Evidence map›Paper›PMID 32497199›Full record

ArticleThe Biochemical journal2020

Heat shock protein 90 inhibitors suppress pyroptosis in THP-1 cells.

Zhou Zhou, Xiuzhen Li, Yisong Qian, Cynthia Liu, Xiaotian Huang, Mingui Fu

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2020. 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
1.8field-weighted citation impact, top 15% 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, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Regulation of Pyroptosis by ncRNA: A Novel Research Direction.Frontiers in cell and developmental biology · 2022
    Review
  15. 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

6 authors at 2 institutions in 2 countries.

Zhou ZhouDepartment of Biomedical Science, School of Medicine, University of Missouri Kansas City, 2411 Holmes Street, Kansas City, MO 64108, U.S.A.
Xiuzhen LiDepartment of Biomedical Science, School of Medicine, University of Missouri Kansas City, 2411 Holmes Street, Kansas City, MO 64108, U.S.A.
Yisong QianDepartment of Biomedical Science, School of Medicine, University of Missouri Kansas City, 2411 Holmes Street, Kansas City, MO 64108, U.S.A.
Cynthia LiuDepartment of Biomedical Science, School of Medicine, University of Missouri Kansas City, 2411 Holmes Street, Kansas City, MO 64108, U.S.A.
Xiaotian HuangDepartment of Microbiology, School of Medicine, Nanchang University, NO 461 Bayi Road, Donghu District, Nanchang 330006, China.
Mingui FuDepartment of Biomedical Science, School of Medicine, University of Missouri Kansas City, 2411 Holmes Street, Kansas City, MO 64108, U.S.A.
Nanchang University · CNUniversity of Missouri–Kansas City · US

Funding

Ribonuclease-mediated control of sepsis-induced systemic inflammationR15AI138116 · NIAID · UNIVERSITY OF MISSOURI KANSAS CITY · PI FU, MINGUI · 2019 to 2019
$465k
NIAID NIH HHS R15 AI138116
6 · The paper itself

Abstract

Pyroptosis is a recently discovered inflammatory form of programmed cell death which is mostly triggered by infection with intracellular pathogens and critically contributes to inflammation. Mitigating pyroptosis may be a potential therapeutic target in inflammatory diseases. However, small chemicals to reduce pyroptosis is still elusive. In the present study, we screened 155 chemicals from a microbial natural product library and found Geldanamycin, an HSP90 inhibitor, profoundly rescued THP-1 cells from pyroptosis induced by LPS plus Nigericin treatment. Consistently, other HSP90 inhibitors, including Radicicol, 17-DMAG and 17-AAG, all ameliorated pyroptosis in THP-1 cells by suppressing the inflammasome/Caspase-1/GSDMD signal pathway in pyroptosis. HSP90 inhibition compromised the protein stability of NLRP3, a critical component of the inflammasome. Moreover, up-regulated HSP70 may also contribute to this effect. HSP90 inhibition may thus be a potential therapeutic strategy in the treatment of inflammatory diseases in which pyroptosis plays a role.

Indexed as

BenzoquinonesCaspase 1Cell SurvivalGasderminsHSP72 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansInflammasomesInflammationIntracellular Signaling Peptides and ProteinsLactams, MacrocyclicLipopolysaccharidesMacrolidesNigericinNLR Family, Pyrin Domain-Containing 3 ProteinPhosphate-Binding Proteins17-(dimethylaminoethylamino)-17-demethoxygeldanamycinBenzoquinonesCaspase 1GasderminsgeldanamycinGSDMD protein, humanHSP72 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsInflammasomesIntracellular Signaling Peptides and ProteinsLactams, MacrocyclicLipopolysaccharidesMacrolidesmonordenNigericinNLR Family, Pyrin Domain-Containing 3 ProteinNLRP3 protein, humanPhosphate-Binding ProteinsProteasome Endopeptidase Complextanespimycingasdemin DinflammasomeNLRP3pyroptosisTHP-1

Identifiers

PMID32497199
PMCPMC7773284
OpenAlexW3033481196

What OpenQuestion holds

Textmetadata
LicenceTDM
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.