Evidence map›Paper›PMID 38767134›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2024

Histone H3K18 and Ezrin Lactylation Promote Renal Dysfunction in Sepsis-Associated Acute Kidney Injury.

Jiao Qiao, Yuan Tan, Hongchao Liu, Boxin Yang, Qian Zhang, Qi Liu, Wenyuan Sun, Zhongxin Li, Qingchen Wang, Weimin Feng and 2 more

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed, 2 pooled it
–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

105 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
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  10. Lactate-Mediated Lysine Lactylation in Renal Fibrosis: Current Progress and Challenges.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
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45 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

12 authors.

Jiao QiaoInstitute of Medical Technology, Peking University Health Science Center, Beijing, 100191, China.
Yuan TanInstitute of Medical Technology, Peking University Health Science Center, Beijing, 100191, China.
Hongchao LiuDepartment of Laboratory Medicine, Peking University Third Hospital, Beijing, 100191, China.
Boxin YangDepartment of Laboratory Medicine, Peking University Third Hospital, Beijing, 100191, China.
Qian ZhangDepartment of Laboratory Medicine, Peking University Third Hospital, Beijing, 100191, China.
Qi LiuInstitute of Medical Technology, Peking University Health Science Center, Beijing, 100191, China.
Wenyuan SunDepartment of Laboratory Medicine, Peking University Third Hospital, Beijing, 100191, China.
Zhongxin LiDepartment of Laboratory Medicine, Peking University Third Hospital, Beijing, 100191, China.
Qingchen WangDepartment of Laboratory Medicine, Peking University Third Hospital, Beijing, 100191, China.
Weimin FengInstitute of Medical Technology, Peking University Health Science Center, Beijing, 100191, China.
Shuo YangDepartment of Laboratory Medicine, Peking University Third Hospital, Beijing, 100191, China.
Liyan CuiInstitute of Medical Technology, Peking University Health Science Center, Beijing, 100191, China.ORCID 0000-0003-1870-3997

Funding

National Natural Science Foundation of China 61771022The Key Clinical Specialty Funding Project of Beijing and Hospital-Enterprise Joint Funding ProjectYoung Scientists Fund of the National Natural Science Foundation of China 81800604
6 · The paper itself

Abstract

Histone lactylation is a metabolic stress-related histone modification. However, the role of histone lactylation in the development of sepsis-associated acute kidney injury (SA-AKI) remains unclear. Here, histone H3K18 lactylation (H3K18la) is elevated in SA-AKI, which is reported in this study. Furthermore, this lactate-dependent histone modification is enriched at the promoter of Ras homolog gene family member A (RhoA) and positively correlated with the transcription. Correction of abnormal lactate levels resulted in a reversal of abnormal histone lactylation at the promoter of RhoA. Examination of related mechanism revealed that histone lactylation promoted the RhoA/Rho-associated protein kinase (ROCK) /Ezrin signaling, the activation of nuclear factor-κB (NF-κB), inflammation, cell apoptosis, and aggravated renal dysfunction. In addition, Ezrin can undergo lactylation modification. Multiple lactylation sites are identified in Ezrin and confirmed that lactylation mainly occurred at the K263 site. The role of histone lactylation is revealed in SA-AKI and reportes a novel post-translational modification in Ezrin. Its potential role in regulating inflammatory metabolic adaptation of renal proximal tubule epithelial cells is also elucidated. The results provide novel insights into the epigenetic regulation of the onset of SA-AKI.

Indexed as

Acute Kidney InjuryHistonesSepsisAnimalsCytoskeletal ProteinsDisease Models, AnimalEzrinHumansMaleMiceMice, Inbred C57BLSignal TransductionCytoskeletal ProteinsEzrinHistonesezringlycolysislactylationRhoAsepsis‐associated acute kidney injury

Identifiers

PMID38767134
PMCPMC11267308

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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.