Evidence map›Paper›PMID 26729407›Full record

ArticleScientific reports2016

Resistin, a fat-derived secretory factor, promotes metastasis of MDA-MB-231 human breast cancer cells through ERM activation.

Jung Ok Lee, Nami Kim, Hye Jeong Lee, Yong Woo Lee, Su Jin Kim, Sun Hwa Park, Hyeon Soo Kim

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 1 synthesis or guideline pooled it, 91 citations in OpenAlex.

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  10. Exploring the multifaceted role of obesity in breast cancer progression.Frontiers in cell and developmental biology · 2024
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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

7 authors at 1 institution in 1 country.

Jung Ok LeeDepartment of Anatomy, Korea University College of Medicine, Seoul, Korea.
Nami KimDepartment of Anatomy, Korea University College of Medicine, Seoul, Korea.
Hye Jeong LeeDepartment of Anatomy, Korea University College of Medicine, Seoul, Korea.
Yong Woo LeeDepartment of Anatomy, Korea University College of Medicine, Seoul, Korea.
Su Jin KimDepartment of Anatomy, Korea University College of Medicine, Seoul, Korea.
Sun Hwa ParkDepartment of Anatomy, Korea University College of Medicine, Seoul, Korea.
Hyeon Soo KimDepartment of Anatomy, Korea University College of Medicine, Seoul, Korea.
Korea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Resistin, an adipocyte-secreted factor, is known to be elevated in breast cancer patients. However, the molecular mechanism by which resistin acts is not fully understood. The aim of this study was to investigate whether resistin could stimulate invasion and migration of breast cancer cells. Here, we report that resistin stimulated invasion and migration of breast cancer cells as well as phosphorylation of c-Src. Inhibition of c-Src blocked resistin-induced breast cancer cell invasion. Resistin increased intracellular calcium concentration, and chelation of intracellular calcium blocked resistin-mediated activation of Src. Resistin also induced phosphorylation of protein phosphatase 2A (PP2A). Inhibition of c-Src blocked resistin-mediated PP2A phosphorylation. In addition, resistin increased phosphorylation of PKCα. Inhibition of PP2A enhanced resistin-induced PKCα phosphorylation, demonstrating that PP2A activity is critical for PKCα phosphorylation. Resistin also increased phosphorylation of ezrin, radixin, and moesin (ERM). Additionally, ezrin interacted with PKCα, and resistin promoted co-localization of ezrin and PKCα. Either inhibition of c-Src and PKCα or knock-down of ezrin blocked resistin-induced breast cancer cells invasion. Moreover, resistin increased expression of vimentin, a key molecule for cancer cell invasion. Knock-down of ezrin abrogated resistin-induced vimentin expression. These results suggest that resistin play as a critical regulator of breast cancer metastasis.

Indexed as

Breast NeoplasmsCalciumCell Line, TumorCell MovementCSK Tyrosine-Protein KinaseCytoskeletal ProteinsDNA-Binding ProteinsEzrinFemaleGene ExpressionHumansPhosphorylationProtein Kinase C-alphaProtein Phosphatase 2ResistinSignal TransductionCalciumCSK protein, humanCSK Tyrosine-Protein KinaseCytoskeletal ProteinsDNA-Binding ProteinsETV5 protein, humanEzrinProtein Kinase C-alphaProtein Phosphatase 2Resistinsrc-Family KinasesTranscription FactorsVimentin

Identifiers

PMID26729407
PMCPMC4700449
OpenAlexW2223576924

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.