Evidence map›Paper›PMID 34381017›Full record

ArticleCell death & disease2021

Lamin-A interacting protein Hsp90 is required for DNA damage repair and chemoresistance of ovarian cancer cells.

Yixuan Wang, Quan Chen, Di Wu, Qifeng Chen, Guanghui Gong, Liuqing He, Xiaoying Wu

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2021. 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
1.1field-weighted citation impact, top 24% 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, 24 citations in OpenAlex.

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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.

Yixuan WangDepartment of Pathology, Xiangya Hospital, Central South University, Changsha, 410008, Hunan Province, P. R. China.
Quan ChenDepartment of Pathology, School of Basic Medical Science, Central South University, Changsha, 410008, Hunan Province, P. R. China.
Di WuDepartment of Pathology, School of Basic Medical Science, Central South University, Changsha, 410008, Hunan Province, P. R. China.
Qifeng ChenDepartment of Pathology, School of Basic Medical Science, Central South University, Changsha, 410008, Hunan Province, P. R. China.
Guanghui GongDepartment of Pathology, Xiangya Hospital, Central South University, Changsha, 410008, Hunan Province, P. R. China.
Liuqing HeDepartment of Pathology, School of Basic Medical Science, Central South University, Changsha, 410008, Hunan Province, P. R. China.
Xiaoying WuDepartment of Pathology, Xiangya Hospital, Central South University, Changsha, 410008, Hunan Province, P. R. China. xyw2007@csu.edu.cn.ORCID 0000-0002-2977-3280
Central South University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ovarian cancer is the most malignant gynecologic cancer. Previous studies found that lamin-A was associated with DNA damage repair proteins but the underlying mechanism remains unclear. We speculate that this may be related to its interacting proteins, such as Hsp90. The aim of this study is to investigate the effects of Hsp90 on DNA damage repair and chemoresistance of ovarian cancer cells. In our research, co-immunoprecipitation (co-IP) and mass spectrometry (MS) were used to identify proteins interacting with lamin-A and the interaction domain. Next, the relationship between lamin-A and Hsp90 was explored by Western blotting (WB) and immunofluorescence staining. Then, effect of Hsp90 inhibition on DNA damage repair was assessed through detecting Rad50 and Ku80 by WB. Furthermore, to test the roles of 17-AAG on cell chemosensitivity, CCK-8 and colony formation assay were carried out. Meanwhile, IC50 of cells were calculated, followed by immunofluorescence to detect DNA damage. At last, the mouse xenograft model was used in determining the capacity of 17-AAG and DDP to suppress tumor growth and metastatic potential. The results showed that lamin-A could interact with Hsp90 via the domain of lamin-A

Indexed as

DNA DamageDNA RepairDrug Resistance, NeoplasmAnimalsBenzoquinonesCell Line, TumorCell ProliferationDNA Breaks, Double-StrandedFemaleGene Knockdown TechniquesHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicLamin Type AMiceMice, Inbred BALB CBenzoquinonesHSP90 Heat-Shock ProteinsLactams, MacrocyclicLamin Type Atanespimycin

Identifiers

PMID34381017
PMCPMC8358027
OpenAlexW3187958809

What OpenQuestion holds

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LicenceCC BY
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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.