Evidence map›Paper›PMID 31020572›Full record

ArticleVirologica Sinica2019

Prion Protein Protects Cancer Cells against Endoplasmic Reticulum Stress Induced Apoptosis.

Zhenxing Gao, Min Peng, Liang Chen, Xiaowen Yang, Huan Li, Run Shi, Guiru Wu, Lili Cai, Qibin Song, Chaoyang Li

Open access · hybridAbstract read
In one paragraph

Article in Virologica Sinica, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. PrPInternational journal of biological sciences · 2022
    Article
  10. What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. The Cellular Prion Protein: A Promising Therapeutic Target for Cancer.International journal of molecular sciences · 2020
    Review
  16. Article
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.

Zhenxing GaoState Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China.
Min PengDepartment of Oncology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Liang ChenDepartment of Oncology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Xiaowen YangDepartment of the First Abdominal Surgery, Jiangxi Tumor Hospital, Nanchang, 330029, China.
Huan LiState Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China.
Run ShiState Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China.
Guiru WuState Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China.
Lili CaiState Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China.
Qibin SongDepartment of Oncology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Chaoyang LiState Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China. cyli@wh.iov.cn.ORCID http://orcid.org/0000-0003-3582-4141
Chinese Academy of Sciences · CNWuhan University · CNJiangxi Provincial Cancer Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Unfolded protein response (UPR) is an adaptive reaction for cells to reduce endoplasmic reticulum (ER) stress. In many types of cancers, such as lung cancer and pancreatic cancer, cancer cells may harness ER stress to facilitate their survival and growth. Prion protein (PrP) is a glycosylated cell surface protein that has been shown to be up-regulated in many cancer cells. Since PrP is a protein prone to misfolding, ER stress can result in under-glycosylated PrP, which in turn may activate ER stress. To assess whether ER stress leads to the production of under-glycosylated PrP and whether under-glycosylated PrP may contribute to ER stress thus leading to cancer cell apoptosis, we treated different cancer cells with brefeldin A (BFA), thapsigargin (Thps), and tunicamycin (TM). We found that although BFA, Thps, and TM treatment activated UPR, only ATF4 was consistently activated by these reagents, but not other branches of ER stress. However, the canonical PERK-eIF2α-ATF4 did not account for the observed activation of ATF4 in lung cancer cells. In addition, BFA, but neither Thps nor TM, significantly stimulated the expression of cytosolic PrP. Finally, we found that the levels of PrP contributed to anti-apoptosis activity of BFA-induced cancer cell death. Thus, the pathway of BFA-induced persistent ER stress may be targeted for lung and pancreatic cancer treatment.

Indexed as

ApoptosisEndoplasmic Reticulum StressActivating Transcription Factor 4Brefeldin ACell Line, TumorGlycosylationHumansLungPrion ProteinsProtein Synthesis InhibitorsSignal TransductionThapsigarginTunicamycinUnfolded Protein ResponseActivating Transcription Factor 4ATF4 protein, humanBrefeldin APrion ProteinsProtein Synthesis InhibitorsThapsigarginTunicamycinApoptosisBrefeldin A (BFA)Endoplasmic reticulum stressGlycosylationPrion protein (PrP)

Identifiers

PMID31020572
PMCPMC6513834
OpenAlexW2940996657

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.