Evidence map›Paper›PMID 12225365›Full record

ArticleImmunology2002

Regulation of adhesion of AML14.3D10 cells by surface clustering of beta2-integrin caused by ERK-independent activation of cPLA2.

Shigeharu Myou, Xiangdong Zhu, Evan Boetticher, Yimin Qin, Saori Myo, Angelo Meliton, Anissa Lambertino, Nilda M Munoz, Kimm J Hamann, Alan R Leff

Open access · greenAbstract read
In one paragraph

Article in Immunology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 12 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

10 authors at 1 institution in 1 country.

Shigeharu MyouSection of Pulmonary and Critical Care Medicine, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Xiangdong Zhu
Evan Boetticher
Yimin Qin
Saori Myo
Angelo Meliton
Anissa Lambertino
Nilda M Munoz
Kimm J Hamann
Alan R Leff
Pulmonary and Critical Care Associates · US

Funding

T CELL CO-STIMULATION IN ALLERGIC ASTHMAP50HL056399 · NHLBI · UNIVERSITY OF CHICAGO · PI WHITE, STEVEN R · 1996 to 2005
$9.1M
MECHANISMS OF AIRWAY HYPERRESPONSIVENESSR01HL046368 · NHLBI · UNIVERSITY OF CHICAGO · PI LEFF, ALAN RICHARD · 1991 to 2005
$1.7M
NHLBI NIH HHS HL-46368NHLBI NIH HHS HL-56399NHLBI NIH HHS P50 HL056399NHLBI NIH HHS R01 HL046368
6 · The paper itself

Abstract

We examined the role of cell surface clustering of beta2-integrin caused by protein kinase C (PKC)-activated-cPLA2 in adhesion of eosinophilic AML14.3D10 (AML) cells. Phorbol 12-myristate 13-acetate (PMA) caused time- and concentration-dependent adhesion of AML cells to plated bovine serum albumin (BSA), which was blocked by anti-CD11b or anti-CD18 monoclonal antibodies (mAb) directed against beta2-integrin. Inhibition of PKC with Ro-31-8220 or rottlerin blocked PMA-induced cell adhesion in a concentration-dependent fashion. Inhibition of cytosolic phospholipase A2 (cPLA2) with trifluoromethyl ketone or methyl arachidonyl fluorophosphonate also blocked PMA-induced cell adhesion. PMA caused time-dependent p42/44 mitogen-activated protein kinase (MAPK) (ERK) phosphorylation in these cells. U0126, a MAPK/extracellular signal-regulated protein kinase kinase (MEK) inhibitor, at the concentrations that blocked PMA-induced ERK phosphorylation, had no effect on PMA stimulated AML cell adhesion. Neither p38 MAPK nor c-Jun N-terminal kinase (JNK) was phosphorylated by PMA. PMA also caused increased cPLA2 activity, which was inhibited by Ro-31-8220, but not U0126. Confocal immunofluorescence microscopy showed that PMA caused clustering of CD11b on the cell surface, which was blocked by either PKC or cPLA2 inhibition. PMA stimulation also caused up-regulation of CD11b on the AML cell surface. However, this up-regulation was not affected by cPLA2- or PKC-inhibition. Using the mAb, CBRM1/5, we also demonstrated that PMA does not induce the active conformation of CD11b/CD18. Our data indicate that PMA causes AML cell adhesion through beta2-integrin by PKC activation of cPLA2. This pathway is independent of MEK/ERK and does not require change of CD11b/CD18 to its active conformation. We find that avidity caused by integrin surface clustering - rather than conformational change or up-regulation of CD11b/CD18 - causes PMA stimulated adhesion of AML cells.

Indexed as

CD11b AntigenCD18 AntigensCell AdhesionCell Culture TechniquesCytosolDose-Response Relationship, DrugEnzyme InhibitorsEosinophilsHumansMitogen-Activated Protein Kinase 1Phospholipases APhospholipases A2PhosphorylationSerum Albumin, BovineTetradecanoylphorbol AcetateTumor Cells, CulturedCD11b AntigenCD18 AntigensEnzyme InhibitorsMitogen-Activated Protein Kinase 1phorbolol myristate acetatePhospholipases APhospholipases A2Serum Albumin, BovineTetradecanoylphorbol Acetate

Identifiers

PMID12225365
PMCPMC1782764
OpenAlexW2038371459

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.