Evidence map›Paper›PMID 42859221›Full record

ArticleCellular and molecular life sciences : CMLS2026

Sirt5 preserves mitochondrial homeostasis to improve cardiac function in ischemia-reperfusion injury by inhibiting ANT2 lysine lactylation modification.

Simeng Li, Siman Shen, Yongfang Hong, Kun Ding, Suyun Chen, Jianning Chen, Changsen Wang, Yaofeng Wen, Guixi Mo, Lili Yu and 2 more

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Simeng Li *Department of Anesthesiology, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Siman Shen *Department of Anesthesiology, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Yongfang Hong *Department of Cardiovascular Internal Medicine, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Kun DingDepartment of Anesthesiology, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Suyun ChenDepartment of Anesthesiology, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Jianning ChenDepartment of Anesthesiology, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Changsen WangDepartment of Anesthesiology, Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Yaofeng WenDepartment of Anesthesiology, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Guixi MoDepartment of Anesthesiology, Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Lili YuFaculty of Chinese Medicine, State Key Laboratory of Mechanism and Quality of Chinese Medicine, Macau University of Science and Technology, Macau, China. llyu@must.edu.mo.ORCID http://orcid.org/0000-0002-4625-3957
De-Li ShiLaboratory of Developmental Biology, Institut de Biologie Paris-Seine (IBPS), CNRS-UMR7622, Sorbonne University, Paris, France. de-li.shi@upmc.fr.ORCID http://orcid.org/0000-0002-6104-9137
Liangqing ZhangDepartment of Anesthesiology, the Second Affiliated Hospital of Guangdong Medical University, Zhanjiang, China. zhangliangqing@gdmu.edu.cn.ORCID http://orcid.org/0000-0003-2061-6147

Funding

National Natural Science Foundation of China 82370281Natural Science Foundation of Guangdong Province 2024A1515013119
6 · The paper itself

Abstract

Myocardial ischemia-reperfusion (IR) injury, a prevalent heart disease, disrupts mitochondrial homeostasis, affecting heart energy metabolism. The role of mitochondrial protein Sirt5 in protecting the heart from IR injury is explored in mice. Reduced Sirt5 levels in IR-injured hearts correlate with increased protein lactylation and impaired mitochondrial function. Sirt5 overexpression mitigates, while its knockout worsens, mitochondrial and cardiac damage. Sirt5 interacts with ANT2, reducing its lysine lactylation to enhance its association with VDAC1. This interaction improves cardiac function post-injury. Targeting ANT2 lactylation may offer a therapeutic approach for cardiac injury.

Indexed as

Adenine Nucleotide Translocator 2LysineMitochondriaMitochondria, HeartMyocardial Reperfusion InjurySirtuinsAnimalsHomeostasisMaleMiceMice, Inbred C57BLMice, KnockoutMyocardiumVoltage-Dependent Anion Channel 1Adenine Nucleotide Translocator 2LysineSIRT5 protein, mouseSirtuinsVoltage-Dependent Anion Channel 1ANT2Cardiac protectionIschemia-reperfusion injuryMitochondrial dysfunctionSirt5VDAC1

Identifiers

PMID42859221
PMCPMC13653916

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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.