Evidence map›Paper›PMID 27409672›Full record

ArticleOncotarget2016

Stress-induced phosphoprotein-1 maintains the stability of JAK2 in cancer cells.

Chia-Lung Tsai, Angel Chao, Shih-Ming Jung, Chi-Neu Tsai, Chiao-Yun Lin, Shun-Hua Chen, Shih-Che Sue, Tzu-Hao Wang, Hsin-Shih Wang, Chyong-Huey Lai

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

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  13. STAT3 Interactors as Potential Therapeutic Targets for Cancer Treatment.International journal of molecular sciences · 2018
    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

10 authors at 3 institutions in 1 country.

Chia-Lung TsaiGenomic Medicine Research Core Laboratory, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
Angel ChaoGenomic Medicine Research Core Laboratory, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
Shih-Ming JungDepartment of Pathology, Chang Gung Memorial Hospital and Chang Gung University, Taoyuan, Taiwan.
Chi-Neu TsaiGraduate Institute of Clinical Medical Sciences, Chang Gung University, Taoyuan, Taiwan.
Chiao-Yun LinDepartment of Obstetrics and Gynecology, Chang Gung Memorial Hospital and Chang Gung University, Taoyuan, Taiwan.
Shun-Hua ChenDepartment of Obstetrics and Gynecology, Chang Gung Memorial Hospital and Chang Gung University, Taoyuan, Taiwan.
Shih-Che SueDepartment of Life Sciences, Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Taiwan.
Tzu-Hao WangGenomic Medicine Research Core Laboratory, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
Hsin-Shih WangDepartment of Obstetrics and Gynecology, Chang Gung Memorial Hospital and Chang Gung University, Taoyuan, Taiwan.
Chyong-Huey LaiDepartment of Obstetrics and Gynecology, Chang Gung Memorial Hospital and Chang Gung University, Taoyuan, Taiwan.
Chang Gung University · TWChang Gung Memorial Hospital · TWNational Tsing Hua University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Overexpression of stress-induced phosphoprotein 1 (STIP1) - a co-chaperone of heat shock protein (HSP) 70/HSP90 - and activation of the JAK2-STAT3 pathway occur in several tumors. Combined treatment with a HSP90 inhibitor and a JAK2 inhibitor exert synergistic anti-cancer effects. Here, we show that STIP1 stabilizes JAK2 protein in ovarian and endometrial cancer cells. Knock-down of endogenous STIP1 decreased JAK2 and phospho-STAT3 protein levels. The N-terminal fragment of STIP1 interacts with the N-terminus of JAK2, whereas the C-terminal DP2 domain of STIP1 mediates the interaction with HSP90 and STAT3. A peptide fragment in the DP2 domain of STIP1 (peptide 520) disrupted the interaction between STIP1 and HSP90 and induced cell death through JAK2 suppression. In an animal model, treatment with peptide 520 inhibited tumor growth. In summary, STIP1 modulates the function of the HSP90-JAK2-STAT3 complex. Peptide 520 may have therapeutic potential in the treatment of JAK2-overexpressing tumors.

Indexed as

Gene Expression Regulation, NeoplasticAnimalsCell Line, TumorCell SurvivalEndometrial NeoplasmsFemaleGene DeletionGene Expression ProfilingHeat-Shock ProteinsHEK293 CellsHumansJanus Kinase 2MiceMice, NudeNeoplasm TransplantationOvarian NeoplasmsHeat-Shock ProteinsJAK2 protein, humanJanus Kinase 2RNA, Small InterferingSTAT3 protein, humanSTAT3 Transcription FactorSTIP1 protein, humancancerJAK2STIP1

Identifiers

PMID27409672
PMCPMC5226602
OpenAlexW2465488219

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.