Key result
Aortic banding-induced cardiac hypertrophy in mice elevates lactylation across 72 mitochondrial and sarcomeric proteins.
Why the study?
The specific role of lysine lactylation, a recently discovered post-translational modification, in cardiac hypertrophy remains poorly understood.
What is the profile of protein lysine lactylation in a mouse model of cardiac hypertrophy compared to sham controls?
What is the profile of protein lysine lactylation in a mouse model of cardiac hypertrophy compared to sham controls?
Protein lysine lactylation is elevated in mitochondrial and sarcomeric proteins during cardiac hypertrophy, suggesting a role in metabolic remodeling and energy deficiency.
Kla changes in hypertrophy may inform metabolic targets; leaves open any clinical role pending validation.
Background: Cardiac 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. Methods: We 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. Results: Our 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. Conclusions: Our 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.
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Zhu et al. (2026) studied Cardiac hypertrophy. Aortic banding vs. Sham-operated was evaluated on Protein lysine lactylation (Kla) sites and levels. Aortic banding-induced cardiac hypertrophy in mice resulted in 159 Kla-modified sites across 80 proteins, with 72 proteins showing elevated lactylation in mitochondrial and sarcomeric proteins.
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