Evidence map›Paper›PMID 9649570›Full record

ArticleThe Journal of clinical investigation1998

Integrin-dependent homotypic adhesion of neutrophils. Arachidonic acid activates Raf-1/Mek/Erk via a 5-lipoxygenase- dependent pathway.

C Capodici, M H Pillinger, G Han, M R Philips, G Weissmann

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 1998. 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
2.2field-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

12 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  9. Review
  10. Article
  11. Article
  12. Modes of action of aspirin-like drugs: salicylates inhibit erk activation and integrin-dependent neutrophil adhesion.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

5 authors at 2 institutions in 1 country.

C CapodiciDepartment of Medicine, New York University School of Medicine, New York 10016, USA.
M H Pillinger
G Han
M R Philips
G Weissmann
New York University · USNew York University Langone Orthopedic Hospital · US

Funding

BIOLOGY OF PRENYLCYSTEINE CARBOXYL METHYLTRANSFERASER01AI036224 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 1998 to 2002
$967k
MECHANISMS OF ARTHRITISR01AR011949 · NIAMS · NEW YORK UNIVERSITY · PI WEISSMANN, GERALD · 1986 to 1986
–
RAS SIGNALING AND NEUTROPHIL ACTIVATION IN SLER29AI036224 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 1993 to 1997
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MECHANISMS OF ARTHRITISR37AR011949 · NIAMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WEISSMANN, GERALD · 1988 to 1997
–
NIAID NIH HHS AI36224NIAMS NIH HHS AR11949NIGMS NIH HHS GM55279
6 · The paper itself

Abstract

AA stimulates integrin-dependent neutrophil adhesion, a critical early step in acute inflammation. However, neither the signaling pathway(s) of AA-stimulated adhesion, nor whether AA acts directly or through the generation of active metabolites, has been elucidated. Previously, we have observed a tight association between neutrophil Erk activation and homotypic adhesion in response to chemoattractants acting through G protein-linked receptors. We now report a similar association between homotypic adhesion and Erk activation in response to AA. Erk activation was cyclooxygenase independent and required AA metabolism to 5(S)- hydroperoxyeicosatetraenoic acid (5-HpETE) via 5-lipoxygenase, but not the further lipoxygenase-dependent metabolism of 5-HpETE to leukotrienes. AA stimulation of Erk was accompanied by Raf-1 activation and was sensitive to inhibitors of Raf-1 and Mek. Whereas activation of Erk by AA was pertussis toxin sensitive, [3H]-AA binding to neutrophils was not saturable, suggesting that an AA metabolite activates a G protein. Consistent with this hypothesis, Erk activation by 5(S)-hydroxyeicosatetraenoic acid (5-HETE; lipoxygenase-independent metabolite of 5-HpETE) was also pertussis toxin sensitive. These data suggest that a 5-lipoxygenase metabolite of AA, e.g., 5-HETE, is released from AA-treated cells to engage a plasma membrane-associated, pertussis toxin-sensitive, G protein-linked receptor, leading to activation of Erk and adhesion via the Raf-1/Mek signal transduction pathway.

Indexed as

MAP Kinase Kinase Kinase 1Arachidonate 5-LipoxygenaseArachidonic AcidCell AdhesionCell AggregationCyclic AMPEnzyme ActivationHumansHydroxyeicosatetraenoic AcidsIntegrinsMitogen-Activated Protein KinasesMyelin Basic ProteinNerve Tissue ProteinsNeutrophilsPertussis ToxinPhosphorylation5-hydroxy-6,8,11,14-eicosatetraenoic acidArachidonate 5-LipoxygenaseArachidonic AcidCyclic AMPHydroxyeicosatetraenoic AcidsIntegrinsMAP3K1 protein, humanMAP Kinase Kinase Kinase 1Mitogen-Activated Protein KinasesMyelin Basic ProteinNerve Tissue ProteinsPertussis ToxinProtein Serine-Threonine KinasesProto-Oncogene Proteins c-rafVirulence Factors, Bordetella

Identifiers

PMID9649570
PMCPMC509078
OpenAlexW2009946807

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.