Evidence map›Paper›PMID 23482564›Full record

Trial reportThe Journal of biological chemistry2013

Selective inhibition of human group IIA-secreted phospholipase A2 (hGIIA) signaling reveals arachidonic acid metabolism is associated with colocalization of hGIIA to vimentin in rheumatoid synoviocytes.

Lawrence K Lee, Katherine J Bryant, Romaric Bouveret, Pei-Wen Lei, Anthony P Duff, Stephen J Harrop, Edwin P Huang, Richard P Harvey, Michael H Gelb, Peter P Gray and 4 more

Open access · hybridAbstract readClinical Trial
In one paragraph

Trial report in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. The innate immune mediator group IIA secreted phospholipase AFrontiers in cell and developmental biology · 2026
    Article
  2. Eburicoic Acid fromJournal of inflammation research · 2026
    Article
  3. Targeting secreted PLACell death & disease · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Secreted Phospholipases AInternational journal of biological sciences · 2022
    Review
  8. Article
  9. Human Group IIA Phospholipase AMolecules (Basel, Switzerland) · 2021
    Review
  10. Article
  11. Review
  12. Article
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

14 authors at 7 institutions in 3 countries.

Lawrence K LeeFaculty of Pharmacy, The University of Sydney, Sydney, New South Wales 2006, Australia.
Katherine J Bryant
Romaric Bouveret
Pei-Wen Lei
Anthony P Duff
Stephen J Harrop
Edwin P Huang
Richard P Harvey
Michael H Gelb
Peter P Gray
Paul M Curmi
Anne M Cunningham
W Bret Church
Kieran F Scott
Saint Vincent's Catholic Medical Center · USSt. Vincent's Birmingham · USUniversity of Sydney · AUUNSW Sydney · AUAustralian Nuclear Science and Technology Organisation · AUSt Vincent's Hospital · AUUniversity of Washington · US

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
Biochemical Studies of 14-kDa Phospholipases A2R37HL036235 · NHLBI · UNIVERSITY OF WASHINGTON · PI GELB, MICHAEL H · 2007 to 2016
$4.1M
NCRR NIH HHS P41 RR007707NCRR NIH HHS RR007707NHLBI NIH HHS R37 HL036235
6 · The paper itself

Abstract

Human group IIA secreted phospholipase A2 (hGIIA) promotes tumor growth and inflammation and can act independently of its well described catalytic lipase activity via an alternative poorly understood signaling pathway. With six chemically diverse inhibitors we show that it is possible to selectively inhibit hGIIA signaling over catalysis, and x-ray crystal structures illustrate that signaling involves a pharmacologically distinct surface to the catalytic site. We demonstrate in rheumatoid fibroblast-like synoviocytes that non-catalytic signaling is associated with rapid internalization of the enzyme and colocalization with vimentin. Trafficking of exogenous hGIIA was monitored with immunofluorescence studies, which revealed that vimentin localization is disrupted by inhibitors of signaling that belong to a rare class of small molecule inhibitors that modulate protein-protein interactions. This study provides structural and pharmacological evidence for an association between vimentin, hGIIA, and arachidonic acid metabolism in synovial inflammation, avenues for selective interrogation of hGIIA signaling, and new strategies for therapeutic hGIIA inhibitor design.

Indexed as

AnimalsArachidonic AcidArthritis, RheumatoidCHO CellsCricetinaeCricetulusDrug DesignEnzyme InhibitorsFemaleGroup II Phospholipases A2HumansMaleSignal TransductionSynovial MembraneVimentinArachidonic AcidEnzyme InhibitorsGroup II Phospholipases A2PLA2G2A protein, humanVimentinEicosanoids BiosynthesisPeptide InhibitorsPhospholipase AProtein Drug InteractionsProtein-Protein InteractionsRheumatoid SynoviocytesVimentinX-ray Crystallography

Identifiers

PMID23482564
PMCPMC3663547
OpenAlexW2076617342

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.