein-Coupled Receptor KinasesGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHeterotrimeric GTP-Binding ProteinsARRB1 protein, humanArrestinsbeta-Arrestin 1beta-ArrestinsCalciumCell Cycle ProteinsClathrinG2A receptorG-protein-coupled receptor kinase 6G-Protein-Coupled Receptor KinasesGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHCK protein, humanHeterotrimeric GTP-Binding ProteinsLysophosphatidylcholinesProtein KinasesProto-Oncogene Proteins c-hckReceptors, G-Protein-Coupled

Identifiers

PMID20799926
PMCPMC3131183
OpenAlexW1966003587

What OpenQuestion holds

Textmetadata
LicenceTDM
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.