Evidence map›Paper›PMID 22393044›Full record

ArticleThe Journal of biological chemistry2012

Phospholipase A2IVα regulates phagocytosis independent of its enzymatic activity.

Pasquale Zizza, Cristiano Iurisci, Matteo Bonazzi, Pascale Cossart, Christina C Leslie, Daniela Corda, Stefania Mariggiò

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Role of arachidonic cascade in COVID-19 infection: A review.Prostaglandins & other lipid mediators · 2021
    Review
  5. The Roles of Phospholipase AFrontiers in cell and developmental biology · 2021
    Review
  6. Article
  7. The Cytosolic Phospholipase ABiomolecules · 2020
    Article
  8. Article
  9. A signalling cascade involving receptor-activated phospholipase ACell communication and signaling : CCS · 2019
    Article
  10. Inhibition of Cytosolic Phospholipase AJournal of virology · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

7 authors at 5 institutions in 3 countries.

Pasquale ZizzaInstitute of Protein Biochemistry, National Research Council, Via Pietro Castellino 111, 80131 Naples, Italy.
Cristiano Iurisci
Matteo Bonazzi
Pascale Cossart
Christina C Leslie
Daniela Corda
Stefania Mariggiò
Mario Negri Sud Foundation · ITInserm · FRInstitut Pasteur · FRNational Jewish Health · USNational Research Council · IT

Funding

TRANSLOCATION AND TRANSCELLULAR BIOSYNTHESISP01HL034303 · NHLBI · NATIONAL JEWISH HEALTH · PI BARKLEY, ROBERT · 1985 to 2015
$25.0M
REGULATION OF PHOSPHOLIPASE A2 NUCLEAR TARGETINGR01HL061378 · NHLBI · NATIONAL JEWISH HEALTH · PI LESLIE, CHRISTINA CARROLL · 1999 to 2011
$4.1M
NHLBI NIH HHS HL34303NHLBI NIH HHS HL61378NHLBI NIH HHS P01 HL034303NHLBI NIH HHS R01 HL061378Telethon GGP030295
6 · The paper itself

Abstract

Group IVα phospholipase A(2) (PLA(2)IVα) is a lipolytic enzyme that catalyzes the hydrolysis of membrane phospholipids to generate precursors of potent inflammatory lipid mediators. Here, the role of PLA(2)IVα in Fc receptor (FcR)-mediated phagocytosis was investigated, demonstrating that PLA(2)IVα is selectively activated upon FcR-mediated phagocytosis in macrophages and that it rapidly translocates to the site of the nascent phagosome. Moreover, pharmacological inhibition of PLA(2)IVα by pyrrophenone reduces particle internalization by up to 50%. In parallel, fibroblasts from PLA(2)IVα knock-out mice overexpressing FcγRIIA and able to internalize IgG-opsonized beads show 50% lower phagocytosis, compared with wild-type cells, and transfection of PLA(2)IVα fully recovers this impaired function. Interestingly, transfection of the catalytically inactive deleted PLA(2)IVα mutant (PLA(2)IVα(1-525)) and point mutant (PLA(2)IVα-S228C) also promotes recovery of this impaired function. Finally, transfection of the PLA(2)IVα C2 domain (which is directly involved in PLA(2)IVα membrane binding), but not of PLA(2)IVα-D43N (which cannot bind to membranes), rescues FcR-mediated phagocytosis. These data unveil a new mechanism of action for PLA(2)IVα, which demonstrates that the membrane binding, and not the enzymatic activity, is required for PLA(2)IVα modulation of FcR-mediated phagocytosis.

Indexed as

Amino Acid SubstitutionAnimalsCell Line, TransformedCell MembraneFibroblastsGroup IV Phospholipases A2HumansMacrophagesMiceMice, KnockoutMutation, MissensePhagocytosisPhagosomesProtein Structure, TertiaryProtein TransportPyrrolidinesFc gamma receptor IIAGroup IV Phospholipases A2PyrrolidinespyrrophenoneReceptors, IgG

Identifiers

PMID22393044
PMCPMC3351341
OpenAlexW2058070463

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.