Evidence map›Paper›PMID 39080660›Full record

ArticleRespiratory research2024

Glycolytic enzyme PGK1 promotes M1 macrophage polarization and induces pyroptosis of acute lung injury via regulation of NLRP3.

Guiyin Zhu, Haiyang Yu, Tian Peng, Kun Yang, Xue Xu, Wen Gu

Abstract read
In one paragraph

Article in Respiratory research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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. Article
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  5. Macrophages with ITIH4 overexpression attenuate inflammatory responses and regulate intestinal epithelial cells.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
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  10. Review
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  15. Article
  16. Article
  17. Tolerance to Lung Infection in TWIK2 KbioRxiv : the preprint server for biology · 2025
    Article
  18. Article
  19. Article
  20. 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.

Guiyin Zhu *1Department of Respiratory Medicine, Xinhua hospital, Shanghai Jiao Tong University School of Medicine, 1665 KongJiang road, shanghai, 200092, China.
Haiyang Yu *1Department of Respiratory Medicine, Xinhua hospital, Shanghai Jiao Tong University School of Medicine, 1665 KongJiang road, shanghai, 200092, China.
Tian Peng1Department of Respiratory Medicine, Xinhua hospital, Shanghai Jiao Tong University School of Medicine, 1665 KongJiang road, shanghai, 200092, China.
Kun Yang1Department of Respiratory Medicine, Xinhua hospital, Shanghai Jiao Tong University School of Medicine, 1665 KongJiang road, shanghai, 200092, China.
Xue Xu1Department of Respiratory Medicine, Xinhua hospital, Shanghai Jiao Tong University School of Medicine, 1665 KongJiang road, shanghai, 200092, China.
Wen Gu1Department of Respiratory Medicine, Xinhua hospital, Shanghai Jiao Tong University School of Medicine, 1665 KongJiang road, shanghai, 200092, China. guwen@xinhuamed.com.cn.

Funding

National Natural Science Foundation of China 81770023Science and Technology Innovation Plan Of Shanghai Science and Technology Commission 22Y11901700
6 · The paper itself

Abstract

Acute lung injury (ALI) is characterized by an unregulated inflammatory reaction, often leading to severe morbidity and ultimately death. Excessive inflammation caused by M1 macrophage polarization and pyroptosis has been revealed to have a critical role in ALI. Recent study suggests that glycolytic reprogramming is important in the regulation of macrophage polarization and pyroptosis. However, the particular processes underlying ALI have yet to be identified. In this study, we established a Lipopolysaccharide(LPS)-induced ALI model and demonstrated that blocking glycolysis by using 2-Deoxy-D-glucose(2-DG) significantly downregulated the expression of M1 macrophage markers and pyroptosis-related genes, which was consistent with the in vitro results. Furthermore, our research has revealed that Phosphoglycerate Kinase 1(PGK1), an essential enzyme in the glycolysis pathway, interacts with NOD-, LRR- and pyrin domain-containing protein 3(NLRP3). We discovered that LPS stimulation improves the combination of PGK1 and NLRP3 both in vivo and in vitro. Interestingly, the absence of PGK1 reduces the phosphorylation level of NLRP3. Based on in vitro studies with mice bone marrow-derived macrophages (BMDMs), we further confirmed that siPGK1 plays a protective role by inhibiting macrophage pyroptosis and M1 macrophage polarization. The PGK1 inhibitor NG52 suppresses the occurrence of excessive inflammation in ALI. In general, it is plausible to consider a therapeutic strategy that focuses on modulating the relationship between PGK1 and NLRP3 as a means to mitigate the activation of inflammatory macrophages in ALI.

Indexed as

Acute Lung InjuryMacrophagesMice, Inbred C57BLNLR Family, Pyrin Domain-Containing 3 ProteinPhosphoglycerate KinasePyroptosisAnimalsCells, CulturedGlycolysisLipopolysaccharidesMaleMiceMice, KnockoutLipopolysaccharidesNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mousePgk1 protein, mousePhosphoglycerate KinaseAcute lung injuryGlycolytic reprogrammingMacrophage polarizationPyroptosis

Identifiers

PMID39080660
PMCPMC11290129

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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.