Evidence map›Paper›PMID 35043518›Full record

ArticleCancer science2022

HSP90 promotes radioresistance of cervical cancer cells via reducing FBXO6-mediated CD147 polyubiquitination.

Qi Song, Juyi Wen, Weiping Li, Janxin Xue, Yufei Zhang, Hongyan Liu, Jixia Han, Tao Ning, Zejun Lu

Open access · goldAbstract read
In one paragraph

Article in Cancer science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.

  1. Pooled it
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  4. Functional and therapeutic significant of heat-shock protein 90 (HSP90) in reproductive cancers.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2025
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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

9 authors at 3 institutions in 1 country.

Qi SongSenior Department of Obstetrics and Gynecology, the Seventh Medical Center of PLA General Hospital, Beijing, China.
Juyi WenOncology Department, the Sixth Medical Center of PLA General Hospital, Beijing, China.
Weiping LiSenior Department of Obstetrics and Gynecology, the Seventh Medical Center of PLA General Hospital, Beijing, China.
Janxin XueDepartment of Thoracic Oncology, Cancer Center and State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yufei ZhangSenior Department of Oncology, the Fifth Medical Center of PLA General Hospital, Beijing, China.
Hongyan LiuSenior Department of Oncology, the Fifth Medical Center of PLA General Hospital, Beijing, China.
Jixia HanSenior Department of Oncology, the Fifth Medical Center of PLA General Hospital, Beijing, China.
Tao NingTianjin Medical University Cancer Institute and Hospital, Tianjin, China.
Zejun LuOncology Department, the Sixth Medical Center of PLA General Hospital, Beijing, China.ORCID https://orcid.org/0000-0002-7263-7049
Chinese PLA General Hospital · CNSichuan University · CNTianjin Medical University Cancer Institute and Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HSP90 inhibition might be a promising strategy to overcome the radioresistance of some cancers. In the current study, we further explored the mechanisms of HSP90 in regulating the radiosensitivity of cervical cancer cells. Bioinformatic analysis was performed based on data from TCGA-CESC. Cellular and molecular studies were conducted using CaSki and SiHa and the derived radioresistant (RR) subclones. Through a proteomics screen, we identified HSP90 chaperones (both HSP90α and HSP90β) as CD147-binding partners supporting its stabilization. Targeting HSP90 sensitized CaSki-RR and SiHa-RR cancer cells to irradiation partially through CD147 destabilization. Mechanistically, HSP90 interacts with FBXO6 and reduces FBXO6-mediated proteasomal degradation of CD147. Enforced FBXO6 overexpression also sensitized CaSki-RR and SiHa-RR cancer cells to irradiation. These effects were enhanced using 17-AAG treatment but were weakened by CD147 overexpression. Survival analysis further confirmed the association between high FBXO6 expression and favorable progression-free survival among patients with cervical cancer. In conclusion, this study showed that HSP90 promotes radioresistance of cervical cancer cells partially via reducing FBXO6 mediated CD147 polyubiquitination. These findings help to explain why HSP90 inhibitor exerts radio-sensitizing effects in cervical cancer.

Indexed as

Uterine Cervical NeoplasmsBasiginCell Line, TumorFemaleHSP90 Heat-Shock ProteinsHumansRadiation ToleranceSKP Cullin F-Box Protein LigasesUbiquitinationBasiginBSG protein, humanFBXO6 protein, humanHSP90 Heat-Shock ProteinsSKP Cullin F-Box Protein LigasesCD147cervical cancerFBXO6HSP90radiotherapy

Identifiers

PMID35043518
PMCPMC8990293
OpenAlexW4205286306

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.