Evidence map›Paper›PMID 28011194›Full record

ArticleExperimental cell research2017

Convergence of eicosanoid and integrin biology: Role of Src in 12-LOX activation.

Ashok-Kumar Dilly, Keqin Tang, Yande Guo, Sangeeta Joshi, Prasanna Ekambaram, Krishna Rao Maddipati, Yinlong Cai, Stephanie C Tucker, Kenneth V Honn

Open access · greenAbstract read
In one paragraph

Article in Experimental cell research, 2017. 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
0.9field-weighted citation impact, top 20% 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, 7 citations in OpenAlex.

  1. Review
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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

9 authors at 2 institutions in 1 country.

Ashok-Kumar DillyDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States. Electronic address: akd37@pitt.edu.
Keqin TangDepartments of Radiation Oncology, Wayne State University School of Medicine, Detroit, MI 48202, United States. Electronic address: ktang@med.wayne.edu.
Yande GuoDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States. Electronic address: guoyande@yahoo.com.
Sangeeta JoshiDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States. Electronic address: sjoshi@tartiscorp.com.
Prasanna EkambaramDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States. Electronic address: pre2@pitt.edu.
Krishna Rao MaddipatiDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States. Electronic address: maddipati@wayne.edu.
Yinlong CaiDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States. Electronic address: aa9873@wayne.edu.
Stephanie C TuckerDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States. Electronic address: stucker@med.wayne.edu.
Kenneth V HonnDepartments of Pathology-Bioactive Lipids Research Program, Detroit, MI 48202, United States; Departments of Karmanos Cancer Institute, Detroit, MI 48202, United States. Electronic address: k.v.honn@wayne.edu.
The Barbara Ann Karmanos Cancer Institute · USWayne State University · US

Funding

THROMBOXANES: ROLE IN TUMOR GROWTH AND METASTASISR01CA029997 · NCI · WAYNE STATE UNIVERSITY · PI HONN, KENNETH V · 1985 to 2008
$1.7M
NCI NIH HHS R01 CA029997
6 · The paper itself

Abstract

12-Lipoxygenase (12-LOX) metabolizes arachidonic acid to 12(S)-hydroxyeicosatetraenoic acid, or 12(S)-HETE, a proinflammatory bioactive lipid implicated in tumor angiogenesis, growth, and metastasis. The mechanisms underlying 12-LOX-mediated signaling in cancer progression are still ill-defined. In the present study we demonstrate that 12-LOX phosphorylation and subsequent enzymatic activity occurs after integrin β4 stimulation and Src kinase recruitment to the integrin subunit. Inhibition of Src activity by PP2 or Src dominant-negative mutants reduced 12-LOX tyrosine phosphorylation and 12(S)-HETE production in response to integrin β4 stimulation in A431 cells. The pertinent Src-targeted residues for 12-LOX activity were mapped to Y19 and Y614, where 12-LOX mutants Y19F and Y614F showed 70% less enzymatic activity. Furthermore, we have shown that the 12-LOX activity modulated by these residues impacts migration. To our knowledge, this is the first report that c-Src kinase activity is required for β4-integrin-mediated phosphorylation of 12-LOX.

Indexed as

Cell Movement12-Hydroxy-5,8,10,14-eicosatetraenoic AcidArachidonate 12-LipoxygenaseCell Line, TumorHEK293 CellsHumansIntegrin beta4src-Family Kinases12-Hydroxy-5,8,10,14-eicosatetraenoic AcidArachidonate 12-LipoxygenaseIntegrin beta4ITGB4 protein, humansrc-Family Kinases12-Lipoxygenase phosphorylationCell migrationC-Src kinaseβ4 Integrin

Identifiers

PMID28011194
PMCPMC5303182
OpenAlexW2565626176

What OpenQuestion holds

Textmetadata
LicenceTDM
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.