Evidence map›Paper›PMID 42505874›Full record

ArticleJournal of cardiovascular development and disease2026

Global Profiling of Protein Lysine Lactylation in Mouse Cardiac Hypertrophy: A Lactylome Analysis.

Wengen Zhu, Siyu Guo, Yunyao Yang, Yugang Dong, Chen Liu, Cong Chen

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Article in Journal of cardiovascular development and disease, 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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5 · Who and what money

Authors and funding

6 authors.

Wengen ZhuDepartment of Cardiology, The University of Hong Kong-Shenzhen Hospital, Shenzhen 518053, China.
Siyu GuoDepartment of Cardiology, The First Affiliated Hospital of Sun Yat-Sen University, Guangzhou 510080, China.
Yunyao YangDepartment of Cardiology, The First Affiliated Hospital of Sun Yat-Sen University, Guangzhou 510080, China.
Yugang DongDepartment of Cardiology, The First Affiliated Hospital of Sun Yat-Sen University, Guangzhou 510080, China.
Chen LiuDepartment of Cardiology, The First Affiliated Hospital of Sun Yat-Sen University, Guangzhou 510080, China.
Cong ChenDepartment of Cardiology, The University of Hong Kong-Shenzhen Hospital, Shenzhen 518053, China.

Funding

Guangdong Natural Science Foundation 2024A1515013289, 2023A1515012798Key R&D Projects of Guangzhou Science and Technology Program 2023B03J1243National Natural Science Foundation of China 82370383, 82100273Young Doctor "Sailing" Project SL2024A04J01866
6 · The paper itself

Abstract

backgroundCardiac hypertrophy, a major feature of heart failure, is closely linked to metabolic remodeling and energy deficiency. Lysine lactylation (Kla), a recently discovered post-translational modification (PTM), has been implicated in various cellular processes. However, its specific role in cardiac hypertrophy remains poorly understood.

methodsWe conducted quantitative proteomics and Kla PTM analysis on left ventricular tissues from both sham-operated and aortic banding-induced hypertrophic mouse hearts. Protein samples were extracted, enriched for lactylation, and subjected to mass spectrometry. Bioinformatic analyses were performed to uncover pathways and protein-protein interactions (PPI) related to Kla-modified proteins.

resultsOur lactylome analysis identified 159 Kla-modified sites across 80 proteins, with 72 proteins exhibiting elevated Kla levels, particularly in mitochondrial and sarcomeric proteins. Pathway enrichment analysis highlighted significant involvement of fatty acid metabolism, the tricarboxylic acid (TCA) cycle, and cardiomyopathy-related pathways, underscoring the role of Kla in energy metabolism and cardiac remodeling. PPI analysis further revealed the central role of metabolic and structural proteins in the hypertrophic response.

conclusionsOur study provides the comprehensive analysis of Kla in cardiac hypertrophy, revealing its significant role in modulating proteins involved in mitochondrial energy metabolism and sarcomeric structure. Our findings provide a comprehensive overview of the lactylation landscape in cardiac hypertrophy and reveal extensive lactylation changes in proteins associated with mitochondrial metabolism and sarcomeric organization. These observations suggest a potential link between Kla and cardiac hypertrophy, which warrants further functional investigation.

Indexed as

cardiac hypertrophyheart failurelysine lactylationmitochondriasarcomere

Identifiers

PMID42505874
PMCPMC13409870

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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 Socratic graph.