Key result
Aortic banding significantly alters cardiac protein lactylation, elevating 141 lysine lactylation sites across 72 proteins.
Why the study?
The specific role of lysine lactylation, a recently discovered post-translational modification, in cardiac hypertrophy remains poorly understood.
Does pressure-overload-induced cardiac hypertrophy via descending aortic banding alter the global protein lysine lactylation (Kla) landscape in mouse left ventricular tissues compared to sham operation?
Does pressure-overload-induced cardiac hypertrophy via descending aortic banding alter the global protein lysine lactylation (Kla) landscape in mouse left ventricular tissues compared to sham operation?
This preclinical lactylome analysis demonstrates extensive lysine lactylation modifications in mitochondrial energy metabolism and sarcomeric structural proteins during pressure-overload cardiac hypertrophy, suggesting a novel post-translational link between metabolic reprogramming and cardiac remodeling.
Lactylation links metabolic remodeling to hypertrophy in mice; leaves open translational relevance and therapeutic targeting in humans.
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 (n=6). Descending aortic banding vs. Sham-operated wild-type controls was evaluated on Differentially regulated lysine lactylation (Kla) post-translational modification sites and proteins in left ventricular tissues (p=<0.05). Aortic banding-induced cardiac hypertrophy resulted in 159 significantly modified lysine lactylation sites across 80 proteins, with 72 proteins showing elevated lactylation at 141 sites.
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