Evidence map›Paper›PMID 26943774›Full record

ArticleOncotarget2016

Nuclear heat shock protein 110 expression is associated with poor prognosis and chemotherapy resistance in gastric cancer.

Akiharu Kimura, Kyoichi Ogata, Bolag Altan, Takehiko Yokobori, Munenori Ide, Erito Mochiki, Yoshitaka Toyomasu, Norimichi Kogure, Toru Yanoma, Masaki Suzuki and 3 more

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 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
4.4field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. Pooled it
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  7. Pre-Conceptional Exposure to Glyphosate Affects the Maternal Hepatic and Ovarian Proteome.Toxicological sciences : an official journal of the Society of Toxicology · 2022
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  20. Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach.International journal of molecular sciences · 2017
    Review
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

13 authors at 2 institutions in 1 country.

Akiharu KimuraDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Kyoichi OgataDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Bolag AltanDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Takehiko YokoboriDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Munenori IdeDepartment of Diagnostic Pathology, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Erito MochikiDepartment of Digestive Tract and General Surgery, Saitama Medical Center, Saitama Medical University, Kawagoe, Saitama, Japan.
Yoshitaka ToyomasuDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Norimichi KogureDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Toru YanomaDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Masaki SuzukiDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Tuya BaiDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Tetsunari OyamaDepartment of Diagnostic Pathology, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Hiroyuki KuwanoDepartment of General Surgical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
Gunma University · JPSocial Insurance Saitama Chuo Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock protein (HSP) expression is induced by the exposure to stress, such as fever, oxidative stress, chemical exposure, and irradiation. In cancer, HSP promotes the survival of malignant cells by inhibiting the induction of apoptosis. In colorectal cancer, a loss-of-function mutation of HSP110 (HSP110ΔE9) has been identified. HSP110ΔE9 inhibits the nuclear translocation of wild-type HSP110, which is important for its chaperone activity and anti-apoptotic effects. The patients carrying HSP110ΔE9 mutation exhibit high sensitivity to anticancer agents, such as oxaliplatin and 5-fluorouracil. There is still insufficient information about HSP110 localization, the clinicopathological significance of HSP110 expression, and its association with chemotherapy resistance in gastric cancer. Here, we found that high nuclear expression of HSP110 in gastric cancer tissues is associated with cancer progression, poor prognosis, and recurrence after adjuvant chemotherapy. In vitro results showed that HSP110 suppression increases the sensitivity to 5-fluorouracil and cisplatin of human gastric cancer cell lines. Our results suggest that nuclear HSP110 may be a new drug sensitivity marker for gastric cancer and a potential molecular therapeutic target for the treatment of gastric cancer patients with acquired anticancer drug resistance.

Indexed as

Disease ProgressionDrug Resistance, NeoplasmFemaleHSP110 Heat-Shock ProteinsHumansImmunohistochemistryMaleMiddle AgedPrognosisStomach NeoplasmsSurvival RateHSP110 Heat-Shock Proteinscancer progressiondrug resistancegastric cancerheat shock proteinheat shock protein 110

Identifiers

PMID26943774
PMCPMC4951298
OpenAlexW2295826405

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.