ArticleNature communications2025
IDH2 lactylation promotes angiogenesis in murine diabetic myocardial infarction via blocking Cav1-eNOS interaction.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- ACAT1-Mediated SP1-K694 Lactylation Promotes M1 Macrophage Polarization via TREM1 Transcription in COPD.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- SYVN1-mediated succinate accumulation exacerbates heart failure.Science China. Life sciences · 2026Article
- Endothelial ATF4 attenuates hypertensive vascular damage via preserving mitochondrial redox homeostasis.Molecular and cellular biochemistry · 2026Article
- Endothelial SP1 lactylation promotes bronchopulmonary dysplasia via regulation of Cdkn1a expression.Scientific reports · 2026Article
- Lactylation in cardiac repair: Nexus and therapeutic opportunity.Journal of molecular and cellular cardiology plus · 2026Review
- Endothelial FOXO1 Lactylation: A New Link Between Disturbed Flow and Atherosclerosis.Circulation research · 2026Article
- Lactylation Modification: From Basic Biological Process to Clinical Cardiovascular Diseases.Research (Washington, D.C.) · 2026Review
- When metabolic enzymes meet lactylation: a bidirectional dialogue in health and disease.Frontiers in cell and developmental biology · 2026Review
- Lactylation: a novel epigenetic bridge connecting metabolic reprogramming and immune dysregulation in sepsis-associated ARDS.Frontiers in immunology · 2026Review
Corrections and comments
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Authors and funding
8 authors.
Funding
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Abstract
Compensatory angiogenesis is critical for preserving left ventricular function after myocardial infarction; however, this process is severely impaired in diabetes, exacerbating adverse outcomes in diabetic myocardial infarction (DMI). This study employed liquid chromatography-tandem mass spectrometry to identify lactylated proteins in the infarct border zone of DMI male mouse hearts. Our findings revealed that IDH2 is lactylated at lysine 272, enhancing its binding to Cav1 while inhibiting the Cav1-eNOS interaction. This modification promotes eNOS activity and facilitates the proliferation, migration, and angiogenesis of cardiac microvascular endothelial cells under high glucose and hypoxic conditions. In endothelial cell-specific IDH2-K272R knock-in male mice, the loss of K272 lactylation impairs cardiac function and exacerbates pathological remodeling due to disrupted angiogenesis. Additionally, ACAT1 and HDAC1 act as lactyltransferase and delactylase, respectively, utilizing intracellular lactate transported via MCT1 as a substrate for IDH2 lactylation. Furthermore, pharmacologic enhancement of IDH2 lactylation, as demonstrated by empagliflozin mitigating post-DMI injury, supports its potential as a therapeutic target for DMI.
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