Evidence map›Paper›PMID 23145121›Full record

ArticlePloS one2012

Luteolin induces carcinoma cell apoptosis through binding Hsp90 to suppress constitutive activation of STAT3.

Jin Fu, Dan Chen, Bo Zhao, Zhihui Zhao, Jiahong Zhou, Yimiao Xu, Yinqiang Xin, Chang Liu, Lan Luo, Zhimin Yin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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
2.0field-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

23 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  6. Review
  7. Recent Trends in anti-tumor mechanisms and molecular targets of celastrol.International journal of biological sciences · 2024
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  9. Evidence-based complementary and alternative medicine : eCAM · 2022
    Article
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  15. A StandardizedFrontiers in pharmacology · 2017
    Article
  16. Article
  17. Molecular targets of luteolin in cancer.European journal of cancer prevention : the official journal of the European Cancer Prevention Organisation (ECP) · 2016
    Review
  18. Review
  19. Article
  20. Luteolin induces apoptosis by activating Fas signaling pathway at the receptor level in laryngeal squamous cell line Hep-2 cells.European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery · 2014
    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

10 authors at 2 institutions in 1 country.

Jin FuJiangsu Province Key Laboratory for Molecular and Medicine Biotechnology, College of Life Science, Nanjing Normal University, Nanjing, People's Republic of China.
Dan Chen
Bo Zhao
Zhihui Zhao
Jiahong Zhou
Yimiao Xu
Yinqiang Xin
Chang Liu
Lan Luo
Zhimin Yin
Nanjing Normal University · CNNanjing University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAbnormal activity of STAT3 is associated with a number of human malignancies. Hsp90 plays a central role in stabilizing newly synthesized proteins and participates in maintaining the functional competency of a number of signaling transducers involved in cell growth, survival and oncogenesis, such as STAT3. Hsp90 interacts with STAT3 and stabilizes Tyr-phosphorylated STAT3. It has been reported that luteolin possesses anticancer activity through degradation of Tyr(705)-phosphorylated STAT3. METHODOLOGY/PRINCIPAL

findingsWe found that overexpression of Hsp90 inhibited luteolin-induced degradation of Tyr(705)-phosphorylated STAT3 and luteolin also reduced the levels of some other Hsp90 interacting proteins. Results from co-immunoprecipitation and immunoblot analysis demonstrated that luteolin prevented the association between Hsp90 and STAT3 and induced both Tyr(705)- and Ser(727)-phosphorylated STAT3 degradation through proteasome-dependent pathway. The molecular modeling analysis with CHARMm-Discovery Studio 2.1(DS 2.1) indicated that luteolin could bind to the ATP-binding pocket of Hsp90. SPR technology-based binding assay confirmed the association between luteolin and Hsp90. ATP-sepharose binding assay displayed that luteolin inhibited Hsp90-ATP binding. CONCLUSIONS/SIGNIFICANCE: Luteolin promoted the degradation of Tyr(705)- and Ser(727)-phosphorylated STAT3 through interacting with Hsp90 and induced apoptosis of cancer cells. This study indicated that luteolin may act as a potent HSP90 inhibitor in antitumor strategies.

Indexed as

CarcinomaHSP90 Heat-Shock ProteinsNeoplasmsSTAT3 Transcription FactorAnimalsApoptosisCell Line, TumorCell ProliferationCell Transformation, NeoplasticHEK293 CellsHeLa CellsHep G2 CellsHumansLuteolinMicePhosphorylationHSP90 Heat-Shock ProteinsLuteolinSTAT3 protein, humanSTAT3 Transcription FactorTyrosine

Identifiers

PMID23145121
PMCPMC3493516
OpenAlexW2135231147

What OpenQuestion holds

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Registered trials

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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.