Evidence map›Paper›PMID 9502418›Full record

ArticleThe American journal of pathology1998

Co-compartmentalization of MAP kinases and cytosolic phospholipase A2 at cytoplasmic arachidonate-rich lipid bodies.

W Yu, P T Bozza, D M Tzizik, J P Gray, J Cassara, A M Dvorak, P F Weller

Registry-linked trialAbstract read
In one paragraph

Article in The American journal of pathology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02498119 (The Role of Arachidonic Acid Metabolites, in the Lipid Droplets of Macrophages From Patients With Metabolic Syndrome), which is not on this map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
2.8field-weighted citation impact, top 9% 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.

NCT02498119 unknown statusnot on this mapstarted 2014, after this paper: background citation

The Role of Arachidonic Acid Metabolites, in the Lipid Droplets of Macrophages From Patients With Metabolic Syndrome

Typeobservational_patient_registrySponsorUniversity of MalayaRan2014 to 2016Enrolled12ConditionsType 2 Diabetes Mellitus
3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 172 citations in OpenAlex.

  1. Review
  2. Article
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  6. Article
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  9. Review
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  11. Review
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  16. Review
  17. Review
  18. Review
  19. Lipid Droplets in Health and Disease.Lipids in health and disease · 2017
    Review
  20. A snake venom group IIA PLAScientific reports · 2017
    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 1 institution in 1 country.

W YuDepartment of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.
P T Bozza
D M Tzizik
J P Gray
J Cassara
A M Dvorak
P F Weller
Harvard University · US

Funding

CYTOPLASMIC LIPID BODIES OF INFLAMMATORY CELLSR01AI022571 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WELLER, PETER F · 1985 to 2013
$4.5M
BASOPHIL/MAST CELL FUNCTIONR01AI033372 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI DVORAK, ANN M · 1992 to 2004
$1.9M
NIAID NIH HHS AI22571NIAID NIH HHS AI33372
6 · The paper itself

Abstract

Lipid bodies are inducible lipid domains abundantly present in leukocytes engaged in inflammation. They are rich in esterified arachidonate and are also potential sites for eicosanoid-forming enzyme localization. It is therefore of interest to know whether arachidonate-releasing cytosolic phospholipase A2 (cPLA2) localizes at lipid bodies. Here, we present evidence that cPLA2 and its activating protein kinases, mitogen-activated protein (MAP) kinases, co-localize at lipid bodies. U937 cells express high levels of cPLA2 and contain numerous cytoplasmic lipid bodies. Using double-labeling immunocytochemistry we demonstrated punctate cytoplasmic localizations of both cPLA2 and MAP kinases in U937 cells that were perfectly concordant with fluorescent fatty-acid-labeled lipid bodies. The co-localization of cPLA2 and MAP kinases at lipid bodies was confirmed by subcellular fractionation and immunoblot. Lipid body fractions free of cytosol and other organelles contained significant amounts of [14C]arachidonate-labeled phosphatidylcholine and cPLA2 enzymatic activities. Immunoblotting with specific antibodies identified cPLA2 as well as MAP kinases, including ERK1, ERK2, p85, and p38, in lipid bodies. The co-compartmentalization within arachidonate-rich lipid bodies of cPLA2 and its potentially activating protein kinases suggests that lipid bodies may be structurally distinct intracellular sites active in extracellular ligand-induced arachidonate release and eicosanoid formation.

Indexed as

Lipid MetabolismArachidonic AcidCalcium-Calmodulin-Dependent Protein KinasesCarbon RadioisotopesCell FractionationCytosolElectrophoresis, Polyacrylamide GelFluorescent Antibody Technique, IndirectHumansInclusion BodiesPhosphatidylinositol 3-KinasesPhospholipases APhospholipases A2Signal TransductionTumor Cells, CulturedArachidonic AcidCalcium-Calmodulin-Dependent Protein KinasesCarbon RadioisotopesPhosphatidylinositol 3-KinasesPhospholipases APhospholipases A2

Identifiers

PMID9502418
PMCPMC1858398
OpenAlexW2147347287

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.