Evidence map›Paper›PMID 31121863›Full record

ReviewInternational journal of molecular sciences2019

Unfolded Protein Response (UPR) in Survival, Dormancy, Immunosuppression, Metastasis, and Treatments of Cancer Cells.

Sheng-Kai Hsu, Chien-Chih Chiu, Hans-Uwe Dahms, Chon-Kit Chou, Chih-Mei Cheng, Wen-Tsan Chang, Kai-Chun Cheng, Hui-Min David Wang, I-Ling Lin

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
8.6field-weighted citation impact, top 1% 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

79 citing papers in PubMed, 123 citations in OpenAlex.

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19 more citing papers are in PubMed but not listed here.

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 4 institutions in 2 countries.

Sheng-Kai HsuDepartment of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. b043100050@gmail.com.
Chien-Chih ChiuDepartment of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. cchiu@kmu.edu.tw.ORCID 0000-0001-7307-2468
Hans-Uwe DahmsDepartment of Biomedical Science and Environmental Biology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. hansd@kmu.edu.tw.
Chon-Kit ChouState Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macau, China. fatchou1988@hotmail.com.
Chih-Mei ChengDepartment of Medical Research, Kaohsiung Medical University Hospital, Kaohsiung 807, Taiwan. chmech@kmu.edu.tw.
Wen-Tsan ChangDivision of General and Digestive Surgery, Department of Surgery, Kaohsiung Medical University Hospital, Kaohsiung 807, Taiwan. wtchang@kmu.edu.tw.ORCID 0000-0001-5622-8299
Kai-Chun ChengDepartment of Ophthalmology, Kaohsiung Municipal Hsiaokang Hospital, Kaohsiung 812, Taiwan. pington64@gmail.com.ORCID 0000-0002-1240-4219
Hui-Min David WangGraduate Institute of Biomedical Engineering, National Chung Hsing University, Taichung 402, Taiwan. davidw@dragon.nchu.edu.tw.ORCID 0000-0002-5162-9752
I-Ling LinDepartment of Medical Laboratory Science and Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. linili@kmu.edu.tw.
Kaohsiung Medical University · TWNational Sun Yat-sen University · TWNational Chung Hsing University · TWUniversity of Macau · MO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) has diverse functions, and especially misfolded protein modification is in the focus of this review paper. With a highly regulatory mechanism, called unfolded protein response (UPR), it protects cells from the accumulation of misfolded proteins. Nevertheless, not only does UPR modify improper proteins, but it also degrades proteins that are unable to recover. Three pathways of UPR, namely PERK, IRE-1, and ATF6, have a significant role in regulating stress-induced physiological responses in cells. The dysregulated UPR may be involved in diseases, such as atherosclerosis, heart diseases, amyotrophic lateral sclerosis (ALS), and cancer. Here, we discuss the relation between UPR and cancer, considering several aspects including survival, dormancy, immunosuppression, angiogenesis, and metastasis of cancer cells. Although several moderate adversities can subject cancer cells to a hostile environment, UPR can ensure their survival. Excessive unfavorable conditions, such as overloading with misfolded proteins and nutrient deprivation, tend to trigger cancer cell death signaling. Regarding dormancy and immunosuppression, cancer cells can survive chemotherapies and acquire drug resistance through dormancy and immunosuppression. Cancer cells can also regulate the downstream of UPR to modulate angiogenesis and promote metastasis. In the end, regulating UPR through different molecular mechanisms may provide promising anticancer treatment options by suppressing cancer proliferation and progression.

Indexed as

Unfolded Protein ResponseAnimalsCell SurvivalDisease ProgressionHumansImmune ToleranceNeoplasm MetastasisNeoplasmsNeovascularization, PathologicATF6cancerendoplasmic reticulum (ER)IRE-1PERKunfolded protein response (UPR)

Identifiers

PMID31121863
PMCPMC6566956
OpenAlexW2945426048

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.