Evidence map›Paper›PMID 27036017›Full record

ArticleOncotarget2016

Docosahexaenoic acid inhibits 12-O-tetradecanoylphorbol-13- acetate-induced fascin-1-dependent breast cancer cell migration by suppressing the PKCδ- and Wnt-1/β-catenin-mediated pathways.

Chong-Kuei Lii, Jer-Wei Chang, Jia-Jing Chen, Haw-Wen Chen, Kai-Li Liu, Shu-Lan Yeh, Tsu-Shing Wang, Shu-Hui Liu, Chia-Han Tsai, Chien-Chun Li

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  4. Comparative Efficacy ofMolecules (Basel, Switzerland) · 2024
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  5. 12-Cells · 2022
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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 5 institutions in 1 country.

Chong-Kuei LiiDepartment of Nutrition, China Medical University, Taichung, Taiwan.
Jer-Wei ChangInstitute of Molecular and Genomic Medicine, National Health Research Institute, Zhunan, Miaoli, Taiwan.
Jia-Jing ChenSchool of Nutrition, Chung Shan Medical University, Taichung, Taiwan.
Haw-Wen ChenDepartment of Nutrition, China Medical University, Taichung, Taiwan.
Kai-Li LiuSchool of Nutrition, Chung Shan Medical University, Taichung, Taiwan.
Shu-Lan YehSchool of Nutrition, Chung Shan Medical University, Taichung, Taiwan.
Tsu-Shing WangDepartment of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan.
Shu-Hui LiuSchool of Nutrition, Chung Shan Medical University, Taichung, Taiwan.
Chia-Han TsaiSchool of Nutrition, Chung Shan Medical University, Taichung, Taiwan.
Chien-Chun LiSchool of Nutrition, Chung Shan Medical University, Taichung, Taiwan.
Chung Shan Medical University · TWAsia University · TWChina Medical University · TWChung Shan Medical University Hospital · TWNational Health Research Institutes · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fascin-1, an actin-bundling protein, plays an important role in cancer cell migration and invasion; however, the underlying mechanism remains unclear. On the basis of a 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced cell migration model, it was shown that TPA increased fascin-1 mRNA and protein expression and fascin-1-dependent cell migration. TPA dose- and time-dependently increased PKCδ and STAT3α activation and GSK3β phosphorylation; up-regulated Wnt-1, β-catenin, and STAT3α expression; and increased the nuclear translocation of β-catenin and STAT3α. Rottlerin, a PKCδ inhibitor, abrogated the increases in STAT3α activation and β-catenin and fascin-1 expression. WP1066, a STAT3 inhibitor, suppressed TPA-induced STAT3α DNA binding activity and β-catenin expression. Knockdown of β-catenin attenuated TPA-induced fascin-1 and STAT3α expression as well as cell migration. In addition to MCF-7, migration of Hs578T breast cancer cells was inhibited by silencing fascin-1, β-catenin, and STAT3α expression as well. TPA also induced Wnt-1 expression and secretion, and blocking Wnt-1 signaling abrogated β-catenin induction. DHA pretreatment attenuated TPA-induced cell migration, PKCδ and STAT3α activation, GSK3β phosphorylation, and Wnt-1, β-catenin, STAT3α, and fascin-1 expression. Our results demonstrated that TPA-induced migration is likely associated with the PKCδ and Wnt-1 pathways, which lead to STAT3α activation, GSK3β inactivation, and β-catenin increase and up-regulation of fascin-1 expression. Moreover, the anti-metastatic potential of DHA is partly attributed to its suppression of TPA-activated PKCδ and Wnt-1 signaling.

Indexed as

Breast NeoplasmsCarcinogensCarrier ProteinsCell Line, TumorCell MovementDocosahexaenoic AcidsFemaleHumansMicrofilament ProteinsProtein Kinase C-deltaTetradecanoylphorbol AcetateWnt Signaling PathwayCarcinogensCarrier ProteinsDocosahexaenoic AcidsFSCN1 protein, humanMicrofilament ProteinsProtein Kinase C-deltaTetradecanoylphorbol Acetatedocosahexaenoic acidfascin-1PKCδTPAWnt-1

Identifiers

PMID27036017
PMCPMC5041895
OpenAlexW2318861303

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.