Evidence map›Paper›PMID 20566634›Full record

ArticleThe Journal of biological chemistry2010

p27 suppresses arsenite-induced Hsp27/Hsp70 expression through inhibiting JNK2/c-Jun- and HSF-1-dependent pathways.

Jinyi Liu, Dongyun Zhang, Xiaoyi Mi, Qing Xia, Yonghui Yu, Zhenghong Zuo, Wei Guo, Xuewei Zhao, Jia Cao, Qing Yang and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mechanisms of Small Heat Shock Proteins.Cold Spring Harbor perspectives in biology · 2019
    Review
  7. Autophagy-mediatedAutophagy · 2019
    Article
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  14. 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

15 authors at 4 institutions in 2 countries.

Jinyi LiuNelson Institute of Environmental Medicine, New York University School of Medicine, Tuxedo, New York 10987, USA.
Dongyun Zhang
Xiaoyi Mi
Qing Xia
Yonghui Yu
Zhenghong Zuo
Wei Guo
Xuewei Zhao
Jia Cao
Qing Yang
Angela Zhu
Wancai Yang
Xianglin Shi
Jingxia Li
Chuanshu Huang
New York University · USArmy Medical University · CNUniversity of Illinois Chicago · USUniversity of Kentucky · US

Funding

Water/sediment &model &criteria for arsenic &chromeP42ES010344 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI COSTA, MAX · 2000 to 2010
$15.0M
Molecular Mechanisms of Nickel-Induced TumorigenicityR01CA112557 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, CHUANSHU · 2004 to 2016
$2.9M
Mechanisms of As-Induced CarcinogenesisR01CA119028 · NCI · UNIVERSITY OF KENTUCKY · PI SHI, XIANGLIN · 2006 to 2010
$1.8M
Mechanisms of Tumor Promotion Effects of B[a]PDER01ES012451 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, CHUANSHU · 2004 to 2008
$1.7M
NCI NIH HHS CA112557NCI NIH HHS CA119028-05S110NCI NIH HHS R01 CA112557NCI NIH HHS R01 CA119028NIEHS NIH HHS ES010344NIEHS NIH HHS ES012451NIEHS NIH HHS P42 ES010344NIEHS NIH HHS R01 ES012451
6 · The paper itself

Abstract

p27 is an atypical tumor suppressor that can regulate the activity of cyclin-dependent kinases and G(0)-to-S phase transitions. More recent studies reveal that p27 may also exhibit its tumor-suppressive function through regulating many other essential cellular events. However, the molecular mechanisms underlying these anticancer effects of p27 are largely unknown. In this study, we found that depletion of p27 expression by either gene knock-out or knockdown approaches resulted in up-regulation of both Hsp27 and Hsp70 expression at mRNA- and promoter-derived transcription as well as protein levels upon arsenite exposure, indicating that p27 provides a negative signal for regulating the expression of Hsp27 and Hsp70. Consistently, arsenite-induced activation of JNK2/c-Jun and HSF-1 pathways was also markedly elevated in p27 knock-out (p27(-/-)) and knockdown (p27 shRNA) cells. Moreover, interference with the expression or function of JNK2, c-Jun, and HSF-1, but not JNK1, led to dramatic inhibition of arsenite-induced Hsp27 and Hsp70 expression. Collectively, our results demonstrate that p27 suppresses Hsp27 and Hsp70 expression at the transcriptional level specifically through JNK2/c-Jun- and HSF-1-dependent pathways upon arsenite exposure, which provides additional important molecular mechanisms for the tumor-suppressive function of p27.

Indexed as

AnimalsArsenitesCells, CulturedCyclin-Dependent Kinase Inhibitor p27DNA-Binding ProteinsFibroblastsHeat Shock Transcription FactorsHSP27 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsJNK Mitogen-Activated Protein KinasesMiceMice, KnockoutMitogen-Activated Protein Kinase 9RNA, MessengerSignal TransductionTeratogensarseniteArsenitesCyclin-Dependent Kinase Inhibitor p27DNA-Binding ProteinsHeat Shock Transcription FactorsHsf1 protein, mouseHSP27 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 9RNA, MessengerTeratogensTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID20566634
PMCPMC2924005
OpenAlexW1978746682

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.