The study investigated lactylation, a novel post-translational protein modification that affects metabolic reprogramming, epigenetic regulation, signal transduction, gene expression and cellular metabolism. Lactylation is involved in diseases such as tumors, Alzheimer's disease, heart failure and myocardial infarction, but it is little studied in the musculoskeletal system. The researchers analyzed lactylation omics on tear samples from the rotator cuff of rabbits and identified 2,624 modification sites on 851 proteins. They found subcellular localization, differentially modified proteins and enrichment of functional pathways, proposing the concept of a "co-lactylation modification effect of lysine". Lactylation is mainly in the cytoplasm, mitochondria and nucleus and enriches functions such as RNA processing, DNA processing and cellular metabolism. In rotator cuff tears, lactylation is widely present and significant, allowing the identification of key targets for intervention and novel therapeutic approaches related to metabolism.